|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-1251 |
0e+00 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 590.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 8 EEMQENYQRNGTAEEQPKLRKEAVGSIEIFRFADGLDITLMILGILASLVNGACLPLMPLVLGEMSDNLisgclvqtntt 87
Cdd:PTZ00265 22 DEVEKELNKKGTFELYKKIKTQKIPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFVSVFGVIMKNM----------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 88 nyqnctqsqeKLNEDMTLLTLYYVGIGVAALIFGYIQISLWIITAARQTKRIRKQFFHSVLAQDiGWFDSCDIGelnTRM 167
Cdd:PTZ00265 91 ----------NLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQD-GQFHDNNPG---SKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 168 TDDID----KISDGIGDKIALLFQNMSTFsIGLAV-GLVKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKA 242
Cdd:PTZ00265 157 TSDLDfyleQVNAGIGTKFITIFTYASAF-LGLYIwSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 243 GAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTIASKVSLGAVYFFMNGTYGLAFWYGTSLIL----NGEP 318
Cdd:PTZ00265 236 MSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIIsdlsNQQP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 319 G--YTIGTVLAVFFSVIHSSYCIGAAVPHFETFAIARGAAFHIFQVIDKKPSIDNfSTAGYKPESIEgTVEFKNVSFNYP 396
Cdd:PTZ00265 316 NndFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 397 SRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMV-DENDIRALNVRHYRDHIGVVSQEPVLFG 475
Cdd:PTZ00265 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFS 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 476 TTISNNIKYG---------------------RDD------------------------------------VTDEEMERAA 498
Cdd:PTZ00265 474 NSIKNNIKYSlyslkdlealsnyynedgndsQENknkrnscrakcagdlndmsnttdsneliemrknyqtIKDSEVVDVS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 499 REANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALE--KASKGRTT 576
Cdd:PTZ00265 554 KKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRIT 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 577 IVVAHRLSTIRSADLIVTL------------------------------KDG-----------------MLAEKGAHAEL 609
Cdd:PTZ00265 634 IIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnKDDnnnnnnnnnnkinnagsYIIEQGTHDAL 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 610 MA-KRGLYYSLVMSQDIKK---------ADEQMESMTYS-TER-----KTNSLPLHSVKSIKSDFIDKAEESTQSKEISL 673
Cdd:PTZ00265 714 MKnKNGIYYTMINNQKVSSkkssnndndKDSDMKSSAYKdSERgydpdEMNGNSKHENESASNKKSCKMSDENASENNAG 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 674 PEVSLLKILKLNKPEWPF---------------VVLGTLASVLNGTVHPVFSIIFAKII-TMFgnnDKTTLKHDAEIYSM 737
Cdd:PTZ00265 794 GKLPFLRNLFKRKPKAPNnlrivyreifsykkdVTIIALSILVAGGLYPVFALLYAKYVsTLF---DFANLEANSNKYSL 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 738 IFVILGVICFVSYFMQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDEKENSTGGLTTILAIDIAQIQGATGSRIGVLT 817
Cdd:PTZ00265 871 YILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFT 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 818 QNATNMGLSVIISF----IYGWEMTFL------ILSIAPVLAVTGMIETAAM----TGFA-NKDKQELKHAGKIATEALE 882
Cdd:PTZ00265 951 HFIVLFLVSMVMSFyfcpIVAAVLTGTyfifmrVFAIRARLTANKDVEKKEInqpgTVFAyNSDDEIFKDPSFLIQEAFY 1030
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 883 NIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRMTPEG-MFIVFTAI 961
Cdd:PTZ00265 1031 NMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDfMKSLFTFL 1110
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 962 AYGAMAiGETLVLAPEYSKAKSGAAHLFALLEKKPNIDSRSQEG---KKPDTCEGNLEFREVSFFYPCRPDVFILRGLSL 1038
Cdd:PTZ00265 1111 FTGSYA-GKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGiriKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTF 1189
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1039 SIERGKTVAFVGSSGCGKSTSVQLLQRLYD-------------------------------------------------- 1068
Cdd:PTZ00265 1190 SCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsged 1269
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1069 ----PVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYGDNSrvVPLDEIKEAANAANIHSFIEGLPEK 1144
Cdd:PTZ00265 1270 stvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNK 1347
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1145 YNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHAL----DKArtGRTCLVVTHRLSAIQNA 1220
Cdd:PTZ00265 1348 YDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRS 1425
|
1450 1460 1470
....*....|....*....|....*....|....*..
gi 255708477 1221 DLIVVLHNGK-----IKEQGTHQELLRNRD-IYFKLV 1251
Cdd:PTZ00265 1426 DKIVVFNNPDrtgsfVQAHGTHEELLSVQDgVYKKYV 1462
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
47-623 |
3.10e-174 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 527.81 E-value: 3.10e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 47 LMILGILASLVNGACLPLMPLVLGEMSDNLISGclvqtnttnyqnctqsqeklnEDMTLLTLY---YVGIGVAALIFGYI 123
Cdd:COG1132 22 LLILALLLLLLSALLELLLPLLLGRIIDALLAG---------------------GDLSALLLLlllLLGLALLRALLSYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 124 QISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKG 203
Cdd:COG1132 81 QRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 204 WKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKR 283
Cdd:COG1132 161 WRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 284 TIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEPgyTIGTVLAVFFSVIHSSYCIGAAVPHFETFAIARGAAFHIFQVI 363
Cdd:COG1132 241 ARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSL--TVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 364 DKKPSIDNfSTAGYKPESIEGTVEFKNVSFNYPsrPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDG 443
Cdd:COG1132 319 DEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 444 FIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGA 523
Cdd:COG1132 396 RILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 524 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEK 603
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
|
570 580
....*....|....*....|
gi 255708477 604 GAHAELMAKRGLYYSLVMSQ 623
Cdd:COG1132 556 GTHEELLARGGLYARLYRLQ 575
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
677-1255 |
3.04e-156 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 480.82 E-value: 3.04e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 677 SLLKILKLNKPEWPFVVLGTLASVLNGTVHPVFSIIFAKII-TMFGNNDKTTLKhdaeIYSMIFVILGVICFVSYFMQGL 755
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGDLSALL----LLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 756 FYGRAGEILTMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGW 835
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDR--RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 836 EMTFLILSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKAFEQMYEEMLQtQHRNTSKKA 915
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANE-ELRRANLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 916 QIIGSCY-AFSHAFIYFAYAAGFRFGAYLIQAGRMTPeGMFIVFtaIAYGAMAIGETLVLA---PEYSKAKSGAAHLFAL 991
Cdd:COG1132 241 ARLSALFfPLMELLGNLGLALVLLVGGLLVLSGSLTV-GDLVAF--ILYLLRLFGPLRQLAnvlNQLQRALASAERIFEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 992 LEKKPNIDSRSQEGKKPDTcEGNLEFREVSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQ 1071
Cdd:COG1132 318 LDEPPEIPDPPGAVPLPPV-RGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1072 GQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYGDNSrvVPLDEIKEAANAANIHSFIEGLPEKYNTQVGL 1151
Cdd:COG1132 395 GRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1152 KGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKI 1231
Cdd:COG1132 473 RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
570 580
....*....|....*....|....
gi 255708477 1232 KEQGTHQELLRNRDIYFKLVNAQS 1255
Cdd:COG1132 553 VEQGTHEELLARGGLYARLYRLQF 576
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
103-620 |
3.35e-143 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 451.10 E-value: 3.35e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 103 MTLLTLyyvgigvAALIFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKI 182
Cdd:TIGR00958 207 MCLLSI-------ASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNV 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 183 ALLFQNMSTFSIGLAVGLVKGWKLTLVTLSTSPLIMASAAACSRmVISLTSKEL-SAYSKAGAVAEEVLSSIRTVIAFRA 261
Cdd:TIGR00958 280 NVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGK-RYQLLSEELqEAVAKANQVAEEALSGMRTVRSFAA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 262 QEKELQRYTQNLKDAKDFGIKRTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGTVLAVffsVIHSSYcIGA 341
Cdd:TIGR00958 359 EEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGK--VSSGNLVSF---LLYQEQ-LGE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 342 AVPHFETF----AIARGAAFHIFQVIDKKPSIDNfsTAGYKPESIEGTVEFKNVSFNYPSRPSIKILKGLNLRIKSGETV 417
Cdd:TIGR00958 433 AVRVLSYVysgmMQAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 418 ALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERA 497
Cdd:TIGR00958 511 ALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 498 AREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAleKASKGRTTI 577
Cdd:TIGR00958 591 AKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVL 668
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 255708477 578 VVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSLV 620
Cdd:TIGR00958 669 LIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
386-623 |
1.46e-140 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 426.19 E-value: 1.46e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIG 465
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKI 545
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 546 LILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSLVMSQ 623
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1016-1254 |
1.50e-139 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 423.49 E-value: 1.50e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1016 EFREVSFFYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAI 1095
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1096 VPQEPVLFNCSIAENIAYGDNSRVVplDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPK 1175
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1176 ILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVNAQ 1254
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
100-623 |
3.54e-138 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 437.73 E-value: 3.54e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 100 NEDMTLLTLYYVGIGVAAL---IFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDdIDKISD 176
Cdd:COG2274 189 NQDLSTLWVLAIGLLLALLfegLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIRE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 177 GIGDKIALLFQNMSTFSIGLAVGLVKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTV 256
Cdd:COG2274 268 FLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 257 IAFRAQEKELQRYTQNLKDAKDFGIKRTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGTVLAvfFSVIhSS 336
Cdd:COG2274 348 KALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQ--LTLGQLIA--FNIL-SG 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 337 YCIGAA---VPHFETFAIARGAAFHIFQVIDKKPSIDNFSTAGyKPESIEGTVEFKNVSFNYPSRpSIKILKGLNLRIKS 413
Cdd:COG2274 423 RFLAPVaqlIGLLQRFQDAKIALERLDDILDLPPEREEGRSKL-SLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKP 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 414 GETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEE 493
Cdd:COG2274 501 GERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEE 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 494 MERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKG 573
Cdd:COG2274 581 IIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKG 660
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 255708477 574 RTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSLVMSQ 623
Cdd:COG2274 661 RTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
682-998 |
2.96e-129 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 399.52 E-value: 2.96e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 682 LKLNKPEWPFVVLGTLASVLNGTVHPVFSIIFAKIITMFGNNDKTTLKHDAEIYSMIFVILGVICFVSYFMQGLFYGRAG 761
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 762 EILTMRLRHLAFKAMLYQDIAWFDEKENSTGGLTTILAIDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGWEMTFLI 841
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 842 LSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGSC 921
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 922 YAFSHAFIYFAYAAGFRFGAYLIQAGRMTPEGMFIVFTAIAYGAMAIGETLVLAPEYSKAKSGAAHLFALLEKKPNI 998
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
678-1254 |
5.28e-129 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 413.08 E-value: 5.28e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 678 LLKILKLNKPEWPFVVLGTLASVLNGTVHPVFS-IIFAKIItmfGNNDKTTLkhdaeiYSMIFVILGVICF--VSYFMQG 754
Cdd:COG2274 147 FLRLLRRYRRLLLQVLLASLLINLLALATPLFTqVVIDRVL---PNQDLSTL------WVLAIGLLLALLFegLLRLLRS 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 755 LFYGRAGEILTMRLRHLAFKAMLYQDIAWFDEKenSTGGLTTILAiDIAQIQGA-TGSRIGVLTqNATNMGLSVIISFIY 833
Cdd:COG2274 218 YLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESR--SVGDLASRFR-DVESIREFlTGSLLTALL-DLLFVLIFLIVLFFY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 834 GWEMTFLILSIAPVLAVTGMIetaAMTGFANKDKQELKHAGKIAT---EALENIRTIVSLTREKAFEQMYEEmLQTQHRN 910
Cdd:COG2274 294 SPPLALVVLLLIPLYVLLGLL---FQPRLRRLSREESEASAKRQSllvETLRGIETIKALGAESRFRRRWEN-LLAKYLN 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 911 TSKKAQIIGSC-YAFSHAFIYFAYAAGFRFGAYLIQAGRMTPeGMFIVFTAIAYGAMA-IGETLVLAPEYSKAKSGAAHL 988
Cdd:COG2274 370 ARFKLRRLSNLlSTLSGLLQQLATVALLWLGAYLVIDGQLTL-GQLIAFNILSGRFLApVAQLIGLLQRFQDAKIALERL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 989 FALLEKKPNIDSrSQEGKKPDTCEGNLEFREVSFFYPcRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYD 1068
Cdd:COG2274 449 DDILDLPPEREE-GRSKLSLPRLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1069 PVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYGDNSrvVPLDEIKEAANAANIHSFIEGLPEKYNTQ 1148
Cdd:COG2274 527 PTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD--ATDEEIIEAARLAGLHDFIEALPMGYDTV 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1149 VGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHN 1228
Cdd:COG2274 605 VGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDK 684
|
570 580
....*....|....*....|....*.
gi 255708477 1229 GKIKEQGTHQELLRNRDIYFKLVNAQ 1254
Cdd:COG2274 685 GRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
93-623 |
1.14e-121 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 389.06 E-value: 1.14e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 93 TQSQEKLNEDMTLLTLYYVGIGVAALIFGYIQISLwiitAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDID 172
Cdd:TIGR02204 51 KDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWL----GERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 173 KISDGIGDKIALLFQNMSTFSIGLAVGLVKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSS 252
Cdd:TIGR02204 127 LLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 253 IRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGTVLA-VFFS 331
Cdd:TIGR02204 207 IRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGK--MSAGTLGQfVFYA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 332 VIHSSyCIGAAVPHFETFAIARGAAFHIFQVIDKKPSIDNFSTAGYKPESIEGTVEFKNVSFNYPSRPSIKILKGLNLRI 411
Cdd:TIGR02204 285 VMVAG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 412 KSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTD 491
Cdd:TIGR02204 364 RPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATD 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 492 EEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKAS 571
Cdd:TIGR02204 444 EEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLM 523
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 255708477 572 KGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSLVMSQ 623
Cdd:TIGR02204 524 KGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
48-359 |
7.71e-118 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 368.34 E-value: 7.71e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 48 MILGILASLVNGACLPLMPLVLGEMSDNLisgclvqtntTNYQNCTQSQEKLNEDMTLLTLYYVGIGVAALIFGYIQISL 127
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAF----------TDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTAC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 128 WIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGWKLT 207
Cdd:cd18577 71 WTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 208 LVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTIAS 287
Cdd:cd18577 151 LVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVS 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 288 KVSLGAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGTVLAVFFSVIHSSYCIGAAVPHFETFAIARGAAFHI 359
Cdd:cd18577 231 GLGLGLLFFIIFAMYALAFWYGSRLVRDGE--ISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
733-1254 |
5.39e-112 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 362.87 E-value: 5.39e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 733 EIYSMIFVILGVICFVSyFMQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQGATGSR 812
Cdd:TIGR02204 59 RYFAFLLVVALVLALGT-AARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDK--NRSGEVVSRLTTDTTLLQSVIGSS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 813 IGVLTQNATNMGLSVIISFIYGWEMTFLILS-----IAPVLAVTGMIETAAMTgfaNKDKqeLKHAGKIATEALENIRTI 887
Cdd:TIGR02204 136 LSMALRNALMCIGGLIMMFITSPKLTSLVLLavplvLLPILLFGRRVRKLSRE---SQDR--IADAGSYAGETLGAIRTV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 888 VSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRMTPE--GMFIVFTAIAYGA 965
Cdd:TIGR02204 211 QAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGtlGQFVFYAVMVAGS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 966 M-AIGETLvlaPEYSKAKSGAAHLFALLEKKPNIDSRSQEGKKPDTCEGNLEFREVSFFYPCRPDVFILRGLSLSIERGK 1044
Cdd:TIGR02204 291 IgTLSEVW---GELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1045 TVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYG--DNSRvvpl 1122
Cdd:TIGR02204 368 TVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGrpDATD---- 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1123 DEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKAR 1202
Cdd:TIGR02204 444 EEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLM 523
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 255708477 1203 TGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVNAQ 1254
Cdd:TIGR02204 524 KGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
661-1251 |
6.52e-110 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 361.73 E-value: 6.52e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 661 KAEESTQSKEISLpevsLLKILKLNKPEWPFVVLGTL---ASVLNGTVHPVFSiifAKII-TMFGNNDKTTLKHDaeIYS 736
Cdd:TIGR00958 136 KEAEQGQSETADL----LFRLLGLSGRDWPWLISAFVfltLSSLGEMFIPFYT---GRVIdTLGGDKGPPALASA--IFF 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 737 MifVILGVICFVSYFMQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQGATGSRIGVL 816
Cdd:TIGR00958 207 M--CLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDE--NKTGELTSRLSSDTQTMSRSLSLNVNVL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 817 TQNATnMGL-SVIISFIYGWEMTFLILSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKA 895
Cdd:TIGR00958 283 LRNLV-MLLgLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 896 FEQMYEEMLQtQHRNTSKKAQIIGSCY----AFSHAFIYFAYAAgfrFGAYLIQAGRMTPEGM--FIVFTaiaygaMAIG 969
Cdd:TIGR00958 362 EASRFKEALE-ETLQLNKRKALAYAGYlwttSVLGMLIQVLVLY---YGGQLVLTGKVSSGNLvsFLLYQ------EQLG 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 970 ETL-VLAPEYSKAKS--GAAH-LFALLEKKPNIdsrSQEGK-KPDTCEGNLEFREVSFFYPCRPDVFILRGLSLSIERGK 1044
Cdd:TIGR00958 432 EAVrVLSYVYSGMMQavGASEkVFEYLDRKPNI---PLTGTlAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGE 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1045 TVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYGDNSrvVPLDE 1124
Cdd:TIGR00958 509 VVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD--TPDEE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1125 IKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHalDKARTG 1204
Cdd:TIGR00958 587 IMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRAS 664
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 255708477 1205 RTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLV 1251
Cdd:TIGR00958 665 RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
47-619 |
9.84e-108 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 351.33 E-value: 9.84e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 47 LMILGILASLVNGACLPLMPLVLGEMSDNLISGclvqtnttnyqnctQSQEKLnedmTLLTLYYVGIGVAALIFGYIQiS 126
Cdd:TIGR02203 15 GLVLAGVAMILVAATESTLAALLKPLLDDGFGG--------------RDRSVL----WWVPLVVIGLAVLRGICSFVS-T 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 127 LWIITAARQTKR-IRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGWK 205
Cdd:TIGR02203 76 YLLSWVSNKVVRdIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 206 LTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTI 285
Cdd:TIGR02203 156 LTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 286 ASKVSLGAVYFFmnGTYGLAFWYGTSLILNGEPGYTIGTVLAVFFSVIHssycIGAAVPHFETFA--IARG--AAFHIFQ 361
Cdd:TIGR02203 236 AGSISSPITQLI--ASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIA----LIRPLKSLTNVNapMQRGlaAAESLFT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 362 VIDKKPSIDnfsTAGYKPESIEGTVEFKNVSFNYPSRpSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPD 441
Cdd:TIGR02203 310 LLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 442 DGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGR-DDVTDEEMERAAREANAYDFIMEFPNKFNTLVGE 520
Cdd:TIGR02203 386 SGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 521 KGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGML 600
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
570
....*....|....*....
gi 255708477 601 AEKGAHAELMAKRGLYYSL 619
Cdd:TIGR02203 546 VERGTHNELLARNGLYAQL 564
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
386-619 |
2.39e-106 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 334.58 E-value: 2.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIG 465
Cdd:cd03251 1 VEFKNVTFRYPGDG-PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKI 545
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 546 LILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSL 619
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
686-1254 |
3.00e-105 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 344.39 E-value: 3.00e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 686 KPEWPFVVLGTLASVLNGTVHPVFSIIFAKIIT-MFGNNDKTTLKHDAEIYSMIFVILGVICFVS-YFMqglfyGRAGEI 763
Cdd:TIGR02203 10 RPYKAGLVLAGVAMILVAATESTLAALLKPLLDdGFGGRDRSVLWWVPLVVIGLAVLRGICSFVStYLL-----SWVSNK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 764 LTMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQGATGSRIGVLTQNatnmGLSVIISFI----YGWEMTF 839
Cdd:TIGR02203 85 VVRDIRVRMFEKLLGLPVSFFDR--QPTGTLLSRITFDSEQVASAATDAFIVLVRE----TLTVIGLFIvllyYSWQLTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 840 LILSIAPVLAVtgmietaAMTGFA------NKDKQELK-HAGKIATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTS 912
Cdd:TIGR02203 159 IVVVMLPVLSI-------LMRRVSkrlrriSKEIQNSMgQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 913 KKAQIIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRMTPEGMFIVFTAIAYGAMAIGETLVLAPEYSKAKSGAAHLFALL 992
Cdd:TIGR02203 232 KMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 993 EKKPNIDsrsqEGKKP-DTCEGNLEFREVSFFYPCRpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQ 1071
Cdd:TIGR02203 312 DSPPEKD----TGTRAiERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1072 GQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYGDnSRVVPLDEIKEAANAANIHSFIEGLPEKYNTQVGL 1151
Cdd:TIGR02203 387 GQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1152 KGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKI 1231
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
570 580
....*....|....*....|...
gi 255708477 1232 KEQGTHQELLRNRDIYFKLVNAQ 1254
Cdd:TIGR02203 546 VERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
386-623 |
1.53e-103 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 327.26 E-value: 1.53e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPsrPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIG 465
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKI 545
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 546 LILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSLVMSQ 623
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
167-623 |
6.57e-103 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 339.10 E-value: 6.57e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 167 MTDDIDKISDGIGDkiaLLfqNMSTFSIG---------LAVGLVK-GWKLTLVTLSTSPLIMASAAACSRMVISLTSKEL 236
Cdd:COG5265 137 LSRDIERGTKGIEF---LL--RFLLFNILptlleialvAGILLVKyDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMN 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 237 SAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKrtiaSKVSLGAVYF----FMNGTYGLAFWYGTSL 312
Cdd:COG5265 212 EADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYERAAVK----SQTSLALLNFgqalIIALGLTAMMLMAAQG 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 313 ILNGEpgYTIGTVLAVffsvihSSYCIGAAVP-HFETFA---IARGAAF--HIFQVIDKKPSIDNfsTAGYKPESI-EGT 385
Cdd:COG5265 288 VVAGT--MTVGDFVLV------NAYLIQLYIPlNFLGFVyreIRQALADmeRMFDLLDQPPEVAD--APDAPPLVVgGGE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNY-PSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHI 464
Cdd:COG5265 358 VRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAI 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPK 544
Cdd:COG5265 435 GIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPP 514
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 545 ILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSLVMSQ 623
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
987-1255 |
4.88e-100 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 331.40 E-value: 4.88e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 987 HLFALLEKKPNIDSRsqEGKKP-DTCEGNLEFREVSFFY-PCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQ 1064
Cdd:COG5265 331 RMFDLLDQPPEVADA--PDAPPlVVGGGEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1065 RLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYG--DNSRvvplDEIKEAANAANIHSFIEGLP 1142
Cdd:COG5265 406 RFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGrpDASE----EEVEAAARAAQIHDFIESLP 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1143 EKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADL 1222
Cdd:COG5265 482 DGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADE 561
|
250 260 270
....*....|....*....|....*....|...
gi 255708477 1223 IVVLHNGKIKEQGTHQELLRNRDIYFKLVNAQS 1255
Cdd:COG5265 562 ILVLEAGRIVERGTHAELLAQGGLYAQMWARQQ 594
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
48-359 |
4.35e-99 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 318.45 E-value: 4.35e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 48 MILGILASLVNGACLPLMPLVLGEMSDNLISGCLVQTNTTNYQNCTQSQ--EKLNEDMTLLTLYYVGIGVAALIFGYIQI 125
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSGLNSSAGpfEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 126 SLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGWK 205
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 206 LTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTI 285
Cdd:cd18558 161 LTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 286 ASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGTVLAVFFSVIHSSYCIGAAVPHFETFAIARGAAFHI 359
Cdd:cd18558 241 TFNISMGAAFLLIYASYALAFWYGTYLVTQQE--YSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1015-1250 |
1.41e-97 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 311.09 E-value: 1.41e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPDvFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLFNCSIAENIAYGDnsRVVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKP 1174
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 1175 KILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKL 1250
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1015-1254 |
1.06e-95 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 306.08 E-value: 1.06e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLFNCSIAENIAYGDNSrvVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKP 1174
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1175 KILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVNAQ 1254
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
384-614 |
2.26e-95 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 304.92 E-value: 2.26e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 384 GTVEFKNVSFNYpsRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDH 463
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 IGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNP 543
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 544 KILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRG 614
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
139-619 |
8.49e-93 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 310.80 E-value: 8.49e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 139 IRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKI-SDGIGDKIALLFQNMSTfsIGL-AVGLVKGWKLTLVTLSTSPL 216
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVaSSSSGALITVVREGASI--IGLfIMMFYYSWQLSLILIVIAPI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 217 IMasaaacsrMVISLTSKELSAYSK-----AGAV---AEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTIASK 288
Cdd:PRK11176 178 VS--------IAIRVVSKRFRNISKnmqntMGQVttsAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 289 VSLGAVYFFmnGTYGLAF-WYGTSLILNGEpGYTIGTVLAVFFSVIHSSYCIGAAVPHFETFAIARGAAFHIFQVIDKKP 367
Cdd:PRK11176 250 ISDPIIQLI--ASLALAFvLYAASFPSVMD-TLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQ 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 368 SIDnfsTAGYKPESIEGTVEFKNVSFNYPSR--PSikiLKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFI 445
Cdd:PRK11176 327 EKD---EGKRVIERAKGDIEFRNVTFTYPGKevPA---LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 446 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDV-TDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQ 524
Cdd:PRK11176 401 LLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 525 MSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKG 604
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERG 560
|
490
....*....|....*
gi 255708477 605 AHAELMAKRGLYYSL 619
Cdd:PRK11176 561 THAELLAQNGVYAQL 575
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
360-641 |
1.09e-91 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 307.66 E-value: 1.09e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 360 FQVIDKKPSIDNFSTAGyKPESIEGTVEFKNVSFNYP-SRPSIKilkGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLY 438
Cdd:PRK13657 310 FEVEDAVPDVRDPPGAI-DLGRVKGAVEFDDVSFSYDnSRQGVE---DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVF 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 439 DPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLV 518
Cdd:PRK13657 386 DPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVV 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 519 GEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDG 598
Cdd:PRK13657 466 GERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNG 545
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 255708477 599 MLAEKGAHAELMAKRGLYYSLVMSQDIKKADEQMESMTYSTER 641
Cdd:PRK13657 546 RVVESGSFDELVARGGRFAALLRAQGMLQEDERRKQPAAEGAN 588
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
48-614 |
1.11e-91 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 307.07 E-value: 1.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 48 MILGILASLVNGACLPLMPLVLGEMSDNLISGclvqtnttnyqnctqsqeklNEDMTLLTLYYVGIGVAAL---IFGYIQ 124
Cdd:COG4988 19 LALAVLLGLLSGLLIIAQAWLLASLLAGLIIG--------------------GAPLSALLPLLGLLLAVLLlraLLAWLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 125 ISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNM-STFSIGLAVGLVkG 203
Cdd:COG4988 79 ERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAAlVPLLILVAVFPL-D 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 204 WKLTLVTLSTSPLI---MA---SAAAcsrmviSLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEkelqRYTQNL-KDA 276
Cdd:COG4988 158 WLSGLILLVTAPLIplfMIlvgKGAA------KASRRQWRALARLSGHFLDRLRGLTTLKLFGRAK----AEAERIaEAS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 277 KDFGiKRT----------------IAS-KVSLGAVYFfmngtyglafwyGTSLiLNGEPGYTIG-TVL---AVFFSvihs 335
Cdd:COG4988 228 EDFR-KRTmkvlrvaflssavlefFASlSIALVAVYI------------GFRL-LGGSLTLFAAlFVLllaPEFFL---- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 336 sycigaavP------HFETFAIARGAAFHIFQVIDKKPSIDNFSTAGyKPESIEGTVEFKNVSFNYPSRPsiKILKGLNL 409
Cdd:COG4988 290 --------PlrdlgsFYHARANGIAAAEKIFALLDAPEPAAPAGTAP-LPAAGPPSIELEDVSFSYPGGR--PALDGLSL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 410 RIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDV 489
Cdd:COG4988 359 TIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 490 TDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 569
Cdd:COG4988 439 SDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR 518
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 255708477 570 ASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRG 614
Cdd:COG4988 519 LAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
681-1243 |
2.26e-91 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 306.30 E-value: 2.26e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 681 ILKLNKPEWPFVVLGTLASVLNGTVHPVFSIIFAKIIT--MFGNNDKttlkhdAEIYSMIFVILGVIC--FVSYFMQGLF 756
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAglIIGGAPL------SALLPLLGLLLAVLLlrALLAWLRERA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 757 YGRAGEILTMRLRHLAFKAMLYQDIAWFDEKenSTGGLTTILaidIAQIQGATGSRIGVLTQnatnMGLSVIISFIygwe 836
Cdd:COG4988 82 AFRAAARVKRRLRRRLLEKLLALGPAWLRGK--STGELATLL---TEGVEALDGYFARYLPQ----LFLAALVPLL---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 837 mtfLILSIAP-------VLAVTG------MIetaaMTGFANKDKQElKHAGKIAT------EALENIRTIVSLTREKAFE 897
Cdd:COG4988 149 ---ILVAVFPldwlsglILLVTApliplfMI----LVGKGAAKASR-RQWRALARlsghflDRLRGLTTLKLFGRAKAEA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 898 QMYEEMLQTQHRNTSKKAQIigscyAF-SHA----FIYFAYA-----AGFRFGAyliqaGRMTPEGMFIVftaiaygama 967
Cdd:COG4988 221 ERIAEASEDFRKRTMKVLRV-----AFlSSAvlefFASLSIAlvavyIGFRLLG-----GSLTLFAALFV---------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 968 igetLVLAPEY--------------SKAKSGAAHLFALLEKKPNIDSRSQEgKKPDTCEGNLEFREVSFFYPcrPDVFIL 1033
Cdd:COG4988 281 ----LLLAPEFflplrdlgsfyharANGIAAAEKIFALLDAPEPAAPAGTA-PLPAAGPPSIELEDVSFSYP--GGRPAL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1034 RGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAY 1113
Cdd:COG4988 354 DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1114 GDnsRVVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKV 1193
Cdd:COG4988 434 GR--PDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAE 511
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 255708477 1194 VQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:COG4988 512 ILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
134-619 |
2.30e-90 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 303.61 E-value: 2.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 134 RQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISD------------GIGDKIALLFqnMSTFSIGLAVGLV 201
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNlylrvllpllvaLLVILAAVAF--LAFFSPALALVLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 202 KGWKLTLVTLstsPLIMASAA-ACSRMVISLTSkELSAYskagavAEEVLSSIRTVIAFRAQEKELQRYT---QNLKDAK 277
Cdd:COG4987 163 LGLLLAGLLL---PLLAARLGrRAGRRLAAARA-ALRAR------LTDLLQGAAELAAYGALDRALARLDaaeARLAAAQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 278 DfgiKRTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEPGytiGTVLAVFFSVIHSSYCIGAAVPH-FETFAIARGAA 356
Cdd:COG4987 233 R---RLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS---GPLLALLVLAALALFEALAPLPAaAQHLGRVRAAA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 357 FHIFQVIDKKPSIDnfSTAGYKPESIEGTVEFKNVSFNYPSRPSIkILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQR 436
Cdd:COG4987 307 RRLNELLDAPPAVT--EPAEPAPAPGGPSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 437 LYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNT 516
Cdd:COG4987 384 FLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDT 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 517 LVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLK 596
Cdd:COG4987 464 WLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLE 543
|
490 500
....*....|....*....|...
gi 255708477 597 DGMLAEKGAHAELMAKRGLYYSL 619
Cdd:COG4987 544 DGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1013-1245 |
2.79e-89 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 287.97 E-value: 2.79e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1013 GNLEFREVSFFYpcRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQ 1092
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1093 IAIVPQEPVLFNCSIAENIAYGDNSrvVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQ 1172
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 1173 KPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRD 1245
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
720-1254 |
5.93e-89 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 300.01 E-value: 5.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 720 FGNNDKTTLKHDAEIYSMIFVILGVICFVS-YFMQGLfygrAGEILtMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTIL 798
Cdd:PRK11176 56 FGKADRSVLKWMPLVVIGLMILRGITSFISsYCISWV----SGKVV-MTMRRRLFGHMMGMPVSFFDK--QSTGTLLSRI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 799 AIDIAQIQGAT-GSRIGVLTQNATNMGLsVIISFIYGWEMTFLILSIAPVLAVTgmIETAAmTGFANKDKQELKHAGKIA 877
Cdd:PRK11176 129 TYDSEQVASSSsGALITVVREGASIIGL-FIMMFYYSWQLSLILIVIAPIVSIA--IRVVS-KRFRNISKNMQNTMGQVT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 878 TEA---LENIRTIVSL----TREKAFEQMYEEMLQTQHRNTSKKA------QIIGScyaFSHAFIYfaYAAGFRFGAYLI 944
Cdd:PRK11176 205 TSAeqmLKGHKEVLIFggqeVETKRFDKVSNRMRQQGMKMVSASSisdpiiQLIAS---LALAFVL--YAASFPSVMDTL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 945 QAGRMTpegmfIVFTAIaYGAMAIGETLV-LAPEYSKAKSGAAHLFALLEKKPNIDsrsqEGK-KPDTCEGNLEFREVSF 1022
Cdd:PRK11176 280 TAGTIT-----VVFSSM-IALMRPLKSLTnVNAQFQRGMAACQTLFAILDLEQEKD----EGKrVIERAKGDIEFRNVTF 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1023 FYPCRpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVL 1102
Cdd:PRK11176 350 TYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1103 FNCSIAENIAYGDN---SRvvplDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLL 1179
Cdd:PRK11176 429 FNDTIANNIAYARTeqySR----EQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILIL 504
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1180 DEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVNAQ 1254
Cdd:PRK11176 505 DEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
824-1250 |
6.73e-85 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 288.20 E-value: 6.73e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 824 GLSVIISFIYGWemtfLILSIAPVLAVTGMIETAAMTGFANKDKQELKHA-GKIATEALENIRTIVSLT---REKAFEQM 899
Cdd:COG4987 145 AAVAFLAFFSPA----LALVLALGLLLAGLLLPLLAARLGRRAGRRLAAArAALRARLTDLLQGAAELAaygALDRALAR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 900 YEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRMTPegmfIVFTAIAYGAMAIGETLVLAP--- 976
Cdd:COG4987 221 LDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSG----PLLALLVLAALALFEALAPLPaaa 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 977 -EYSKAKSGAAHLFALLEKKPNIDSRSQEGKKPDtcEGNLEFREVSFFYPCRPDvFILRGLSLSIERGKTVAFVGSSGCG 1055
Cdd:COG4987 297 qHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPG--GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1056 KSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYGDNSrvVPLDEIKEAANAANIH 1135
Cdd:COG4987 374 KSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD--ATDEELWAALERVGLG 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1136 SFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLS 1215
Cdd:COG4987 452 DWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLA 531
|
410 420 430
....*....|....*....|....*....|....*
gi 255708477 1216 AIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKL 1250
Cdd:COG4987 532 GLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
379-600 |
1.28e-84 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 275.12 E-value: 1.28e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 379 PESIEGTVEFKNVSFNYPSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVR 458
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 459 HYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARA 538
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 539 LVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGML 600
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1008-1231 |
1.72e-83 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 272.04 E-value: 1.72e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1008 PDTCEGNLEFREVSFFYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQ 1087
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1088 WLRSQIAIVPQEPVLFNCSIAENIAYGDNSrvVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIA 1167
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 1168 RALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKI 1231
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
386-623 |
1.90e-83 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 272.05 E-value: 1.90e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNY-PSRPsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHI 464
Cdd:cd03252 1 ITFEHVRFRYkPDGP--VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPK 544
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 545 ILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSLVMSQ 623
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1015-1254 |
2.03e-80 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 263.58 E-value: 2.03e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYpcRPD-VFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQI 1093
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1094 AIVPQEPVLFNCSIAENIAYGDNSrvVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQK 1173
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1174 PKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVNA 1253
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 255708477 1254 Q 1254
Cdd:cd03252 237 Q 237
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
693-988 |
1.11e-79 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 264.52 E-value: 1.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 693 VLGTLASVLNGTVHPVFSIIFAKIITMFGNNDKT-----------------TLKHDAEIYSMIFVILGVICFVSYFMQGL 755
Cdd:cd18558 2 VVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTnitgnssglnssagpfeKLEEEMTLYAYYYLIIGAIVLITAYIQGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 756 FYGRAGEILTMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGW 835
Cdd:cd18558 82 FWGLAAGRQTKKIRYKFFHAIMRQEIGWFDV--NDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 836 EMTFLILSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKA 915
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 916 QIIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRM-TPEGMFIVFTAIAYGAMAIGETLVLAPeYSKAKSGAAHL 988
Cdd:cd18558 240 ITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYsIGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
103-623 |
1.42e-79 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 277.01 E-value: 1.42e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 103 MTLLTLYYVGIGVAALIFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDdIDKISDGI-GDK 181
Cdd:TIGR01846 178 LSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNFLtGSA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 182 IALLFQNMSTFsIGLAVGLVKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRA 261
Cdd:TIGR01846 257 LTVVLDLLFVV-VFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATAT 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 262 QEKELQRYTQNLKDAKDFGIKRTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGTVLAVFFSVIHSSYCIGA 341
Cdd:TIGR01846 336 EPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGA--LSPGQLVAFNMLAGRVTQPVLR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 342 AVPHFETFAIARGAAFHIFQVIDKkPSIDNFSTAGYKPEsIEGTVEFKNVSFNY-PSRPsiKILKGLNLRIKSGETVALV 420
Cdd:TIGR01846 414 LAQLWQDFQQTGIALERLGDILNS-PTEPRSAGLAALPE-LRGAITFENIRFRYaPDSP--EVLSNLNLDIKPGEFIGIV 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 421 GLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAARE 500
Cdd:TIGR01846 490 GPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKL 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 501 ANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVA 580
Cdd:TIGR01846 570 AGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIA 649
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 255708477 581 HRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSLVMSQ 623
Cdd:TIGR01846 650 HRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1015-1230 |
9.61e-78 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 253.46 E-value: 9.61e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPdVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLFNCSIAENIaygdnsrvvpldeikeaanaanihsfieglpekyntqvglkgaqLSGGQKQRLAIARALLQKP 1174
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 1175 KILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGK 1230
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
386-598 |
3.57e-77 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 251.92 E-value: 3.57e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPSiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIG 465
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLFGTTISNNIkygrddvtdeemeraareanaydfimefpnkfntlvgekgaqMSGGQKQRIAIARALVRNPKI 545
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255708477 546 LILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDG 598
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
878-1255 |
4.73e-75 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 263.91 E-value: 4.73e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 878 TEALENIRTIVSLTREKAFEQMYEEMLqTQHRNTSKKAQIIGSCYAFSHAFIY-FAYAAGFRFGAYLIQAGRMTPeGMFI 956
Cdd:TIGR01846 321 VESVTGIETIKATATEPQFQNRWDRQL-AAYVAASFRVTNLGNIAGQAIELIQkLTFAILLWFGAHLVIGGALSP-GQLV 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 957 VFTAIAygAMAIGETLVLAPEYSKAKsgaaHLFALLEKKPNI-DSRSQEGK--KPDTCE--GNLEFREVSFFYpcRPDV- 1030
Cdd:TIGR01846 399 AFNMLA--GRVTQPVLRLAQLWQDFQ----QTGIALERLGDIlNSPTEPRSagLAALPElrGAITFENIRFRY--APDSp 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1031 FILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAEN 1110
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDN 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1111 IAYGDNSrvVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDS 1190
Cdd:TIGR01846 551 IALCNPG--APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYES 628
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1191 EKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVNAQS 1255
Cdd:TIGR01846 629 EALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQS 693
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
937-1254 |
5.40e-75 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 260.66 E-value: 5.40e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 937 FRFGAYLIQAGRMTPeGMFIVFTAIAygAMAIGETLVLAPEYSKAKSGAAHL---FALLEKKPNIDSRsQEGKKPDTCEG 1013
Cdd:PRK13657 258 LVLGAALVQKGQLRV-GEVVAFVGFA--TLLIGRLDQVVAFINQVFMAAPKLeefFEVEDAVPDVRDP-PGAIDLGRVKG 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1014 NLEFREVSFFYP-CRPDVFilrGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQ 1092
Cdd:PRK13657 334 AVEFDDVSFSYDnSRQGVE---DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1093 IAIVPQEPVLFNCSIAENIAYGDNSrvVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQ 1172
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIRVGRPD--ATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1173 KPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVN 1252
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLR 568
|
..
gi 255708477 1253 AQ 1254
Cdd:PRK13657 569 AQ 570
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
677-1251 |
2.18e-71 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 253.71 E-value: 2.18e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 677 SLLKILKLNKPEWPFVVLGTLASVLNGTVHPVFSIIFAKIITMFGNNDKTTlkhdAEIYSMIFVIL--GVICFvsyfMQG 754
Cdd:TIGR03796 144 ALWRRLRGSRGALLYLLLAGLLLVLPGLVIPAFSQIFVDEILVQGRQDWLR----PLLLGMGLTALlqGVLTW----LQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 755 LFYGRAGEILTMRLRHLAFKAMLYQDIAWFDEKenSTGGLTTilAIDIAQIQGATGSriGVLTQNATN---MGLSVIISF 831
Cdd:TIGR03796 216 YYLRRLEIKLAVGMSARFLWHILRLPVRFFAQR--HAGDIAS--RVQLNDQVAEFLS--GQLATTALDavmLVFYALLML 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 832 IYGWEMTFLILSIAPVLAVTGMIETAAMTGFANKDKQElkhAGKIATEALENIRTIVSLtreKA-------FEQ---MYE 901
Cdd:TIGR03796 290 LYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQD---AGKLTGVAISGLQSIETL---KAsglesdfFSRwagYQA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 902 EMLQTQHRnTSKKAQIIGscyAFSHAFIYFAYAAGFRFGAYLIQAGRMTPeGMFIVFTAIAYGAMAIGETLV-LAPEYSK 980
Cdd:TIGR03796 364 KLLNAQQE-LGVLTQILG---VLPTLLTSLNSALILVVGGLRVMEGQLTI-GMLVAFQSLMSSFLEPVNNLVgFGGTLQE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 981 AKSGAAHL--------FALLEKKPNIDSRSQEGKKpdtCEGNLEFREVSFFYPcRPDVFILRGLSLSIERGKTVAFVGSS 1052
Cdd:TIGR03796 439 LEGDLNRLddvlrnpvDPLLEEPEGSAATSEPPRR---LSGYVELRNITFGYS-PLEPPLIENFSLTLQPGQRVALVGGS 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1053 GCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYGDNSrvVPLDEIKEAANAA 1132
Cdd:TIGR03796 515 GSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKDA 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1133 NIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALdkARTGRTCLVVTH 1212
Cdd:TIGR03796 593 AIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAH 670
|
570 580 590
....*....|....*....|....*....|....*....
gi 255708477 1213 RLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLV 1251
Cdd:TIGR03796 671 RLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
693-988 |
6.98e-70 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 236.60 E-value: 6.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 693 VLGTLASVLNGTVHPVFSIIFAKIITMF-----GNNDKTTLKHDAEIYSMIFVILGVICFVSYFMQGLFYGRAGEILTMR 767
Cdd:cd18577 2 IIGLLAAIAAGAALPLMTIVFGDLFDAFtdfgsGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 768 LRHLAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGWEMTFLILSIAPV 847
Cdd:cd18577 82 IRKRYLKALLRQDIAWFDK--NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 848 LAVTGMIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHA 927
Cdd:cd18577 160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFF 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 928 FIYFAYAAGFRFGAYLIQAGRMTPEGMFIVFTAIAYGAMAIGETLVLAPEYSKAKSGAAHL 988
Cdd:cd18577 240 IIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
142-620 |
4.21e-69 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 247.16 E-value: 4.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 142 QFFHSVLAQDIGWFDSCDIGELNTRMTDDiDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGWKLTLVTLSTSPLIMASA 221
Cdd:TIGR03796 232 RFLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLAL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 222 AACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIA------FRAQ-----------EKELQRYTQNLkdakdfgikRT 284
Cdd:TIGR03796 311 QLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKAsglesdFFSRwagyqakllnaQQELGVLTQIL---------GV 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 285 IASkvslgavyFFMNGTYGLAFWYGTSLILNGEpgYTIG------TVLAVFFSVIHSSYCIGAAVPHFE----------T 348
Cdd:TIGR03796 382 LPT--------LLTSLNSALILVVGGLRVMEGQ--LTIGmlvafqSLMSSFLEPVNNLVGFGGTLQELEgdlnrlddvlR 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 349 FAIARgaafhifQVIDKKPSidnfSTAGYKPESIEGTVEFKNVSFNYpSRPSIKILKGLNLRIKSGETVALVGLNGSGKS 428
Cdd:TIGR03796 452 NPVDP-------LLEEPEGS----AATSEPPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 429 TVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIM 508
Cdd:TIGR03796 520 TIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVIT 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 509 EFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKasKGRTTIVVAHRLSTIRS 588
Cdd:TIGR03796 600 SRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRD 677
|
490 500 510
....*....|....*....|....*....|..
gi 255708477 589 ADLIVTLKDGMLAEKGAHAELMAKRGLYYSLV 620
Cdd:TIGR03796 678 CDEIIVLERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
787-1254 |
4.82e-68 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 243.33 E-value: 4.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 787 KENSTGGLTTiLAIDIAQI-QGATGSRIGVLtqnatnmgLSVIIS-------FIYGWEMTF----LILSIAPVLAVTGMI 854
Cdd:TIGR03797 228 RQYSTGDLAS-RAMGISQIrRILSGSTLTTL--------LSGIFAllnlglmFYYSWKLALvavaLALVAIAVTLVLGLL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 855 ETaamtgfaNKDKQELKHAGKIATEALENIRTIVSL----TREKAFEQMYEEMlqTQHRNTSKKAQIIGSCYA-FSHAFI 929
Cdd:TIGR03797 299 QV-------RKERRLLELSGKISGLTVQLINGISKLrvagAENRAFARWAKLF--SRQRKLELSAQRIENLLTvFNAVLP 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 930 YFAYAAGFRFGAYLIQAGRMTPeGMFIVFTAiAYG---------AMAIGETLVLAPEYSKAKSgaahlfaLLEKKPNIDS 1000
Cdd:TIGR03797 370 VLTSAALFAAAISLLGGAGLSL-GSFLAFNT-AFGsfsgavtqlSNTLISILAVIPLWERAKP-------ILEALPEVDE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1001 rsqEGKKPDTCEGNLEFREVSFFYpcRPD-VFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGV 1079
Cdd:TIGR03797 441 ---AKTDPGKLSGAIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1080 DAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYGDnsrVVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGG 1159
Cdd:TIGR03797 516 DLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA---PLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGG 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1160 QKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRtcLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQE 1239
Cdd:TIGR03797 593 QRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDE 670
|
490
....*....|....*
gi 255708477 1240 LLRNRDIYFKLVNAQ 1254
Cdd:TIGR03797 671 LMAREGLFAQLARRQ 685
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
47-369 |
1.79e-67 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 230.42 E-value: 1.79e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 47 LMILGILASLVNGACLPLMPLVLGEMSDNLISgclvqtnttnyqnctQSQEKLNEDMTLLTLYYVGIGVAALIFGYIQIS 126
Cdd:cd18578 10 LLLLGLIGAIIAGAVFPVFAILFSKLISVFSL---------------PDDDELRSEANFWALMFLVLAIVAGIAYFLQGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 127 LWIITAARQTKRIRKQFFHSVLAQDIGWFDSCD--IGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGW 204
Cdd:cd18578 75 LFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 205 KLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRT 284
Cdd:cd18578 155 KLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 285 IASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGTVLAVFFSVIHSSYCIGAAVPHFETFAIARGAAFHIFQVID 364
Cdd:cd18578 235 LISGLGFGLSQSLTFFAYALAFWYGGRLVANGE--YTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLD 312
|
....*
gi 255708477 365 KKPSI 369
Cdd:cd18578 313 RKPEI 317
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
697-1256 |
2.00e-67 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 250.33 E-value: 2.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 697 LASVLNGTVHPVFSIIFAKIITMFGNNDKTtlkhDAEIYSMifVILGVICFVSYFMQGLFYGR-AGEIL-TMRLRHLafK 774
Cdd:PTZ00265 67 VCATISGGTLPFFVSVFGVIMKNMNLGENV----NDIIFSL--VLIGIFQFILSFISSFCMDVvTTKILkTLKLEFL--K 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 775 AMLYQDIAWFDEKENSTggLTTILAIDIAQIQGATGSR-IGVLTQNATNMGLsVIISFIYGWEMTFLILSIAPVLAVTGM 853
Cdd:PTZ00265 139 SVFYQDGQFHDNNPGSK--LTSDLDFYLEQVNAGIGTKfITIFTYASAFLGL-YIWSLFKNARLTLCITCVFPLIYICGV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 854 IETAAMTgfANKDKQEL--KHAGKIATEALENIRTIVSLTREKAFEQMYEeMLQTQHRNTSKKAQIIGSCY-AFSHAFIY 930
Cdd:PTZ00265 216 ICNKKVK--INKKTSLLynNNTMSIIEEALVGIRTVVSYCGEKTILKKFN-LSEKLYSKYILKANFMESLHiGMINGFIL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 931 FAYAAGFRFGAYLI--QAGRMTPEGMF--IVFTAIAYGAM--AIGETLVLA--PEYSKAKSGAAHLFALLEKKPNIDSrS 1002
Cdd:PTZ00265 293 ASYAFGFWYGTRIIisDLSNQQPNNDFhgGSVISILLGVLisMFMLTIILPniTEYMKSLEATNSLYEIINRKPLVEN-N 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1003 QEGKK-PDTceGNLEFREVSFFYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLF-DGVD 1080
Cdd:PTZ00265 372 DDGKKlKDI--KKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHN 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1081 AKELNVQWLRSQIAIVPQEPVLFNCSIAENIAY------------------------GDNSR------------------ 1118
Cdd:PTZ00265 450 LKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqeNKNKRnscrakcagdlndmsntt 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1119 -------------VVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSA 1185
Cdd:PTZ00265 530 dsneliemrknyqTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSS 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1186 LDNDSEKVVQHALD--KARTGRTCLVVTHRLSAIQNADLIVVLHNGK--------------------------------- 1230
Cdd:PTZ00265 610 LDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnn 689
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 255708477 1231 --------------IKEQGTHQELLRNRD-IYFKLVNAQSV 1256
Cdd:PTZ00265 690 nnnnnnkinnagsyIIEQGTHDALMKNKNgIYYTMINNQKV 730
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1013-1235 |
5.73e-67 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 225.16 E-value: 5.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1013 GNLEFREVSFFYPCRPDVfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQ 1092
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIP-ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1093 IAIVPQEPVLFNCSIAENIAYGDnsRVVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQ 1172
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 1173 KPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQG 1235
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
48-333 |
9.69e-67 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 226.37 E-value: 9.69e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 48 MILGILASLVNGACLPLMPLVLGEMSDNLISgclvqTNTTNYQnctqsqeklneDMTLLTLYYVGIGVAALIFGYIQISL 127
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLP-----DGDPETQ-----------ALNVYSLALLLLGLAQFILSFLQSYL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 128 WIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGWKLT 207
Cdd:pfam00664 65 LNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 208 LVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTIAS 287
Cdd:pfam00664 145 LVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVAN 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 255708477 288 KVSLGAVYFFMNGTYGLAFWYGTSLILNGEPGYTIGTVLAVFFSVI 333
Cdd:pfam00664 225 GLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQL 270
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
384-598 |
2.07e-65 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 220.54 E-value: 2.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 384 GTVEFKNVSFNYPSRPsIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDH 463
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 IGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNP 543
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 544 KILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDG 598
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
105-595 |
6.56e-65 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 229.87 E-value: 6.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 105 LLTLYYVGIGVAALifGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKIsDGIGDKIal 184
Cdd:TIGR02857 47 LGALALVLLLRALL--GWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEAL-DGYFARY-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 185 LFQNMSTFSIGLAVGLVKG---WKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRA 261
Cdd:TIGR02857 122 LPQLVLAVIVPLAILAAVFpqdWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 262 QEkelqRYTQNLKDAKDFGIKRTIaskvslgavyffmnGTYGLAFWygTSLILngEPGYTIGT-VLAVF--FSVIHSSYC 338
Cdd:TIGR02857 202 AK----AQAAAIRRSSEEYRERTM--------------RVLRIAFL--SSAVL--ELFATLSVaLVAVYigFRLLAGDLD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 339 IGAA------VPHFetFAIAR--GAAFH-----------IFQVIDKKPSIdnfsTAGYKP--ESIEGTVEFKNVSFNYPS 397
Cdd:TIGR02857 260 LATGlfvlllAPEF--YLPLRqlGAQYHaradgvaaaeaLFAVLDAAPRP----LAGKAPvtAAPASSLEFSGVSVAYPG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 398 RPsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTT 477
Cdd:TIGR02857 334 RR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGT 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 478 ISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDS 557
Cdd:TIGR02857 412 IAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
490 500 510
....*....|....*....|....*....|....*...
gi 255708477 558 ESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTL 595
Cdd:TIGR02857 492 ETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
127-616 |
1.39e-63 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 227.29 E-value: 1.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 127 LWIITAARQTK-RIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMStfsIGLAVGLVK--- 202
Cdd:PRK10789 58 VLLFGASYQLAvELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLV---MGCAVLIVMstq 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 203 -GWKLTLVTLSTSPlIMAsaaacsrMVISLTSKEL--------SAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQnl 273
Cdd:PRK10789 135 iSWQLTLLALLPMP-VMA-------IMIKRYGDQLherfklaqAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAA-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 274 kDAKDFGIKRTIASKVSL---GAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGTvLAVFfsVIHSSYCIGAAVPHFETFA 350
Cdd:PRK10789 205 -DAEDTGKKNMRVARIDArfdPTIYIAIGMANLLAIGGGSWMVVNGS--LTLGQ-LTSF--VMYLGLMIWPMLALAWMFN 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 351 IA-RGAAFH--IFQVIDKKPSIDNfstaGYKPESIE-GTVEFKNVSFNYP--SRPsikILKGLNLRIKSGETVALVGLNG 424
Cdd:PRK10789 279 IVeRGSAAYsrIRAMLAEAPVVKD----GSEPVPEGrGELDVNIRQFTYPqtDHP---ALENVNFTLKPGQMLGICGPTG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 425 SGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAY 504
Cdd:PRK10789 352 SGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVH 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 505 DFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLS 584
Cdd:PRK10789 432 DDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLS 511
|
490 500 510
....*....|....*....|....*....|..
gi 255708477 585 TIRSADLIVTLKDGMLAEKGAHAELMAKRGLY 616
Cdd:PRK10789 512 ALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
384-605 |
1.41e-62 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 212.35 E-value: 1.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 384 GTVEFKNVSFNYpsRPSIK-ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRD 462
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEPVLFGTTISNNI----KYgrddvTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARA 538
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLdpfgEY-----SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 539 LVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGA 605
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
971-1226 |
7.35e-62 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 221.01 E-value: 7.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 971 TLVLAPEY--------------SKAKSGAAHLFALLEKKPNIDSRSQEgkKPDTCEGNLEFREVSFFYPCRPDVfiLRGL 1036
Cdd:TIGR02857 266 VLLLAPEFylplrqlgaqyharADGVAAAEALFAVLDAAPRPLAGKAP--VTAAPASSLEFSGVSVAYPGRRPA--LRPV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1037 SLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYGDn 1116
Cdd:TIGR02857 342 SFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1117 sRVVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQH 1196
Cdd:TIGR02857 421 -PDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLE 499
|
250 260 270
....*....|....*....|....*....|
gi 255708477 1197 ALDKARTGRTCLVVTHRLSAIQNADLIVVL 1226
Cdd:TIGR02857 500 ALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1013-1236 |
2.67e-61 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 208.89 E-value: 2.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1013 GNLEFREVSFFYpcRPD-VFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRS 1091
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1092 QIAIVPQEPVLFNCSIAENIA----YGDnsrvvplDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIA 1167
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDpfgeYSD-------EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1168 RALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGT 1236
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
940-1242 |
9.74e-60 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 215.77 E-value: 9.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 940 GAYLIQAGRMTPEGMfivftaIAyGAMAIGetLVLAP---------EYSKAKSGAAHLFALLEKKPnidSRSQEGKKPDT 1010
Cdd:COG4618 260 GAYLVIQGEITPGAM------IA-ASILMG--RALAPieqaiggwkQFVSARQAYRRLNELLAAVP---AEPERMPLPRP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1011 cEGNLEFREVSFFYPCRpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKelnvQWLR 1090
Cdd:COG4618 328 -KGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS----QWDR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1091 SQ----IAIVPQEPVLFNCSIAENIA-YGDnsrvVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLA 1165
Cdd:COG4618 402 EElgrhIGYLPQDVELFDGTIAENIArFGD----ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIG 477
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1166 IARALLQKPKILLLDEATSALDNDSEKVVQHALDKART-GRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLR 1242
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
153-623 |
2.10e-59 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 217.90 E-value: 2.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 153 GWFDSCDIGELNTRmTDDIDKISDGIGDK--IALLFQNMSTFSIGLAvgLVKGWKLTLVTLstsplIMASAAACSRMVIS 230
Cdd:TIGR03797 225 SFFRQYSTGDLASR-AMGISQIRRILSGStlTTLLSGIFALLNLGLM--FYYSWKLALVAV-----ALALVAIAVTLVLG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 231 L--TSKELSAYSKAGAVAEEVLSSIRTVIAFR----------------AQEKELQRYTQNLKDAKD-FGikrTIASKVSL 291
Cdd:TIGR03797 297 LlqVRKERRLLELSGKISGLTVQLINGISKLRvagaenrafarwaklfSRQRKLELSAQRIENLLTvFN---AVLPVLTS 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 292 GAVYFFMNGTYG-LAFWYGTSLILNGEPGYTIGTVLAVFFSVIHssycIGAAVPHFEtfaiargaafHIFQVIDKKPSID 370
Cdd:TIGR03797 374 AALFAAAISLLGgAGLSLGSFLAFNTAFGSFSGAVTQLSNTLIS----ILAVIPLWE----------RAKPILEALPEVD 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 371 nfsTAGYKPESIEGTVEFKNVSFNY-PSRPsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDE 449
Cdd:TIGR03797 440 ---EAKTDPGKLSGAIEVDRVTFRYrPDGP--LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDG 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 450 NDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMErAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQ 529
Cdd:TIGR03797 515 QDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWE-AARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQ 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 530 KQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRttIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAEL 609
Cdd:TIGR03797 594 RQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDEL 671
|
490
....*....|....
gi 255708477 610 MAKRGLYYSLVMSQ 623
Cdd:TIGR03797 672 MAREGLFAQLARRQ 685
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
379-1250 |
4.45e-59 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 224.05 E-value: 4.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 379 PESIE---------GTVEFKNVSFNYpSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFImvde 449
Cdd:TIGR00957 621 PDSIErrtikpgegNSITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV---- 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 450 ndiralnvrHYRDHIGVVSQEPVLFGTTISNNIKYGRDdvTDEEMERAAREANAYDFIME-FPNKFNTLVGEKGAQMSGG 528
Cdd:TIGR00957 696 ---------HMKGSVAYVPQQAWIQNDSLRENILFGKA--LNEKYYQQVLEACALLPDLEiLPSGDRTEIGEKGVNLSGG 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 529 QKQRIAIARALVRNPKILILDEATSALDSE-SKSAVQAAL--EKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGA 605
Cdd:TIGR00957 765 QKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGS 844
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 606 HAELMAKRGLYYSLVMS-----QDIKKADE-------------QME---SMTYSTERKTnslpLHSVKSIKSDFIDKAEE 664
Cdd:TIGR00957 845 YQELLQRDGAFAEFLRTyapdeQQGHLEDSwtalvsgegkeakLIEngmLVTDVVGKQL----QRQLSASSSDSGDQSRH 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 665 STQSKEISLPEVSLL--KILKLNKPE---------WPFV----VLGTLASVLNGTVHPVFSIIFAKIITMF-------GN 722
Cdd:TIGR00957 921 HGSSAELQKAEAKEEtwKLMEADKAQtgqvelsvyWDYMkaigLFITFLSIFLFVCNHVSALASNYWLSLWtddpmvnGT 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 723 NDKTTLKhdAEIYSMIFVILGVICFvSYFMQGlfygRAGEILTMRLRHLAF-KAMLYQDIAWFDEkeNSTGGLTTILAID 801
Cdd:TIGR00957 1001 QNNTSLR--LSVYGALGILQGFAVF-GYSMAV----SIGGIQASRVLHQDLlHNKLRSPMSFFER--TPSGNLVNRFSKE 1071
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 802 IAQIQGATGSRIGVLTQNATNMGLSVIIsfiygwemtflILSIAPVLAVT----GMIETAAMTGFANKDKQeLKHAGKIA 877
Cdd:TIGR00957 1072 LDTVDSMIPPVIKMFMGSLFNVIGALIV-----------ILLATPIAAVIipplGLLYFFVQRFYVASSRQ-LKRLESVS 1139
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 878 --------TEALENIRTIVSLTREKAFEQMYEEMLQTQHRN----------TSKKAQIIGSC-------------YAFSH 926
Cdd:TIGR00957 1140 rspvyshfNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAyypsivanrwLAVRLECVGNCivlfaalfavisrHSLSA 1219
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 927 AFIYFAYAAGFRFGAYLIQAGRMTPEGmfivftaiaygamaigETLVLA----PEYSKAKSGAAHLFallekkpnidsrs 1002
Cdd:TIGR00957 1220 GLVGLSVSYSLQVTFYLNWLVRMSSEM----------------ETNIVAverlKEYSETEKEAPWQI------------- 1270
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1003 QEGKKPDTC--EGNLEFREVSFFYpcRPDV-FILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGV 1079
Cdd:TIGR00957 1271 QETAPPSGWppRGRVEFRNYCLRY--REDLdLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGL 1348
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1080 DAKELNVQWLRSQIAIVPQEPVLFNCSIAENI----AYGDnsrvvplDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQ 1155
Cdd:TIGR00957 1349 NIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYSD-------EEVWWALELAHLKTFVSALPDKLDHECAEGGEN 1421
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1156 LSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQG 1235
Cdd:TIGR00957 1422 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFG 1501
|
970
....*....|....*
gi 255708477 1236 THQELLRNRDIYFKL 1250
Cdd:TIGR00957 1502 APSNLLQQRGIFYSM 1516
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
386-1253 |
8.52e-59 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 222.93 E-value: 8.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQ-LLQRLYDPDDGFIMVdendiralnvrhyRDHI 464
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI-------------RGSV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQEPVLFGTTISNNIKYGrddvTDEEMERAAREANA----YDFIMeFPNKFNTLVGEKGAQMSGGQKQRIAIARALV 540
Cdd:PLN03232 682 AYVPQVSWIFNATVRENILFG----SDFESERYWRAIDVtalqHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVY 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 541 RNPKILILDEATSALDSE-SKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELmAKRGLYYSL 619
Cdd:PLN03232 757 SNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL-SKSGSLFKK 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 620 VM--------SQDIKKADEQMESMTYSTERKTNSLPLHSV---KSIKSDFIDKAEESTQSkeislpeVSLLKILKLNKPE 688
Cdd:PLN03232 836 LMenagkmdaTQEVNTNDENILKLGPTVTIDVSERNLGSTkqgKRGRSVLVKQEERETGI-------ISWNVLMRYNKAV 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 689 ---WpfVVLGTLASVLNGTVHPVFSIIFAKIITmfgnnDKTTLK-HDAEIYSMIFVILGVICFVSYFMQGLFYGRAGEIL 764
Cdd:PLN03232 909 gglW--VVMILLVCYLTTEVLRVSSSTWLSIWT-----DQSTPKsYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHA 981
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 765 TMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQgatgSRIGVLTQNATNMGLSVIISF-IYGWEMTFLILS 843
Cdd:PLN03232 982 AKRLHDAMLNSILRAPMLFFHT--NPTGRVINRFSKDIGDID----RNVANLMNMFMNQLWQLLSTFaLIGTVSTISLWA 1055
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 844 IAPVLavtgMIETAAMTGFANKDKqELKHAGKIATEAL-----ENIRTIVSLTREKAFEQM-------YEEMLQTQHRNT 911
Cdd:PLN03232 1056 IMPLL----ILFYAAYLYYQSTSR-EVRRLDSVTRSPIyaqfgEALNGLSSIRAYKAYDRMakingksMDNNIRFTLANT 1130
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 912 SKKAQIIGSCYAFSHAFIYF-AYAAGFRFGAYLIQAGRMTPEGMFIVFTaiaygamaIGETLVLAPEYSKAKSGAAHLFA 990
Cdd:PLN03232 1131 SSNRWLTIRLETLGGVMIWLtATFAVLRNGNAENQAGFASTMGLLLSYT--------LNITTLLSGVLRQASKAENSLNS 1202
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 991 LLEKKPNIDSRSQ-----EGKKPDT---CEGNLEFREVSFFYpcRPDVF-ILRGLSLSIERGKTVAFVGSSGCGKSTSVQ 1061
Cdd:PLN03232 1203 VERVGNYIDLPSEataiiENNRPVSgwpSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLN 1280
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1062 LLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAygdnsrvvPLDE-----IKEAANAANIHS 1136
Cdd:PLN03232 1281 ALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID--------PFSEhndadLWEALERAHIKD 1352
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1137 FIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSA 1216
Cdd:PLN03232 1353 VIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNT 1432
|
890 900 910
....*....|....*....|....*....|....*...
gi 255708477 1217 IQNADLIVVLHNGKIKEQGTHQELL-RNRDIYFKLVNA 1253
Cdd:PLN03232 1433 IIDCDKILVLSSGQVLEYDSPQELLsRDTSAFFRMVHS 1470
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
266-619 |
3.32e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 208.53 E-value: 3.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 266 LQRYTQNLKDAKD--FGIKRTIASKVSLG-AVYFFMNG-TYGLAFWYGTSLILNGEPGytiGTVLAVFFsvihssYCIGA 341
Cdd:PRK11160 219 EDRYRQQLEQTEQqwLAAQRRQANLTGLSqALMILANGlTVVLMLWLAAGGVGGNAQP---GALIALFV------FAALA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 342 AvphFETFAIARGAAFHIFQVI----------DKKPSIDnFSTAGyKPESIEGTVEFKNVSFNYPSRPSiKILKGLNLRI 411
Cdd:PRK11160 290 A---FEALMPVAGAFQHLGQVIasarrineitEQKPEVT-FPTTS-TAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQI 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 412 KSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTD 491
Cdd:PRK11160 364 KAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASD 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 492 EEMERAAREANaYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKAS 571
Cdd:PRK11160 444 EALIEVLQQVG-LEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA 522
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 255708477 572 KGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSL 619
Cdd:PRK11160 523 QNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
814-1247 |
3.27e-56 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 205.72 E-value: 3.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 814 GVLTQ-NATNMGLSVII--SFIYGWEMTFLILSIAPVLAVtgMIE----------TAAMTGFANKDKQelkhagkiATEA 880
Cdd:PRK10789 113 GVLTLvDSLVMGCAVLIvmSTQISWQLTLLALLPMPVMAI--MIKrygdqlherfKLAQAAFSSLNDR--------TQES 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 881 LENIRTIvsltreKAF--EQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFAYA-------AGfrfGAYLIQAGRMTp 951
Cdd:PRK10789 183 LTSIRMI------KAFglEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGmanllaiGG---GSWMVVNGSLT- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 952 EGMFIVFtaIAYGAMAIGETLVLAPEYSKAKSGAA---HLFALLEKKPNIDSRSQ---EGKkpdtceGNLEFREVSFFYP 1025
Cdd:PRK10789 253 LGQLTSF--VMYLGLMIWPMLALAWMFNIVERGSAaysRIRAMLAEAPVVKDGSEpvpEGR------GELDVNIRQFTYP 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1026 cRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNC 1105
Cdd:PRK10789 325 -QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1106 SIAENIAYG--DNSRvvplDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEAT 1183
Cdd:PRK10789 404 TVANNIALGrpDATQ----QEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1184 SALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRN----RDIY 1247
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQsgwyRDMY 547
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
383-612 |
5.05e-56 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 204.98 E-value: 5.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 383 EGTVEFKNVSFNYP--SRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHY 460
Cdd:COG4618 328 KGRLSVENLTVVPPgsKRP---ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 461 RDHIGVVSQEPVLFGTTISNNIkyGR-DDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARAL 539
Cdd:COG4618 405 GRHIGYLPQDVELFDGTIAENI--ARfGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 540 VRNPKILILDEATSALDSESKSAVQAALEKA-SKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAK 612
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
991-1250 |
5.61e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 205.06 E-value: 5.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 991 LLEKKPNIDSRSQEGKKPDtcEGNLEFREVSFFYPCRPDVfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPV 1070
Cdd:PRK11160 317 ITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQPQP-VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1071 QGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYGDNSrvvPLDE-IKEAANAANIHSFIEGlPEKYNTQV 1149
Cdd:PRK11160 394 QGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPN---ASDEaLIEVLQQVGLEKLLED-DKGLNAWL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1150 GLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNG 1229
Cdd:PRK11160 470 GEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNG 549
|
250 260
....*....|....*....|.
gi 255708477 1230 KIKEQGTHQELLRNRDIYFKL 1250
Cdd:PRK11160 550 QIIEQGTHQELLAQQGRYYQL 570
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
161-583 |
1.46e-55 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 202.59 E-value: 1.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 161 GELNTRMTDDIDKISDGIgdkIALLFQNMSTFSIGLAVGLVKGWkltlvTLSTSPLIMASAAACSRMVISLTS------K 234
Cdd:TIGR02868 110 GDLLGRLGADVDALQDLY---VRVIVPAGVALVVGAAAVAAIAV-----LSVPAALILAAGLLLAGFVAPLVSlraaraA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 235 ELSAYSKAGAVAEEVLSSIR---TVIAFRAQEKELQRYTQNLKDAKDFGIKRTIASKVSLGAVYFFMNGTYGLAFWYGTS 311
Cdd:TIGR02868 182 EQALARLRGELAAQLTDALDgaaELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 312 LILNGEPGytiGTVLAVF----FSVIHSSYCIGAAVPHFETfaiARGAAFHIFQVIDKKPSIDNFSTAGYKPESIEG-TV 386
Cdd:TIGR02868 262 AVADGRLA---PVTLAVLvllpLAAFEAFAALPAAAQQLTR---VRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPSRPsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGV 466
Cdd:TIGR02868 336 ELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 467 VSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKIL 546
Cdd:TIGR02868 414 CAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPIL 493
|
410 420 430
....*....|....*....|....*....|....*..
gi 255708477 547 ILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRL 583
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
384-623 |
5.34e-54 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 199.56 E-value: 5.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 384 GTVEFKNVSFNYpsRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDH 463
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 IGVVSQEPVLFGTTISNNIKYGRDdVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNP 543
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 544 KILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSLVMSQ 623
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1015-1246 |
9.84e-54 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 187.54 E-value: 9.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPV--LFNCSIAENIAYGDNSRVVPLDEIKEAANAAnihsfiegLpekynTQVGLKG------AQLSGGQKQRLAI 1166
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEA--------L-----ELVGLEHladrppHELSGGQKQRVAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1167 ARALLQKPKILLLDEATSALDNDSEKVVQHALDK-ARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELLRNR 1244
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDlVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
..
gi 255708477 1245 DI 1246
Cdd:COG1122 226 EL 227
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
692-962 |
1.76e-53 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 188.62 E-value: 1.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 692 VVLGTLASVLNGTVHPVFSIIFAKII-TMFGNNDKTTlkHDAEIYSMIFVILGVICFVSYFMQGLFYGRAGEILTMRLRH 770
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILdVLLPDGDPET--QALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 771 LAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGWEMTFLILSIAPVLAV 850
Cdd:pfam00664 79 KLFKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 851 TGMIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIY 930
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
|
250 260 270
....*....|....*....|....*....|..
gi 255708477 931 FAYAAGFRFGAYLIQAGRMTPeGMFIVFTAIA 962
Cdd:pfam00664 237 LSYALALWFGAYLVISGELSV-GDLVAFLSLF 267
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
972-1257 |
4.80e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 196.60 E-value: 4.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 972 LVLAPEY------------SKAKS-GAAH-LFALLEKkpNIDSRSQEGKKPDTCEGN-LEFREVSFFypcRPDVFILRG- 1035
Cdd:PRK11174 294 LILAPEFyqplrdlgtfyhAKAQAvGAAEsLVTFLET--PLAHPQQGEKELASNDPVtIEAEDLEIL---SPDGKTLAGp 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1036 LSLSIERGKTVAFVGSSGCGKSTsvqLLQRL--YDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAY 1113
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTS---LLNALlgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1114 GDNSrvVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKV 1193
Cdd:PRK11174 446 GNPD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 1194 VQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQElLRNRDIYFKLVNAQSVQ 1257
Cdd:PRK11174 524 VMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAE-LSQAGGLFATLLAHRQE 586
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
740-1241 |
1.17e-52 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 194.49 E-value: 1.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 740 VILGVICFVSYFMQGLFYG-------RAGEILTMRLRHLAFKAMlyqdiawFDEKENSTGGLTTILAIDIAQIQGatgsr 812
Cdd:TIGR01842 46 LMLTVLALGLYLFLGLLDAlrsfvlvRIGEKLDGALNQPIFAAS-------FSATLRRGSGDGLQALRDLDQLRQ----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 813 igVLTQNATN-------MGLSVIISFIYGWEMTFLILSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKIATEALENIR 885
Cdd:TIGR01842 114 --FLTGPGLFaffdapwMPIYLLVCFLLHPWIGILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADSALRNAE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 886 TIVSLTREKAFEQMYEEMLQ---TQHRNTSKKAQIIGscyAFSHAFIYFAYAAGFRFGAYLIQAGRMTPeGMFIVFTAIA 962
Cdd:TIGR01842 192 VIEAMGMMGNLTKRWGRFHSkylSAQSAASDRAGMLS---NLSKYFRIVLQSLVLGLGAYLAIDGEITP-GMMIAGSILV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 963 YGAMAIGETLV-LAPEYSKAKSGAAHLFALLEKKPnidSRSQEGKKPDTcEGNLEFREVSFFYPcRPDVFILRGLSLSIE 1041
Cdd:TIGR01842 268 GRALAPIDGAIgGWKQFSGARQAYKRLNELLANYP---SRDPAMPLPEP-EGHLSVENVTIVPP-GGKKPTLRGISFSLQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1042 RGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIA-YGDNsrvV 1120
Cdd:TIGR01842 343 AGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIArFGEN---A 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1121 PLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALD- 1199
Cdd:TIGR01842 420 DPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKa 499
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 255708477 1200 -KARtGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELL 1241
Cdd:TIGR01842 500 lKAR-GITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1013-1256 |
1.49e-52 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 195.32 E-value: 1.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1013 GNLEFREVSFFYpcRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQ 1092
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1093 IAIVPQEPVLFNCSIAENIAYGdnsRVVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQ 1172
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1173 KPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVN 1252
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
|
....
gi 255708477 1253 AQSV 1256
Cdd:PRK10790 574 LQLA 577
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1015-1231 |
7.00e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 181.55 E-value: 7.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLFNCSIAENIAYGDNSRVVPLDEikEAANAAnIHSFieGLPEKY-NTQVglkgAQLSGGQKQRLAIARALLQK 1173
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQLRERKFDR--ERALEL-LERL--GLPPDIlDKPV----ERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 1174 PKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKI 1231
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1015-1238 |
9.62e-52 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 181.61 E-value: 9.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYD-----PVQGQVLFDGVD--AKELNVQ 1087
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiyDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1088 WLRSQIAIVPQEPVLFNCSIAENIAYGDNSRVV----PLDEI-KEAANAAnihsfieGLPEKYNTQvgLKGAQLSGGQKQ 1162
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRLHGIklkeELDERvEEALRKA-------ALWDEVKDR--LHALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1163 RLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQG-THQ 1238
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGpTEQ 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
402-619 |
2.56e-50 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 188.52 E-value: 2.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 402 KILKG-LNLRIKSGETVALVGLNGSGKSTVVQLLqrL-YDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTIS 479
Cdd:PRK11174 363 KTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNAL--LgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 480 NNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSES 559
Cdd:PRK11174 441 DNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 560 KSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSL 619
Cdd:PRK11174 521 EQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1015-1247 |
2.63e-50 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 186.65 E-value: 2.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRP--DVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVD---AKELNVQWL 1089
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltkLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1090 RSQIAIVPQEPVL-FNC--SIAENIAYG-DNSRVVPLDEIKEAANAAnihsfIEglpekyntQVGLKGA-------QLSG 1158
Cdd:COG1123 341 RRRVQMVFQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAERRERVAEL-----LE--------RVGLPPDladryphELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1159 GQKQRLAIARALLQKPKILLLDEATSALDndseKVVQHA-LD-----KARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKI 1231
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQiLNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
250
....*....|....*..
gi 255708477 1232 KEQGTHQELLRN-RDIY 1247
Cdd:COG1123 484 VEDGPTEEVFANpQHPY 500
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
383-612 |
5.85e-49 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 183.70 E-value: 5.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 383 EGTVEFKNVSFnYPSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRD 462
Cdd:TIGR01842 314 EGHLSVENVTI-VPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRN 542
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGD 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 543 PKILILDEATSALDSESKSAVQAALEKASK-GRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAK 612
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
978-1214 |
7.20e-49 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 182.95 E-value: 7.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 978 YSKAKSGAAHLFALLEKKPNIDSRSQEGKKPDTCEG-NLEFREVSFFYPCRPDVfiLRGLSLSIERGKTVAFVGSSGCGK 1056
Cdd:TIGR02868 297 LTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1057 STSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAEN--IAYGDnsrvVPLDEIKEAANAANI 1134
Cdd:TIGR02868 375 STLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENlrLARPD----ATDEELWAALERVGL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1135 HSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRL 1214
Cdd:TIGR02868 451 ADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
822-1253 |
8.43e-49 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 186.48 E-value: 8.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 822 NMGLSVIISFIYGWEMTFLILSIAPVLAVTGMIETAAMTGFaNKDKQELKHAGKIAT----EALENIRTIVSLTRE---- 893
Cdd:TIGR01193 279 DMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTF-NKLNHDAMQANAVLNssiiEDLNGIETIKSLTSEaery 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 894 KAFEQMYEEMLQTQHRNTSKKA--QIIGSCYAFS-HAFIYFayaagfrFGAYLIQAGRMTPeGMFIVFTA-IAYGAMAIG 969
Cdd:TIGR01193 358 SKIDSEFGDYLNKSFKYQKADQgqQAIKAVTKLIlNVVILW-------TGAYLVMRGKLTL-GQLITFNAlLSYFLTPLE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 970 ETLVLAPEYSKAKSGAAHLFALLEkkpnIDSRSQEGKKPDTCE---GNLEFREVSFFYP-CRPdvfILRGLSLSIERGKT 1045
Cdd:TIGR01193 430 NIINLQPKLQAARVANNRLNEVYL----VDSEFINKKKRTELNnlnGDIVINDVSYSYGyGSN---ILSDISLTIKMNSK 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1046 VAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYGdNSRVVPLDEI 1125
Cdd:TIGR01193 503 TTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLG-AKENVSQDEI 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1126 KEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKArTGR 1205
Cdd:TIGR01193 582 WAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDK 660
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 255708477 1206 TCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVNA 1253
Cdd:TIGR01193 661 TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1015-1234 |
1.16e-47 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 169.57 E-value: 1.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYP-CRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNvqwlrSQI 1093
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1094 AIVPQEPVLFN-CSIAENIAYGDNSRVVPLDEIKEAAnaaniHSFIEglpekyntQVGLKGA------QLSGGQKQRLAI 1166
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERA-----EELLE--------LVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 1167 ARALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLS-AIQNADLIVVLHN--GKIKEQ 1234
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
387-598 |
1.79e-47 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 168.80 E-value: 1.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPSRPSiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGV 466
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 467 VSQEP--VLFGTTISNNIKYG--RDDVTDEEMERAAREANAydfimefpnkfntLVGEKG------AQMSGGQKQRIAIA 536
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGleNLGLPEEEIEERVEEALE-------------LVGLEGlrdrspFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 537 RALVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDG 598
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
98-620 |
2.38e-47 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 181.86 E-value: 2.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 98 KLNEDMTLLTLYYVGIGVAALIFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDdIDKISDG 177
Cdd:TIGR01193 190 KMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 178 IGDKIALLFQNMStfsIGLAVGLVKGW---KLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIR 254
Cdd:TIGR01193 269 LASTILSLFLDMW---ILVIVGLFLVRqnmLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 255 TVIAFRAQEKELQRYTQNLKD--AKDFGIKRTIASKVSLGAVYFFMNGTYGLafWYGTSLILNGEpgYTIGTVLAvfFSV 332
Cdd:TIGR01193 346 TIKSLTSEAERYSKIDSEFGDylNKSFKYQKADQGQQAIKAVTKLILNVVIL--WTGAYLVMRGK--LTLGQLIT--FNA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 333 IHSSYC-----IGAAVPHFETFAIARGAAFHIFQVidkkPSIDNFSTAGYKPESIEGTVEFKNVSFNYPSrpSIKILKGL 407
Cdd:TIGR01193 420 LLSYFLtplenIINLQPKLQAARVANNRLNEVYLV----DSEFINKKKRTELNNLNGDIVINDVSYSYGY--GSNILSDI 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 408 NLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYG-R 486
Cdd:TIGR01193 494 SLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaK 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 487 DDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAA 566
Cdd:TIGR01193 574 ENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNN 653
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 255708477 567 LEKAsKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSLV 620
Cdd:TIGR01193 654 LLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
386-613 |
3.27e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 168.66 E-value: 3.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPsrPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIG 465
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPV--LFGTTISNNIKYG--RDDVTDEEMERAAREA----NAYDFIMEFPNkfntlvgekgaQMSGGQKQRIAIAR 537
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpeNLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 538 ALVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKGAHAELMAKR 613
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
387-598 |
1.23e-46 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 165.08 E-value: 1.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYP--SRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHI 464
Cdd:cd03246 2 EVENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQEPVLFGTTISNNIkygrddvtdeemeraareanaydfimefpnkfntlvgekgaqMSGGQKQRIAIARALVRNPK 544
Cdd:cd03246 79 GYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 545 ILILDEATSALDSESKSAVQAALEKASK-GRTTIVVAHRLSTIRSADLIVTLKDG 598
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDG 171
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
386-1257 |
1.58e-46 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 183.40 E-value: 1.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQ-LLQRLYDPDDGFIMVdendiralnvrhyRDHI 464
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI-------------RGTV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQEPVLFGTTISNNIKYGrDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPK 544
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 545 ILILDEATSALDSESKSAV-QAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSLVmsQ 623
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLM--E 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 624 DIKKADEQMESMTYSTERKTNSLPLhsVKSIKSDFIDKAEESTQSKEislpEVSLLkiLKLNKPEWPFV---VLGTLASV 700
Cdd:PLN03130 839 NAGKMEEYVEENGEEEDDQTSSKPV--ANGNANNLKKDSSSKKKSKE----GKSVL--IKQEERETGVVswkVLERYKNA 910
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 701 LNGTVhpVFSIIFAKII----------TMFGN-NDKTTLK-HDAEIYSMIFVIL--GVICFV---SYF--MQGLFYGRag 761
Cdd:PLN03130 911 LGGAW--VVMILFLCYVltevfrvsssTWLSEwTDQGTPKtHGPLFYNLIYALLsfGQVLVTllnSYWliMSSLYAAK-- 986
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 762 eiltmRLRHLAFKAMLYQDIAWFdeKENSTGGLTTILAIDIAQIQGATGsrigvltqNATNMGLSVIIS-----FIYGWE 836
Cdd:PLN03130 987 -----RLHDAMLGSILRAPMSFF--HTNPLGRIINRFAKDLGDIDRNVA--------VFVNMFLGQIFQllstfVLIGIV 1051
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 837 MTFLILSIAPVLavtgMIETAAMTGFANKDKqELKHAGKIAT--------EALENIRTIVSLtreKAFEQMYEEMLQTQH 908
Cdd:PLN03130 1052 STISLWAIMPLL----VLFYGAYLYYQSTAR-EVKRLDSITRspvyaqfgEALNGLSTIRAY---KAYDRMAEINGRSMD 1123
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 909 RNTskkaqiigscyafshafiyfayaagfRFGAYLIQAGRM------TPEGMFIVFTAI------------AYGAMAIGE 970
Cdd:PLN03130 1124 NNI--------------------------RFTLVNMSSNRWlairleTLGGLMIWLTASfavmqngraenqAAFASTMGL 1177
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 971 TLVLAPEYSKAKSGAAHLFALLEKKPN--------IDSRSQ-----EGKKPDT---CEGNLEFREVSFFYpcRPDVF-IL 1033
Cdd:PLN03130 1178 LLSYALNITSLLTAVLRLASLAENSLNavervgtyIDLPSEaplviENNRPPPgwpSSGSIKFEDVVLRY--RPELPpVL 1255
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1034 RGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENI-A 1112
Cdd:PLN03130 1256 HGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLdP 1335
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1113 YGDNSRVvpldEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEK 1192
Cdd:PLN03130 1336 FNEHNDA----DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDA 1411
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 1193 VVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYF-KLV------NAQSVQ 1257
Cdd:PLN03130 1412 LIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFsKMVqstgaaNAQYLR 1483
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1015-1255 |
2.10e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 166.78 E-value: 2.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWlRSQIA 1094
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLF-NCSIAENIAYGDNSRVVPLDEIKEAANAAnIHSFieGLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQK 1173
Cdd:COG1131 77 YVPQEPALYpDLTVRENLRFFARLYGLPRKEARERIDEL-LELF--GLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1174 PKILLLDEATSALD-NDSEKVVQHALDKARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLRNR--DIYFK 1249
Cdd:COG1131 150 PELLILDEPTSGLDpEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKARLleDVFLE 229
|
....*.
gi 255708477 1250 LVNAQS 1255
Cdd:COG1131 230 LTGEEA 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1015-1243 |
3.21e-46 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 174.71 E-value: 3.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDP---VQGQVLFDGVDAKELNVQWLRS 1091
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1092 QIAIVPQEP--VLFNCSIAENIAYGDNSRVVPLDEIKEAANAANIHSFIEGLPEKYNtqvglkgAQLSGGQKQRLAIARA 1169
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYP-------HQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 1170 LLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGvVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1015-1235 |
3.62e-46 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 164.02 E-value: 3.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPDVfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwLRSQIA 1094
Cdd:cd03247 1 LSINNVSFSYPEQEQQ-VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLFNCSIAENIaygdnsrvvpldeikeaanaanihsfieglpekyntqvglkGAQLSGGQKQRLAIARALLQKP 1174
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 1175 KILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQG 1235
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1015-1243 |
9.53e-46 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 168.74 E-value: 9.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwlRSQIA 1094
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLF-NCSIAENIAYGDNSRVVPLDEIKEAANAAnihsfIEglpekyntQVGLKG------AQLSGGQKQRLAIA 1167
Cdd:COG3842 81 MVFQDYALFpHLTVAENVAFGLRMRGVPKAEIRARVAEL-----LE--------LVGLEGladrypHQLSGGQQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1168 RALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLS---AIqnADLIVVLHNGKIKEQGTHQELLR 1242
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEIYE 225
|
.
gi 255708477 1243 N 1243
Cdd:COG3842 226 R 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1015-1235 |
9.60e-46 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 163.84 E-value: 9.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwlRSQIA 1094
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLF-NCSIAENIAYGDNSRVVPLDEIKEAANAANIHSFIEGLPEKYNtqvglkgAQLSGGQKQRLAIARALLQK 1173
Cdd:cd03259 76 MVFQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYP-------HELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1174 PKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQG 1235
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1016-1230 |
1.17e-45 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 163.79 E-value: 1.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1016 EFREVSFFYPcRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAI 1095
Cdd:cd03225 1 ELKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1096 VPQEP--VLFNCSIAENIAYGDNSRVVPLDEIKEAANAANIHSFIEGLPEKyNTQvglkgaQLSGGQKQRLAIARALLQK 1173
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDR-SPF------TLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1174 PKILLLDEATSALDNDSEKVVQHALDK-ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGK 1230
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1032-1243 |
1.93e-45 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 164.01 E-value: 1.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDG--VDAKELNVQWLRSQIAIVPQEPVLF-NCSIA 1108
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedLTDSKKDINKLRRKVGMVFQQFNLFpHLTVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1109 ENIAYGdnSRVV---PLDEIKEAAnaanihsfieglpEKYNTQVGLKG------AQLSGGQKQRLAIARALLQKPKILLL 1179
Cdd:COG1126 96 ENVTLA--PIKVkkmSKAEAEERA-------------MELLERVGLADkadaypAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1180 DEATSALD----NDSEKVVQhalDKARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:COG1126 161 DEPTSALDpelvGEVLDVMR---DLAKEGMTMVVVTHEMGfAREVADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1015-1235 |
2.47e-45 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 163.45 E-value: 2.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPD-VFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWL---R 1090
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1091 SQIAIVPQEPVL-FN--CSIAENIA--YGDNSRVVPLDEIKEAANAANIHSfieGLPEKYntqVGLKGAQLSGGQKQRLA 1165
Cdd:cd03257 82 KEIQMVFQDPMSsLNprMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGV---GLPEEV---LNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 1166 IARALLQKPKILLLDEATSALDNDSEKVVQHALDKART--GRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQG 1235
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1015-1241 |
2.97e-45 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 164.06 E-value: 2.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVL-FNCSIAENIAYG------DNSRVVPLDEikEAANAAnihsfIEglpekyntQVGLKG------AQLSGGQK 1161
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlgLFGRPSAEDR--EAVEEA-----LE--------RTGLEHladrpvDELSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1162 QRLAIARALLQKPKILLLDEATSALDndsekvVQHALD--------KARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIK 1232
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLD------LAHQLEvlellrrlARERGRTVVMVLHDLNlAARYADRLVLLKDGRIV 217
|
....*....
gi 255708477 1233 EQGTHQELL 1241
Cdd:COG1120 218 AQGPPEEVL 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1015-1233 |
3.33e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 164.11 E-value: 3.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRP-DVFILRGLSLSIERGKTVAFVGSSGCGKSTsvqLLqR----LYDPVQGQVLFDGVDAKELnvqwl 1089
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKST---LL-RliagLEKPTSGEVLVDGKPVTGP----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1090 RSQIAIVPQEPVLFN-CSIAENIAYGDNSRVVPLDEIKEAANAAnihsfIEglpekyntQVGLKGA------QLSGGQKQ 1162
Cdd:COG1116 79 GPDRGVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERAREL-----LE--------LVGLAGFedayphQLSGGMRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1163 RLAIARALLQKPKILLLDEATSALD--------NDSEKVVQhaldkaRTGRTCLVVTHRLS-AIQNADLIVVLHN--GKI 1231
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDaltrerlqDELLRLWQ------ETGKTVLFVTHDVDeAVFLADRVVVLSArpGRI 219
|
..
gi 255708477 1232 KE 1233
Cdd:COG1116 220 VE 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1015-1231 |
6.84e-45 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 160.07 E-value: 6.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYP--CRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQ 1092
Cdd:cd03246 1 LEVENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1093 IAIVPQEPVLFNCSIAENIaygdnsrvvpldeikeaanaanihsfieglpekyntqvglkgaqLSGGQKQRLAIARALLQ 1172
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1173 KPKILLLDEATSALDNDSEKVVQHALDKAR-TGRTCLVVTHRLSAIQNADLIVVLHNGKI 1231
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1015-1242 |
1.52e-44 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 161.89 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYP-CRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQI 1093
Cdd:COG1124 2 LEVRNLSVSYGqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1094 AIVPQEPVL-FN------CSIAEniaygdnsrvvPLDEIKEAANAANIHSFIEglpekyntQVGLKGA-------QLSGG 1159
Cdd:COG1124 82 QMVFQDPYAsLHprhtvdRILAE-----------PLRIHGLPDREERIAELLE--------QVGLPPSfldryphQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1160 QKQRLAIARALLQKPKILLLDEATSALDndseKVVQ-HALD-----KARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIK 1232
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALD----VSVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIV 218
|
250
....*....|
gi 255708477 1233 EQGTHQELLR 1242
Cdd:COG1124 219 EELTVADLLA 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
386-604 |
1.52e-43 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 158.11 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYD-----PDDGFIMVDENDIRALNVR-- 458
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 459 HYRDHIGVVSQEPVLFGTTISNNIKYG-------RDDVTDEEMERAAREANAYDfimEFPNKFNtlvgekGAQMSGGQKQ 531
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWD---EVKDRLH------ALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 532 RIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLS-TIRSADLIVTLKDGMLAEKG 604
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFG 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1033-1184 |
2.48e-43 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 154.73 E-value: 2.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFN-CSIAENI 1111
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1112 AYGdnsrvVPLDEIKEAANAANIHSFIE--GLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATS 1184
Cdd:pfam00005 81 RLG-----LLLKGLSKREKDARAEEALEklGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
404-553 |
3.87e-43 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 153.96 E-value: 3.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 404 LKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLF-GTTISNNI 482
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 483 KYGR------DDVTDEEMERAAREANAYDFImefpnkfNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATS 553
Cdd:pfam00005 81 RLGLllkglsKREKDARAEEALEKLGLGDLA-------DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
387-600 |
3.97e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 156.13 E-value: 3.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGV 466
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 467 VSQEPVLFGTTISNNIKYG---RDDVTDEEMERAAREAnaydfiMEFPNKF-NTLVGEkgaqMSGGQKQRIAIARALVRN 542
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPfqlRERKFDRERALELLER------LGLPPDIlDKPVER----LSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 543 PKILILDEATSALDSESKSAVQAALEK--ASKGRTTIVVAHRLSTI-RSADLIVTLKDGML 600
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIeRVADRVLTLEAGRL 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1015-1243 |
5.37e-43 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 157.08 E-value: 5.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPdvFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLF-NCSIAENIAygdnsrVVP-LDEIKEAANAANIHSFIE--GLPEKyntqvGLKG---AQLSGGQKQRLAIA 1167
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIA------LVPkLLKWPKEKIRERADELLAlvGLDPA-----EFADrypHELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1168 RALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRL-SAIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRlqQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
386-611 |
7.07e-43 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 164.69 E-value: 7.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPS--IKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN---VRHY 460
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 461 RDHIGVVSQEPV--LF-GTTISNNIKYG---RDDVTDEEMERAAREANA-----YDFIMEFPnkfntlvgekgAQMSGGQ 529
Cdd:COG1123 341 RRRVQMVFQDPYssLNpRMTVGDIIAEPlrlHGLLSRAERRERVAELLErvglpPDLADRYP-----------HELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 530 KQRIAIARALVRNPKILILDEATSALDseskSAVQAA-LE-----KASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAE 602
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALD----VSVQAQiLNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
....*....
gi 255708477 603 KGAHAELMA 611
Cdd:COG1123 486 DGPTEEVFA 494
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
387-598 |
1.35e-42 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 152.78 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGV 466
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 467 VSQepvlfgttisnnikygrddvtdeemeraareanaydfimefpnkfntlvgekgaqMSGGQKQRIAIARALVRNPKIL 546
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255708477 547 ILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTI-RSADLIVTLKDG 598
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAeLAADRVIVLKDG 156
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1015-1230 |
1.88e-42 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 154.16 E-value: 1.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPDV--FILRGLSLSIERGKTVAFVGSSGCGKSTsvqLLQRL---YDPVQGQVlfdgvdakelnvqWL 1089
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSV-------------SV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1090 RSQIAIVPQEPVLFNCSIAENIAYGdnsrvVPLDE--IKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIA 1167
Cdd:cd03250 65 PGSIAYVSQEPWIQNGTIRENILFG-----KPFDEerYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1168 RALLQKPKILLLDEATSALDND-SEKVVQHALDKA-RTGRTCLVVTHRLSAIQNADLIVVLHNGK 1230
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLlLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1015-1230 |
3.38e-42 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 152.34 E-value: 3.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDG--VDAKELNVQWLRSQ 1092
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedLTDLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1093 IAIVPQEPVLF-NCSIAENIAYGdnsrvvpldeikeaanaanihsfieglpekyntqvglkgaqLSGGQKQRLAIARALL 1171
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG-----------------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 1172 QKPKILLLDEATSALDNDSEKVVQHALD--KARTGRTCLVVTHRLS-AIQNADLIVVLHNGK 1230
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
386-602 |
4.34e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.05 E-value: 4.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPS-RPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN------VR 458
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelarLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 459 hyRDHIGVVSQEPVLFGT-TISNNIKYGR--DDVTDEEMERAAREANAY----DFIMEFPNkfntlvgekgaQMSGGQKQ 531
Cdd:COG1136 85 --RRHIGFVFQFFNLLPElTALENVALPLllAGVSRKERRERARELLERvglgDRLDHRPS-----------QLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 532 RIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTIRSADLIVTLKDGMLAE 602
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
51-327 |
2.01e-41 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 154.26 E-value: 2.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 51 GILASLVNGACLPLMPLVLGEMSDNLISGclvqtnttnyqnctQSQEKLNEdmtlLTLYYVGIGVAALIFGYIQISLWII 130
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKG--------------GDLDVLNE----LALILLAIYLLQSVFTFVRYYLFNI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 131 TAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGWKLTLVT 210
Cdd:cd18557 63 AGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 211 LSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTIASKVS 290
Cdd:cd18557 143 LLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALF 222
|
250 260 270
....*....|....*....|....*....|....*..
gi 255708477 291 LGAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGTVLA 327
Cdd:cd18557 223 QGITSLLIYLSLLLVLWYGGYLVLSGQ--LTVGELTS 257
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1015-1234 |
2.32e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 151.73 E-value: 2.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPC-RPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELN----VQWL 1089
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1090 RSQIAIVPQE----PVLfncSIAENIAYGDNSRVVPLDEIKEAANAAnihsfIEglpekyntQVGLKG------AQLSGG 1159
Cdd:COG1136 85 RRHIGFVFQFfnllPEL---TALENVALPLLLAGVSRKERRERAREL-----LE--------RVGLGDrldhrpSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 1160 QKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQ 1234
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
384-604 |
2.55e-41 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 151.03 E-value: 2.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 384 GTVEFKNVSFNY-PSRPsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRD 462
Cdd:cd03369 5 GEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEPVLFGTTISNNIKYgRDDVTDEEMERAAReanaydfimefpnkfntlVGEKGAQMSGGQKQRIAIARALVRN 542
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLDP-FDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 543 PKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKG 604
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1015-1243 |
2.83e-41 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 152.88 E-value: 2.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYD--P---VQGQVLFDGVD--AKELNVQ 1087
Cdd:COG1117 12 IEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDiyDPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1088 WLRSQIAIVPQEPVLFNCSIAENIAYG-----DNSRVVpLDEIKEAAnaanihsfiegLpekynTQVGL----------K 1152
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgIKSKSE-LDEIVEES-----------L-----RKAALwdevkdrlkkS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1153 GAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLS-AIQNADLIVVLHNGKI 1231
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGEL 231
|
250
....*....|..
gi 255708477 1232 KEQGTHQELLRN 1243
Cdd:COG1117 232 VEFGPTEQIFTN 243
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1015-1246 |
3.35e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 152.97 E-value: 3.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAK-ELNVQWLRSQI 1093
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1094 AIVPQEP----VlfnCSIAEN-IAYGDNSRVVPLDEIK----EAANAANIHSFIEGLPekyntqvglkgAQLSGGQKQRL 1164
Cdd:TIGR04520 80 GMVFQNPdnqfV---GATVEDdVAFGLENLGVPREEMRkrvdEALKLVGMEDFRDREP-----------HLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1165 AIARALLQKPKILLLDEATSALDNDSEK-VVQ--HALdKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELL 1241
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKeVLEtiRKL-NKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIF 224
|
....*
gi 255708477 1242 RNRDI 1246
Cdd:TIGR04520 225 SQVEL 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1015-1231 |
4.41e-41 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 150.72 E-value: 4.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPD-VFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWL---- 1089
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1090 RSQIAIVPQE----PVLfncSIAENIAYGDNSRVVPLDEIKEAAnaaniHSFIE--GLPEKYNTQVglkgAQLSGGQKQR 1163
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERA-----EELLErvGLGDRLNHYP----SELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1164 LAIARALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAIQNADLIVVLHNGKI 1231
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
386-604 |
1.12e-40 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 148.23 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPSiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAL--NVRHYrdh 463
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLekALSSL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 IGVVSQEPVLFGTTISNNIkygrddvtdeemeraareanaydfimefpnkfntlvgekGAQMSGGQKQRIAIARALVRNP 543
Cdd:cd03247 77 ISVLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 544 KILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKG 604
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
386-604 |
1.13e-40 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 149.96 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRP-SIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN---VRHYR 461
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 462 DHIGVVSQEPVL-------FGTTISNNIKYGRDDVTDEEMERAAREA-----NAYDFIMEFPNkfntlvgekgaQMSGGQ 529
Cdd:cd03257 82 KEIQMVFQDPMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYPH-----------ELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 530 KQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKG 604
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1013-1236 |
1.42e-40 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 149.10 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1013 GNLEFREVSFFYpcRPDV-FILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRS 1091
Cdd:cd03369 5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1092 QIAIVPQEPVLFNCSIAENI----AYGDnsrvvplDEIKEAANAAnihsfiEGlpekyntqvglkGAQLSGGQKQRLAIA 1167
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdpfdEYSD-------EEIYGALRVS------EG------------GLNLSQGQRQLLCLA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1168 RALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGT 1236
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
386-598 |
1.56e-40 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 149.18 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPS-RPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVR---HYR 461
Cdd:cd03255 1 IELKNLSKTYGGgGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 462 -DHIGVVSQEPVLFGT-TISNNIKY-----GrddVTDEEMERAAREANAYdfiMEFPNKFNTLVgekgAQMSGGQKQRIA 534
Cdd:cd03255 81 rRHIGFVFQSFNLLPDlTALENVELplllaG---VPKKERRERAEELLER---VGLGDRLNHYP----SELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 535 IARALVRNPKILILDEATSALDSESKSAVQAALEK--ASKGRTTIVVAHRLSTIRSADLIVTLKDG 598
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
51-324 |
1.82e-40 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 151.63 E-value: 1.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 51 GILASLVNGACLPLMPLVLGEMSDNLISGCLVQTnttnyqncTQSQEKLNEDMTLLTLYYVGIGVAALIFGyiqislWII 130
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGG--------EEALRALNQAVLILLGVVLIGSIATFLRS------WLF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 131 TAA--RQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGWKLTL 208
Cdd:cd18780 67 TLAgeRVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 209 VTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTIASK 288
Cdd:cd18780 147 VMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASG 226
|
250 260 270
....*....|....*....|....*....|....*.
gi 255708477 289 VSLGAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGT 324
Cdd:cd18780 227 GFNGFMGAAAQLAIVLVLWYGGRLVIDGE--LTTGL 260
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1033-1243 |
1.86e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 153.38 E-value: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAK-ELNVQwlRSQIAIVPQEPVLF-NCSIAEN 1110
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPR--ERRVGFVFQHYALFpHMTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1111 IAYGDNSRVVPLDEIKeaanaANIHSFIEglpekyntQVGLKG------AQLSGGQKQRLAIARALLQKPKILLLDEATS 1184
Cdd:COG1118 96 IAFGLRVRPPSKAEIR-----ARVEELLE--------LVQLEGladrypSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 1185 ALD----NDSEKVVQHALDkaRTGRTCLVVTH-RLSAIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:COG1118 163 ALDakvrKELRRWLRRLHD--ELGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
386-612 |
2.36e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.44 E-value: 2.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAlNVRHYRDHIG 465
Cdd:COG1131 1 IEVRGLTKRYGDK---TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLFGT-TISNNIKYGRD--DVTDEEMERAAREANAydfIMEFPNKFNTLVGekgaQMSGGQKQRIAIARALVRN 542
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFFARlyGLPRKEARERIDELLE---LFGLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 543 PKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKGAHAELMAK 612
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1016-1230 |
3.30e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 145.85 E-value: 3.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1016 EFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAI 1095
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1096 VPQepvlfncsiaeniaygdnsrvvpldeikeaanaanihsfieglpekyntqvglkgaqLSGGQKQRLAIARALLQKPK 1175
Cdd:cd00267 78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 1176 ILLLDEATSALDNDS-EKVVQHALDKARTGRTCLVVTHRLSAIQNA-DLIVVLHNGK 1230
Cdd:cd00267 101 LLLLDEPTSGLDPASrERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
386-610 |
4.41e-40 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 149.04 E-value: 4.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIG 465
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVL-FGTTISNNIKYGR---------DDVTDEEM-ERAAREANAYDFIMEFpnkFNTLvgekgaqmSGGQKQRIA 534
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREAvEEALERTGLEHLADRP---VDEL--------SGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 535 IARALVRNPKILILDEATSALDSESKSAVQAALEK--ASKGRTTIVVAHRLS-TIRSADLIVTLKDGMLAEKGAHAELM 610
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-624 |
6.53e-40 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 162.04 E-value: 6.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 12 ENYQRNGTAEEQPKL---RKEAVGSIEIFRFAD-----GLDITLMIlgILASLVNGACLPLMPLVLGEMSDNLISgclvq 83
Cdd:TIGR00957 925 AELQKAEAKEETWKLmeaDKAQTGQVELSVYWDymkaiGLFITFLS--IFLFVCNHVSALASNYWLSLWTDDPMV----- 997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 84 tnttnyqNCTQSQEKLNedmtlLTLY-YVGIGVAALIFGY-IQISLWIITAARqtkRIRKQFFHSVLAQDIGWFDSCDIG 161
Cdd:TIGR00957 998 -------NGTQNNTSLR-----LSVYgALGILQGFAVFGYsMAVSIGGIQASR---VLHQDLLHNKLRSPMSFFERTPSG 1062
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 162 ELNTRMTDDIDKISDGIGDKIaLLFQNmSTFS-IGLAVGLVKGWKLTLVTLSTSPLIMASA----AACSRMVISLTSKEL 236
Cdd:TIGR00957 1063 NLVNRFSKELDTVDSMIPPVI-KMFMG-SLFNvIGALIVILLATPIAAVIIPPLGLLYFFVqrfyVASSRQLKRLESVSR 1140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 237 S-AYSKAgavaEEVLSSIRTVIAFRAQEkelqrytqnlkdakDFGIKRTIASKVSLGAVYFFMNGTYGLAF---WYGTSL 312
Cdd:TIGR00957 1141 SpVYSHF----NETLLGVSVIRAFEEQE--------------RFIHQSDLKVDENQKAYYPSIVANRWLAVrleCVGNCI 1202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 313 ILngepgytigtvLAVFFSVIH----SSYCIGAAVPHfeTFAIARGAAFHIFQVIDKKPSI------DNFS-TAGYKPES 381
Cdd:TIGR00957 1203 VL-----------FAALFAVISrhslSAGLVGLSVSY--SLQVTFYLNWLVRMSSEMETNIvaverlKEYSeTEKEAPWQ 1269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 382 IEGT-----------VEFKNVSFNYpsRPSIK-ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDE 449
Cdd:TIGR00957 1270 IQETappsgwpprgrVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG 1347
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 450 NDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIK-YGRddVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGG 528
Cdd:TIGR00957 1348 LNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVG 1425
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 529 QKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAE 608
Cdd:TIGR00957 1426 QRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSN 1505
|
650
....*....|....*.
gi 255708477 609 LMAKRGLYYSlvMSQD 624
Cdd:TIGR00957 1506 LLQQRGIFYS--MAKD 1519
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1032-1245 |
7.83e-40 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 147.82 E-value: 7.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVD-----AKELNVqwLRSQIAIVPQEPVLF-NC 1105
Cdd:COG1127 20 VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitglsEKELYE--LRRRIGMLFQGGALFdSL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1106 SIAENIAYgdnsrvvPL--------DEIKEAANaanihsfieglpEKYNtQVGLKGA------QLSGGQKQRLAIARALL 1171
Cdd:COG1127 98 TVFENVAF-------PLrehtdlseAEIRELVL------------EKLE-LVGLPGAadkmpsELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1172 QKPKILLLDEATSALDNDSEKVV-------QHALdkartGRTCLVVTHRL-SAIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIdelirelRDEL-----GLTSVVVTHDLdSAFAIADRVAVLADGKIIAEGTPEELLAS 232
|
..
gi 255708477 1244 RD 1245
Cdd:COG1127 233 DD 234
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
108-317 |
8.30e-40 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 149.62 E-value: 8.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 108 LYYVGIGVAALIFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQ 187
Cdd:cd18572 40 LLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 188 NMSTFSIGLAVGLVKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQ 267
Cdd:cd18572 120 NLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREAR 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 255708477 268 RYTQNLKDAKDFGIKRTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGE 317
Cdd:cd18572 200 RYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGR 249
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
386-598 |
8.83e-40 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 146.46 E-value: 8.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPSI--KILKGLNLRIKSGETVALVGLNGSGKSTvvqLLQRL---YDPDDGFImvdendiralnvrHY 460
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSV-------------SV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 461 RDHIGVVSQEPVLFGTTISNNIKYGRDdvTDEEMERAAREANA--YDFIMeFPNKFNTLVGEKGAQMSGGQKQRIAIARA 538
Cdd:cd03250 65 PGSIAYVSQEPWIQNGTIRENILFGKP--FDEERYEKVIKACAlePDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 539 LVRNPKILILDEATSALDSES-----KSAVQAALekaSKGRTTIVVAHRLSTIRSADLIVTLKDG 598
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
387-632 |
9.13e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 147.70 E-value: 9.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNvRHYRDHIGV 466
Cdd:COG4555 3 EVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 467 VSQEPVLF-GTTISNNIKYGRddvTDEEMERAAREANAYDFI--MEFPNKFNTLVGEkgaqMSGGQKQRIAIARALVRNP 543
Cdd:COG4555 79 LPDERGLYdRLTVRENIRYFA---ELYGLFDEELKKRIEELIelLGLEEFLDRRVGE----LSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 544 KILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKGAHAELMAKRGL--YYSL 619
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIGEenLEDA 231
|
250
....*....|...
gi 255708477 620 VMsQDIKKADEQM 632
Cdd:COG4555 232 FV-ALIGSEEGEA 243
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
386-612 |
1.47e-39 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 147.96 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRpSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIR-ALNVRHYRDHI 464
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQEP--VLFGTTISNNIKYGRDD--VTDEEMER----AAREANAYDFIMEFPnkfntlvgekgAQMSGGQKQRIAIA 536
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKrvdeALKLVGMEDFRDREP-----------HLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 537 RALVRNPKILILDEATSALDSESKSAVQAALEK--ASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAK 612
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKlnKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
386-612 |
2.06e-39 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 146.57 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRP-SIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN---VRHYR 461
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 462 DHIGVVSQEPVLFGT-TISNNIKY-----GrddvtdeeMERAAREANAYDFImefpnkfnTLVG--EKG----AQMSGGQ 529
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALpleiaG--------VPKAEIEERVLELL--------ELVGleDKAdaypAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 530 KQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAH 606
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*.
gi 255708477 607 AELMAK 612
Cdd:cd03258 226 EEVFAN 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1015-1243 |
3.49e-39 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 145.80 E-value: 3.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPDVFI-LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELN---VQWLR 1090
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1091 SQIAIVPQEPVLFNC-SIAENIAYGDNSRVVPLDEIKEAANaanihsfiEGLpekynTQVGLKG------AQLSGGQKQR 1163
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVL--------ELL-----ELVGLEDkadaypAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1164 LAIARALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQEL 1240
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
...
gi 255708477 1241 LRN 1243
Cdd:cd03258 229 FAN 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1015-1252 |
5.90e-39 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 145.39 E-value: 5.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNvQWLRSQIA 1094
Cdd:COG4555 2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLF-NCSIAENIAYGDNSRVVPLDEIKEAANAAnIHSFieGLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQK 1173
Cdd:COG4555 78 VLPDERGLYdRLTVRENIRYFAELYGLFDEELKKRIEEL-IELL--GLEEFLDRRVG----ELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1174 PKILLLDEATSALD-NDSEKVVQHALDKARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLRNR------D 1245
Cdd:COG4555 151 PKVLLLDEPTNGLDvMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIgeenleD 230
|
....*..
gi 255708477 1246 IYFKLVN 1252
Cdd:COG4555 231 AFVALIG 237
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1015-1231 |
7.14e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 145.58 E-value: 7.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELN---VQWLRS 1091
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1092 QIAIVPQEPVLF-NCSIAENI---AYGDNS------RVVPLDEIKEAANAanihsfIE--GLPEKYNTQVGlkgaQLSGG 1159
Cdd:COG3638 81 RIGMIFQQFNLVpRLSVLTNVlagRLGRTStwrsllGLFPPEDRERALEA------LErvGLADKAYQRAD----QLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1160 QKQRLAIARALLQKPKILLLDEATSALD-NDSEKVVQHALDKART-GRTCLVVTHRLS-AIQNADLIVVLHNGKI 1231
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDpKTARQVMDLLRRIAREdGITVVVNLHQVDlARRYADRIIGLRDGRV 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1015-1245 |
7.30e-39 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 144.95 E-value: 7.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNV---QWLRS 1091
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1092 QIAIVPQEPVLFNC-SIAENIAYgdnsrvvPLDEikeaaNAANIHSFIEGLPEKYNTQVGLKG------AQLSGGQKQRL 1164
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAF-------PLRE-----HTRLSEEEIREIVLEKLEAVGLRGaedlypAELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1165 AIARALLQKPKILLLDEATSALDN-DSEKVVQHALD-KARTGRTCLVVTHRL-SAIQNADLIVVLHNGKIKEQGTHQELL 1241
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPiASGVIDDLIRSlKKELGLTSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
....
gi 255708477 1242 RNRD 1245
Cdd:cd03261 226 ASDD 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
386-608 |
9.70e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 144.04 E-value: 9.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPsrPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN---VRHYRD 462
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQE-PVLFGTTISNNIKY-----GRDDvtdEEMERAAREAnaydfiMEfpnkfntLVG--EKG----AQMSGGQK 530
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSR---KEIRRRVREV------LD-------LVGlsDKAkalpHELSGGEQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 531 QRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVA-HRLSTIRSADL-IVTLKDGMLAEKGAHAE 608
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1015-1240 |
1.24e-38 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 144.30 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAkeLNVQWLRSQIA 1094
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLF-NCSIAENIAYGDNSRVVPLDEIKEAANAAnIHsfieglpekyntQVGLKG------AQLSGGQKQRLAIA 1167
Cdd:cd03300 76 TVFQNYALFpHLTVFENIAFGLRLKKLPKAEIKERVAEA-LD------------LVQLEGyanrkpSQLSGGQQQRVAIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 1168 RALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQEL 1240
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1015-1243 |
1.45e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 147.91 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTsvqLLqR----LYDPVQGQVLFDGVDAKELNVQwlR 1090
Cdd:COG3839 4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKST---LL-RmiagLEDPTSGEILIGGRDVTDLPPK--D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1091 SQIAIVPQEPVLF-NCSIAENIAYGDNSRVVPLDEIK----EAANAANIHSFIEGLPekyntqvglkgAQLSGGQKQRLA 1165
Cdd:COG3839 75 RNIAMVFQSYALYpHMTVYENIAFPLKLRKVPKAEIDrrvrEAAELLGLEDLLDRKP-----------KQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1166 IARALLQKPKILLLDEATSALDND------SE-KVVQhaldkARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTH 1237
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKlrvemrAEiKRLH-----RRLGTTTIYVTHDQVeAMTLADRIAVMNDGRIQQVGTP 218
|
....*.
gi 255708477 1238 QELLRN 1243
Cdd:COG3839 219 EELYDR 224
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
48-330 |
1.49e-38 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 146.16 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 48 MILGILASLVNGACLPLMPLVLGEMSDNLIsgclvqtnttnyqnctqsQEKLNEDMTLLTLYYVGIGVAALIFGYIQISL 127
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVI------------------PAGDLSLLLWIALLLLLLALLRALLSYLRRYL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 128 WIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGWKLT 207
Cdd:cd07346 63 AARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 208 LVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTIAS 287
Cdd:cd07346 143 LVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLS 222
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 255708477 288 KVSLGAVYFFMNGTYGLAFWYGTSLILNGEPgyTIGTVLAVFF 330
Cdd:cd07346 223 ALFSPLIGLLTALGTALVLLYGGYLVLQGSL--TIGELVAFLA 263
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1015-1233 |
2.38e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.88 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELN---VQWLRS 1091
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1092 QIAIVPQE-PVLFNCSIAENIAYgdnsrvvPL-------DEIKEAANAAnihsfiegLpekynTQVGLKG------AQLS 1157
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVAL-------PLrvtgksrKEIRRRVREV--------L-----DLVGLSDkakalpHELS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1158 GGQKQRLAIARALLQKPKILLLDEATSALDND-SEKVVQHALDKARTGRTCLVVTHRLSAIQNADL-IVVLHNGKIKE 1233
Cdd:COG2884 140 GGEQQRVAIARALVNRPELLLADEPTGNLDPEtSWEIMELLEEINRRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1015-1243 |
6.02e-38 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 145.20 E-value: 6.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFR--EVSFFYPcRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDP---VQGQVLFDGVD-----AKEL 1084
Cdd:COG0444 2 LEVRnlKVYFPTR-RGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDllklsEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1085 nvQWLR-SQIAIVPQEPvlFNC---------SIAENIAYgdnSRVVPLDEIKEAAnaanihsfIEGLpekynTQVGLKGA 1154
Cdd:COG0444 81 --RKIRgREIQMIFQDP--MTSlnpvmtvgdQIAEPLRI---HGGLSKAEARERA--------IELL-----ERVGLPDP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1155 ---------QLSGGQKQRLAIARALLQKPKILLLDEATSALDndsekV-VQhA--LD-----KARTGRTCLVVTHRLSAI 1217
Cdd:COG0444 141 errldryphELSGGMRQRVMIARALALEPKLLIADEPTTALD-----VtIQ-AqiLNllkdlQRELGLAILFITHDLGVV 214
|
250 260
....*....|....*....|....*..
gi 255708477 1218 -QNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:COG0444 215 aEIADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
386-598 |
7.80e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 140.01 E-value: 7.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSrpsIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN--VRHYRDH 463
Cdd:cd03229 1 LELKNVSKRYGQ---KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 IGVVSQEPVLF-GTTISNNIKYGrddvtdeemeraareanaydfimefpnkfntlvgekgaqMSGGQKQRIAIARALVRN 542
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 543 PKILILDEATSALDSESKSAVQAALE--KASKGRTTIVVAHRLS-TIRSADLIVTLKDG 598
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDeAARLADRVVVLRDG 177
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
109-646 |
1.33e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 154.36 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 109 YYVGIgVAALIFGYIQI----SLWIITAA-RQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDK-- 181
Cdd:PLN03232 951 FYIVV-YALLGFGQVAVtftnSFWLISSSlHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLmn 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 182 --IALLFQNMSTFSIGLAVGLVKGWKLTlvtlstsPLIMASAAA------CSRMVISLTSKELSA-YSKAGAvAEEVLSS 252
Cdd:PLN03232 1030 mfMNQLWQLLSTFALIGTVSTISLWAIM-------PLLILFYAAylyyqsTSREVRRLDSVTRSPiYAQFGE-ALNGLSS 1101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 253 IRTVIAFRAQEKELQRYTQNlkdakdfGIKRTIASK----------VSLGAVYFFMNGTYGLaFWYGTSlilNGEPGY-- 320
Cdd:PLN03232 1102 IRAYKAYDRMAKINGKSMDN-------NIRFTLANTssnrwltirlETLGGVMIWLTATFAV-LRNGNA---ENQAGFas 1170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 321 TIGTVLAVFFSV--IHSSYCIGAAVPHFETFAIARGAAFhiFQVIDKKPSID--NFSTAGYkPESieGTVEFKNVSFNYp 396
Cdd:PLN03232 1171 TMGLLLSYTLNIttLLSGVLRQASKAENSLNSVERVGNY--IDLPSEATAIIenNRPVSGW-PSR--GSIKFEDVHLRY- 1244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 397 sRPSIK-ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFG 475
Cdd:PLN03232 1245 -RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFS 1323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 476 TTISNNIKYGRDDvTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSAL 555
Cdd:PLN03232 1324 GTVRFNIDPFSEH-NDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 556 DSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSLvMSQDIKKADEQ-MES 634
Cdd:PLN03232 1403 DVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFR-MVHSTGPANAQyLSN 1481
|
570
....*....|..
gi 255708477 635 MTYstERKTNSL 646
Cdd:PLN03232 1482 LVF--ERRENGM 1491
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
387-613 |
1.41e-37 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 141.55 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPSrpSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAL---NVRHYRDH 463
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 IGVVSQEPVLFG-TTISNNIKYGRDD-----------VTDEEMERAAREANAYDfIMEFPNKfntlvgeKGAQMSGGQKQ 531
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRLGrrstwrslfglFPKEEKQRALAALERVG-LLDKAYQ-------RADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 532 RIAIARALVRNPKILILDEATSALDSESKSAVQAALEKA--SKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAE 608
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAE 231
|
....*
gi 255708477 609 LMAKR 613
Cdd:cd03256 232 LTDEV 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
386-611 |
3.29e-37 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 147.74 E-value: 3.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPD---DGFIMVDENDIRALNVRHYRD 462
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEP--VLFGTTISNNIKYG--RDDVTDEEMERAAREANAYDFIMEFPNKFNtlvgekgAQMSGGQKQRIAIARA 538
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYP-------HQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 539 LVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKGAHAELMA 611
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
386-611 |
4.94e-37 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 140.13 E-value: 4.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIG 465
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLF-GTTISNNI-------KYGRddvtdEEMERAAREANAydfIMEFPNKfnTLVGEKGAQMSGGQKQRIAIAR 537
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIalvpkllKWPK-----EKIRERADELLA---LVGLDPA--EFADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 538 ALVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRL-STIRSADLIVTLKDGMLAEKGAHAELMA 611
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
374-1253 |
5.07e-37 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 152.63 E-value: 5.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 374 TAGYKPESIEGTVEFKNVSFnYPSRPSiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENdir 453
Cdd:PTZ00243 648 EATPTSERSAKTPKMKTDDF-FELEPK-VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS--- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 454 alnvrhyrdhIGVVSQEPVLFGTTISNNIKYgrddvTDEEmeRAAREANAYDF------IMEFPNKFNTLVGEKGAQMSG 527
Cdd:PTZ00243 723 ----------IAYVPQQAWIMNATVRGNILF-----FDEE--DAARLADAVRVsqleadLAQLGGGLETEIGEKGVNLSG 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 528 GQKQRIAIARALVRNPKILILDEATSALDSE-SKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAH 606
Cdd:PTZ00243 786 GQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSS 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 607 AELMAK---RGLYYSLVMSQDIKKADEQMESMTYSTErktNSLPLHSVKSIKsdfidKAEESTQSKEISLPEVSLLKILK 683
Cdd:PTZ00243 866 ADFMRTslyATLAAELKENKDSKEGDADAEVAEVDAA---PGGAVDHEPPVA-----KQEGNAEGGDGAALDAAAGRLMT 937
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 684 LNKPEWPFVVLGTLASVLN--GTVHPVFSIIFAKIITMF---GNN------DKTTLKHDAEIYSMIF---VILGVI---- 745
Cdd:PTZ00243 938 REEKASGSVPWSTYVAYLRfcGGLHAAGFVLATFAVTELvtvSSGvwlsmwSTRSFKLSAATYLYVYlgiVLLGTFsvpl 1017
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 746 -CFVSYFMQglfygRAGeilTMRLRHLAFKAMLYQDIAWFDekenstgglTTILAidiaQIQGATGSRIGVLtQNATNMG 824
Cdd:PTZ00243 1018 rFFLSYEAM-----RRG---SRNMHRDLLRSVSRGTMSFFD---------TTPLG----RILNRFSRDIDIL-DNTLPMS 1075
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 825 LSVIISFIYGWEMTFLILSIAPVLAVTGMIETA----AMTGFANKDKQELKHAGKIA--------TEALENIRTIVSLTR 892
Cdd:PTZ00243 1076 YLYLLQCLFSICSSILVTSASQPFVLVALVPCGylyyRLMQFYNSANREIRRIKSVAkspvftllEEALQGSATITAYGK 1155
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 893 EKAFEQMYEEMLQTQH-----RNTSKK-------------------AQIIGSCYAFSH---AFIYFAYAAGFRFGAYL-- 943
Cdd:PTZ00243 1156 AHLVMQEALRRLDVVYscsylENVANRwlgvrveflsnivvtvialIGVIGTMLRATSqeiGLVSLSLTMAMQTTATLnw 1235
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 944 -------IQAGRMTPEGMFIVFTAIAYGAMAIGETLVLApeySKAKSGAAhlfALLEKKPNIDSRSQEGKKPDTCE-GNL 1015
Cdd:PTZ00243 1236 lvrqvatVEADMNSVERLLYYTDEVPHEDMPELDEEVDA---LERRTGMA---ADVTGTVVIEPASPTSAAPHPVQaGSL 1309
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1016 EFREVSFFYpcRPDV-FILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:PTZ00243 1310 VFEGVQMRY--REGLpLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFS 1387
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLFNCSIAENiaygdnsrVVPLDEikeaANAANIHSFIE--GLPEKY-------NTQVGLKGAQLSGGQKQRLA 1165
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQN--------VDPFLE----ASSAEVWAALElvGLRERVasesegiDSRVLEGGSNYSVGQRQLMC 1455
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1166 IARALLQK-PKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNR 1244
Cdd:PTZ00243 1456 MARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
970
....*....|
gi 255708477 1245 D-IYFKLVNA 1253
Cdd:PTZ00243 1536 QsIFHSMVEA 1545
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1016-1235 |
5.14e-37 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 137.57 E-value: 5.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1016 EFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAI 1095
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1096 VPQepvlfncsiaeniaygdnsrvvpldeikeAANAANIHSFIEglpEKYNTqvglkgaqLSGGQKQRLAIARALLQKPK 1175
Cdd:cd03214 78 VPQ-----------------------------ALELLGLAHLAD---RPFNE--------LSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1176 ILLLDEATSALDndsekvVQHALD--------KARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQG 1235
Cdd:cd03214 118 ILLLDEPTSHLD------IAHQIEllellrrlARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1032-1231 |
5.61e-37 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 138.82 E-value: 5.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDG--VDAKELNVQWLRSQIAIVPQEPVLF-NCSIA 1108
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQKVGMVFQQFNLFpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1109 ENIAYGD-NSRVVPLDEIKEAAnaanihsfieglpEKYNTQVGLKG------AQLSGGQKQRLAIARALLQKPKILLLDE 1181
Cdd:cd03262 95 ENITLAPiKVKGMSKAEAEERA-------------LELLEKVGLADkadaypAQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1182 ATSALD----NDSEKVVQhalDKARTGRTCLVVTHRLS-AIQNADLIVVLHNGKI 1231
Cdd:cd03262 162 PTSALDpelvGEVLDVMK---DLAEEGMTMVVVTHEMGfAREVADRVIFMDDGRI 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1015-1243 |
5.88e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 142.91 E-value: 5.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRP-DVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVD-----AKELNVqw 1088
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltalsERELRA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1089 LRSQIAIVPQEPVLFN-CSIAENIAYgdnsrvvPLDeikeaanaanihsfIEGLPEKYNTQ--------VGLKG------ 1153
Cdd:COG1135 80 ARRKIGMIFQHFNLLSsRTVAENVAL-------PLE--------------IAGVPKAEIRKrvaellelVGLSDkadayp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1154 AQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGK 1230
Cdd:COG1135 139 SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDinRELGLTIVLITHEMDVVRRiCDRVAVLENGR 218
|
250
....*....|...
gi 255708477 1231 IKEQGTHQELLRN 1243
Cdd:COG1135 219 IVEQGPVLDVFAN 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1033-1243 |
6.50e-37 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 139.40 E-value: 6.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwlRSQIAIVPQEPVLF-NCSIAENI 1111
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1112 AYG----DNSRVVPLDEIKEAANAANIHSFIEGLPEKYNtqvglkgAQLSGGQKQRLAIARALLQKPKILLLDEATSALD 1187
Cdd:cd03296 96 AFGlrvkPRSERPPEAEIRAKVHELLKLVQLDWLADRYP-------AQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1188 NDSEKVVQHALDKA--RTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:cd03296 169 AKVRKELRRWLRRLhdELHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
386-609 |
8.88e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 138.97 E-value: 8.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNV--SFNypsrpSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDI--RALNVRHYR 461
Cdd:COG1126 2 IEIENLhkSFG-----DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 462 DHIGVVSQEPVLFG-TTISNNI--------KYGRDDVTDEEMERAAR-----EANAYdfimefPnkfntlvgekgAQMSG 527
Cdd:COG1126 77 RKVGMVFQQFNLFPhLTVLENVtlapikvkKMSKAEAEERAMELLERvgladKADAY------P-----------AQLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 528 GQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGA 605
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
....
gi 255708477 606 HAEL 609
Cdd:COG1126 220 PEEF 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
386-611 |
1.20e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 139.17 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRP-SIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHI 464
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQEP---------VlfGTTISNNIK-YGRDDVtDEEMERAAREAN-AYDFIMEFPnkfntlvgekgAQMSGGQKQRI 533
Cdd:COG1124 82 QMVFQDPyaslhprhtV--DRILAEPLRiHGLPDR-EERIAELLEQVGlPPSFLDRYP-----------HQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 534 AIARALVRNPKILILDEATSALDseskSAVQAAL------EKASKGRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKGAH 606
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALD----VSVQAEIlnllkdLREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTV 223
|
....*
gi 255708477 607 AELMA 611
Cdd:COG1124 224 ADLLA 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
386-598 |
2.66e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 138.27 E-value: 2.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN---VRHYRD 462
Cdd:COG3638 3 LELRNLSKRYPGGT--PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEPVLFG--TTISN----------NIKYGRDDVTDEEMERAaREAnaydfimefpnkfntL--VG------EKG 522
Cdd:COG3638 81 RIGMIFQQFNLVPrlSVLTNvlagrlgrtsTWRSLLGLFPPEDRERA-LEA---------------LerVGladkayQRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 523 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTIRS-ADLIVTLKDG 598
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDG 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
386-652 |
2.86e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 138.99 E-value: 2.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYP--SRPSikiLKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDH 463
Cdd:PRK13635 6 IRVEHISFRYPdaATYA---LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 IGVVSQEP--VLFGTTISNNIKYGRDD--VTDEEM-ER---AAREANAYDFIMEFPnkfntlvgekgAQMSGGQKQRIAI 535
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGLENigVPREEMvERvdqALRQVGMEDFLNREP-----------HRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 536 ARALVRNPKILILDEATSALDSESKSAVQAALE--KASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKG------AHA 607
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGtpeeifKSG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 255708477 608 ELMAKRGL--YYSLVMSQDIKKADEQMESMTYSTERKTNSL-PLHSVK 652
Cdd:PRK13635 232 HMLQEIGLdvPFSVKLKELLKRNGILLPNTYLTMESLVDELwTLHSKK 279
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
386-598 |
3.11e-36 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 136.50 E-value: 3.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRhyRDHIG 465
Cdd:cd03259 1 LELKGLSKTYGSVR---ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLFGT-TISNNIKYG--RDDVTDEEMERAAREANAydfIMEFPNkfntLVGEKGAQMSGGQKQRIAIARALVRN 542
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlkLRGVPKAEIRARVRELLE---LVGLEG----LLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 543 PKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLS-TIRSADLIVTLKDG 598
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEG 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
386-600 |
3.16e-36 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 135.22 E-value: 3.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAlNVRHYRDHIG 465
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLFGT-TISNNIKYgrddvtdeemeraareanaydfimefpnkfntlvgekgaqmSGGQKQRIAIARALVRNPK 544
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 545 ILILDEATSALDSESKSAVQAALEKASKGRTTIVVA-HRLSTIRS-ADLIVTLKDGML 600
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1015-1231 |
4.61e-36 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 134.83 E-value: 4.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwLRSQIA 1094
Cdd:cd03230 1 IEVRNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLF-NCSIAENIaygdnsrvvpldeikeaanaanihsfieglpekyntqvglkgaQLSGGQKQRLAIARALLQK 1173
Cdd:cd03230 77 YLPEEPSLYeNLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1174 PKILLLDEATSALDNDSEKVVQHALDK-ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKI 1231
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1031-1243 |
5.13e-36 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 136.70 E-value: 5.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1031 FILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwlRSQIAIVPQEPVLF-NCSIAE 1109
Cdd:cd03299 13 FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1110 NIAYGDNSRVVPLDEIK----EAANAANIHSFIEGLPEKyntqvglkgaqLSGGQKQRLAIARALLQKPKILLLDEATSA 1185
Cdd:cd03299 91 NIAYGLKKRKVDKKEIErkvlEIAEMLGIDHLLNRKPET-----------LSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 1186 LDNDSEKVVQHALDKAR--TGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:cd03299 160 LDVRTKEKLREELKKIRkeFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1015-1246 |
6.90e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 136.76 E-value: 6.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELnvqwlRSQIA 1094
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVL---FNCSIAENIAYGDNSRVVPL----DEIKEAANAAnihsfIE--GLPEKYNTQVGlkgaQLSGGQKQRLA 1165
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVLMGRYGRRGLFrrpsRADREAVDEA-----LErvGLEDLADRPIG----ELSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1166 IARALLQKPKILLLDEATSALDNDSEKVVQHALDK-ARTGRTCLVVTHRLSAI-QNADLIVVLhNGKIKEQGTHQELLRN 1243
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPPEEVLTP 228
|
...
gi 255708477 1244 RDI 1246
Cdd:COG1121 229 ENL 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1016-1246 |
7.19e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 137.43 E-value: 7.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1016 EFREVSFFYPcRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAI 1095
Cdd:PRK13632 9 KVENVSFSYP-NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1096 VPQEP--VLFNCSIAENIAYGDNSRVVPLDEIK----EAANAANIHSFIEGLPEKyntqvglkgaqLSGGQKQRLAIARA 1169
Cdd:PRK13632 88 IFQNPdnQFIGATVEDDIAFGLENKKVPPKKMKdiidDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1170 LLQKPKILLLDEATSALD-NDSEKVVQHALDKARTGRTCLV-VTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDI 1246
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDpKGKREIKKIMVDLRKTRKKTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
386-610 |
1.28e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.99 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFImvdenDIRALNVRHYRDHIG 465
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTV-----RLFGKPPRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQ-------------EPVLFGTTISNNI--KYGRDDvtdeemERAAREA----NAYDFImefpnkfNTLVGEkgaqMS 526
Cdd:COG1121 79 YVPQraevdwdfpitvrDVVLMGRYGRRGLfrRPSRAD------REAVDEAlervGLEDLA-------DRPIGE----LS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 527 GGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEkG 604
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-G 220
|
....*.
gi 255708477 605 AHAELM 610
Cdd:COG1121 221 PPEEVL 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
386-581 |
2.33e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 135.60 E-value: 2.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRP-SIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALnvrhyRDHI 464
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-----GPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQEPVLFG-TTISNNIKYGRDDVTdeeMERAAREANAYDFImefpnkfnTLVGEKGA------QMSGGQKQRIAIAR 537
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRG---VPKAERRERARELL--------ELVGLAGFedayphQLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 255708477 538 ALVRNPKILILDEATSALDSESKSAVQAALEK--ASKGRTTIVVAH 581
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH 197
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
386-581 |
2.47e-35 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 134.14 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSR-PSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNvrhyrDHI 464
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQEPVLFG-TTISNNIKYGRDDVtdeEMERAAREANAYDFImefpnkfnTLVGEKGA------QMSGGQKQRIAIAR 537
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQ---GVPKAEARERAEELL--------ELVGLSGFenayphQLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 255708477 538 ALVRNPKILILDEATSALDSESKSAVQAALEK--ASKGRTTIVVAH 581
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
384-622 |
3.08e-35 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 135.42 E-value: 3.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 384 GTVEFKNVSFNYPSrpSIK-ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRD 462
Cdd:cd03288 18 GEIKIHDLCVRYEN--NLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEPVLFGTTISNNIKYGRDdVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRN 542
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 543 PKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKR-GLYYSLVM 621
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLVR 254
|
.
gi 255708477 622 S 622
Cdd:cd03288 255 T 255
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
386-598 |
7.74e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 137.15 E-value: 7.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVrhYRDHIG 465
Cdd:COG3842 6 LELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP--EKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLFG-TTISNNIKYG--RDDVTDEEMERAAREAnaydfiMEfpnkfntLVGEKG------AQMSGGQKQRIAIA 536
Cdd:COG3842 81 MVFQDYALFPhLTVAENVAFGlrMRGVPKAEIRARVAEL------LE-------LVGLEGladrypHQLSGGQQQRVALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 537 RALVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLS---TIrsADLIVTLKDG 598
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDG 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1036-1242 |
1.01e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 136.77 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1036 LSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwlRSQIAIVPQEPVLF-NCSIAENIAYG 1114
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGENVGYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1115 DNSRVVPLDEIKEAANAANIHSFIEGLPEKYNTQVglkgaqlSGGQKQRLAIARALLQKPKILLLDEATSALDND----- 1189
Cdd:PRK11432 103 LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFDEPLSNLDANlrrsm 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255708477 1190 SEKVVQhaLDKaRTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELLR 1242
Cdd:PRK11432 176 REKIRE--LQQ-QFNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
386-604 |
1.27e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 135.98 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRP-SIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN---VRHYR 461
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSereLRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 462 DHIGVVSQEPVLFGT-TISNNIKY-----GrddvtdeeMERAAREANAYDFImefpnkfnTLVG--EKG----AQMSGGQ 529
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENVALpleiaG--------VPKAEIRKRVAELL--------ELVGlsDKAdaypSQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 530 KQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKG 604
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQG 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
387-604 |
1.28e-34 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 130.63 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGV 466
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 467 VSQepvlfgttisnnikygrddvtdeemerAAREANAYDFIMEFpnkFNTLvgekgaqmSGGQKQRIAIARALVRNPKIL 546
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADRP---FNEL--------SGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 547 ILDEATSALDSESKSAVQAAL--EKASKGRTTIVVAHRLS-TIRSADLIVTLKDGMLAEKG 604
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLrrLARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
386-611 |
3.16e-34 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 131.47 E-value: 3.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNV---RHYRD 462
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEPVLFGT-TISNNIKYG---RDDVTDEEMERAAREanaydfIMEFpnkfntlVGEKG------AQMSGGQKQR 532
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIVLE------KLEA-------VGLRGaedlypAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 533 IAIARALVRNPKILILDEATSALDSESKSAVQAALE--KASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAEL 609
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRslKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
..
gi 255708477 610 MA 611
Cdd:cd03261 225 RA 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1015-1242 |
3.36e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.22 E-value: 3.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:PRK13635 6 IRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEP--VLFNCSIAENIAYGDNSRVVPLDE----IKEAANAANIHSFIEGLPekyntqvglkgAQLSGGQKQRLAIAR 1168
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLENIGVPREEmverVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 1169 ALLQKPKILLLDEATSALD-NDSEKVVQHALD-KARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLR 1242
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDpRGRREVLETVRQlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
386-604 |
3.48e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.81 E-value: 3.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRpSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIG 465
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEP--VLFGTTISNNIKYGRDD--VTDEEM----ERAAREANAYDFIMEFPNKfntlvgekgaqMSGGQKQRIAIAR 537
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENkkVPPKKMkdiiDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIAS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 538 ALVRNPKILILDEATSALDSESKSAVQAALE--KASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKG 604
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQG 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1015-1240 |
5.43e-34 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 131.15 E-value: 5.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVD---AKELNVQWLRS 1091
Cdd:cd03256 1 IEVENLSKTYP--NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1092 QIAIVPQEPVLFN-CSIAENIAYGDNSRV---------VPLDEIKEAANAanihsfIE--GLPEKYNTQVGlkgaQLSGG 1159
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGRRstwrslfglFPKEEKQRALAA------LErvGLLDKAYQRAD----QLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1160 QKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKART--GRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGT 1236
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDlAREYADRIVGLKDGRIVFDGP 228
|
....
gi 255708477 1237 HQEL 1240
Cdd:cd03256 229 PAEL 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1028-1235 |
8.67e-34 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 129.68 E-value: 8.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1028 PDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVD-----AKELNvqwlrsqIAIVPQEPVL 1102
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtdlpPKDRD-------IAMVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1103 F-NCSIAENIAYGDNSRVVPLDEIKEAAN-AANIHSfIEGLPEKyntqvglKGAQLSGGQKQRLAIARALLQKPKILLLD 1180
Cdd:cd03301 84 YpHMTVYDNIAFGLKLRKVPKDEIDERVReVAELLQ-IEHLLDR-------KPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1181 EATSALDNDSEKVVQHALDK--ARTGRTCLVVTH-RLSAIQNADLIVVLHNGKIKEQG 1235
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
386-612 |
1.00e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 131.85 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPSiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDD---GFIMVDENDIRALNVRHYRD 462
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEP--VLFGTTISNNIKYGRDD--VTDEEMERAAREANAYDFIMEFPNKfntlvgeKGAQMSGGQKQRIAIARA 538
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLADVGMLDYIDS-------EPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 539 LVRNPKILILDEATSALDSESKSAVQAALEK--ASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAK 612
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1032-1239 |
1.19e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 134.30 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwlRSQIAIVPQEPVLF-NCSIAEN 1110
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1111 IAYGDNSRVVPLDEIKEAANAANIHSFIEGLPEKyntqvglKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDS 1190
Cdd:PRK09452 107 VAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQR-------KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255708477 1191 EKVVQHALdKA---RTGRTCLVVTH-RLSAIQNADLIVVLHNGKIKEQGTHQE 1239
Cdd:PRK09452 180 RKQMQNEL-KAlqrKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
384-618 |
1.32e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 141.41 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 384 GTVEFKNVSFNYpsRPSIK-ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRD 462
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEPVLFGTTISNNIK-YGRDDVTD--EEMERAareaNAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARAL 539
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLDpFNEHNDADlwESLERA----HLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 540 VRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYS 618
Cdd:PLN03130 1390 LRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1033-1243 |
1.43e-33 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 130.84 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRS----QIAIVPQEPVLF-NCSI 1107
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1108 AENIAYGDNSRVVPLDEIKEAAnaanihsfIEGLpekynTQVGLKG------AQLSGGQKQRLAIARALLQKPKILLLDE 1181
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERA--------AEAL-----ELVGLEGwehkypDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1182 ATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:cd03294 187 AFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
386-612 |
2.77e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 130.24 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIG 465
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEP--VLFGTTISNNIKYGRDD--VTDEEMERAAREANAYDFIMEFPNKfntlvgeKGAQMSGGQKQRIAIARALVR 541
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEALELVGMQDFKER-------EPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 542 NPKILILDEATSALDSESKSAVQAALE--KASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAK 612
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKgiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
386-610 |
2.96e-33 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 129.43 E-value: 2.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGfimvdeNDIRAL-------NVR 458
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG------NDVRLFgerrggeDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 459 HYRDHIGVVS---------QEPVL-------FGTTisnnikyGRDDVTDEEMERAAREanaydfIMEFpnkFN--TLVGE 520
Cdd:COG1119 75 ELRKRIGLVSpalqlrfprDETVLdvvlsgfFDSI-------GLYREPTDEQRERARE------LLEL---LGlaHLADR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 521 KGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIV-VAHRLSTIRSA-DLIVTLKD 597
Cdd:COG1119 139 PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIPPGiTHVLLLKD 218
|
250
....*....|...
gi 255708477 598 GMLAEKGAHAELM 610
Cdd:COG1119 219 GRVVAAGPKEEVL 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
386-611 |
3.04e-33 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 128.94 E-value: 3.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHY---RD 462
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEPVLFGT-TISNNIKYG---RDDVTDEEMERAARE-------ANAYDFimeFPnkfntlvgekgAQMSGGQKQ 531
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVLEklelvglPGAADK---MP-----------SELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 532 RIAIARALVRNPKILILDEATSALDSESKSAV-------QAALekaskGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEK 603
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIdelirelRDEL-----GLTSVVVTHDLDSAFAiADRVAVLADGKIIAE 223
|
....*...
gi 255708477 604 GAHAELMA 611
Cdd:COG1127 224 GTPEELLA 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1016-1235 |
3.30e-33 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 128.03 E-value: 3.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1016 EFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELnvqwlRSQIAI 1095
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1096 VPQEPVL---FNCSIAENIAYGDNSRVVPLDEI----KEAANAAnihsfIE--GLPEKYNTQVGlkgaQLSGGQKQRLAI 1166
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLskadKAKVDEA-----LErvGLSELADRQIG----ELSGGQQQRVLL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1167 ARALLQKPKILLLDEATSALDNDSEKVVQHALDK-ARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQG 1235
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
386-598 |
8.26e-33 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 126.88 E-value: 8.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDI--RALNVRHYRDH 463
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 IGVVSQEPVLFG-TTISNNIKYGRddVTDEEMERAAREANAYDF-----IMEFPNKFNtlvgekgAQMSGGQKQRIAIAR 537
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAP--IKVKGMSKAEAEERALELlekvgLADKADAYP-------AQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 538 ALVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDG 598
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREvADRVIFMDDG 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
386-600 |
1.40e-32 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 126.37 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPsrPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVR---HYRD 462
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEPVLFGT-TISNNIKYGRDdVTDEEMERAAREANAYDFIMEFPNKFNTLvgekGAQMSGGQKQRIAIARALVR 541
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALE-VTGVPPREIRKRVPAALELVGLSHKHRAL----PAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 542 NPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTI--RSADLIVTLKDGML 600
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELvdTTRHRVIALERGKL 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1020-1232 |
2.40e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 125.06 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1020 VSFFYpcRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKElnvQWLRSQIAIVPQE 1099
Cdd:cd03226 5 ISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1100 P--VLFNCSIAENIAYGDNsrvvPLDEIKEAANAA----NIHSFIEGLPekyntqvglkgAQLSGGQKQRLAIARALLQK 1173
Cdd:cd03226 80 VdyQLFTDSVREELLLGLK----ELDAGNEQAETVlkdlDLYALKERHP-----------LSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 1174 PKILLLDEATSALDNDSEKVVQHALDK-ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIK 1232
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1014-1245 |
2.59e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.02 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1014 NLEFREVSFFYPcrpdVFILRgLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVqwlrSQ- 1092
Cdd:COG3840 1 MLRLDDLTYRYG----DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AEr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1093 -IAIVPQEPVLFN-CSIAENIAYG--DNSRVVPLD--EIKEAANAANIHSFIEGLPekyntqvglkgAQLSGGQKQRLAI 1166
Cdd:COG3840 72 pVSMLFQENNLFPhLTVAQNIGLGlrPGLKLTAEQraQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1167 ARALLQKPKILLLDEATSALD----NDSEKVVQHALDkaRTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELL 1241
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCR--ERGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALL 218
|
....
gi 255708477 1242 RNRD 1245
Cdd:COG3840 219 DGEP 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
387-601 |
5.18e-32 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 124.57 E-value: 5.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDendirALNVRHYRDHIGV 466
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF-----GKPLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 467 VSQ-------------EPVLFGTTISNNI--KYGRDDvtdeemERAAREA----NAYDFImefpnkfNTLVGEkgaqMSG 527
Cdd:cd03235 73 VPQrrsidrdfpisvrDVVLMGLYGHKGLfrRLSKAD------KAKVDEAlervGLSELA-------DRQIGE----LSG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 528 GQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTI-RSADLIVTLKDGMLA 601
Cdd:cd03235 136 GQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVlEYFDRVLLLNRTVVA 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
386-601 |
5.21e-32 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 122.54 E-value: 5.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSrpsIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDH-I 464
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQepvlfgttisnnikygrddvtdeemeraareanaydfimefpnkfntlvgekgaqMSGGQKQRIAIARALVRNPK 544
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 545 ILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLA 601
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRlRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1016-1236 |
5.54e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 128.38 E-value: 5.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1016 EFREVSFFYPC-RPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRS--- 1091
Cdd:PRK11153 3 ELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1092 QIAIVPQEpvlFNC----SIAENIAYgdnsrvvPLdeikEAAN--AANIHSFIEGLPEKyntqVGLKG------AQLSGG 1159
Cdd:PRK11153 83 QIGMIFQH---FNLlssrTVFDNVAL-------PL----ELAGtpKAEIKARVTELLEL----VGLSDkadrypAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1160 QKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAI-QNADLIVVLHNGKIKEQGT 1236
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDinRELGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1032-1241 |
5.68e-32 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 126.07 E-value: 5.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELN---VQWLRSQIAIVPQE-PVLFNC-- 1105
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDsPSAVNPrm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1106 ----SIAENIAYgdnsrvvpLDEIKEAANAANIHSFIE--GLPEKYNTQVglkGAQLSGGQKQRLAIARALLQKPKILLL 1179
Cdd:TIGR02769 106 tvrqIIGEPLRH--------LTSLDESEQKARIAELLDmvGLRSEDADKL---PRQLSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1180 DEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELL 1241
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLL 239
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
386-610 |
5.97e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 125.21 E-value: 5.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSrpsIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIR--ALNVRHYRDH 463
Cdd:PRK09493 2 IEFKNVSKHFGP---TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 IGVVSQEPVLF-GTTISNNIKYGRDDVtdeemeRAAREANAYDFIMEFPNKfntlVG--EKG----AQMSGGQKQRIAIA 536
Cdd:PRK09493 79 AGMVFQQFYLFpHLTALENVMFGPLRV------RGASKEEAEKQARELLAK----VGlaERAhhypSELSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 537 RALVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAELM 610
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1032-1248 |
7.25e-32 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 125.79 E-value: 7.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENI 1111
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1112 aygDNSRVVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSE 1191
Cdd:cd03288 116 ---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 1192 KVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYF 1248
Cdd:cd03288 193 NILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
383-604 |
7.97e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 126.02 E-value: 7.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 383 EGTVEFKNVSFNYPSRPSIKiLKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRD 462
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEP--VLFGTTISNNIKYGRDD--VTDEEMER----AAREANAYDFIMEFPNkfntlvgekgaQMSGGQKQRIA 534
Cdd:PRK13648 84 HIGIVFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHRrvseALKQVDMLERADYEPN-----------ALSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 535 IARALVRNPKILILDEATSALDSESKSAVQAALE--KASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKG 604
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
404-604 |
1.01e-31 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 124.37 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 404 LKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRhyRDHIGVVSQEPVLF-GTTISNNI 482
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 483 KYGRDDVTDEEMERAAReanaydfIMEFPNKFNT--LVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESK 560
Cdd:cd03299 93 AYGLKKRKVDKKEIERK-------VLEIAEMLGIdhLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255708477 561 SAVQAALEKASK--GRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKG 604
Cdd:cd03299 166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVG 212
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1015-1243 |
1.08e-31 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 127.16 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPDVFI--------LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELN- 1085
Cdd:COG4608 8 LEVRDLKKHFPVRGGLFGrtvgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1086 --VQWLRSQIAIVPQEP--VLfN--CSIAENIAYG-DNSRVVPLDEIKEAANAAnihsfIEglpekyntQVGLKGA---- 1154
Cdd:COG4608 88 reLRPLRRRMQMVFQDPyaSL-NprMTVGDIIAEPlRIHGLASKAERRERVAEL-----LE--------LVGLRPEhadr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1155 ---QLSGGQKQRLAIARALLQKPKILLLDEATSALDndsekV-VQhA------LD-KARTGRTCLVVTHRLSAIQN-ADL 1222
Cdd:COG4608 154 yphEFSGGQRQRIGIARALALNPKLIVCDEPVSALD-----VsIQ-AqvlnllEDlQDELGLTYLFISHDLSVVRHiSDR 227
|
250 260
....*....|....*....|.
gi 255708477 1223 IVVLHNGKIKEQGTHQELLRN 1243
Cdd:COG4608 228 VAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1032-1243 |
1.72e-31 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 123.31 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNV-QWLRSQIAIVPQEPVLF-NCSIAE 1109
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGIGYVPEGRRIFpELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1110 NI---AYGDNSRVVP--LDEIKEAanaanihsFIEgLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQKPKILLLDEATS 1184
Cdd:cd03224 95 NLllgAYARRRAKRKarLERVYEL--------FPR-LKERRKQLAG----TLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 1185 ALdndSEKVVQH---ALDK-ARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:cd03224 162 GL---APKIVEEifeAIRElRDEGVTILLVEQNARfALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
389-600 |
2.26e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 122.37 E-value: 2.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 389 KNVSFNYpsRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAlnvRHYRDHIGVVS 468
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 469 QEP--VLFGTTISNNIKYGRDDvTDEEMERAA---REANAYDFIMEFPnkfntlvgekgAQMSGGQKQRIAIARALVRNP 543
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKE-LDAGNEQAEtvlKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 544 KILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTI-RSADLIVTLKDGML 600
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLaKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1015-1246 |
2.71e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 124.46 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYpcRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEP--VLFNCSIAENIAYGDNSRVVPLDEIKEAANAA----NIHSFIEGLPEkyntqvglkgaQLSGGQKQRLAIAR 1168
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1169 ALLQKPKILLLDEATSALDNDSEKVVQHALDK-ARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGThQELLRNRDI 1246
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLTDEDI 230
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
45-343 |
4.83e-31 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 124.13 E-value: 4.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 45 ITLMILGILASLVngaclplMPLVLGEMSDNLISGclvqtnttnyqnctqsqeKLNEDMTLLTLYYVGIGVAALIFGYIQ 124
Cdd:cd18576 2 LILLLLSSAIGLV-------FPLLAGQLIDAALGG------------------GDTASLNQIALLLLGLFLLQAVFSFFR 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 125 ISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGW 204
Cdd:cd18576 57 IYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISW 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 205 KLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRT 284
Cdd:cd18576 137 KLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRA 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 285 IASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGTVLA-VFFSVIhssycIGAAV 343
Cdd:cd18576 217 RIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGE--LTAGDLVAfLLYTLF-----IAGSI 269
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1015-1225 |
7.17e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 121.05 E-value: 7.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFypcRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWlRSQIA 1094
Cdd:COG4133 3 LEAENLSCR---RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLF-NCSIAENIA-----YGdnsRVVPLDEIKEAANAANIHSFIEglpekyntqvgLKGAQLSGGQKQRLAIAR 1168
Cdd:COG4133 79 YLGHADGLKpELTVRENLRfwaalYG---LRADREAIDEALEAVGLAGLAD-----------LPVRQLSAGQKRRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1169 ALLQKPKILLLDEATSALDNDSEKVVQHAL-DKARTGRTCLVVTHRLSAIQNADLIVV 1225
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIaAHLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
736-986 |
8.58e-31 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 123.44 E-value: 8.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 736 SMIFVILGVICFVSYFMQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQGATGSRIGV 815
Cdd:cd18557 39 ALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDK--HKTGELTSRLSSDTSVLQSAVTDNLSQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 816 LTQNATNMGLSVIISFIYGWEMTFLILSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKA 895
Cdd:cd18557 117 LLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 896 FEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRMTPEGM--FIVFTAIAygAMAIGETLV 973
Cdd:cd18557 197 EIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELtsFILYTIMV--ASSVGGLSS 274
|
250
....*....|...
gi 255708477 974 LAPEYSKAkSGAA 986
Cdd:cd18557 275 LLADIMKA-LGAS 286
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
386-609 |
9.95e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 127.83 E-value: 9.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSrpsIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDH-I 464
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQEPVLFGT-TISNNIKYGRDDVT-----DEEMERAAREANAYdfiMEFPNKFNTLVGEkgaqMSGGQKQRIAIARA 538
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGREPRRgglidWRAMRRRARELLAR---LGLDIDPDTPVGD----LSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 539 LVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAEL 609
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRlKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
155-1247 |
1.23e-30 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 131.57 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 155 FDSCDIGELNTRMTDDIDKISDGIGdkiALLFQNMSTFSIGLAVGLVkgWKLTLVTL--STSPLIMAS--AAACSRMVIS 230
Cdd:TIGR01271 173 LDKISTGQLVSLLSNNLNKFDEGLA---LAHFVWIAPLQVILLMGLI--WELLEVNGfcGLGFLILLAlfQACLGQKMMP 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 231 LTSKELSAYSKAGAVAEEVLSSIRTVIAFrAQEKELQRYTQNLKDAkDFGIKRTIASkvslgaVYFFMNGTYglaFWYGT 310
Cdd:TIGR01271 248 YRDKRAGKISERLAITSEIIENIQSVKAY-CWEEAMEKIIKNIRQD-ELKLTRKIAY------LRYFYSSAF---FFSGF 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 311 SLILNGEPGYTI--GTVLAVFFSVIhsSYCIGAAVPHFETFAIARGAAFHIFQVIDKKPSI---DNFSTAGYKPESIEgt 385
Cdd:TIGR01271 317 FVVFLSVVPYALikGIILRRIFTTI--SYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFlckEEYKTLEYNLTTTE-- 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVS-------------------------------FNYPSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLL 434
Cdd:TIGR01271 393 VEMVNVTaswdegigelfekikqnnkarkqpngddglfFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMI 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 435 QRLYDPDDGfimvdendiralNVRHyRDHIGVVSQEPVLFGTTISNNIKYGRDdvTDEEMERAAREA-NAYDFIMEFPNK 513
Cdd:TIGR01271 473 MGELEPSEG------------KIKH-SGRISFSPQTSWIMPGTIKDNIIFGLS--YDEYRYTSVIKAcQLEEDIALFPEK 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 514 FNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALD-SESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLI 592
Cdd:TIGR01271 538 DKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDvVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKI 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 593 VTLKDGMLAEKGAHAELMAKRGLYYSLVM---SQDIKKADEQMESMTYS------------------------------T 639
Cdd:TIGR01271 618 LLLHEGVCYFYGTFSELQAKRPDFSSLLLgleAFDNFSAERRNSILTETlrrvsidgdstvfsgpetikqsfkqpppefA 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 640 ERKTNSLPLHSVKSIKS-DFIDKAEESTQSKEI-----------------------SLPEVSLLK------------ILK 683
Cdd:TIGR01271 698 EKRKQSIILNPIASARKfSFVQMGPQKAQATTIedavrepserkfslvpedeqgeeSLPRGNQYHhglqhqaqrrqsVLQ 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 684 L--NKPEWPFVVLGTLASVLNGTVHPVFSI------IFAKIITMFGNND---------------------------KTTL 728
Cdd:TIGR01271 778 LmtHSNRGENRREQLQTSFRKKSSITQQNElaseldIYSRRLSKDSVYEiseeineedlkecfaderenvfetttwNTYL 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 729 KHDAEIYSMIFVIlgVICFV------------------------------------------------SYFMQGLFYGRA 760
Cdd:TIGR01271 858 RYITTNRNLVFVL--IFCLViflaevaasllglwlitdnpsapnyvdqqhanasspdvqkpviitptsAYYIFYIYVGTA 935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 761 GEILTM-----------------RLRHLAFKAMLYQDIAWFDEKEnsTGGLTTILAIDIAQIQGATGSRIGVLTQnatnm 823
Cdd:TIGR01271 936 DSVLALgffrglplvhtlltvskRLHEQMLHSVLQAPMAVLNTMK--AGRILNRFTKDMAIIDDMLPLTLFDFIQ----- 1008
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 824 gLSVIIS---FIYGWEMTFLILSIAPVLAVTGMIETAAMtgfanKDKQELKhagKIATEA-----------LENIRTIVS 889
Cdd:TIGR01271 1009 -LTLIVLgaiFVVSVLQPYIFIAAIPVAVIFIMLRAYFL-----RTSQQLK---QLESEArspifshlitsLKGLWTIRA 1079
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 890 LTREKAFEQMYEEMLQTqhrntskkaqiigscyafsHAFIYFAYAAGFRFGAYLIQagrMTPEGMFIVFTAIAYG----- 964
Cdd:TIGR01271 1080 FGRQSYFETLFHKALNL-------------------HTANWFLYLSTLRWFQMRID---IIFVFFFIAVTFIAIGtnqdg 1137
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 965 ----------AMAIGETLVLAPEYSKAKSG----AAHLFALLEKkPNIDSRSQEGKKPDTCEGNL--EFREVSFFYPCRP 1028
Cdd:TIGR01271 1138 egevgiiltlAMNILSTLQWAVNSSIDVDGlmrsVSRVFKFIDL-PQEEPRPSGGGGKYQLSTVLviENPHAQKCWPSGG 1216
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1029 DVF--------------ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDpVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:TIGR01271 1217 QMDvqgltakyteagraVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFG 1295
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLFNCSIAENI----AYGDnsrvvplDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARAL 1170
Cdd:TIGR01271 1296 VIPQKVFIFSGTFRKNLdpyeQWSD-------EEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSI 1368
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 1171 LQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIY 1247
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
408-612 |
1.37e-30 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 122.37 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 408 NLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN------VRhyRDHIGVVSQEPVLF-GTTISN 480
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelreLR--RKKISMVFQSFALLpHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 481 NIKYGRD--DVTDEEMERAAREAnaydfiMEfpnkfntLVGEKG------AQMSGGQKQRIAIARALVRNPKILILDEAT 552
Cdd:cd03294 122 NVAFGLEvqGVPRAEREERAAEA------LE-------LVGLEGwehkypDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 553 SALDSESKSAVQAALEK--ASKGRTTIVVAHRLS-TIRSADLIVTLKDGMLAEKGAHAELMAK 612
Cdd:cd03294 189 SALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1015-1243 |
1.51e-30 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 127.88 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPDVF--------ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLyDPVQGQVLFDGVD-----A 1081
Cdd:COG4172 276 LEARDLKVWFPIKRGLFrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDldglsR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1082 KELnvQWLRSQIAIVPQEPvlFNC-----SIAENIAYG------DNSRvvplDEIKEAANAAnihsfiegLpekynTQVG 1150
Cdd:COG4172 355 RAL--RPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhgpGLSA----AERRARVAEA--------L-----EEVG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1151 LKGA-------QLSGGQKQRLAIARALLQKPKILLLDEATSALDndseKVVQHA-LD-----KARTGRTCLVVTHRLSAI 1217
Cdd:COG4172 414 LDPAarhryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQiLDllrdlQREHGLAYLFISHDLAVV 489
|
250 260
....*....|....*....|....*..
gi 255708477 1218 QN-ADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:COG4172 490 RAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1002-1248 |
2.14e-30 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 130.84 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1002 SQEGKKPDTCE--------GN-LEFREVSFFYpCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQG 1072
Cdd:TIGR00957 615 SHEELEPDSIErrtikpgeGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1073 QVLFDGvdakelnvqwlrsQIAIVPQEPVLFNCSIAENIAYGDnsrvvPLDE--IKEAANAANIHSFIEGLPEKYNTQVG 1150
Cdd:TIGR00957 694 HVHMKG-------------SVAYVPQQAWIQNDSLRENILFGK-----ALNEkyYQQVLEACALLPDLEILPSGDRTEIG 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1151 LKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNdseKVVQHALDKA------RTGRTCLVVTHRLSAIQNADLIV 1224
Cdd:TIGR00957 756 EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA---HVGKHIFEHVigpegvLKNKTRILVTHGISYLPQVDVII 832
|
250 260
....*....|....*....|....
gi 255708477 1225 VLHNGKIKEQGTHQELLrNRDIYF 1248
Cdd:TIGR00957 833 VMSGGKISEMGSYQELL-QRDGAF 855
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
386-611 |
2.36e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 121.74 E-value: 2.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIG 465
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEP--VLFGTTISNNIKYGRDD--VTDEEMERAAREA----NAYDFIMEFPnkfntlvgekgAQMSGGQKQRIAIAR 537
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 538 ALVRNPKILILDEATSALDSESKSAVQAALE--KASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMA 611
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHeiKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1015-1246 |
4.69e-30 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 119.70 E-value: 4.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDakelnVQWLRSQ-- 1092
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-----ITGLPPHri 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1093 ----IAIVPQEPVLF-NCSIAENI---AYGDNSRVvpldeiKEAANAANIHSFIEGLPEKYNTqvglKGAQLSGGQKQRL 1164
Cdd:COG0410 76 arlgIGYVPEGRRIFpSLTVEENLllgAYARRDRA------EVRADLERVYELFPRLKERRRQ----RAGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1165 AIARALLQKPKILLLDEATSALdndSEKVVQ---HALDK-ARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQE 1239
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGL---APLIVEeifEIIRRlNREGVTILLVEQNARfALEIADRAYVLERGRIVLEGTAAE 222
|
....*..
gi 255708477 1240 LLRNRDI 1246
Cdd:COG0410 223 LLADPEV 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
386-604 |
7.68e-30 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 118.13 E-value: 7.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHyRDhIG 465
Cdd:cd03301 1 VELENVTKRFGNV---TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RD-IA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLF-GTTISNNIKYG------RDDVTDEEMERAAReanaydfIMefpnKFNTLVGEKGAQMSGGQKQRIAIARA 538
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGlklrkvPKDEIDERVREVAE-------LL----QIEHLLDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 539 LVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAH-RLSTIRSADLIVTLKDGMLAEKG 604
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
386-604 |
9.11e-30 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 118.06 E-value: 9.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRpsiKILKGLNLRIKSGETvALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAlNVRHYRDHIG 465
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLF-GTTISNNIKYG------RDDVTDEEMERAAREANAYDFimefpnkfntlVGEKGAQMSGGQKQRIAIARA 538
Cdd:cd03264 76 YLPQEFGVYpNFTVREFLDYIawlkgiPSKEVKARVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 539 LVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKG 604
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1015-1243 |
1.05e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 118.66 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAK--ELNVQWLRSQ 1092
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1093 IAIVPQEPVLFNCSIA-ENIAYGdnsrvvPLdEIKEAANAAnihsfIEGLPEKYNTQVGLKG------AQLSGGQKQRLA 1165
Cdd:PRK09493 79 AGMVFQQFYLFPHLTAlENVMFG------PL-RVRGASKEE-----AEKQARELLAKVGLAErahhypSELSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1166 IARALLQKPKILLLDEATSALD----NDSEKVVQhalDKARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQEL 1240
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDpelrHEVLKVMQ---DLAEEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVL 223
|
...
gi 255708477 1241 LRN 1243
Cdd:PRK09493 224 IKN 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
384-609 |
1.13e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 121.72 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 384 GTVEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHyRDh 463
Cdd:COG3839 2 ASLELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 IGVVSQEPVLFGT-TISNNIKYG--RDDVTDEEMERAAREANAydfIMEFPNkfntLVGEKGAQMSGGQKQRIAIARALV 540
Cdd:COG3839 77 IAMVFQSYALYPHmTVYENIAFPlkLRKVPKAEIDRRVREAAE---LLGLED----LLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 541 RNPKILILDEATSALDSESK-------SAVQAALekaskGRTTIVVAHRLS---TIrsADLIVTLKDGMLAEKGAHAEL 609
Cdd:COG3839 150 REPKVFLLDEPLSNLDAKLRvemraeiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGTPEEL 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1032-1242 |
1.43e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 119.41 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELN-VQW--LRSQIAIVPQEPV-LFN--- 1104
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNrAQRkaFRRDIQMVFQDSIsAVNprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1105 ---CSIAENIAYgdnsrvvpLDEIKEAANAANIHSFIE--GLPEKYNTQvglKGAQLSGGQKQRLAIARALLQKPKILLL 1179
Cdd:PRK10419 107 tvrEIIREPLRH--------LLSLDKAERLARASEMLRavDLDDSVLDK---RPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1180 DEATSALDndseKVVQ-HALD-----KARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLR 1242
Cdd:PRK10419 176 DEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1015-1243 |
2.17e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 118.60 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYD-----PVQGQVLFDG--VDAKELNVQ 1087
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNqnIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1088 WLRSQIAIVPQEPVLFNCSIAENIAYGDN----SRVVPLDEIKEAANAAnihsfiEGLPEKYNTQVGLKGAQLSGGQKQR 1163
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1164 LAIARALLQKPKILLLDEATSALDNDSEKVVQHALD--KARTGRTCLVVTHRLSAIQN-ADLIVVLHN-----GKIKEQG 1235
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFG 238
|
....*...
gi 255708477 1236 THQELLRN 1243
Cdd:PRK14258 239 LTKKIFNS 246
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1010-1229 |
2.74e-29 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 124.53 E-value: 2.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1010 TCEGNLEFREVSFFypcRPD-VFILRGLSLSIERGKTVAFVGSSGCGKSTsvqLLQ-----------RLYDPVQGQVLFd 1077
Cdd:COG4178 358 SEDGALALEDLTLR---TPDgRPLLEDLSLSLKPGERLLITGPSGSGKST---LLRaiaglwpygsgRIARPAGARVLF- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1078 gvdakelnvqwlrsqiaiVPQEPVLFNCSIAENIAYGDNSRVVPLDEIKEAANAANIHSFIEGLPEKYN-TQVglkgaqL 1156
Cdd:COG4178 431 ------------------LPQRPYLPLGTLREALLYPATAEAFSDAELREALEAVGLGHLAERLDEEADwDQV------L 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 1157 SGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNG 1229
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
401-611 |
3.15e-29 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 124.03 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 401 IKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLyDPDDGFIMVDENDIRALN---VRHYRDHIGVVSQEPvlFGT- 476
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FGSl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 477 ----TISNNIKYG----RDDVTDEEMERAAREAnaydfiME-----------FPNKFntlvgekgaqmSGGQKQRIAIAR 537
Cdd:COG4172 376 sprmTVGQIIAEGlrvhGPGLSAAERRARVAEA------LEevgldpaarhrYPHEF-----------SGGQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 538 ALVRNPKILILDEATSALDseskSAVQA---ALEK---ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAELM 610
Cdd:COG4172 439 ALILEPKLLVLDEPTSALD----VSVQAqilDLLRdlqREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVF 514
|
.
gi 255708477 611 A 611
Cdd:COG4172 515 D 515
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1033-1245 |
4.04e-29 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 116.77 E-value: 4.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwLRSQIAIVP--QEPVLF-NCSIAE 1109
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1110 NI----------AYGDNSRVVPLDEIKEAANAAnihsfIE--GLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQKPKIL 1177
Cdd:cd03219 95 NVmvaaqartgsGLLLARARREEREARERAEEL-----LErvGLADLADRPAG----ELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 1178 LLDEATSALdNDSEK--VVQHALDKARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLRNRD 1245
Cdd:cd03219 166 LLDEPAAGL-NPEETeeLAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
386-587 |
4.18e-29 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 119.39 E-value: 4.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRP-SIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDP---DDGFIMVDENDIRALN---VR 458
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekeLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 459 HYR-DHIGVVSQEP---------VlfGTTISNNIKYGRDdVTDEEMERAAREA-------NAYDFIMEFPNkfntlvgek 521
Cdd:COG0444 82 KIRgREIQMIFQDPmtslnpvmtV--GDQIAEPLRIHGG-LSKAEARERAIELlervglpDPERRLDRYPH--------- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 522 gaQMSGGQKQRIAIARALVRNPKILILDEATSALD-SesksaVQAA-LE-----KASKGRTTIVVAHRLSTIR 587
Cdd:COG0444 150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALDvT-----IQAQiLNllkdlQRELGLAILFITHDLGVVA 215
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1015-1240 |
5.59e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 117.91 E-value: 5.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEP--VLFNCSIAENIAYGDNSRVVPLDEIKEAANAA----NIHSFIEGLPekyntqvglkgAQLSGGQKQRLAIAR 1168
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 1169 ALLQKPKILLLDEATSALDNDSEKVVQHALDKART--GRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQEL 1240
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
95-317 |
6.23e-29 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 118.00 E-value: 6.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 95 SQEKLNEDMTLLTLYYVGIGVAALIFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKI 174
Cdd:cd18573 32 DIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 175 SDGIGDKIALLFQNMSTFSIGLAVGLVKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIR 254
Cdd:cd18573 112 GKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIR 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 255 TVIAFRAQEKELQRYTQNLKDAKDFGIKRTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGE 317
Cdd:cd18573 192 TVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGE 254
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
386-602 |
6.85e-29 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 115.99 E-value: 6.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRP-SIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN------VR 458
Cdd:COG4181 9 IELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedararLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 459 hyRDHIGVVSQEPVLFGT-TISNNIKY-----GRDDVtdeeMERAARE---------ANAYdfimefPnkfntlvgekgA 523
Cdd:COG4181 89 --ARHVGFVFQSFQLLPTlTALENVMLplelaGRRDA----RARARALlervglghrLDHY------P-----------A 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 524 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALE--KASKGRTTIVVAHRLSTIRSADLIVTLKDGMLA 601
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLRAGRLV 225
|
.
gi 255708477 602 E 602
Cdd:COG4181 226 E 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
386-581 |
7.30e-29 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 115.68 E-value: 7.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPSIkILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAlNVRHYRDHIG 465
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLFGT-TISNNIKY------GRDDVTDEEMERAAREANAYDFImefpnkfNTLVGekgaQMSGGQKQRIAIARA 538
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkgLPKSEIKEEVELLLRVLGLTDKA-------NKRAR----TLSGGMKRKLSLAIA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255708477 539 LVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAH 581
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1015-1228 |
8.82e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 115.27 E-value: 8.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTsvqLLQRL---YDP---VQGQVLFDGVDAKELNVQw 1088
Cdd:COG4136 2 LSLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKST---LLAAIagtLSPafsASGEVLLNGRRLTALPAE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1089 lRSQIAIVPQEPVLF-NCSIAENIAYGDNSRVvPLDEIKEAANAAnihsfiegLpekynTQVGLKG------AQLSGGQK 1161
Cdd:COG4136 75 -QRRIGILFQDDLLFpHLSVGENLAFALPPTI-GRAQRRARVEQA--------L-----EEAGLAGfadrdpATLSGGQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1162 QRLAIARALLQKPKILLLDEATSALDND-SEKVVQHALDKART-GRTCLVVTHRLSAIQNADLIVVLHN 1228
Cdd:COG4136 140 ARVALLRALLAEPRALLLDEPFSKLDAAlRAQFREFVFEQIRQrGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1032-1231 |
9.54e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 116.72 E-value: 9.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVqWLRSQ-IAIVPQEPVL---FNCSI 1107
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAKyIGRVFQDPMMgtaPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1108 AEN--IAYGDNSRVvPLdeiKEAANAANIHSFIE-------GLPEKYNTQVGLkgaqLSGGQKQRLAIARALLQKPKILL 1178
Cdd:COG1101 100 EENlaLAYRRGKRR-GL---RRGLTKKRRELFREllatlglGLENRLDTKVGL----LSGGQRQALSLLMATLTKPKLLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 1179 LDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLS-AIQNADLIVVLHNGKI 1231
Cdd:COG1101 172 LDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
692-969 |
1.08e-28 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 117.27 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 692 VVLGTLASVLNGTVHPVFSIIFAKIItmfgnnDKTTLKHDAE---IYSMIFVILGVICFVSYFMQGLFYGRAGEILTMRL 768
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLI------DDVIPAGDLSlllWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 769 RHLAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGWEMTFLILSIAPVL 848
Cdd:cd07346 75 RRDLFRHLQRLSLSFFDR--NRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 849 AVTGMIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAF 928
Cdd:cd07346 153 VLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLL 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 255708477 929 IYFAYAAGFRFGAYLIQAGRMTPeGMFIVFtaIAYGAMAIG 969
Cdd:cd07346 233 TALGTALVLLYGGYLVLQGSLTI-GELVAF--LAYLGMLFG 270
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1015-1245 |
1.28e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 117.04 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFY-PCRPdvFILRGL---SLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQV------LFDGVDAKEL 1084
Cdd:PRK13634 3 ITFQKVEHRYqYKTP--FERRALydvNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervITAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1085 NVqwLRSQIAIVPQ--EPVLFNCSIAENIAYGDNSRVVPLDEIKEAANAAnihsfIE--GLPEKYNTQVGLkgaQLSGGQ 1160
Cdd:PRK13634 81 KP--LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREM-----IElvGLPEELLARSPF---ELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1161 KQRLAIARALLQKPKILLLDEATSALDNDSEKVVQ---HALDKaRTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGT 1236
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEdAARYADQIVVMHKGTVFLQGT 229
|
....*....
gi 255708477 1237 HQELLRNRD 1245
Cdd:PRK13634 230 PREIFADPD 238
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
402-604 |
1.31e-28 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 114.70 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 402 KILKGLNLRIK---SGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDE---NDIR-ALNVRHYRDHIGVVSQEPVLF 474
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRkKINLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 475 -GTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEfpnkfntLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATS 553
Cdd:cd03297 88 pHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDH-------LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255708477 554 ALDSESKSAVQAALEKASK--GRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKG 604
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
403-611 |
1.40e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 116.00 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 403 ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDI---RALN-----VRHYRDHIGVVSQEPVLF 474
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 475 -GTTISNNIKYGRDDVTDEEMERAAREANaydfimEFPNKFNtLVGEKGA---QMSGGQKQRIAIARALVRNPKILILDE 550
Cdd:PRK11264 98 pHRTVLENIIEGPVIVKGEPKEEATARAR------ELLAKVG-LAGKETSyprRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 551 ATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAELMA 611
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
386-609 |
1.70e-28 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 115.03 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIraLNVRHYRDHIG 465
Cdd:cd03300 1 IELENVSKFYGGFV---ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLF-GTTISNNIKYGRDDVTDEEMERAAREANAYDFI--MEFPNKfntlvgeKGAQMSGGQKQRIAIARALVRN 542
Cdd:cd03300 76 TVFQNYALFpHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVqlEGYANR-------KPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 543 PKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAEL 609
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEI 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
385-608 |
2.16e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 116.30 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFNY-PSRP-SIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDI--RALNVRHY 460
Cdd:PRK13637 2 SIKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 461 RDHIGVVSQEP--VLFGTTISNNIKYG--RDDVTDEEMERAAREAnaydfiMEFPN-KFNTLVGEKGAQMSGGQKQRIAI 535
Cdd:PRK13637 82 RKKVGLVFQYPeyQLFEETIEKDIAFGpiNLGLSEEEIENRVKRA------MNIVGlDYEDYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 536 ARALVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKGAHAE 608
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1032-1242 |
2.62e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 115.25 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVL-FNCSIAEN 1110
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1111 IAYGdnsrVVPLDEIKEAANAanihsfiegLPEKYNTQVGLKG------AQLSGGQKQRLAIARALLQ------KPKILL 1178
Cdd:PRK13548 97 VAMG----RAPHGLSRAEDDA---------LVAAALAQVDLAHlagrdyPQLSGGEQQRVQLARVLAQlwepdgPPRWLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 1179 LDEATSALDndsekvVQHALDKARTGRTC--------LVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELLR 1242
Cdd:PRK13548 164 LDEPTSALD------LAHQHHVLRLARQLaherglavIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1015-1231 |
2.77e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 113.66 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELN---VQWLRS 1091
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1092 QIAIVPQE-PVLFNCSIAENIAYGDNSRVVPLDEIKEAANAAnihsfIEglpekyntQVGLKG------AQLSGGQKQRL 1164
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAA-----LE--------LVGLSHkhralpAELSGGEQQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1165 AIARALLQKPKILLLDEATSALDNDSEKVVQHALDKA-RTGRTCLVVTHRLSAIQN-ADLIVVLHNGKI 1231
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTtRHRVIALERGKL 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
386-592 |
5.77e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 112.57 E-value: 5.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAlNVRHYRDHIG 465
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLFGT-TISNNI----KYGRDDVTDEEMERAAREANAYDFImefpnkfNTLVGekgaQMSGGQKQRIAIARALV 540
Cdd:COG4133 79 YLGHADGLKPElTVRENLrfwaALYGLRADREAIDEALEAVGLAGLA-------DLPVR----QLSAGQKRRVALARLLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255708477 541 RNPKILILDEATSALDSESKSAVQAAL-EKASKGRTTIVVAHRLSTIRSADLI 592
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIaAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1015-1235 |
6.98e-28 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 112.67 E-value: 6.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYP-CRpdvfILRGLSLSIERGKTvAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKElNVQWLRSQI 1093
Cdd:cd03264 1 LQLENLTKRYGkKR----ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1094 AIVPQEPVLF-NCSIAENIAYgdnsrVVPLDEIkeaaNAANIHSFIEGLPEKyntqVGL------KGAQLSGGQKQRLAI 1166
Cdd:cd03264 75 GYLPQEFGVYpNFTVREFLDY-----IAWLKGI----PSKEVKARVDEVLEL----VNLgdrakkKIGSLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1167 ARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQG 1235
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1043-1235 |
9.04e-28 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 112.39 E-value: 9.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1043 GKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGV----DAKELNVQWLRSQIAIVPQEPVLF-NCSIAENIAYG--- 1114
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFpHLNVRENLAFGlkr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1115 --DNSRVVPLDEIKEAANaanihsfIEGLPEKYNtqvglkgAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEK 1192
Cdd:cd03297 103 krNREDRISVDELLDLLG-------LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 255708477 1193 VVQHALDK--ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQG 1235
Cdd:cd03297 169 QLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
385-612 |
9.19e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 114.49 E-value: 9.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFNY-PSRP-SIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN----VR 458
Cdd:PRK13646 2 TIRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 459 HYRDHIGVVSQ--EPVLFGTTISNNIKYGRDDVtdeEMERAAREANAYDFIMEFpnKFNTLVGEKGA-QMSGGQKQRIAI 535
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNF---KMNLDEVKNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 536 ARALVRNPKILILDEATSALDSESKSAVQAALEK--ASKGRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKGAHAELMAK 612
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1036-1240 |
1.06e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 116.47 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1036 LSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKelNVQWLRSQIAIVPQEPVLF-NCSIAENIAYG 1114
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFpHMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1115 DNSRVVPLDEIK----EAANAANIHSFIEGLPEkyntqvglkgaQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDS 1190
Cdd:PRK11607 116 LKQDKLPKAEIAsrvnEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255708477 1191 EKVVQHALDK--ARTGRTCLVVTH-RLSAIQNADLIVVLHNGKIKEQGTHQEL 1240
Cdd:PRK11607 185 RDRMQLEVVDilERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1015-1238 |
1.08e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 113.72 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYD-----PVQGQVLFDGVD--AKELNVQ 1087
Cdd:PRK14243 11 LRTENLNVYYG---SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNlyAPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1088 WLRSQIAIVPQEPVLFNCSIAENIAYGD--NSRVVPLDEIKEAA--NAAnihsfiegLPEKYNTQVGLKGAQLSGGQKQR 1163
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPKSIYDNIAYGAriNGYKGDMDELVERSlrQAA--------LWDEVKDKLKQSGLSLSGGQQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1164 LAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQ 1238
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRY 234
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1015-1240 |
1.49e-27 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 111.83 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPDVfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKElNVQWLRSQIA 1094
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLF-NCSIAENIAYgdNSRV--VPLDEIKEaanaaNIHSFIE--GLPEKYNTQVGlkgaQLSGGQKQRLAIARA 1169
Cdd:cd03263 79 YCPQFDALFdELTVREHLRF--YARLkgLPKSEIKE-----EVELLLRvlGLTDKANKRAR----TLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 1170 LLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQEL 1240
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
385-609 |
1.70e-27 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 112.43 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFNYPSRPSikiLKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRhyRDHI 464
Cdd:cd03296 2 SIEVRNVSKRFGDFVA---LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQEPVLFG-TTISNNIKYGRddvtdeEMERAAREANAyDFIMEFPNKFNTLVGEKG------AQMSGGQKQRIAIAR 537
Cdd:cd03296 77 GFVFQHYALFRhMTVFDNVAFGL------RVKPRSERPPE-AEIRAKVHELLKLVQLDWladrypAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 538 ALVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLS-TIRSADLIVTLKDGMLAEKGAHAEL 609
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1032-1233 |
1.84e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 111.73 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENI 1111
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1112 AYGDNSRVVPLDEIKEAANAANIhsfieGLPEKYNTQvglKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSE 1191
Cdd:PRK10247 102 IFPWQIRNQQPDPAIFLDDLERF-----ALPDTILTK---NIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255708477 1192 KVVQ---HALDKARtGRTCLVVTHRLSAIQNADLIVVL--HNGKIKE 1233
Cdd:PRK10247 174 HNVNeiiHRYVREQ-NIAVLWVTHDKDEINHADKVITLqpHAGEMQE 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1015-1235 |
1.98e-27 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 111.43 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPDVFILrglslSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwlRSQIA 1094
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDL-----TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLF-NCSIAENIAYGDNS--RVVPLDE--IKEAANAANIHSFIEGLPEkyntqvglkgaQLSGGQKQRLAIARA 1169
Cdd:cd03298 74 MLFQENNLFaHLTVEQNVGLGLSPglKLTAEDRqaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1170 LLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQG 1235
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1015-1231 |
2.22e-27 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 109.44 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGvdakelnvqwlrsqia 1094
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 ivpqEPVLFNCsiaeniaygdnsrvvpldeIKEAANA--ANIHsfieglpekyntqvglkgaQLSGGQKQRLAIARALLQ 1172
Cdd:cd03216 62 ----KEVSFAS-------------------PRDARRAgiAMVY-------------------QLSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 1173 KPKILLLDEATSAL-DNDSEKVVQHALDKARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKI 1231
Cdd:cd03216 100 NARLLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
386-583 |
2.24e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 112.44 E-value: 2.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGF-----IMVDENDIRA--LNVR 458
Cdd:COG1117 12 IEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIYDpdVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 459 HYRDHIGVVSQEPVLFGTTISNNIKYG--------RDDVtDEEMERAAREANAYDfimEFPNKFNtlvgEKGAQMSGGQK 530
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiksKSEL-DEIVEESLRKAALWD---EVKDRLK----KSALGLSGGQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255708477 531 QRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRL 583
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNM 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1015-1241 |
2.90e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.88 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEP--VLFNCSIAENIAYGDNSRVVPLDE----IKEAANAANIHSFIEGLPekyntqvglkgAQLSGGQKQRLAIAR 1168
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEmikrVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 1169 ALLQKPKILLLDEATSALD----NDSEKVVQHALDKARTgrTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELL 1241
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1015-1243 |
3.05e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.97 E-value: 3.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPdVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDP---VQGQVLFDGVDAKELNVQWLRS 1091
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1092 QIAIVPQEP--VLFNCSIAENIAYGDNSRVVPLDE----IKEAANAANIHSFIEGLPekyntqvglkgAQLSGGQKQRLA 1165
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEmikiVRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1166 IARALLQKPKILLLDEATSALD-NDSEKVVQHALD-KARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDpAGKEQILKLIRKlKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
385-609 |
3.10e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 114.47 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRA-LNVRHyRdH 463
Cdd:COG1118 2 SIEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRE-R-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 IGVVSQEPVLFG-TTISNNIKYG-RDDVTDEEmERAAReanaydfIMEFPNKFNtLVGEKG---AQMSGGQKQRIAIARA 538
Cdd:COG1118 77 VGFVFQHYALFPhMTVAENIAFGlRVRPPSKA-EIRAR-------VEELLELVQ-LEGLADrypSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 539 LVRNPKILILDEATSALDseskSAVQAALEK------ASKGRTTIVVAH------RLstirsADLIVTLKDGMLAEKGAH 606
Cdd:COG1118 148 LAVEPEVLLLDEPFGALD----AKVRKELRRwlrrlhDELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTP 218
|
...
gi 255708477 607 AEL 609
Cdd:COG1118 219 DEV 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
386-612 |
3.65e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 114.13 E-value: 3.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYP-SRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNV---RHYR 461
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 462 DHIGVVSQ-----------EPVLFGTTISNNIKYGRDDVTDEEMERA--AREANAYdfimefPnkfntlvgekgAQMSGG 528
Cdd:PRK11153 82 RQIGMIFQhfnllssrtvfDNVALPLELAGTPKAEIKARVTELLELVglSDKADRY------P-----------AQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 529 QKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGA 605
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
....*..
gi 255708477 606 HAELMAK 612
Cdd:PRK11153 225 VSEVFSH 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1015-1212 |
3.77e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.88 E-value: 3.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYP-CRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDakelnVQWLRSQI 1093
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-----VTGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1094 AIVPQEPVLFN-CSIAENIAYGDNSRVVPLDEIKEAAnaanihsfieglpEKYNTQVGLKGA------QLSGGQKQRLAI 1166
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARA-------------EELLALVGLADFarrriwQLSGGMRQRVGI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 255708477 1167 ARALLQKPKILLLDEATSALDN-DSEKVVQHALD-KARTGRTCLVVTH 1212
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDAlTREQMQELLLDvWQRTGKGVFLITH 193
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1029-1243 |
4.05e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 111.54 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1029 DVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYD-----PVQGQVLFDGVDAKELNVQWLRSQIAIVPQEP-VL 1102
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1103 FNCSIAENIAYG------DNSRVVPLDEIKEAANAANihsfiegLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKI 1176
Cdd:PRK14247 95 PNLSIFENVALGlklnrlVKSKKELQERVRWALEKAQ-------LWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1177 LLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTH-RLSAIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1015-1243 |
4.61e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 112.00 E-value: 4.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELN-VQWLRSQI 1093
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1094 AIVPQEP--VLFNCSIAENIAYGDNSRVVPLDEIKEAANAAnihsFIEGLPEKYNTQvglKGAQLSGGQKQRLAIARALL 1171
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 1172 QKPKILLLDEATSALDNDSEKVVQHALDKA-RTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1015-1245 |
5.12e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.77 E-value: 5.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:PRK13648 8 IVFKNVSFQYQ-SDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPV-LFNCSIAE-NIAYGDNSRVVPLDEIKEAANAA----NIHSFIEGLPEkyntqvglkgaQLSGGQKQRLAIAR 1168
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHRRVSEAlkqvDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1169 ALLQKPKILLLDEATSALDNDSEK----VVQHAldKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNR 1244
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQnlldLVRKV--KSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
.
gi 255708477 1245 D 1245
Cdd:PRK13648 234 E 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1030-1243 |
5.20e-27 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 117.09 E-value: 5.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1030 VFILRGLSLSIERGKTVAFVGSSGCGKSTS----VQLLQRLYDPVQGQVLFDGVD---AKELNVQWLR-SQIAIVPQEPV 1101
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDllgLSERELRRIRgNRIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1102 -----LFncSIAENIAygdnsrvvpldEI--------KEAANAAnihsFIEGLpekynTQVGLKGA---------QLSGG 1159
Cdd:COG4172 103 tslnpLH--TIGKQIA-----------EVlrlhrglsGAAARAR----ALELL-----ERVGIPDPerrldayphQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1160 QKQRLAIARALLQKPKILLLDEATSALDndsekV-VQHA-LD-----KARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKI 1231
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALD-----VtVQAQiLDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEI 235
|
250
....*....|..
gi 255708477 1232 KEQGTHQELLRN 1243
Cdd:COG4172 236 VEQGPTAELFAA 247
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1015-1231 |
5.35e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 109.56 E-value: 5.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRP---DVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLL--QRLYDPVQGQVLFDGVDAKElnvQWL 1089
Cdd:cd03213 4 LSFRNLTVTVKSSPsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1090 RSQIAIVPQEPVLFNC-SIAENIAYgdnsrvvpldeikeaanAANihsfieglpekyntqvgLKGaqLSGGQKQRLAIAR 1168
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLMF-----------------AAK-----------------LRG--LSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 1169 ALLQKPKILLLDEATSALDNDSEKVVQHALDK-ARTGRTCLVVTHRLSA--IQNADLIVVLHNGKI 1231
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRV 190
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
406-587 |
5.59e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 113.29 E-value: 5.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 406 GLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN---VRHYRDHIGVVSQEP---------Vl 473
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPyaslnprmtV- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 474 fGTTISNNIKYGRDdVTDEEMERAAREA------NAyDFIMEFPNKFntlvgekgaqmSGGQKQRIAIARALVRNPKILI 547
Cdd:COG4608 115 -GDIIAEPLRIHGL-ASKAERRERVAELlelvglRP-EHADRYPHEF-----------SGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 255708477 548 LDEATSALDsesKSaVQAA----LE--KASKGRTTIVVAHRLSTIR 587
Cdd:COG4608 181 CDEPVSALD---VS-IQAQvlnlLEdlQDELGLTYLFISHDLSVVR 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1037-1243 |
5.69e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 115.13 E-value: 5.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1037 SLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRS----QIAIVPQEPVLF-NCSIAENI 1111
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1112 AYGDNSRVVPLDEIKEAANAA----NIHSFIEGLPEkyntqvglkgaQLSGGQKQRLAIARALLQKPKILLLDEATSALD 1187
Cdd:PRK10070 128 AFGMELAGINAEERREKALDAlrqvGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1188 NDSEKVVQHALDK--ARTGRTCLVVTHRL-SAIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:PRK10070 197 PLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
401-611 |
6.76e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 110.22 E-value: 6.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 401 IKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVrHYRDHIGV--VSQEPVLFGT-T 477
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP-HERARAGIgyVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 478 ISNNIKYGRDDVTDEEmeRAAREANAYDFimeFPnKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALds 557
Cdd:cd03224 92 VEENLLLGAYARRRAK--RKARLERVYEL---FP-RLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL-- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 558 eSKSAVQ---AALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAELMA 611
Cdd:cd03224 164 -APKIVEeifEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
386-604 |
7.54e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 111.76 E-value: 7.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPSI--KILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAL----NVRH 459
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 460 YRDHIGVVSQ--EPVLFGTTISNNIKYGRDD--VTDEEMERAAREANAYDFIMEfpnkfnTLVGEKGAQMSGGQKQRIAI 535
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGISE------SLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 536 ARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIV-VAHRLSTIRS-ADLIVTLKDGMLAEKG 604
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
386-604 |
1.32e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 113.50 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRalNVRHYRDHIG 465
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLF-GTTISNNIKYG--RDDVTDEEMERAAREANAYDFIMEFPNKfntlvgeKGAQMSGGQKQRIAIARALVRN 542
Cdd:PRK09452 90 TVFQSYALFpHMTVFENVAFGlrMQKTPAAEITPRVMEALRMVQLEEFAQR-------KPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 543 PKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAH-RLSTIRSADLIVTLKDGMLAEKG 604
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1033-1245 |
1.95e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.52 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVD--AKELNVQWLRSQIAIVPQEP--VLFNCSIA 1108
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1109 ENIAYGDNSRVVPLDEIKEAANAAnihsfIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDn 1188
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD- 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 1189 dsEKVVQHALDKART-----GRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLRNRD 1245
Cdd:PRK13637 177 --PKGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFKEVE 237
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1032-1247 |
2.78e-26 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 109.94 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDpVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENI 1111
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1112 -AYGDNSRvvplDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDS 1190
Cdd:cd03289 98 dPYGKWSD----EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 1191 EKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIY 1247
Cdd:cd03289 174 YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1033-1235 |
3.81e-26 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 107.30 E-value: 3.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWlrSQIAIVPQEPVLF-NCSIAENI 1111
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYpNLTARENL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1112 AYGDNSRVVPLDEIKEAANaanihsfieglpekyntQVGLKGA------QLSGGQKQRLAIARALLQKPKILLLDEATSA 1185
Cdd:cd03268 94 RLLARLLGIRKKRIDEVLD-----------------VVGLKDSakkkvkGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 255708477 1186 LDNDSEKVVQHAL-DKARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQG 1235
Cdd:cd03268 157 LDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1015-1246 |
4.22e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.40 E-value: 4.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDG----VDAKEL-NVqwl 1089
Cdd:PRK13639 2 LETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikYDKKSLlEV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1090 RSQIAIVPQEP--VLFNCSIAENIAYGDNSRVVPLDEI----KEAANAANIHSFIEGLPEkyntqvglkgaQLSGGQKQR 1163
Cdd:PRK13639 77 RKTVGIVFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVekrvKEALKAVGMEGFENKPPH-----------HLSGGQKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1164 LAIARALLQKPKILLLDEATSALD-NDSEKVVQHALDKARTGRTCLVVTHRLSAIQ-NADLIVVLHNGKIKEQGTHQELL 1241
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDpMGASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVF 225
|
....*
gi 255708477 1242 RNRDI 1246
Cdd:PRK13639 226 SDIET 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
382-620 |
4.24e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.44 E-value: 4.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 382 IEGTVEFKNVSFNYPSrpSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYR 461
Cdd:PRK13647 1 MDNIIEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 462 DHIGVVSQEP--VLFGTTISNNIKYGRDD--VTDEEMERAAREA----NAYDFIMEFPNkfntlvgekgaQMSGGQKQRI 533
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFGPVNmgLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 534 AIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVA-HRLSTIRS-ADLIVTLKDG-MLAEKG----AH 606
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGrVLAEGDksllTD 227
|
250
....*....|....
gi 255708477 607 AELMAKRGLYYSLV 620
Cdd:PRK13647 228 EDIVEQAGLRLPLV 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
386-615 |
4.33e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 109.72 E-value: 4.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNY-PSRPSIKI-LKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDI----RALNVRH 459
Cdd:PRK13634 3 ITFQKVEHRYqYKTPFERRaLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 460 YRDHIGVVSQ--EPVLFGTTISNNIKYGRDD--VTDEEMERAAREANAydfimefpnkfntLVG------EKGA-QMSGG 528
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIE-------------LVGlpeellARSPfELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 529 QKQRIAIARALVRNPKILILDEATSALDSESKSAVQ---AALEKaSKGRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKG 604
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQG 228
|
250
....*....|....*..
gi 255708477 605 ------AHAELMAKRGL 615
Cdd:PRK13634 229 tpreifADPDELEAIGL 245
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1015-1246 |
4.78e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.55 E-value: 4.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDG--VDAKELNVQWLRSQ 1092
Cdd:PRK13636 6 LKVEELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1093 IAIVPQEP--VLFNCSIAENIAYGDNSRVVPLDEIKEAANAANIHSFIEGLPEKyntqvglKGAQLSGGQKQRLAIARAL 1170
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1171 LQKPKILLLDEATSALD--NDSE--KVVQHALDKarTGRTCLVVTHRLSAIQ-NADLIVVLHNGKIKEQGTHQELLRNRD 1245
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmGVSEimKLLVEMQKE--LGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKE 234
|
.
gi 255708477 1246 I 1246
Cdd:PRK13636 235 M 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
388-581 |
4.94e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.01 E-value: 4.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 388 FKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDeNDIRalnvrhyrdhIGVV 467
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 468 SQEPVLF-GTTISNNIKYGRDDV----------------TDEEMERAAR------EANAYDF------IME---FP-NKF 514
Cdd:COG0488 67 PQEPPLDdDLTVLDTVLDGDAELraleaeleeleaklaePDEDLERLAElqeefeALGGWEAearaeeILSglgFPeEDL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 515 NTLVGEkgaqMSGGQKQRIAIARALVRNPKILILDEATSALDSESKsavqAALE---KASKGrTTIVVAH 581
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESI----EWLEeflKNYPG-TVLVVSH 207
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1036-1246 |
7.62e-26 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 110.59 E-value: 7.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1036 LSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGV----DAKELNVQWLRSQIAIVPQEPVLF-NCSIAEN 1110
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdSRKGIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1111 IAYGDNSRVVPLDEIKEAANAA--NIHSFIEGLPekyntqvglkgAQLSGGQKQRLAIARALLQKPKILLLDEATSALDN 1188
Cdd:TIGR02142 96 LRYGMKRARPSERRISFERVIEllGIGHLLGRLP-----------GRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 1189 DSEKVVQHALDK--ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLRNRDI 1246
Cdd:TIGR02142 165 PRKYEILPYLERlhAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1023-1229 |
7.75e-26 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 107.03 E-value: 7.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1023 FYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQ----IAIVPQ 1098
Cdd:cd03290 7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1099 EPVLFNCSIAENIAYGDnsrvvPLDE--IKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKI 1176
Cdd:cd03290 87 KPWLLNATVEENITFGS-----PFNKqrYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 1177 LLLDEATSALD-NDSEKVVQHALDK--ARTGRTCLVVTHRLSAIQNADLIVVLHNG 1229
Cdd:cd03290 162 VFLDDPFSALDiHLSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
94-316 |
8.48e-26 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 108.94 E-value: 8.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 94 QSQEKLNEDMTLLTLYYVGIGVAALIFGyiqiSLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDK 173
Cdd:cd18784 30 KSQDKFSRAIIIMGLLAIASSVAAGIRG----GLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 174 ISDGIGDKIALLFQNMSTfSIGLAVGLVK-GWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSS 252
Cdd:cd18784 106 MSDTVSLNLNIFLRSLVK-AIGVIVFMFKlSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISS 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 253 IRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNG 316
Cdd:cd18784 185 IRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITG 248
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1033-1231 |
1.78e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.03 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDG--------VDAKELnvqwlrsQIAIVPQEPVLF- 1103
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvrfrspRDAQAA-------GIAIIHQELNLVp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1104 NCSIAENIAYGD---NSRVVPLDEIKEAANAAnIHSFieGLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQKPKILLLD 1180
Cdd:COG1129 93 NLSVAENIFLGReprRGGLIDWRAMRRRAREL-LARL--GLDIDPDTPVG----DLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 1181 EATSALDnDSEkvVQHALD-----KARtGRTCLVVTHRLSAIQN-ADLIVVLHNGKI 1231
Cdd:COG1129 166 EPTASLT-ERE--VERLFRiirrlKAQ-GVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1032-1242 |
2.48e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.02 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwlRSQIAIVPQEPVLF-NCSIAEN 1110
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1111 IAYGdnSRVVPLdeiKEAANAANIHSFI---------EGLPEKYNtqvglkgAQLSGGQKQRLAIARALLQKPKILLLDE 1181
Cdd:PRK10851 95 IAFG--LTVLPR---RERPNAAAIKAKVtqllemvqlAHLADRYP-------AQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 1182 ATSALDNDSEKVVQHALDK--ARTGRTCLVVTH-RLSAIQNADLIVVLHNGKIKEQGTHQELLR 1242
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQlhEELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1029-1241 |
2.52e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 109.93 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1029 DVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVL-FNCSI 1107
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1108 AENIAYGDN---SRVVPLDE-----IKEAANAANIHSFieglpekyntqVGLKGAQLSGGQKQRLAIARALLQKPKILLL 1179
Cdd:PRK09536 95 RQVVEMGRTphrSRFDTWTEtdraaVERAMERTGVAQF-----------ADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 1180 DEATSALD-NDSEKVVQHALDKARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELL 1241
Cdd:PRK09536 164 DEPTASLDiNHQVRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1032-1241 |
3.84e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.87 E-value: 3.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVL-FNCSIAEN 1110
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1111 IAYGdNSRVVPL-----DEIKEAANAANIHSFIEGLPEKyntqvglKGAQLSGGQKQRLAIARALLQKPKILLLDEATSA 1185
Cdd:PRK11231 97 VAYG-RSPWLSLwgrlsAEDNARVNQAMEQTRINHLADR-------RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1186 LDNDSEKVVQHALDKART-GRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELL 1241
Cdd:PRK11231 169 LDINHQVELMRLMRELNTqGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
387-595 |
4.38e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.80 E-value: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGV 466
Cdd:PRK10247 9 QLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 467 VSQEPVLFGTTISNNIKYG---RDDVTDEEMERaareanayDFIMEFPNKFNTLvgEKG-AQMSGGQKQRIAIARALVRN 542
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFPwqiRNQQPDPAIFL--------DDLERFALPDTIL--TKNiAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 543 PKILILDEATSALDSESKSAVQAALEK--ASKGRTTIVVAHRLSTIRSADLIVTL 595
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRyvREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
386-611 |
4.41e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.32 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSrpSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIR-----ALNVRHy 460
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkksLLEVRK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 461 rdHIGVVSQEP--VLFGTTISNNIKYGRDDV--TDEEMERAAREANAYDFIMEFPNKfntlvgeKGAQMSGGQKQRIAIA 536
Cdd:PRK13639 79 --TVGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEALKAVGMEGFENK-------PPHHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 537 RALVRNPKILILDEATSALDSESKSAVQAALEKASK-GRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKGAHAELMA 611
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1020-1241 |
5.54e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.51 E-value: 5.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1020 VSFFYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRL---YDP---VQGQVLFDGVDAKELNVQWLRSQI 1093
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1094 AIVPQEPVLF-NCSIAENIAYGDNSRVVplDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQ 1172
Cdd:PRK14246 93 GMVFQQPNPFpHLSIYDNIAYPLKSHGI--KEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1173 KPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHR-LSAIQNADLIVVLHNGKIKEQGTHQELL 1241
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
385-604 |
7.70e-25 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 103.40 E-value: 7.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFNYPSRPSI---KILKGLNLRIKSGETVALVGLNGSGKSTVVQLL--QRLYDPDDGFIMVDENDIRAlnvRH 459
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKsgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 460 YRDHIGVVSQEPVLFGT-TIsnnikygrddvtdeemeraaREAnaydfiMEFPNKFNTLvgekgaqmSGGQKQRIAIARA 538
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTV--------------------RET------LMFAAKLRGL--------SGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 539 LVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLST--IRSADLIVTLKDGMLAEKG 604
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
407-617 |
8.25e-25 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 107.51 E-value: 8.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 407 LNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDE---NDIRA-LNVRHYRDHIGVVSQEPVLFG-TTISNN 481
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgIFLPPEKRRIGYVFQEARLFPhLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 482 IKYGRDDVTDEEmeRAAREANAYDFIMEFPnkfntLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKS 561
Cdd:TIGR02142 96 LRYGMKRARPSE--RRISFERVIELLGIGH-----LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 562 AVQAALEK--ASKGRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKGAHAELMAKRGLYY 617
Cdd:TIGR02142 169 EILPYLERlhAEFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
395-595 |
8.88e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 103.08 E-value: 8.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 395 YPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHyrdhigvvSQEPVLF 474
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQR--------SEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 475 GTTISNNIKYGR------------DD--VTDEEMERAAREANAydfimefPNKFNTLvgekgaqmSGGQKQRIAIARALV 540
Cdd:NF040873 71 PLTVRDLVAMGRwarrglwrrltrDDraAVDDALERVGLADLA-------GRQLGEL--------SGGQRQRALLAQGLA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 541 RNPKILILDEATSALDSESKSAVQAAL-EKASKGRTTIVVAHRLSTIRSADLIVTL 595
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1032-1243 |
9.57e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 104.92 E-value: 9.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYD-----PVQGQVLFDGVD--AKELNVQWLRSQIAIVPQEPVLF- 1103
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNiySPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1104 NCSIAENIAYGD--NSRVVPLDEIKEAANAANIHSfieGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDE 1181
Cdd:PRK14267 99 HLTIYDNVAIGVklNGLVKSKKELDERVEWALKKA---ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 1182 ATSALDNDSEKVVQHALDKARTGRTCLVVTHR-LSAIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
385-607 |
1.19e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 104.32 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMV-----------DENDIR 453
Cdd:COG4161 2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaghqfdfsqkpSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 454 ALnvrhyRDHIGVVSQE----PVLfgTTISNNI-------KYGRDDVTDEEMERAAREANAyDFIMEFPNkfntlvgekg 522
Cdd:COG4161 79 LL-----RQKVGMVFQQynlwPHL--TVMENLIeapckvlGLSKEQAREKAMKLLARLRLT-DKADRFPL---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 523 aQMSGGQKQRIAIARALVRNPKILILDEATSALDSE-SKSAVQAALEKASKGRTTIVVAHRLSTIRS-ADLIVTLKDGML 600
Cdd:COG4161 141 -HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRI 219
|
....*..
gi 255708477 601 AEKGAHA 607
Cdd:COG4161 220 IEQGDAS 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1032-1233 |
1.25e-24 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 103.67 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELN----VQWLRSQIAIVPQ-EPVLFNCS 1106
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLRARHVGFVFQsFQLLPTLT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1107 IAENIAygdnsrvVPLdEIKEAANAanihsfiEGLPEKYNTQVGLKG------AQLSGGQKQRLAIARALLQKPKILLLD 1180
Cdd:COG4181 107 ALENVM-------LPL-ELAGRRDA-------RARARALLERVGLGHrldhypAQLSGGEQQRVALARAFATEPAILFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1181 EATSALDND-SEKVVQHALDKARTGRTCLV-VTHRLSAIQNADLIVVLHNGKIKE 1233
Cdd:COG4181 172 EPTGNLDAAtGEQIIDLLFELNRERGTTLVlVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
48-331 |
1.27e-24 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 105.59 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 48 MILGILASLVNGACLPLMPLVLGEMSDNLISGclvqtnttnyqnctqsqeKLNEDMTLLTLYYVGIGVAALIFGYIQISL 127
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGG------------------GLRELLWLLALLILGVALLRGVFRYLQGYL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 128 WIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGWKLT 207
Cdd:cd18542 63 AEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 208 LVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTIAS 287
Cdd:cd18542 143 LISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLL 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 255708477 288 KVSLGAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGTvLAVFFS 331
Cdd:cd18542 223 AKYWPLMDFLSGLQIVLVLWVGGYLVINGE--ITLGE-LVAFIS 263
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
387-598 |
2.19e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 109.81 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPS-RPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN----VRHYR 461
Cdd:PRK10535 6 ELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 462 DHIGVVSQE-PVLFGTTISNNIK----YGrddvtdeEMERAAREANAYDFIMEFpnKFNTLVGEKGAQMSGGQKQRIAIA 536
Cdd:PRK10535 86 EHFGFIFQRyHLLSHLTAAQNVEvpavYA-------GLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 537 RALVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRSADLIVTLKDG 598
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1029-1235 |
2.51e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 102.36 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1029 DVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNvqwlRSQIAIVPQEPVLF-NCSI 1107
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1108 AENIAYGDNSRVVPLDEIKeaanaANIHSFIE--GLPEKYNTQVglkgAQLSGGQKQRLAIARALLQKPKILLLDEATSA 1185
Cdd:cd03269 88 IDQLVYLAQLKGLKKEEAR-----RRIDEWLErlELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 255708477 1186 LDNDSEKVVQHAL-DKARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQG 1235
Cdd:cd03269 159 LDPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1015-1236 |
2.67e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 105.43 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPDVF-------ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELN-- 1085
Cdd:PRK11308 6 LQAIDLKKHYPVKRGLFkperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1086 -VQWLRSQIAIVPQEPvlfncsiaeniaYGD-NSRVV-------PLD---EIKEAANAANIHSFIEglpekyntQVGLKG 1153
Cdd:PRK11308 86 aQKLLRQKIQIVFQNP------------YGSlNPRKKvgqileePLLintSLSAAERREKALAMMA--------KVGLRP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1154 AQ-------LSGGQKQRLAIARALLQKPKILLLDEATSALD-NDSEKVVQHALD-KARTGRTCLVVTHRLSAIQN-ADLI 1223
Cdd:PRK11308 146 EHydryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDvSVQAQVLNLMMDlQQELGLSYVFISHDLSVVEHiADEV 225
|
250
....*....|...
gi 255708477 1224 VVLHNGKIKEQGT 1236
Cdd:PRK11308 226 MVMYLGRCVEKGT 238
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1032-1243 |
2.69e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 103.29 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVD---AKELNVQW-----LRSQIAIVPQEPVLF 1103
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidtARSLSQQKglirqLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1104 -NCSIAENIAYGDnsrVVPLDEIKEAANAanihsfiegLPEKYNTQVGLKGAQ------LSGGQKQRLAIARALLQKPKI 1176
Cdd:PRK11264 98 pHRTVLENIIEGP---VIVKGEPKEEATA---------RARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 1177 LLLDEATSALDndsEKVVQHALDKART----GRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:PRK11264 166 ILFDEPTSALD---PELVGEVLNTIRQlaqeKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
402-604 |
3.35e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 103.32 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 402 KILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYD--PD---DGFIMVDENDIRALNVR--HYRDHIGVVSQEPVLF 474
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDtvDLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 475 GTTISNNIKYG------RD-DVTDEEMERAAREANAYDfimEFPNKFNtlvgEKGAQMSGGQKQRIAIARALVRNPKILI 547
Cdd:PRK14239 99 PMSIYENVVYGlrlkgiKDkQVLDEAVEKSLKGASIWD---EVKDRLH----DSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 548 LDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKG 604
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYN 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1041-1245 |
4.53e-24 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 105.57 E-value: 4.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1041 ERGKTVAFvGSSGCGKSTSVQLLQRLYDPVQGQVLFDG---VDAKelNVQWL---RSQIAIVPQEPVLF-NCSIAENIAY 1113
Cdd:COG4148 24 GRGVTALF-GPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSA--RGIFLpphRRRIGYVFQEARLFpHLSVRGNLLY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1114 G-----DNSRVVPLDEIKEAANaanihsfIEGLPEKYNtqvglkgAQLSGGQKQRLAIARALLQKPKILLLDEATSALDN 1188
Cdd:COG4148 101 GrkrapRAERRISFDEVVELLG-------IGHLLDRRP-------ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1189 DS--------EKV----------VQHALDKARtgrtclvvthRLsaiqnADLIVVLHNGKIKEQGTHQELLRNRD 1245
Cdd:COG4148 167 ARkaeilpylERLrdeldipilyVSHSLDEVA----------RL-----ADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1033-1243 |
4.66e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 103.63 E-value: 4.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQW-LRSQIAIVPQEP--VLFNCSIAE 1109
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKAGMVFQNPdnQIVATIVEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1110 NIAYGDNSRVVPLDEIK----EAANAANIHSFIEGLPEkyntqvglkgaQLSGGQKQRLAIARALLQKPKILLLDEATSA 1185
Cdd:PRK13633 106 DVAFGPENLGIPPEEIRervdESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1186 LDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:PRK13633 175 LDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
401-598 |
4.86e-24 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 102.13 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 401 IKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDEN----DI-RA-----LNVRhyRDHIGVVSQ- 469
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLaQAspreiLALR--RRTIGYVSQf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 470 --------------EPVLfgttisnnikygRDDVTDEEMERAAREANAYDFIME-----FPNKFntlvgekgaqmSGGQK 530
Cdd:COG4778 102 lrviprvsaldvvaEPLL------------ERGVDREEARARARELLARLNLPErlwdlPPATF-----------SGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 531 QRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIV-VAHRLSTI-RSADLIVTLKDG 598
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVReAVADRVVDVTPF 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1033-1248 |
5.92e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 102.42 E-value: 5.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVqwlrSQIA---IVP--QEPVLF-NCS 1106
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP----HRIArlgIARtfQNPRLFpELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1107 IAENIA----------YGDNSRVVPLDEIKEAANAANIHSFIE--GLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQKP 1174
Cdd:COG0411 96 VLENVLvaaharlgrgLLAALLRLPRARREEREARERAEELLErvGLADRADEPAG----NLSYGQQRRLEIARALATEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1175 KILLLDEATSALdNDSEK--VVQHALD-KARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLRN---RDIY 1247
Cdd:COG0411 172 KLLLLDEPAAGL-NPEETeeLAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRADprvIEAY 250
|
.
gi 255708477 1248 F 1248
Cdd:COG0411 251 L 251
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
386-617 |
8.22e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 102.76 E-value: 8.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSrpSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMV---DENDIRALnvRHYRD 462
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgiDTGDFSKL--QGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEP--VLFGTTISNNIKYGRDDV------TDEEMERAAREANAYDFIMEFPNkfntlvgekgaQMSGGQKQRIA 534
Cdd:PRK13644 78 LVGIVFQNPetQFVGRTVEEDLAFGPENLclppieIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 535 IARALVRNPKILILDEATSALDSESKSAVQAALEKA-SKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKR 613
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
....
gi 255708477 614 GLYY 617
Cdd:PRK13644 227 SLQT 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
402-610 |
8.42e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.01 E-value: 8.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 402 KILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVL-FGTTISN 480
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 481 NIKYGRD-------DVTDEEMERAAREanaydfiMEfPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATS 553
Cdd:PRK11231 96 LVAYGRSpwlslwgRLSAEDNARVNQA-------ME-QTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 554 ALDSESksavQAAL-----EKASKGRTTIVVAHRLS-TIRSADLIVTLKDGMLAEKGAHAELM 610
Cdd:PRK11231 168 YLDINH----QVELmrlmrELNTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
387-613 |
9.09e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 101.37 E-value: 9.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPSRPsikilKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVrhYRDHIGV 466
Cdd:COG3840 3 RLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP--AERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 467 VSQEPVLFG-TTISNNIKYGRDD---VTDEE---MERAAREANAYDFIMEFPnkfntlvgekgAQMSGGQKQRIAIARAL 539
Cdd:COG3840 76 LFQENNLFPhLTVAQNIGLGLRPglkLTAEQraqVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 540 VRNPKILILDEATSALDsesksavqAALEK----------ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAE 608
Cdd:COG3840 145 VRKRPILLLDEPFSALD--------PALRQemldlvdelcRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAA 216
|
....*
gi 255708477 609 LMAKR 613
Cdd:COG3840 217 LLDGE 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
396-604 |
1.24e-23 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 100.52 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 396 PSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIrALNVRHYRDHIGVVSQEPVLFG 475
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 476 -TTISNNIKY-----GrddvtdeeMERAAREANAYDFIMEFpnKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILD 549
Cdd:cd03266 92 rLTARENLEYfaglyG--------LKGDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 550 EATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKG 604
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1032-1243 |
1.70e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 101.20 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDG---------------VDAKELnvQWLRSQIAIV 1096
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvADKNQL--RLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1097 PQEPVLFN-CSIAENIAYGDnSRVVPLDEiKEAANAAnihsfieglpEKYNTQVGLKGAQ-------LSGGQKQRLAIAR 1168
Cdd:PRK10619 98 FQHFNLWShMTVLENVMEAP-IQVLGLSK-QEARERA----------VKYLAKVGIDERAqgkypvhLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 1169 ALLQKPKILLLDEATSALDNDSEKVVQHALDK-ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1033-1243 |
1.86e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.01 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYD-----PVQGQVLFDGVD--AKELNVQWLRSQIAIVPQEPVLFNC 1105
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNiySPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1106 SIAENIAYG-------DNSRvvpLDEIKEAA-NAANIhsFIEGLPEKYNTQVGLkgaqlSGGQKQRLAIARALLQKPKIL 1177
Cdd:PRK14239 101 SIYENVVYGlrlkgikDKQV---LDEAVEKSlKGASI--WDEVKDRLHDSALGL-----SGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 1178 LLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRL-SAIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqQASRISDRTGFFLDGDLIEYNDTKQMFMN 237
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1033-1240 |
2.08e-23 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 99.75 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDA-KE-LNVqwlRSQIAIVPQEPVLFNCSIA-E 1109
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREpREV---RRRIGIVFQDLSVDDELTGwE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1110 NIA-----YGdnsrvVPLDEIKEaaNAANIHSFIeGLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQKPKILLLDEATS 1184
Cdd:cd03265 93 NLYiharlYG-----VPGAERRE--RIDELLDFV-GLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1185 ALDNDSEKVVQHALDK--ARTGRTCLVVTHRL-SAIQNADLIVVLHNGKIKEQGTHQEL 1240
Cdd:cd03265 161 GLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMeEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1024-1226 |
2.23e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.85 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1024 YPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGvdakelnvqwlRSQIAIVPQ---EP 1100
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1101 VLFNCSIAENIAYGDNSRVVPLDEIKEAANAANIHSFieglpekynTQVGLKG------AQLSGGQKQRLAIARALLQKP 1174
Cdd:NF040873 68 DSLPLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDAL---------ERVGLADlagrqlGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255708477 1175 KILLLDEATSALDNDSEKVVQHAL-DKARTGRTCLVVTHRLSAIQNADLIVVL 1226
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
389-602 |
2.56e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.92 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 389 KNVSFNYPS------RPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFI----------------- 445
Cdd:PRK10419 7 SGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplaklnraqrka 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 446 ------MVDENDIRALNVRHyrdHIGVVSQEPVLFGTTISnnikygrddvtdeEMERAAREANAYDfIMEFPNkfnTLVG 519
Cdd:PRK10419 87 frrdiqMVFQDSISAVNPRK---TVREIIREPLRHLLSLD-------------KAERLARASEMLR-AVDLDD---SVLD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 520 EKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTT--IVVAHRLSTI-RSADLIVTLK 596
Cdd:PRK10419 147 KRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMD 226
|
....*.
gi 255708477 597 DGMLAE 602
Cdd:PRK10419 227 NGQIVE 232
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1032-1240 |
2.77e-23 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 99.91 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWL-RSQIAIVPQEPVLF-NCSIAE 1109
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFpRLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1110 NI-----AYGDNSRVVPlDEIKEAANAanIHSFIeglpekyntqvGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATS 1184
Cdd:TIGR03410 95 NLltglaALPRRSRKIP-DEIYELFPV--LKEML-----------GRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 1185 ALD----NDSEKVVQHAldKARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQEL 1240
Cdd:TIGR03410 161 GIQpsiiKDIGRVIRRL--RAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
386-613 |
3.34e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.08 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSrpSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDEN--DIRALNVRHYRDH 463
Cdd:PRK13636 6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 IGVVSQEP--VLFGTTISNNIKYGRDDVT--DEEMERAAREANAYDFIMEFPNKfntlvgeKGAQMSGGQKQRIAIARAL 539
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 540 VRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTIR-SADLIVTLKDGMLAEKGAHAELMAKR 613
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1027-1235 |
3.74e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 99.27 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1027 RPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLL-QRLYDP--VQGQVLFDGvdaKELNVQWLRSQIAIVPQEPVLF 1103
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNG---QPRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1104 NC-SIAENIAYGDNSR------------VVPLDEIKEAANAANIHSFIEGLpekyntqvglkgaqlSGGQKQRLAIARAL 1170
Cdd:cd03234 94 PGlTVRETLTYTAILRlprkssdairkkRVEDVLLRDLALTRIGGNLVKGI---------------SGGERRRVSIAVQL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1171 LQKPKILLLDEATSALDNDSE-KVVQHALDKARTGRTCLVVTH--RLSAIQNADLIVVLHNGKIKEQG 1235
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
408-611 |
4.77e-23 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 102.49 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 408 NLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDE----NDIRALNVRHYRDHIGVVSQEPVLFGT-TISNNI 482
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqDSARGIFLPPHRRRIGYVFQEARLFPHlSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 483 KYGrddvtdeeMERAAREANAYDF--IMEfpnkfntLVG-----EKG-AQMSGGQKQRIAIARALVRNPKILILDEATSA 554
Cdd:COG4148 99 LYG--------RKRAPRAERRISFdeVVE-------LLGighllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 555 LDSESKSAVQAALEK-ASKGRTTIV-VAHRLSTI-RSADLIVTLKDGMLAEKGAHAELMA 611
Cdd:COG4148 164 LDLARKAEILPYLERlRDELDIPILyVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1032-1238 |
4.92e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 99.32 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQV-----LFD---GVDAKElnVQWLRSQIAIVPQEPVLF 1103
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHFDfskTPSDKA--IRELRRNVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1104 -NCSIAENIAYGDnSRVVPLDEiKEAANAA-------NIHSFIEGLPekyntqvglkgAQLSGGQKQRLAIARALLQKPK 1175
Cdd:PRK11124 95 pHLTVQQNLIEAP-CRVLGLSK-DQALARAekllerlRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1176 ILLLDEATSALDND-SEKVVQHALDKARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQ 1238
Cdd:PRK11124 162 VLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEvARKTASRVVYMENGHIVEQGDAS 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
386-604 |
8.19e-23 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 97.95 E-value: 8.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPSikilkGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRhyRDHIG 465
Cdd:cd03298 1 VRLDKIRFSYGEQPM-----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLFG-TTISNNIKYGR------DDVTDEEMERAAREANAYDFIMEFPNkfntlvgekgaQMSGGQKQRIAIARA 538
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLspglklTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 539 LVRNPKILILDEATSALDSESKSAVQAALEK--ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKG 604
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1015-1213 |
9.34e-23 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 96.45 E-value: 9.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGvdakelnvqwlRSQIA 1094
Cdd:cd03223 1 IELENLSLATP--DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLFNCSIAENIAYgdnsrvvPLDEIkeaanaanihsfieglpekyntqvglkgaqLSGGQKQRLAIARALLQKP 1174
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-------PWDDV------------------------------LSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 255708477 1175 KILLLDEATSALDNDSEKVVQHALDKARTgrTCLVVTHR 1213
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
387-611 |
1.01e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 99.14 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNY------PSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENdirALNVRHY 460
Cdd:COG4167 6 EVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---KLEYGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 461 RD---HIGVVSQEPvlfGTTISNNIKYGRddvtdeemeraareanaydfIMEFPNKFNT----------------LVG-- 519
Cdd:COG4167 83 KYrckHIRMIFQDP---NTSLNPRLNIGQ--------------------ILEEPLRLNTdltaeereerifatlrLVGll 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 520 ----EKGAQM-SGGQKQRIAIARALVRNPKILILDEATSALDSESKS-AVQAALE-KASKGRTTIVVAHRLSTIRS-ADL 591
Cdd:COG4167 140 pehaNFYPHMlSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqIINLMLElQEKLGISYIYVSQHLGIVKHiSDK 219
|
250 260
....*....|....*....|
gi 255708477 592 IVTLKDGMLAEKGAHAELMA 611
Cdd:COG4167 220 VLVMHQGEVVEYGKTAEVFA 239
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1023-1235 |
1.11e-22 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 97.82 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1023 FYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKElNVQWLRSQIAIVPQEPVL 1102
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1103 FN-CSIAENIAY--------GDNSrvvpLDEIKEAANAANIHSFIEglpekyntqvgLKGAQLSGGQKQRLAIARALLQK 1173
Cdd:cd03266 90 YDrLTARENLEYfaglyglkGDEL----TARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 1174 PKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVV-THRLSAIQN-ADLIVVLHNGKIKEQG 1235
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFsTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1014-1237 |
1.12e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1014 NLEFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVL-----FD---GVDAKEln 1085
Cdd:COG4161 2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqFDfsqKPSEKA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1086 VQWLRSQIAIVPQEPVLF-NCSIAENIAygdNSRVVPLDEIKEAANAAnihsfieglPEKYNTQVGLKG------AQLSG 1158
Cdd:COG4161 77 IRLLRQKVGMVFQQYNLWpHLTVMENLI---EAPCKVLGLSKEQAREK---------AMKLLARLRLTDkadrfpLHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1159 GQKQRLAIARALLQKPKILLLDEATSALDND-SEKVVQHALDKARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGT 1236
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEfARKVASQVVYMEKGRIIEQGD 224
|
.
gi 255708477 1237 H 1237
Cdd:COG4161 225 A 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
386-615 |
1.16e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.39 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPSIK---ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAL-NVRHYR 461
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 462 DHIGVVSQEP--VLFGTTISNNIKYGRDD--VTDEEM----ERAAREANAYDFIMEFPNkfntlvgekgaQMSGGQKQRI 533
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIrervDESLKKVGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 534 AIARALVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTIRSADLIVTLKDGMLAEKG------A 605
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGtpkeifK 233
|
250
....*....|
gi 255708477 606 HAELMAKRGL 615
Cdd:PRK13633 234 EVEMMKKIGL 243
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1032-1231 |
1.32e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.60 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLfdgvdAKELNVQWLRSQIAIVPQEPVLFNC-SIAEN 1110
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEAREDTRLMFQDARLLPWkKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1111 IAYG--DNSRvvplDEIKEAANAAnihsfieGLPEKYNTQvglkGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDN 1188
Cdd:PRK11247 102 VGLGlkGQWR----DAALQALAAV-------GLADRANEW----PAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 255708477 1189 DSEKVVQHALDK--ARTGRTCLVVTHRLS-AIQNADLIVVLHNGKI 1231
Cdd:PRK11247 167 LTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
385-610 |
1.87e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.46 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFnypSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHI 464
Cdd:PRK09536 3 MIDVSDLSV---EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQEPVL-FGTTISNNIKYGRD------DVTDEEMERAAREANAYDFIMEFPNKFNTlvgekgaQMSGGQKQRIAIAR 537
Cdd:PRK09536 80 ASVPQDTSLsFEFDVRQVVEMGRTphrsrfDTWTETDRAAVERAMERTGVAQFADRPVT-------SLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 538 ALVRNPKILILDEATSALD-SESKSAVQAALEKASKGRTTIVVAHRLS-TIRSADLIVTLKDGMLAEKGAHAELM 610
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDiNHQVRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
127-339 |
1.98e-22 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 98.95 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 127 LWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNM--STFSIGLAVGLvkGW 204
Cdd:cd18590 59 LFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLvkTLGMLGFMLSL--SW 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 205 KLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRT 284
Cdd:cd18590 137 QLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRD 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 285 IASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGTVLAVFFSVIHSSYCI 339
Cdd:cd18590 217 TVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGH--LTTGSLVSFILYQKNLGSYV 269
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
737-1251 |
2.35e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 104.67 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 737 MIF--VILGVICFVSYFMQglfYGRAGeiltMRLRHLAFKAMLYQDIAWFDE--KENSTGGLTTILAIDIAQIQgatgsR 812
Cdd:PLN03232 346 LIFfgVTFGVLCESQYFQN---VGRVG----FRLRSTLVAAIFHKSLRLTHEarKNFASGKVTNMITTDANALQ-----Q 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 813 IGVLTQNATNMGLSVIISFIYGWEMtFLILSIAPVLAVTGMIETAA-----MTGFANKDKQELKHAGKIATEALENIRTI 887
Cdd:PLN03232 414 IAEQLHGLWSAPFRIIVSMVLLYQQ-LGVASLFGSLILFLLIPLQTlivrkMRKLTKEGLQWTDKRVGIINEILASMDTV 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 888 VSLTREKAFEQMYEEmLQTQHRNTSKKAQIIGSCYAFSHAFIYFAYAAgFRFGAYLIQAGRMTPEGMFIVFTAIAYGAMA 967
Cdd:PLN03232 493 KCYAWEKSFESRIQG-IRNEELSWFRKAQLLSAFNSFILNSIPVVVTL-VSFGVFVLLGGDLTPARAFTSLSLFAVLRSP 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 968 IGETLVLAPEYSKAKSGAAHLFALLEKKPNIDSRS---QEGKKPDTCEGNlefrevSFFYPCRPDVFILRGLSLSIERGK 1044
Cdd:PLN03232 571 LNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNpplQPGAPAISIKNG------YFSWDSKTSKPTLSDINLEIPVGS 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1045 TVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFdgvdakelnvqwLRSQIAIVPQEPVLFNCSIAENIAYGdnSRVVPlDE 1124
Cdd:PLN03232 645 LVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENILFG--SDFES-ER 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1125 IKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALD-NDSEKVVQHALDKART 1203
Cdd:PLN03232 710 YWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDaHVAHQVFDSCMKDELK 789
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 255708477 1204 GRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLV 1251
Cdd:PLN03232 790 GKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
380-598 |
2.56e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.96 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 380 ESIEGTVEFKNVSFNYPS-RPsikILKGLNLRIKSGETVALVGLNGSGKSTvvqLLqrlydpddgfimvdendiRALN-- 456
Cdd:COG4178 357 TSEDGALALEDLTLRTPDgRP---LLEDLSLSLKPGERLLITGPSGSGKST---LL------------------RAIAgl 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 457 --------VRHYRDHIGVVSQEPVLFGTTISNNIKY--GRDDVTDEEMERAAREANAYDFImefpNKFNTlVGEKGAQMS 526
Cdd:COG4178 413 wpygsgriARPAGARVLFLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLA----ERLDE-EADWDQVLS 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 527 GGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDG 598
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
386-581 |
2.58e-22 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 94.05 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENdiraLNVRHYrdhig 465
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----VKIGYF----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 vvsqepvlfgttisnnikygrddvtdeemeraareanaydfimefpnkfntlvgekgAQMSGGQKQRIAIARALVRNPKI 545
Cdd:cd03221 69 ---------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*.
gi 255708477 546 LILDEATSALDSESKSAVQAALeKASKGrTTIVVAH 581
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
386-610 |
2.69e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.46 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIG 465
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEP-----------VLFGttisnniKY----GRDDVTDEEMeraAREANAYDFIMEFPNKF-NTLvgekgaqmSGGQ 529
Cdd:COG4604 79 ILRQENhinsrltvrelVAFG-------RFpyskGRLTAEDREI---IDEAIAYLDLEDLADRYlDEL--------SGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 530 KQRIAIARALVRNPKILILDEATSALDseSKSAVQ--AALEKAS--KGRTTIVVAHRLS-TIRSADLIVTLKDGMLAEKG 604
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLD--MKHSVQmmKLLRRLAdeLGKTVVIVLHDINfASCYADHIVAMKDGRVVAQG 218
|
....*.
gi 255708477 605 AHAELM 610
Cdd:COG4604 219 TPEEII 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1033-1229 |
3.24e-22 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 96.77 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNvqwlrsqiaivPQEPVLFN-------C 1105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-----------PDRMVVFQnysllpwL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1106 SIAENIAYGDNsRVVPLDEIKEAANAANIHSFIEGLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQKPKILLLDEATSA 1185
Cdd:TIGR01184 70 TVRENIALAVD-RVLPDLSKSERRAIVEEHIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255708477 1186 LDNDSEKVVQHALDK--ARTGRTCLVVTHRL-SAIQNADLIVVLHNG 1229
Cdd:TIGR01184 145 LDALTRGNLQEELMQiwEEHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1032-1236 |
3.51e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 97.06 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTsvqLLQRL-----YDPVQGQVLFDGVDAKELNVQwLRSQ--IAIVPQEPV--- 1101
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKST---LAKVLmghpkYEVTSGSILLDGEDILELSPD-ERARagIFLAFQYPVeip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1102 -------LfncSIAENIAYGDNSRVVP-LDEIKEAANAAnihsfieGLPEKY-----NtqVGLkgaqlSGGQKQRLAIAR 1168
Cdd:COG0396 91 gvsvsnfL---RTALNARRGEELSAREfLKLLKEKMKEL-------GLDEDFldryvN--EGF-----SGGEKKRNEILQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 1169 ALLQKPKILLLDEATSALDNDSEKVVQHALDKART-GRTCLVVTH--RLSAIQNADLIVVLHNGKIKEQGT 1236
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1029-1240 |
3.75e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 100.10 E-value: 3.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1029 DVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGvdaKELN-VQWLRSQIAIVPQEPVLF-NCS 1106
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNdVPPAERGVGMVFQSYALYpHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1107 IAENIAYGDNSRVVPLDEIKEAAN-AANIHSfIEGLPEKyntqvglKGAQLSGGQKQRLAIARALLQKPKILLLDEATSA 1185
Cdd:PRK11000 92 VAENMSFGLKLAGAKKEEINQRVNqVAEVLQ-LAHLLDR-------KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1186 LdnDSEKVVQHALDKA----RTGRTCLVVTH-RLSAIQNADLIVVLHNGKIKEQGTHQEL 1240
Cdd:PRK11000 164 L--DAALRVQMRIEISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
401-611 |
3.79e-22 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 96.74 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 401 IKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVrHYRDHIGVVS--QEPVLFGT-T 477
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP-HEIARLGIGRtfQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 478 ISNNI--------KYGRDDVTDEEMERAAREAnAYDfIMEF---PNKFNTLVGEkgaqMSGGQKQRIAIARALVRNPKIL 546
Cdd:cd03219 92 VLENVmvaaqartGSGLLLARARREEREARER-AEE-LLERvglADLADRPAGE----LSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 547 ILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDG-MLAEkGAHAELMA 611
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGrVIAE-GTPDEVRN 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
93-333 |
3.89e-22 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 97.94 E-value: 3.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 93 TQSQEKLNEdmTLLTLYYVGIGVAalIFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDID 172
Cdd:cd18575 29 AGNTALLNR--AFLLLLAVALVLA--LASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 173 KISDGIGDKIALLFQNMSTFSIGLAVGLVKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSS 252
Cdd:cd18575 105 LIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 253 IRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGTVLA-VFFS 331
Cdd:cd18575 185 IKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGR--MSAGELSQfVFYA 262
|
..
gi 255708477 332 VI 333
Cdd:cd18575 263 VL 264
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
738-952 |
4.15e-22 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 98.00 E-value: 4.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 738 IFVILGVICFVSYFMQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQGATGSRIGVLT 817
Cdd:cd18572 41 LLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDA--TKTGELTSRLTSDCQKVSDPLSTNLNVFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 818 QNATNMGLSVIISFIYGWEMTFLILSIAPVLAVtgmietaaMTGF--------ANKDKQELKHAGKIATEALENIRTIVS 889
Cdd:cd18572 119 RNLVQLVGGLAFMFSLSWRLTLLAFITVPVIAL--------ITKVygryyrklSKEIQDALAEANQVAEEALSNIRTVRS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 890 LTREKAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRMTPE 952
Cdd:cd18572 191 FATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAG 253
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
385-606 |
4.28e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.62 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMV-----------DENDIR 453
Cdd:PRK11124 2 SIQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsktpSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 454 ALnvrhyRDHIGVVSQE----PVLfgTTISNNIK-----YGRDDvtDEEMERAAREANAY---DFIMEFPnkfntlvgek 521
Cdd:PRK11124 79 EL-----RRNVGMVFQQynlwPHL--TVQQNLIEapcrvLGLSK--DQALARAEKLLERLrlkPYADRFP---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 522 gAQMSGGQKQRIAIARALVRNPKILILDEATSALDSE-SKSAVQAALEKASKGRTTIVVAHRLSTIRS-ADLIVTLKDGM 599
Cdd:PRK11124 140 -LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGH 218
|
....*..
gi 255708477 600 LAEKGAH 606
Cdd:PRK11124 219 IVEQGDA 225
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
67-583 |
4.48e-22 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 103.84 E-value: 4.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 67 LVLGEMSDNLISGCLVQTNTTNYQNCTQSQEKLNEDMTLLTLYYVGIGVA--ALIFGYIQISLWIITAARQTKRIRKQFF 144
Cdd:TIGR01271 886 LGLWLITDNPSAPNYVDQQHANASSPDVQKPVIITPTSAYYIFYIYVGTAdsVLALGFFRGLPLVHTLLTVSKRLHEQML 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 145 HSVLAQDIGWFDSCDIGELNTRMTDDIDKISD----GIGDKIALLFQNMSTFSIglaVGLVKGWKLtlvtLSTSPLIMAS 220
Cdd:TIGR01271 966 HSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDmlplTLFDFIQLTLIVLGAIFV---VSVLQPYIF----IAAIPVAVIF 1038
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 221 AAAcsRMVISLTSKELSAYSKAG--AVAEEVLSSIR---TVIAFRAQE--KELQRYTQNLKDAKDF---GIKRTIASKVS 290
Cdd:TIGR01271 1039 IML--RAYFLRTSQQLKQLESEArsPIFSHLITSLKglwTIRAFGRQSyfETLFHKALNLHTANWFlylSTLRWFQMRID 1116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 291 LGAVYFFMNGTYglafwygTSLILNGEPGYTIGTVLAVFFSVIhsSYCIGAAVPHFETFAIARGAAfHIFQVIDKKPSID 370
Cdd:TIGR01271 1117 IIFVFFFIAVTF-------IAIGTNQDGEGEVGIILTLAMNIL--STLQWAVNSSIDVDGLMRSVS-RVFKFIDLPQEEP 1186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 371 NFSTAG--YKPESI--------------EGTVEFKNVSFNYPSRPSiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLL 434
Cdd:TIGR01271 1187 RPSGGGgkYQLSTVlvienphaqkcwpsGGQMDVQGLTAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL 1265
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 435 QRLYDpDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIK-YGRddVTDEEMERAAREANAYDFIMEFPNK 513
Cdd:TIGR01271 1266 LRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDpYEQ--WSDEEIWKVAEEVGLKSVIEQFPDK 1342
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 514 FNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRL 583
Cdd:TIGR01271 1343 LDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1015-1236 |
4.63e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.89 E-value: 4.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPC-----RPDVFilrGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGV----DAKELN 1085
Cdd:PRK13649 3 INLQNVSYTYQAgtpfeGRALF---DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitsTSKNKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1086 VQWLRSQIAIVPQ--EPVLFNCSIAENIAYG-DNSRVVPLDEIKEAANAANIHSFIEGLPEKyntqvglKGAQLSGGQKQ 1162
Cdd:PRK13649 80 IKQIRKKVGLVFQfpESQLFEETVLKDVAFGpQNFGVSQEEAEALAREKLALVGISESLFEK-------NPFELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 1163 RLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKA-RTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGT 1236
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
384-624 |
4.87e-22 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 97.62 E-value: 4.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 384 GTVEFKNVSFNYpSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDdGFIMVDENDIRALNVRHYRDH 463
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 IGVVSQEPVLFGTTISNNIK-YGRddVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRN 542
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGK--WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 543 PKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSLVMS 622
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISP 236
|
..
gi 255708477 623 QD 624
Cdd:cd03289 237 SD 238
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
386-604 |
5.03e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 95.36 E-value: 5.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIraLNVRHYRDHIG 465
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLFGT-TISNNIKYGRD--DVTDEEMERAAREANaydfimefpnkFNTLVGEKGAQMSGGQKQRIAIARALVRN 542
Cdd:cd03268 76 ALIEAPGFYPNlTARENLRLLARllGIRKKRIDEVLDVVG-----------LKDSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 543 PKILILDEATSALDSESKSAVQAAL-EKASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKG 604
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1015-1245 |
6.11e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.59 E-value: 6.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFY-PCRPdvFILRGL---SLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDG----VDAKELNV 1086
Cdd:PRK13641 3 IKFENVDYIYsPGTP--MEKKGLdniSFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1087 QWLRSQIAIVPQ--EPVLFNCSIAENIAYGDNSRVVPLDEIKEAAnaanihsfieglpEKYNTQVGLKGA-------QLS 1157
Cdd:PRK13641 81 KKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKA-------------LKWLKKVGLSEDliskspfELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1158 GGQKQRLAIARALLQKPKILLLDEATSALDNDSEK-VVQHALDKARTGRTCLVVTHRLSAI-QNADLIVVLHNGKIKEQG 1235
Cdd:PRK13641 148 GGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHA 227
|
250
....*....|
gi 255708477 1236 THQELLRNRD 1245
Cdd:PRK13641 228 SPKEIFSDKE 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
400-609 |
6.20e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.52 E-value: 6.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 400 SIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYD--PD---DGFIMVDENDIRALNVRHYRDHIGVVSQEP--- 471
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 472 --------VLFGTTISNNIKYGRDdvTDEEMERAAREANAYDfimEFPNKFNTLVGekgaQMSGGQKQRIAIARALVRNP 543
Cdd:PRK14247 95 pnlsifenVALGLKLNRLVKSKKE--LQERVRWALEKAQLWD---EVKDRLDAPAG----KLSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 544 KILILDEATSALDSESKSAVQAALEKASKGRTTIVVAH-RLSTIRSADLIVTLKDGMLAEKGAHAEL 609
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
48-327 |
6.34e-22 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 97.50 E-value: 6.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 48 MILGILASLVNGACLPLMPLVLGEMSDNLISGCLVQTnttnyqnctqsqeklnedmTLLTLyyVGIGVAALIFGYIQISL 127
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGG-------------------LLALL--VALFLLQAVLSALSSYL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 128 WIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGWKLT 207
Cdd:cd18551 60 LGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 208 LVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTIAS 287
Cdd:cd18551 140 LVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIE 219
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 255708477 288 KVSLGAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGTVLA 327
Cdd:cd18551 220 ALIGPLMGLAVQLALLVVLGVGGARVASGA--LTVGTLVA 257
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1033-1243 |
8.29e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.46 E-value: 8.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKEL------------------------NVQW 1088
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviqktrfkkikKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1089 LRSQIAIVPQ--EPVLFNCSIAENIAYGDNSRVVPLDEIKEAANaanihSFIE--GLPEKYntqvgLKGA--QLSGGQKQ 1162
Cdd:PRK13651 103 IRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAA-----KYIElvGLDESY-----LQRSpfELSGGQKR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1163 RLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKA-RTGRTCLVVTHRL-SAIQNADLIVVLHNGKIKEQGTHQEL 1240
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGDTYDI 252
|
...
gi 255708477 1241 LRN 1243
Cdd:PRK13651 253 LSD 255
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
386-586 |
9.21e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 96.26 E-value: 9.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPD-----DGFIMVDENDI--RALNVR 458
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 459 HYRDHIGVVSQEPVLFGTTISNNIKYGRDDV-------TDEEMERAAREANAYDfimEFPNKFNtlvgEKGAQMSGGQKQ 531
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVgwrpkleIDDIVESALKDADLWD---EIKHKIH----KSALDLSGGQQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 532 RIAIARALVRNPKILILDEATSALDSESKSAVQAALEKAS--KGRTTIVVAHRLSTI 586
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQV 214
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1016-1247 |
1.03e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.92 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1016 EFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAI 1095
Cdd:COG4604 3 EIKNVSKRYG---GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1096 VPQEPVL-FNCSIAENIAYG--DNSRVVPLDEIKEAANAAnIHSF-IEGLPEKYntqvgLKgaQLSGGQKQRLAIARALL 1171
Cdd:COG4604 80 LRQENHInSRLTVRELVAFGrfPYSKGRLTAEDREIIDEA-IAYLdLEDLADRY-----LD--ELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1172 QKPKILLLDEATSALDndsekvVQHALDKART--------GRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELLR 1242
Cdd:COG4604 152 QDTDYVLLDEPLNNLD------MKHSVQMMKLlrrladelGKTVVIVLHDINfASCYADHIVAMKDGRVVAQGTPEEIIT 225
|
....*...
gi 255708477 1243 N---RDIY 1247
Cdd:COG4604 226 PevlSDIY 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
386-598 |
1.28e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.10 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVS--FnypsrPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDH 463
Cdd:COG3845 6 LELRGITkrF-----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 -IGVVSQEPVLFGT-TISNNIKYGRDD----VTDeeMERAAREanaydfIMEFPNKF------NTLVGekgaQMSGGQKQ 531
Cdd:COG3845 81 gIGMVHQHFMLVPNlTVAENIVLGLEPtkggRLD--RKAARAR------IRELSERYgldvdpDAKVE----DLSVGEQQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 532 RIAIARALVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDG 598
Cdd:COG3845 149 RVEILKALYRGARILILDEPTAVLTPQEADELFEILRRlAAEGKSIIFITHKLREVMAiADRVTVLRRG 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
386-641 |
1.32e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.73 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNY-PSRP-SIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDE----NDIRALNVRH 459
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 460 YRDHIGVVSQEP--VLFGTTISNNIKYGRDD--VTDEEMERAAREAnaydfiMEFPNKFNTLVGEKGAQMSGGQKQRIAI 535
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEK------LEMVGLADEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 536 ARALVRNPKILILDEATSALDSESKSAVQAALEKASK-GRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAELMAKR 613
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQEV 235
|
250 260 270
....*....|....*....|....*....|
gi 255708477 614 GLY--YSLVMSQDIKKADEQMESMTYSTER 641
Cdd:PRK13643 236 DFLkaHELGVPKATHFADQLQKTGAVTFEK 265
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
386-609 |
1.50e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.87 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPSIKilkGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHyRDhIG 465
Cdd:PRK11432 7 VVLKNITKRFGSNTVID---NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RD-IC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLF-GTTISNNIKYG--RDDVTDEEMERAAREANAYDFIMEFPNKFNTlvgekgaQMSGGQKQRIAIARALVRN 542
Cdd:PRK11432 82 MVFQSYALFpHMSLGENVGYGlkMLGVPKEERKQRVKEALELVDLAGFEDRYVD-------QISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 543 PKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLS-TIRSADLIVTLKDGMLAEKGAHAEL 609
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
386-607 |
2.07e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.21 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAlNVRHYRDHIG 465
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVL---FgTTISNNIKYGRddvtdeEMERAAREANA-YDFIMEFP---NKFNTLVgekgAQMSGGQKQRIAIARA 538
Cdd:PRK13536 118 VVPQFDNLdleF-TVRENLLVFGR------YFGMSTREIEAvIPSLLEFArleSKADARV----SDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 539 LVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTI-RSADLIVTLKDGM-LAEKGAHA 607
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVLEAGRkIAEGRPHA 258
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
48-333 |
2.39e-21 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 95.95 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 48 MILGILASLVNGACLPLMPLVLGEMSDNLISgclvqtnttnyqnctqsqeklNEDMTLLtlYYVGIGVAAL-----IFGY 122
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFV---------------------EKDLEAL--LLVPLAIIGLfllrgLASY 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 123 IQIslWIITAARQ--TKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGL 200
Cdd:cd18552 58 LQT--YLMAYVGQrvVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 201 VKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFG 280
Cdd:cd18552 136 YLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLS 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 255708477 281 IKRTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGTvlavFFSVI 333
Cdd:cd18552 216 MKIARARALSSPLMELLGAIAIALVLWYGGYQVISGE--LTPGE----FISFI 262
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
404-609 |
2.59e-21 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 93.97 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 404 LKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAlNVRHYRDHIGVVSQEPVLFG--TTISNN 481
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDelTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 482 IKYGR-DDVTDEEMERAAREANAYDFIMEFPNKfntLVGekgaQMSGGQKQRIAIARALVRNPKILILDEATSALDSESK 560
Cdd:cd03265 95 YIHARlYGVPGAERRERIDELLDFVGLLEAADR---LVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 255708477 561 SAVQAALEK--ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAEL 609
Cdd:cd03265 168 AHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
386-598 |
2.65e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFImvdendIRALNVRhyrdhIG 465
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV------KLGETVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLF--GTTISNNIKYGRDDVTDeemeraaREANAY--DFImeF-PNKFNTLVGEkgaqMSGGQKQRIAIARALV 540
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPGGTE-------QEVRGYlgRFL--FsGDDAFKPVGV----LSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 541 RNPKILILDEATSALDSESKSAVQAALEkASKGrTTIVVAH-R--LSTIrsADLIVTLKDG 598
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDG 505
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
403-613 |
2.76e-21 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 94.87 E-value: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 403 ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN---VRHYRDHIGVVSQE-PVLFG--T 476
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDsPSAVNprM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 477 TISNNIKYGRDDVTD-EEMERAAREANAYDfIMEFPNKfntLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSAL 555
Cdd:TIGR02769 106 TVRQIIGEPLRHLTSlDESEQKARIAELLD-MVGLRSE---DADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 556 DSESKSAVQAALEK--ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAELMAKR 613
Cdd:TIGR02769 182 DMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1029-1247 |
2.83e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.46 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1029 DVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQV----------------LFDGVDAKELNVQWLRSQ 1092
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnhelITNPYSKKIKNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1093 IAIVPQEP--VLFNCSIAENIAYGDNSRVVPLDEIKEAAnaanihsfieglpEKYNTQVGLKGA-------QLSGGQKQR 1163
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLA-------------KFYLNKMGLDDSylerspfGLSGGQKRR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1164 LAIARALLQKPKILLLDEATSALDNDSEK-VVQHALDKARTGRTCLVVTHRL-SAIQNADLIVVLHNGKIKEQGTHQELL 1241
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
....*.
gi 255708477 1242 RNRDIY 1247
Cdd:PRK13631 265 TDQHII 270
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
404-583 |
2.96e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.85 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 404 LKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGF------IMVDEN----DIRALNVRHyrdHIGVVSQEPVL 473
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFrvegkvTFHGKNlyapDVDPVEVRR---RIGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 474 FGTTISNNIKYG------RDDVtDEEMERAAREANAYDfimEFPNKFNtlvgEKGAQMSGGQKQRIAIARALVRNPKILI 547
Cdd:PRK14243 103 FPKSIYDNIAYGaringyKGDM-DELVERSLRQAALWD---EVKDKLK----QSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 255708477 548 LDEATSALDSESKSAVQAALEKASKGRTTIVVAHRL 583
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1015-1241 |
3.00e-21 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 94.38 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFypcRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQV--LFD----GVDakelnVQW 1088
Cdd:COG1119 4 LELRNVTVR---RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrLFGerrgGED-----VWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1089 LRSQIAIVpqepvlfNCSIAENIAYGDNSR-VV-------------PLDEIKEAANAAnIHSFieGLPEKYNTQVGlkga 1154
Cdd:COG1119 76 LRKRIGLV-------SPALQLRFPRDETVLdVVlsgffdsiglyrePTDEQRERAREL-LELL--GLAHLADRPFG---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1155 QLSGGQKQRLAIARALLQKPKILLLDEATSALDNDS-EKVVQhALDK-ARTGRTCLV-VTHRLSAIQNA-DLIVVLHNGK 1230
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArELLLA-LLDKlAAEGAPTLVlVTHHVEEIPPGiTHVLLLKDGR 220
|
250
....*....|.
gi 255708477 1231 IKEQGTHQELL 1241
Cdd:COG1119 221 VVAAGPKEEVL 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1015-1242 |
3.31e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.01 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPDVF--------ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYdPVQGQVLFDGVDAKELNV 1086
Cdd:PRK15134 276 LDVEQLQVAFPIRKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1087 QWL---RSQIAIVPQEPvlfNCSIaeniaygdNSRVVPLDEIKEA--------ANAANIHSFIEGLPEkyntqVGLKG-- 1153
Cdd:PRK15134 355 RQLlpvRHRIQVVFQDP---NSSL--------NPRLNVLQIIEEGlrvhqptlSAAQREQQVIAVMEE-----VGLDPet 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1154 -----AQLSGGQKQRLAIARALLQKPKILLLDEATSALDndseKVVQH---ALDKArtgrtcLVVTHRLSAI-QNADL-- 1222
Cdd:PRK15134 419 rhrypAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAqilALLKS------LQQKHQLAYLfISHDLhv 488
|
250 260
....*....|....*....|....*..
gi 255708477 1223 -------IVVLHNGKIKEQGTHQELLR 1242
Cdd:PRK15134 489 vralchqVIVLRQGEVVEQGDCERVFA 515
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
399-599 |
3.59e-21 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 93.55 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 399 PSIKILKGLNLRIKSGETVALVGLNGSGKSTVV--------QLLQRLYDPDDGFIMVDENDIRALNvrhyRDHIGVVSQE 470
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlailgemqTLEGKVHWSNKNESEPSFEATRSRN----RYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 471 PVLFGTTISNNIKYGRDdvTDEEMERAAREANAYDFIME-FPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILD 549
Cdd:cd03290 88 PWLLNATVEENITFGSP--FNKQRYKAVTDACSLQPDIDlLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255708477 550 EATSALDSE-SKSAVQAALEK--ASKGRTTIVVAHRLSTIRSADLIVTLKDGM 599
Cdd:cd03290 166 DPFSALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1037-1241 |
3.72e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.88 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1037 SLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwlRSQIAIVPQEPVLFN-CSIAENIAYG- 1114
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1115 ------DNSRVVPLDEIkeaANAANIHSFIEGLPekyntqvglkgAQLSGGQKQRLAIARALLQKPKILLLDEATSALD- 1187
Cdd:PRK10771 97 npglklNAAQREKLHAI---ARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDp 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1188 ---NDSEKVVQHALDKARTgrTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELL 1241
Cdd:PRK10771 163 alrQEMLTLVSQVCQERQL--TLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1032-1235 |
4.11e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 92.59 E-value: 4.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTsvqLLQRL-----YDPVQGQVLFDGVDAKELNVQwLRSQ--IAIVPQEPVlfn 1104
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKST---LAKTImghpkYEVTEGEILFKGEDITDLPPE-ERARlgIFLAFQYPP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1105 csiaeniaygdnsrvvpldEIKEAANAanihSFIEGLPEKyntqvglkgaqLSGGQKQRLAIARALLQKPKILLLDEATS 1184
Cdd:cd03217 88 -------------------EIPGVKNA----DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255708477 1185 ALDNDSEKVVQHALDKART-GRTCLVVTH--RLSAIQNADLIVVLHNGKIKEQG 1235
Cdd:cd03217 134 GLDIDALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
402-611 |
4.67e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 94.27 E-value: 4.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 402 KILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAL-------------NVRHYRDHIGVVS 468
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 469 QEPVLFG-TTISNNIKYGRDDV----TDEEMERAAREANAYDFIMEFPNKFNtlvgekgAQMSGGQKQRIAIARALVRNP 543
Cdd:PRK10619 99 QHFNLWShMTVLENVMEAPIQVlglsKQEARERAVKYLAKVGIDERAQGKYP-------VHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 544 KILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAELMA 611
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
377-610 |
4.84e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 94.47 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 377 YKPESIEGTVEFKNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN 456
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 457 VRHYRDHIGVVSQE-PVLFGTTISNNI---KY------GRDDVTD-EEMERAAreanaydfimefpnkfnTLVGEKG-AQ 524
Cdd:PRK10575 80 SKAFARKVAYLPQQlPAAEGMTVRELVaigRYpwhgalGRFGAADrEKVEEAI-----------------SLVGLKPlAH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 525 -----MSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKAS--KGRTTIVVAHRLS-TIRSADLIVTLK 596
Cdd:PRK10575 143 rlvdsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSqeRGLTVIAVLHDINmAARYCDYLVALR 222
|
250
....*....|....
gi 255708477 597 DGMLAEKGAHAELM 610
Cdd:PRK10575 223 GGEMIAQGTPAELM 236
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1029-1242 |
5.09e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.18 E-value: 5.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1029 DVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGvdaKELNvQWLRSQIAIVPQEPVLF-NCSI 1107
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLD-PEDRRRIGYLPEERGLYpKMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1108 AENIAY-----GdnsrvVPLDEIKEAANAanihsFIE--GLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQKPKILLLD 1180
Cdd:COG4152 89 GEQLVYlarlkG-----LSKAEAKRRADE-----WLErlGLGDRANKKVE----ELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1181 EATSALD--NdSEKVVQHALDKARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLR 1242
Cdd:COG4152 155 EPFSGLDpvN-VELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRR 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
387-552 |
5.73e-21 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 93.12 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPSrpsIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN----VRHyrd 462
Cdd:COG0410 5 EVENLHAGYGG---IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPphriARL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEPVLFGT-TISNNIK---YGRDDVTdeemERAAREANAYDFimeFPNkfntlVGE----KGAQMSGGQKQRIA 534
Cdd:COG0410 79 GIGYVPEGRRIFPSlTVEENLLlgaYARRDRA----EVRADLERVYEL---FPR-----LKErrrqRAGTLSGGEQQMLA 146
|
170
....*....|....*...
gi 255708477 535 IARALVRNPKILILDEAT 552
Cdd:COG0410 147 IGRALMSRPKLLLLDEPS 164
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
403-609 |
5.77e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.96 E-value: 5.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 403 ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDEN------DIRALNVRHYRDHIGVVSQEPVLF-G 475
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 476 TTISNNIKY--GRDDVTDEE-----MERAAREANAYDfimEFPNKFNTlvgeKGAQMSGGQKQRIAIARALVRNPKILIL 548
Cdd:PRK14246 105 LSIYDNIAYplKSHGIKEKReikkiVEECLRKVGLWK---EVYDRLNS----PASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 549 DEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKGAHAEL 609
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
381-615 |
6.56e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 94.69 E-value: 6.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 381 SIEGTVEFKNVSFNYPSRP--SIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRA---- 454
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 455 -LNVRHYRDHIGVVSQEP--VLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFImEFPNKFntlVGEKGAQMSGGQKQ 531
Cdd:PRK13645 82 iKEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPEDY---VKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 532 RIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKGAHAE 608
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFE 237
|
....*..
gi 255708477 609 LMAKRGL 615
Cdd:PRK13645 238 IFSNQEL 244
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
385-613 |
6.76e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.51 E-value: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFNY-PSRPSIKI-LKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRA----LNVR 458
Cdd:PRK13641 2 SIKFENVDYIYsPGTPMEKKgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 459 HYRDHIGVVSQ--EPVLFGTTISNNIKYGRDD--VTDEEMERAAREANAYDFIMEfpnkfnTLVGEKGAQMSGGQKQRIA 534
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKALKWLKKVGLSE------DLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 535 IARALVRNPKILILDEATSALDSES-KSAVQAALEKASKGRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKGAHAELMAK 612
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSD 235
|
.
gi 255708477 613 R 613
Cdd:PRK13641 236 K 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1027-1235 |
7.69e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 92.60 E-value: 7.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1027 RPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGvdakelNVQW-LRSQIAIVPQ----EPV 1101
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSlLGLGGGFNPEltgrENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1102 LFNCSIaeniaYGdnsrvVPLDEIKEAANAanIHSFIEgLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQKPKILLLDE 1181
Cdd:cd03220 106 YLNGRL-----LG-----LSRKEIDEKIDE--IIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 1182 ATSALDND-SEKVVQHALDKARTGRTCLVVTHRLSAI-QNADLIVVLHNGKIKEQG 1235
Cdd:cd03220 169 VLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1032-1244 |
9.06e-21 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 94.15 E-value: 9.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGvdakelnvqwlrsQIAIVPQEPVLFNCSIAENI 1111
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1112 AYGdnsrvVPLDEI--KEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDND 1189
Cdd:cd03291 119 IFG-----VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 1190 SEK-VVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNR 1244
Cdd:cd03291 194 TEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
404-610 |
9.31e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.26 E-value: 9.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 404 LKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRD----HIGVVSQEPVLF-GTTI 478
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 479 SNNIKYGRDDVTDEEMER------AAREANAYDFIMEFPNkfntlvgekgaQMSGGQKQRIAIARALVRNPKILILDEAT 552
Cdd:PRK10070 124 LDNTAFGMELAGINAEERrekaldALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 553 SALDSESKSAVQAALEK--ASKGRTTIVVAHRL-STIRSADLIVTLKDGMLAEKGAHAELM 610
Cdd:PRK10070 193 SALDPLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
48-327 |
9.95e-21 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 93.99 E-value: 9.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 48 MILGILASLVNGACLPLMPLVLGEMSDNLISGclvqtnttnyqnctqsQEKLNEDMTLLTLYYVGIGVAALIFGYIQISL 127
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVP----------------GQGDLQGLLLLALLYLGLLLLSFLLQYLQTYL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 128 WIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFsIGLAVG-LVKGWKL 206
Cdd:cd18544 65 LQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLL-IGILIAmFLLNWRL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 207 TLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTIA 286
Cdd:cd18544 144 ALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 255708477 287 SKVSLGAVYFFMNGTYGLAFWYGTSLILNGepGYTIGTVLA 327
Cdd:cd18544 224 FALFRPLVELLSSLALALVLWYGGGQVLSG--AVTLGVLYA 262
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1017-1232 |
1.01e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1017 FREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGvDAKelnvqwlrsqIAIV 1096
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1097 PQEPVLF-NCSIAENIAYGDNSRVVPLDEIKEAANA---------------------------ANIHSFIEGL---PEKY 1145
Cdd:COG0488 67 PQEPPLDdDLTVLDTVLDGDAELRALEAELEELEAKlaepdedlerlaelqeefealggweaeARAEEILSGLgfpEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1146 NTQVGlkgaQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDS----EKVVqhaldKARTGrTCLVVTH-R--LSAIq 1218
Cdd:COG0488 147 DRPVS----ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSHdRyfLDRV- 215
|
250
....*....|....
gi 255708477 1219 nADLIVVLHNGKIK 1232
Cdd:COG0488 216 -ATRILELDRGKLT 228
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
402-604 |
1.08e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.82 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 402 KILKGLNLRIKSGETVALVGLNGSGKSTVVQLL--QRLYDPDDGFIMVDENDIRALNVrHYRDH--IGVVSQEPVLF-GT 476
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSP-DERARagIFLAFQYPVEIpGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 477 TISNNIKYGRDDVTDEEMERAAreanaydfimefpnkFNTLVGEKGAQM---------------SGGQKQRIAIARALVR 541
Cdd:COG0396 93 SVSNFLRTALNARRGEELSARE---------------FLKLLKEKMKELgldedfldryvnegfSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 542 NPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAH--RLSTIRSADLIVTLKDGMLAEKG 604
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIVAEGVNKlRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSG 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1033-1242 |
1.24e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 93.69 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVD----AKELNVQWLRSQIAIVPQ--EPVLFNCS 1106
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIRPVRKRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1107 IAENIAYGDNSRVVPLDEIKEAAnaaniHSFIEGLPEKYNTqVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSAL 1186
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVKNYA-----HRLLMDLGFSRDV-MSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1187 DNDSEKVVQHALDKART--GRTCLVVTHRLSAI-QNADLIVVLHNGKIKEQGTHQELLR 1242
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1029-1236 |
1.48e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 94.91 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1029 DVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDG-----VDAKELNvqwlrsqIAIVPQEPVLF 1103
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvneLEPADRD-------IAMVFQNYALY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1104 -NCSIAENIAYGDNSRVVPLDEIKE-AANAANIHSfIEGLPEKyntqvglKGAQLSGGQKQRLAIARALLQKPKILLLDE 1181
Cdd:PRK11650 89 pHMSVRENMAYGLKIRGMPKAEIEErVAEAARILE-LEPLLDR-------KPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 1182 ATSALDndsEKV-VQHALD----KARTGRTCLVVTH-RLSAIQNADLIVVLHNGKIKEQGT 1236
Cdd:PRK11650 161 PLSNLD---AKLrVQMRLEiqrlHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
402-558 |
1.52e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.77 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 402 KILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALnvrHYRD-HIGVVSQEPVLF-GTTIS 479
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL---HARDrKVGFVFQHYALFrHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 480 NNIKYG---------------RDDVTDE-EMERAAREANAYdfimefPnkfntlvgekgAQMSGGQKQRIAIARALVRNP 543
Cdd:PRK10851 93 DNIAFGltvlprrerpnaaaiKAKVTQLlEMVQLAHLADRY------P-----------AQLSGGQKQRVALARALAVEP 155
|
170
....*....|....*
gi 255708477 544 KILILDEATSALDSE 558
Cdd:PRK10851 156 QILLLDEPFGALDAQ 170
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
712-950 |
1.86e-20 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 93.35 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 712 IFAKIITMFGNNDKTTLKHDAEIYSMIFVILGVICF--VSYFMQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDEkeN 789
Cdd:cd18573 18 AIGKLIDVASKESGDIEIFGLSLKTFALALLGVFVVgaAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDK--N 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 790 STGGLTTILAIDIAQIQGAtgsrigvLTQN------ATNMGL-SVIISFIYGWEMTFLILSIAPVLAVTGMIETAAMTGF 862
Cdd:cd18573 96 KTGELVSRLSSDTSVVGKS-------LTQNlsdglrSLVSGVgGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 863 ANKDKQELKHAGKIATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFAYAAGFRFGAY 942
Cdd:cd18573 169 SKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGS 248
|
....*...
gi 255708477 943 LIQAGRMT 950
Cdd:cd18573 249 LVASGELT 256
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
402-565 |
2.00e-20 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 91.45 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 402 KILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVrHYRDHIGV--VSQEPVLF-GTTI 478
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 479 SNNIKygrddVTDEEME--RAAREANAYDFIMEFpnKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALD 556
Cdd:cd03218 93 EENIL-----AVLEIRGlsKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
....*....
gi 255708477 557 SESKSAVQA 565
Cdd:cd03218 166 PIAVQDIQK 174
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
386-604 |
2.29e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 93.23 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPS--IKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDG---FIMVDENDIRAL----- 455
Cdd:PRK13651 3 IKVKNIVKIFNKKLPteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtieWIFKDEKNKKKTkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 456 ----------------NVRHYRDHIGVVSQ--EPVLFGTTISNNIKYGRDD--VTDEE-MERAAREANAYDFIMEFPNK- 513
Cdd:PRK13651 83 vleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSmgVSKEEaKKRAAKYIELVGLDESYLQRs 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 514 -FNtlvgekgaqMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASK-GRTTIVVAHRL-STIRSAD 590
Cdd:PRK13651 163 pFE---------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLdNVLEWTK 233
|
250
....*....|....
gi 255708477 591 LIVTLKDGMLAEKG 604
Cdd:PRK13651 234 RTIFFKDGKIIKDG 247
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
386-629 |
2.45e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.52 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPSIKilkGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRalNVRHYRDHIG 465
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLF-GTTISNNIKYG--RDDVTDEEMERAAREANAYDFIMEFPNKfntlvgeKGAQMSGGQKQRIAIARALVRN 542
Cdd:PRK11607 95 MMFQSYALFpHMTVEQNIAFGlkQDKLPKAEIASRVNEMLGLVHMQEFAKR-------KPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 543 PKILILDEATSALDSESKSAVQAA----LEKAskGRTTIVVAH----------RLSTIR--------------------- 587
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEvvdiLERV--GVTCVMVTHdqeeamtmagRIAIMNrgkfvqigepeeiyehpttry 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 255708477 588 SADLI--VTLKDGMLAEKGAHAELMAKRGLYYSLVMSQDIKKAD 629
Cdd:PRK11607 246 SAEFIgsVNVFEGVLKERQEDGLVIDSPGLVHPLKVDADASVVD 289
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1027-1255 |
2.85e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 91.68 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1027 RPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGvdakelNVQWLrsqIAI----VPQ---- 1098
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSAL---LELgagfHPEltgr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1099 EPVLFNCSIaeniaYGdnsrvVPLDEIKEAANA----ANIHSFIEgLPEKYntqvglkgaqLSGGQKQRLAIARALLQKP 1174
Cdd:COG1134 107 ENIYLNGRL-----LG-----LSRKEIDEKFDEivefAELGDFID-QPVKT----------YSSGMRARLAFAVATAVDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1175 KILLLDEATSALDND-SEKVVQHALDKARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLrnrDIYFKLVN 1252
Cdd:COG1134 166 DILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVI---AAYEALLA 242
|
...
gi 255708477 1253 AQS 1255
Cdd:COG1134 243 GRE 245
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
385-567 |
2.85e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 91.85 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFNYP-SRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHyrdh 463
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 iGVVSQEPVLFG-TTISNNIKYGrddVTDEEMERAAREANAYDFImefpnkfnTLVGEKGA------QMSGGQKQRIAIA 536
Cdd:COG4525 79 -GVVFQKDALLPwLNVLDNVAFG---LRLRGVPKAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVGIA 146
|
170 180 190
....*....|....*....|....*....|.
gi 255708477 537 RALVRNPKILILDEATSALDSESKSAVQAAL 567
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELL 177
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
386-583 |
2.96e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.07 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVS--FNYPSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVrHYR-D 462
Cdd:COG1101 2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRaK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEPVLfGT----TISNN--IKYGRDD-------VTDEEMERaAREANAyDFIMEFPNKFNTLVGekgaQMSGGQ 529
Cdd:COG1101 81 YIGRVFQDPMM-GTapsmTIEENlaLAYRRGKrrglrrgLTKKRREL-FRELLA-TLGLGLENRLDTKVG----LLSGGQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 530 KQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK--ASKGRTTIVVAHRL 583
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
386-598 |
3.26e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 90.42 E-value: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSrpsIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNvrhyRDHIG 465
Cdd:cd03269 1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLF-GTTISNNIKY-GR-DDVTDEEmerAAREANAYDFIMEFPNKFNtlvgEKGAQMSGGQKQRIAIARALVRN 542
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlAQlKGLKKEE---ARRRIDEWLERLELSEYAN----KRVEELSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 543 PKILILDEATSALDSESKSAV-QAALEKASKGRTTIVVAHRLSTI-RSADLIVTLKDG 598
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLkDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKG 204
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
389-610 |
3.45e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.76 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 389 KNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVS 468
Cdd:PRK13548 6 RNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 469 QEPVL-FGTTISNNIKYGR----------DDVTDEEMERAAREAnaydfimefpnkfntLVGEKGAQMSGGQKQRIAIAR 537
Cdd:PRK13548 83 QHSSLsFPFTVEEVVAMGRaphglsraedDALVAAALAQVDLAH---------------LAGRDYPQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 538 ALVR------NPKILILDEATSALD-SESKSAVQAALEKASK-GRTTIVVAHRLS-TIRSADLIVTLKDGMLAEKGAHAE 608
Cdd:PRK13548 148 VLAQlwepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAE 227
|
..
gi 255708477 609 LM 610
Cdd:PRK13548 228 VL 229
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
96-316 |
3.92e-20 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 92.15 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 96 QEKLNEDMTLLTLYYVGIGVAALIFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKIS 175
Cdd:cd18589 28 NKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 176 DGIGDKIALLFQNMSTFSIGLAVGLVKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRT 255
Cdd:cd18589 108 ESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKT 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 256 VIAFRAQEKELQRYTQNLKDAKDFGIKRTIASKVSLgavyfFMNGTYGLA-----FWYGTSLILNG 316
Cdd:cd18589 188 VRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSM-----WTSSFSGLAlkvgiLYYGGQLVTAG 248
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1035-1241 |
4.61e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.54 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1035 GLSLSIERGKTVAFVGSSGCGKS-TSVQLLQRLYDP----VQGQVLFDG---VDAKELNVQWLR-SQIAIVPQEP-VLFN 1104
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGeslLHASEQTLRGVRgNKIAMIFQEPmVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1105 csiaeniaygdnsrvvPLDEI---------------KEAANAaNIHSFIEglpekyntQVGLKGA---------QLSGGQ 1160
Cdd:PRK15134 107 ----------------PLHTLekqlyevlslhrgmrREAARG-EILNCLD--------RVGIRQAakrltdyphQLSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1161 KQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALD--KARTGRTCLVVTHRLSAI-QNADLIVVLHNGKIKEQGTH 1237
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRA 241
|
....
gi 255708477 1238 QELL 1241
Cdd:PRK15134 242 ATLF 245
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1032-1247 |
4.68e-20 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 90.68 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVqWLRSQIAI--VPQEPVLF-NCSIA 1108
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1109 ENIAYGDNSRVVPLDEIKEAANAAnIHSF-IEGLPEKyntqvglKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALD 1187
Cdd:cd03218 94 ENILAVLEIRGLSKKEREEKLEEL-LEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1188 ----NDSEKVVQHALDKartGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELLRN---RDIY 1247
Cdd:cd03218 166 piavQDIQKIIKILKDR---GIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANelvRKVY 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1015-1246 |
5.63e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.40 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYpcRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEP--VLFNCSIAENIAYGDNSrvVPLDE------IKEAANAANIHSFIEGLPEkyntqvglkgaQLSGGQKQRLAI 1166
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPIN--LGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1167 ARALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAI-QNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
...
gi 255708477 1244 RDI 1246
Cdd:PRK13652 229 PDL 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1015-1212 |
6.42e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.91 E-value: 6.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVdakelNVQWLRSQIA 1094
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQ-EPVLFNCSIAENIAYGDNSRVVPLDEIKEAANAANIhsfieglpekyntQVGLKGA------QLSGGQKQRLAIA 1167
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLK-------------KVGLEGAekryiwQLSGGQRQRVGIA 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255708477 1168 RALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTH 1212
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1001-1236 |
6.49e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 97.01 E-value: 6.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1001 RSQEGKKPDTCEGNLefreVSFFYPC-RPDVfilRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGV 1079
Cdd:TIGR01257 920 RELPGLVPGVCVKNL----VKIFEPSgRPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK 992
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1080 DAkELNVQWLRSQIAIVPQEPVLFN-CSIAENIAYGDNSRVVPLDEIKeaanaANIHSFIE--GLPEKYNTQvglkGAQL 1156
Cdd:TIGR01257 993 DI-ETNLDAVRQSLGMCPQHNILFHhLTVAEHILFYAQLKGRSWEEAQ-----LEMEAMLEdtGLHHKRNEE----AQDL 1062
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1157 SGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRL-SAIQNADLIVVLHNGKIKEQG 1235
Cdd:TIGR01257 1063 SGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMdEADLLGDRIAIISQGRLYCSG 1142
|
.
gi 255708477 1236 T 1236
Cdd:TIGR01257 1143 T 1143
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
402-604 |
7.31e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 89.12 E-value: 7.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 402 KILKGLNLRIKSGETVALVGLNGSGKSTvvqLLQRL-----YDPDDGFIMVDENDIRALNV-RHYRDHIGVVSQEPVLF- 474
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKST---LAKTImghpkYEVTEGEILFKGEDITDLPPeERARLGIFLAFQYPPEIp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 475 GTTISNNIKYgrddvtdeemeraareanaydfimefpnkfntlVGEKgaqMSGGQKQRIAIARALVRNPKILILDEATSA 554
Cdd:cd03217 91 GVKNADFLRY---------------------------------VNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255708477 555 LDSESKSAVQAALEK-ASKGRTTIVVAH--RLSTIRSADLIVTLKDGMLAEKG 604
Cdd:cd03217 135 LDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
404-604 |
7.90e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 89.83 E-value: 7.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 404 LKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNvrhyRDHIGVVSQEPVLFGTTISNNIK 483
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG----PDRMVVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 484 YGRDDVTdEEMERAAREANAYDFImefpnkfnTLVG------EKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDS 557
Cdd:TIGR01184 77 LAVDRVL-PDLSKSERRAIVEEHI--------ALVGlteaadKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 255708477 558 ESKSAVQAALEKASK--GRTTIVVAHRL-STIRSADLIVTLKDGMLAEKG 604
Cdd:TIGR01184 148 LTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1015-1245 |
8.74e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.59 E-value: 8.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFfypCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWL---RS 1091
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1092 QIAIVPQEPVLF-NCSIAENIAYgdnsrvvPLDEiKEAANAANIHSFIEGLPEKyntqVGLKGA------QLSGGQKQRL 1164
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAY-------PLRE-HTQLPAPLLHSTVMMKLEA----VGLRGAaklmpsELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1165 AIARALLQKPKILLLDEATSALDNDSEKV-------VQHALdkartGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGT 1236
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVlvkliseLNSAL-----GVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGS 227
|
....*....
gi 255708477 1237 HQELLRNRD 1245
Cdd:PRK11831 228 AQALQANPD 236
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1015-1254 |
9.14e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 90.67 E-value: 9.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCR------PDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQW 1088
Cdd:COG4167 5 LEVRNLSKTFKYRtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1089 lRSQ-IAIVPQEPvlfncsiaeNIAYgdNSRVvpldeikeaanaaNIHSFIEGlPEKYNT----------------QVGL 1151
Cdd:COG4167 85 -RCKhIRMIFQDP---------NTSL--NPRL-------------NIGQILEE-PLRLNTdltaeereerifatlrLVGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1152 KGAQ-------LSGGQKQRLAIARALLQKPKILLLDEATSALDND-SEKVVQHALD-KARTGRTCLVVTHRLSAIQN-AD 1221
Cdd:COG4167 139 LPEHanfyphmLSSGQKQRVALARALILQPKIIIADEALAALDMSvRSQIINLMLElQEKLGISYIYVSQHLGIVKHiSD 218
|
250 260 270
....*....|....*....|....*....|....*
gi 255708477 1222 LIVVLHNGKIKEQGTHQELLRN--RDIYFKLVNAQ 1254
Cdd:COG4167 219 KVLVMHQGEVVEYGKTAEVFANpqHEVTKRLIESH 253
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
403-552 |
1.13e-19 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 89.51 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 403 ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVrHYRDH--IGVVSQEPVLFGT-TIS 479
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPP-HERARagIAYVPQGREIFPRlTVE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 480 NNIKYGrddvtdeeME-RAAREANAYDFIME-FPNKFNTLvGEKGAQMSGGQKQRIAIARALVRNPKILILDEAT 552
Cdd:TIGR03410 94 ENLLTG--------LAaLPRRSRKIPDEIYElFPVLKEML-GRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1021-1235 |
1.38e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 89.31 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1021 SFFYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRsQIAIV--PQ 1098
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1099 EPVLFNCSIAENIAYgdNSRVVPLDEIKEAANAANIHSFIEgLPEKYNTQVglkgAQLSGGQKQRLAIARALLQKPKILL 1178
Cdd:cd03267 104 TQLWWDLPVIDSFYL--LAAIYDLPPARFKKRLDELSELLD-LEELLDTPV----RQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1179 LDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQG 1235
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEynRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1032-1229 |
1.61e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 88.86 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDgvdakelnvqwlrsqiaiVPQEPVLFNCSIAENI 1111
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQFGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1112 AygdnsRVVPLDEIKEAANAAnihsfieGLPEKYNTQVglKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSE 1191
Cdd:COG2401 107 G-----RKGDFKDAVELLNAV-------GLSDAVLWLR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255708477 1192 KVVQHALDKA--RTGRTCLVVTHR---LSAIQnADLIVVLHNG 1229
Cdd:COG2401 173 KRVARNLQKLarRAGITLVVATHHydvIDDLQ-PDLLIFVGYG 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1015-1245 |
1.78e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.18 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFY-PCRPdvFILRGL---SLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGV----DAKELNV 1086
Cdd:PRK13643 2 IKFEKVNYTYqPNSP--FASRALfdiDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvssTSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1087 QWLRSQIAIVPQEP--VLFNCSIAENIAYGDNSRVVPLDEIKEAAnAANIHsfIEGLPEKYNTQVGLkgaQLSGGQKQRL 1164
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIA-AEKLE--MVGLADEFWEKSPF---ELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1165 AIARALLQKPKILLLDEATSALDNDSEKVVQHALDKA-RTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLR 1242
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
...
gi 255708477 1243 NRD 1245
Cdd:PRK13643 234 EVD 236
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
390-624 |
1.81e-19 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 90.30 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 390 NVSFNYPSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFImvdendiralnvRHyRDHIGVVSQ 469
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------------KH-SGRISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 470 EPVLFGTTISNNIKYGrddVT-DEEMERAAREA-NAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILI 547
Cdd:cd03291 106 FSWIMPGTIKENIIFG---VSyDEYRYKSVVKAcQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 548 LDEATSALD-SESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSLVMSQD 624
Cdd:cd03291 183 LDSPFGYLDvFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYD 260
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1015-1231 |
2.43e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.02 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPC-RPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWL---- 1089
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1090 RSQIAIVPQE-PVLFNCSIAENI----AYGDNSRvvplDEIKEAANAANIHSfieGLPEKyntqVGLKGAQLSGGQKQRL 1164
Cdd:PRK10535 85 REHFGFIFQRyHLLSHLTAAQNVevpaVYAGLER----KQRLLRAQELLQRL---GLEDR----VEYQPSQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1165 AIARALLQKPKILLLDEATSALDNDSEKVVQHALDKAR-TGRTCLVVTHRLSAIQNADLIVVLHNGKI 1231
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
389-598 |
2.53e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.97 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 389 KNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGfimvdenDIRALN--VRHYRDHIGV 466
Cdd:PRK11247 16 NAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-------ELLAGTapLAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 467 VSQEPVLFG-TTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPnkfntlvgekgAQMSGGQKQRIAIARALVRNPKI 545
Cdd:PRK11247 86 MFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 546 LILDEATSALDSESKSAVQAALEK--ASKGRTTIVVAHRLS-TIRSADLIVTLKDG 598
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEG 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1029-1241 |
2.67e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.30 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1029 DVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDG--VDAKELNVQWLRSQIAIVPQEP--VLFN 1104
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPeqQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1105 CSIAENIAYGDNSRVVPLDEIKEAANAAnihsfieglpekyntqVGLKGAQ---------LSGGQKQRLAIARALLQKPK 1175
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAEITRRVDEA----------------LTLVDAQhfrhqpiqcLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1176 ILLLDEATSALDNDSEKVVQHALDK-ARTGRTCLVVTHRLSAI-QNADLIVVLHNGKIKEQGTHQELL 1241
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1015-1233 |
4.94e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFdGVdakelNVQwlrsqIA 1094
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLFNcsiaeniayGDNSrvvPLDEIKEAANAAN---IHSFIEGL---PEKYNTQVGlkgaQLSGGQKQRLAIAR 1168
Cdd:COG0488 382 YFDQHQEELD---------PDKT---VLDELRDGAPGGTeqeVRGYLGRFlfsGDDAFKPVG----VLSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1169 ALLQKPKILLLDEATSALDNDSEKVVQHALDkARTGrTCLVVTH-R--LSAIqnADLIVVLHNGKIKE 1233
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
718-967 |
5.83e-19 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 88.69 E-value: 5.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 718 TMFGNNDKTTLKHDAEIYSMIFVILGVIcfvSYFMQGLFyGRAGEILTMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTI 797
Cdd:cd18576 25 AALGGGDTASLNQIALLLLGLFLLQAVF---SFFRIYLF-ARVGERVVADLRKDLYRHLQRLPLSFFHE--RRVGELTSR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 798 LAIDIAQIQGA-TGSRIGVLTQNATNMGlSVIISFIYGWEMTFLILSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKI 876
Cdd:cd18576 99 LSNDVTQIQDTlTTTLAEFLRQILTLIG-GVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 877 ATEALENIRTIVSLTREkAFE-QMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRMTPEG-- 953
Cdd:cd18576 178 VEETLQGIRVVKAFTRE-DYEiERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDlv 256
|
250
....*....|....
gi 255708477 954 MFIVFTAIAYGAMA 967
Cdd:cd18576 257 AFLLYTLFIAGSIG 270
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
386-609 |
6.04e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.09 E-value: 6.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSrpsIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDenDIRALNVRHYRDHIG 465
Cdd:PRK11000 4 VTLRNVTKAYGD---VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--EKRMNDVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLF-GTTISNNIKYGRDDVTDEEMERAAREANAYDFImefpnKFNTLVGEKGAQMSGGQKQRIAIARALVRNPK 544
Cdd:PRK11000 79 MVFQSYALYpHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVL-----QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 545 ILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAH-RLSTIRSADLIVTLKDGMLAEKGAHAEL 609
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
385-556 |
6.46e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.64 E-value: 6.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVR-HYRDH 463
Cdd:PRK10895 3 TLTAKNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 IGVVSQEPVLFGT-TISNNIKYG---RDDVTDEEmeraaREANAYDFIMEFpnKFNTLVGEKGAQMSGGQKQRIAIARAL 539
Cdd:PRK10895 80 IGYLPQEASIFRRlSVYDNLMAVlqiRDDLSAEQ-----REDRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARAL 152
|
170
....*....|....*..
gi 255708477 540 VRNPKILILDEATSALD 556
Cdd:PRK10895 153 AANPKFILLDEPFAGVD 169
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
48-327 |
6.93e-19 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 88.61 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 48 MILGILASLVNGACLPLMPLVLGEMSDNLISGcLVQTNTTNYQNctqsqeklnedMTLLTLYYVGIGVAALIFGYIQiSL 127
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEG-LGGGGGVDFSG-----------LLRILLLLLGLYLLSALFSYLQ-NR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 128 WIITAARQT-KRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGWKL 206
Cdd:cd18547 68 LMARVSQRTvYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 207 TLVTLSTSPLIMasaaACSRMVISLTSKELSAYSKA-GAV---AEEVLSSIRTVIAFRAQEKELQR---YTQNLKDAkdf 279
Cdd:cd18547 148 TLIVLVTVPLSL----LVTKFIAKRSQKYFRKQQKAlGELngyIEEMISGQKVVKAFNREEEAIEEfdeINEELYKA--- 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 255708477 280 GIKRTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGepGYTIGTVLA 327
Cdd:cd18547 221 SFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVING--ALTVGVIQA 266
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
399-598 |
7.39e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 91.53 E-value: 7.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 399 PSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYdPD---DGFIMVDENDIRALNVRHY-RDHIGVVSQEPVLF 474
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 475 -GTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFpnKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATS 553
Cdd:PRK13549 95 kELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 255708477 554 ALdSESKSAVQAALEK--ASKGRTTIVVAHRLSTIRS-ADLIVTLKDG 598
Cdd:PRK13549 173 SL-TESETAVLLDIIRdlKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1013-1250 |
7.69e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.53 E-value: 7.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1013 GNLEFREVSFFYpCRPDVFILRGL---SLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDG----VDAKELN 1085
Cdd:PRK13645 5 KDIILDNVSYTY-AKKTPFEFKALnntSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1086 -VQWLRSQIAIVPQEP--VLFNCSIAENIAYGDnsrvVPLDEIKEAAnAANIHSFIE--GLPEKYNTQVGLkgaQLSGGQ 1160
Cdd:PRK13645 84 eVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGP----VNLGENKQEA-YKKVPELLKlvQLPEDYVKRSPF---ELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1161 KQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAI-QNADLIVVLHNGKIKEQGTH 1237
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSP 235
|
250
....*....|...
gi 255708477 1238 QELLRNRDIYFKL 1250
Cdd:PRK13645 236 FEIFSNQELLTKI 248
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
49-317 |
7.92e-19 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 88.62 E-value: 7.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 49 ILGILASLVNGACLPLMPLVLGEMSDNLISGCLVQTNTTNYqnctqsqeklnedmtllTLYYVGIGVAALIFGYIQiSLW 128
Cdd:cd18541 2 LLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRY-----------------ALLILLLALLIGIFRFLW-RYL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 129 IITAARQ-TKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGWKLT 207
Cdd:cd18541 64 IFGASRRiEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 208 LVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTIAS 287
Cdd:cd18541 144 LIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVD 223
|
250 260 270
....*....|....*....|....*....|
gi 255708477 288 KVSLGAVYFFMNGTYGLAFWYGTSLILNGE 317
Cdd:cd18541 224 ALFFPLIGLLIGLSFLIVLWYGGRLVIRGT 253
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
101-550 |
8.48e-19 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 91.78 E-value: 8.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 101 EDMTLLTLYYVGIGVAALIFGYIqiSLWIITAARQ--TKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGI 178
Cdd:COG4615 45 AALARLLLLFAGLLVLLLLSRLA--SQLLLTRLGQhaVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 179 GDkIALLFQNMSTFSIGLAVGLVKGWKLTLVTLstspLIMASAAACSRMVISLTSKELSaysKAGAVAEEVLSSIRTVI- 257
Cdd:COG4615 123 VR-LPELLQSVALVLGCLAYLAWLSPPLFLLTL----VLLGLGVAGYRLLVRRARRHLR---RAREAEDRLFKHFRALLe 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 258 --------AFRAQ---EKELQRYTQNLKDAKDFGIkRTIASKVSLGAVYFFmnGTYGLAFWYGTSLiLNGEPGYTIGTVL 326
Cdd:COG4615 195 gfkelklnRRRRRaffDEDLQPTAERYRDLRIRAD-TIFALANNWGNLLFF--ALIGLILFLLPAL-GWADPAVLSGFVL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 327 AVFFSVIHSSYCIGAaVPhfeTFAIARGAAFHIFQVIDKKPSIDNFSTAGYKPESIEG--TVEFKNVSFNYPSRPSIK-- 402
Cdd:COG4615 271 VLLFLRGPLSQLVGA-LP---TLSRANVALRKIEELELALAAAEPAAADAAAPPAPADfqTLELRGVTYRYPGEDGDEgf 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 403 ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTisnni 482
Cdd:COG4615 347 TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL----- 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 483 kYGRDDVTDEEmeraarEANAYDFIMEFPNK-------FNTLvgekgaQMSGGQKQRIAIARALVRNPKILILDE 550
Cdd:COG4615 422 -LGLDGEADPA------RARELLERLELDHKvsvedgrFSTT------DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1007-1242 |
9.91e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 87.54 E-value: 9.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1007 KPDTCEGNLEFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNV 1086
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1087 QWLRSQIAIVPQE-PVLFNCSIAENIAYGDNSRVVPLDEIKeAANAANIHSFIeglpekynTQVGLKG-AQ-----LSGG 1159
Cdd:PRK10575 81 KAFARKVAYLPQQlPAAEGMTVRELVAIGRYPWHGALGRFG-AADREKVEEAI--------SLVGLKPlAHrlvdsLSGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1160 QKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQ---HALDKARtGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQG 1235
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLalvHRLSQER-GLTVIAVLHDINmAARYCDYLVALRGGEMIAQG 230
|
....*..
gi 255708477 1236 THQELLR 1242
Cdd:PRK10575 231 TPAELMR 237
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
386-582 |
1.00e-18 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 84.51 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSrpSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFImvdendiralnVRHYRDHIG 465
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLFGTTIsnnikygrddvtdeemeraaREANAYDFIMEFpnkfntlvgekgaqmSGGQKQRIAIARALVRNPKI 545
Cdd:cd03223 68 FLPQRPYLPLGTL--------------------REQLIYPWDDVL---------------SGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 255708477 546 LILDEATSALDSESKSAVQAALEKASkgrTTIV-VAHR 582
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELG---ITVIsVGHR 147
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
401-602 |
1.07e-18 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 87.40 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 401 IKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAL------------------------- 455
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLpphriarlgiartfqnprlfpeltv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 456 --NVRhyrdhIGVVSQEPVLFGTTISNNIKYGRDDvtdEEMERAAREanaydfIMEFPN---KFNTLVGEkgaqMSGGQK 530
Cdd:COG0411 97 leNVL-----VAAHARLGRGLLAALLRLPRARREE---REARERAEE------LLERVGladRADEPAGN----LSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 531 QRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK--ASKGRTTIVVAHRLSTIRS-ADLIVTLKDG-MLAE 602
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRlrDERGITILLIEHDMDLVMGlADRIVVLDFGrVIAE 234
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
677-1233 |
1.29e-18 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 91.01 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 677 SLLKILKlnKPEWPFVVLGTLASVLNGtvhpVFSIIFAKIITmfgnndkTTLKHDAEIYSMIFVILGVICFVSYFMQglf 756
Cdd:COG4615 2 NLLRLLL--RESRWLLLLALLLGLLSG----LANAGLIALIN-------QALNATGAALARLLLLFAGLLVLLLLSR--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 757 ygRAGEILTMRLRHlAFKAMLYQDIAWfdekenstggltTILAIDIAQIQGATGSRI-GVLTQNATN------------- 822
Cdd:COG4615 66 --LASQLLLTRLGQ-HAVARLRLRLSR------------RILAAPLERLERIGAARLlAALTEDVRTisqafvrlpellq 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 823 MGLSVIISFIYgweMTFLILSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKIATEALENIRTIVS------LTREKAf 896
Cdd:COG4615 131 SVALVLGCLAY---LAWLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEgfkelkLNRRRR- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 897 EQMYEEMLQ---TQHRNTSKKAQII-GSCYAFSHAFIYFAYAAGFrFGAYLIQAgrMTPEGMFIVFTAIAYGAMAIGETL 972
Cdd:COG4615 207 RAFFDEDLQptaERYRDLRIRADTIfALANNWGNLLFFALIGLIL-FLLPALGW--ADPAVLSGFVLVLLFLRGPLSQLV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 973 VLAPEYSKAKSGAAHLFALLEKKPNIDSRSQEGKKPDTCEG--NLEFREVSFFYPCRPD--VFILRGLSLSIERGKTVAF 1048
Cdd:COG4615 284 GALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADfqTLELRGVTYRYPGEDGdeGFTLGPIDLTIRRGELVFI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1049 VGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNcsiaeniaygdnsRVVPLDeikEA 1128
Cdd:COG4615 364 VGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD-------------RLLGLD---GE 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1129 ANAANIHSFIEGLpeKYNTQVGLKGA-----QLSGGQKQRLAIARALL-QKPkILLLDEAtsALDNDSE------KVVQH 1196
Cdd:COG4615 428 ADPARARELLERL--ELDHKVSVEDGrfsttDLSQGQRKRLALLVALLeDRP-ILVFDEW--AADQDPEfrrvfyTELLP 502
|
570 580 590
....*....|....*....|....*....|....*..
gi 255708477 1197 ALdKARtGRTCLVVTHRLSAIQNADLIVVLHNGKIKE 1233
Cdd:COG4615 503 EL-KAR-GKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
386-615 |
1.48e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.17 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYpsRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIG 465
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEP--VLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFImefpnKFNTLVGEKGAQMSGGQKQRIAIARALVRNP 543
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 544 KILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAELMAKRGL 615
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
403-604 |
1.74e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 86.43 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 403 ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDgfIMVDENDIRALNVRHY---------RDHIGVVSQEPVL 473
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNE--EARVEGEVRLFGRNIYspdvdpievRREVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 474 F-GTTISNNIKYG--------RDDVTDEEMERAAREANAYDfimEFPNKFNtlvgEKGAQMSGGQKQRIAIARALVRNPK 544
Cdd:PRK14267 97 FpHLTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWD---EVKDRLN----DYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 545 ILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHR-LSTIRSADLIVTLKDGMLAEKG 604
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
379-604 |
1.86e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.53 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 379 PESIEGTVEFKNVSFNYPSRPSIK--------ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYdPDDGFIMVDEN 450
Cdd:PRK15134 269 PEPASPLLDVEQLQVAFPIRKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 451 DIRALNVRH---YRDHIGVVSQEP---------VLfgTTISNNIKygrddVTDEEMERAAREANAYDFIME--------- 509
Cdd:PRK15134 348 PLHNLNRRQllpVRHRIQVVFQDPnsslnprlnVL--QIIEEGLR-----VHQPTLSAAQREQQVIAVMEEvgldpetrh 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 510 -FPNKFntlvgekgaqmSGGQKQRIAIARALVRNPKILILDEATSALDseskSAVQA---ALEKASKGR---TTIVVAHR 582
Cdd:PRK15134 421 rYPAEF-----------SGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHD 485
|
250 260
....*....|....*....|...
gi 255708477 583 LSTIRS-ADLIVTLKDGMLAEKG 604
Cdd:PRK15134 486 LHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
695-950 |
2.14e-18 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 87.31 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 695 GTLASVLNGTVHPVFSIIFAKIITMFGNNDKTTLKHD-AEIYSMIFVILGVICF--VSYFMQGLFYGRAGEILTMRLRHL 771
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEAlRALNQAVLILLGVVLIgsIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 772 AFKAMLYQDIAWFDekENSTGGLTTILAIDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGWEMTFLILSIAPVLAVT 851
Cdd:cd18780 81 LFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 852 GMIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYF 931
Cdd:cd18780 159 AVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQL 238
|
250
....*....|....*....
gi 255708477 932 AYAAGFRFGAYLIQAGRMT 950
Cdd:cd18780 239 AIVLVLWYGGRLVIDGELT 257
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1033-1231 |
2.93e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.93 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELN---VQWLRSQIAIVPQEP-VLFNCSIA 1108
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1109 ENIAygdnsrvVPLdeIKEAANAANIHSFIEGLPEKyntqVGLKGA------QLSGGQKQRLAIARALLQKPKILLLDEA 1182
Cdd:PRK10908 98 DNVA-------IPL--IIAGASGDDIRRRVSAALDK----VGLLDKaknfpiQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255708477 1183 TSALDND-SEKVVQHALDKARTGRTCLVVTHRLSAIQNADL-IVVLHNGKI 1231
Cdd:PRK10908 165 TGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHL 215
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
393-615 |
3.12e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.21 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 393 FNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDEN--DIRALNVRHYRDHIGVVSQE 470
Cdd:PRK13638 9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 471 P--VLFGTTISNNIKYGRDDVTDEEMERAAREANAYdfimefpnkfnTLVGEKGAQ------MSGGQKQRIAIARALVRN 542
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEAL-----------TLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 543 PKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKG------AHAELMAKRG 614
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGapgevfACTEAMEQAG 234
|
.
gi 255708477 615 L 615
Cdd:PRK13638 235 L 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
408-611 |
4.53e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 84.63 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 408 NLRIKSGETVALVGLNGSGKSTVVQLLQrlydpddGFIMVDENDIRALNVRHYRDHIgvvSQEPV--------LFG-TTI 478
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIA-------GFLTPASGSLTLNGQDHTTTPP---SRRPVsmlfqennLFShLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 479 SNNIKYGRD------DVTDEEMERAAREANAYDFIMEFPnkfntlvgekgAQMSGGQKQRIAIARALVRNPKILILDEAT 552
Cdd:PRK10771 89 AQNIGLGLNpglklnAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 553 SALDSESKSAVQAALEKASKGR--TTIVVAHRLS-TIRSADLIVTLKDGMLAEKGAHAELMA 611
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
387-556 |
4.89e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.07 E-value: 4.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPD---DGFIMVDENDIRALNVrhYRDH 463
Cdd:COG4136 3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA--EQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 IGVVSQEPVLFG-TTISNNIKYGrddvTDEEMERAAREANAYDFIMEfpnkfntlVGEKG------AQMSGGQKQRIAIA 536
Cdd:COG4136 78 IGILFQDDLLFPhLSVGENLAFA----LPPTIGRAQRRARVEQALEE--------AGLAGfadrdpATLSGGQRARVALL 145
|
170 180
....*....|....*....|
gi 255708477 537 RALVRNPKILILDEATSALD 556
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLD 165
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1032-1215 |
5.28e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.48 E-value: 5.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQW---LRSQ-IAIVPQ-EPVLFNCS 1106
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1107 IAENIAygdnsrvVPL-------DEIKEAAnaanihsfIEGLpekynTQVGL------KGAQLSGGQKQRLAIARALLQK 1173
Cdd:PRK11629 104 ALENVA-------MPLligkkkpAEINSRA--------LEML-----AAVGLehranhRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 255708477 1174 PKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLS 1215
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
401-612 |
8.90e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 86.17 E-value: 8.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 401 IKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDG--FI---------------------MVDENDIRALNV 457
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGelYYqgqdllkadpeaqkllrqkiqIVFQNPYGSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 458 RHyrdHIGVVSQEPVLFGTTISnniKYGRDDVTDEEMERAAREANAYDfimEFPNKFntlvgekgaqmSGGQKQRIAIAR 537
Cdd:PRK11308 108 RK---KVGQILEEPLLINTSLS---AAERREKALAMMAKVGLRPEHYD---RYPHMF-----------SGGQRQRIAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 538 ALVRNPKILILDEATSALDseskSAVQAA-------LEKaSKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAEL 609
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALD----VSVQAQvlnlmmdLQQ-ELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
...
gi 255708477 610 MAK 612
Cdd:PRK11308 243 FNN 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
403-611 |
1.09e-17 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 88.20 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 403 ILKGLNLRIKSGETVALVGLNGSGKS----TVVQLLQRLYDPDDGFIMVDENDIRALN---VRHYR-DHIGVVSQEPV-- 472
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSereLRRIRgNRIAMIFQEPMts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 473 ---LFgtTISNNI--------KYGRDDVTDEEME--------RAAREANAYDFimefpnkfntlvgekgaQMSGGQKQRI 533
Cdd:COG4172 105 lnpLH--TIGKQIaevlrlhrGLSGAAARARALEllervgipDPERRLDAYPH-----------------QLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 534 AIARALVRNPKILILDEATSALDseskSAVQAA-LE-----KASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAH 606
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALD----VTVQAQiLDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPT 241
|
....*
gi 255708477 607 AELMA 611
Cdd:COG4172 242 AELFA 246
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
386-604 |
1.31e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 83.35 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPS-------------------RPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIM 446
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 447 VDENdiralnvrhyrdhigVVSqePVLFGTTISNNIKyGRDDV---------TDEEMERaareanAYDFIMEF---PNKF 514
Cdd:cd03220 81 VRGR---------------VSS--LLGLGGGFNPELT-GRENIylngrllglSRKEIDE------KIDEIIEFselGDFI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 515 NTLVGEkgaqMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL-EKASKGRTTIVVAHRLSTIRS-ADLI 592
Cdd:cd03220 137 DLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRlCDRA 212
|
250
....*....|..
gi 255708477 593 VTLKDGMLAEKG 604
Cdd:cd03220 213 LVLEKGKIRFDG 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1033-1231 |
1.47e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 81.71 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNV-QWLRSQIAIVPQEP----VLFNCSI 1107
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1108 AENIAYGdnsrvvpldeikeaanaanihsfieglpekyntqvglkgAQLSGGQKQRLAIARALLQKPKILLLDEATSALD 1187
Cdd:cd03215 96 AENIALS---------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 255708477 1188 NDS-EKVVQHALDKARTGRTCLVVTHRLS-AIQNADLIVVLHNGKI 1231
Cdd:cd03215 137 VGAkAEIYRLIRELADAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1033-1230 |
1.53e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.39 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGV--------DAkelnvqwLRSQIAIVPQEPVLF- 1103
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprDA-------IALGIGMVHQHFMLVp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1104 NCSIAENIAYGDNSRVVPLDEIKEAANAanihsfIEGLPEKYNTQVGL--KGAQLSGGQKQRLAIARALLQKPKILLLDE 1181
Cdd:COG3845 94 NLTVAENIVLGLEPTKGGRLDRKAARAR------IRELSERYGLDVDPdaKVEDLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 255708477 1182 ATSAL-DNDSEKVVQhALDK-ARTGRTCLVVTHRLS-AIQNADLIVVLHNGK 1230
Cdd:COG3845 168 PTAVLtPQEADELFE-ILRRlAAEGKSIIFITHKLReVMAIADRVTVLRRGK 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
400-587 |
1.63e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.14 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 400 SIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN---VRHYRDHIGVVSQEPV---- 472
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDPLasln 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 473 ---LFGTTISNNI-----KYGRDDVTDEEMERAAREANAYDFIMEFPNKFntlvgekgaqmSGGQKQRIAIARALVRNPK 544
Cdd:PRK15079 113 prmTIGEIIAEPLrtyhpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 255708477 545 ILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTIR 587
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVK 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1015-1230 |
1.79e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 80.19 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVdakelnvqwlrsqia 1094
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 ivpqepvlfncsiaENIAYgdnsrvvpldeikeaanaanihsFieglpekyntqvglkgAQLSGGQKQRLAIARALLQKP 1174
Cdd:cd03221 63 --------------VKIGY-----------------------F----------------EQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 1175 KILLLDEATSALDNDSEKVVQHALDKarTGRTCLVVTHRLSAIQN-ADLIVVLHNGK 1230
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEALKE--YPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
52-317 |
2.16e-17 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 84.13 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 52 ILASLVNgaclPLMPLVLGEMSdNLISGCLVQTNTTNYQNctqsqekLNEDMTLLTLYYVGigVAALIFGYIqiSLWIIT 131
Cdd:cd18574 6 LAAALVN----IQIPLLLGDLV-NVISRSLKETNGDFIED-------LKKPALKLLGLYLL--QSLLTFAYI--SLLSVV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 132 AARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDK--------ISDGIgdkiallfQNMsTFSIGLAVGLVK- 202
Cdd:cd18574 70 GERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEfkssfkqcVSQGL--------RSV-TQTVGCVVSLYLi 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 203 GWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAkdfgik 282
Cdd:cd18574 141 SPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKA------ 214
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 255708477 283 RTIASKVSLG-AVY-----FFMNGTYGLAFWYGTSLILNGE 317
Cdd:cd18574 215 AKLNEKLGLGiGIFqglsnLALNGIVLGVLYYGGSLVSRGE 255
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
385-581 |
2.63e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 82.32 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFNYPS-RPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDD---GFIMVDEndiRALNVRHY 460
Cdd:cd03234 3 VLPWWDVGLKAKNwNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNG---QPRKPDQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 461 RDHIGVVSQEPVLF-GTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNkfNTLVG-EKGAQMSGGQKQRIAIARA 538
Cdd:cd03234 80 QKCVAYVRQDDILLpGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLA--LTRIGgNLVKGISGGERRRVSIAVQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 255708477 539 LVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAH 581
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIH 201
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
386-611 |
2.74e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.09 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDI--RAlnvRHYRDH 463
Cdd:PRK13537 8 IDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpsRA---RHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 IGVVSQ----EPVLfgTTISNNIKYGRDDVTDEEMERAAREAnaydfIMEFP---NKFNTLVGEkgaqMSGGQKQRIAIA 536
Cdd:PRK13537 82 VGVVPQfdnlDPDF--TVRENLLVFGRYFGLSAAAARALVPP-----LLEFAkleNKADAKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 537 RALVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKGAHAELMA 611
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
386-604 |
3.27e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.44 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYP----SRPSIK---------------ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIM 446
Cdd:COG1134 5 IEVENVSKSYRlyhePSRSLKelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 447 VDENdIRAL---------------NVRhyrdHIGVVsqepvlfgttisnnikYGrddVTDEEMERaareanAYDFIMEF- 510
Cdd:COG1134 85 VNGR-VSALlelgagfhpeltgreNIY----LNGRL----------------LG---LSRKEIDE------KFDEIVEFa 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 511 --PNKFNTLVGekgaQMSGGQKQRIAIARALVRNPKILILDEATSALDSE-SKSAVQAALEKASKGRTTIVVAHRLSTIR 587
Cdd:COG1134 135 elGDFIDQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVR 210
|
250
....*....|....*...
gi 255708477 588 S-ADLIVTLKDGMLAEKG 604
Cdd:COG1134 211 RlCDRAIWLEKGRLVMDG 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1028-1230 |
3.64e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.14 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1028 PDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYdPV---QGQVLFDGvdaKELNVQWLR----SQIAIVPQEP 1100
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEG---EELQASNIRdterAGIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1101 VLF-NCSIAENIAYGdnSRVVPLDEIKEAANAANIHSFIEGLpeKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLL 1179
Cdd:PRK13549 92 ALVkELSVLENIFLG--NEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 1180 DEATSALdndSEKVVQHALD-----KARtGRTCLVVTHRLSAIQN-ADLIVVLHNGK 1230
Cdd:PRK13549 168 DEPTASL---TESETAVLLDiirdlKAH-GIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
389-550 |
3.83e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.38 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 389 KNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKST----VVQLLQrlydPDDGFIMVDENDIRALNVrHYRDH- 463
Cdd:COG1137 7 ENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDITHLPM-HKRARl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 464 -IGVVSQEPVLF-GTTISNNIK-----YGRDdvtdeemeRAAREANAYDFIMEFpnKFNTLVGEKGAQMSGGQKQRIAIA 536
Cdd:COG1137 79 gIGYLPQEASIFrKLTVEDNILavlelRKLS--------KKEREERLEELLEEF--GITHLRKSKAYSLSGGERRRVEIA 148
|
170
....*....|....
gi 255708477 537 RALVRNPKILILDE 550
Cdd:COG1137 149 RALATNPKFILLDE 162
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
404-598 |
4.18e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 80.55 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 404 LKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDH-IGVVSQEPVLFGttisnni 482
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKREG------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 483 kygrddvtdeemeraareanaydFIMEFPNKFNTLVGekgAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSA 562
Cdd:cd03215 89 -----------------------LVLDLSVAENIALS---SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 255708477 563 VQAAL-EKASKGRTTIVVAHRLSTIRS-ADLIVTLKDG 598
Cdd:cd03215 143 IYRLIrELADAGKAVLLISSELDELLGlCDRILVMYEG 180
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1028-1243 |
4.68e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.44 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1028 PDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDP----VQGQVLFDGvdaKELNVQWLRSQ-IAIVPQEP-V 1101
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDG---KPVAPCALRGRkIATIMQNPrS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1102 LFNcsIAENIAygDNSRVVPLDEIKEAANAANIHSFIE-GLPEKyNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLD 1180
Cdd:PRK10418 91 AFN--PLHTMH--THARETCLALGKPADDATLTAALEAvGLENA-ARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1181 EATSALDndseKVVQ-HALD-----KARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:PRK10418 166 EPTTDLD----VVAQaRILDllesiVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1032-1241 |
5.56e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.84 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQG-----QVLFDGVDA-KELNVQWLRSQIAIVPQEPVLFNC 1105
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1106 SIAENIAYGDNS-RVVPLDEIKEAANAANIHSfieGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATS 1184
Cdd:PRK14271 116 SIMDNVLAGVRAhKLVPRKEFRGVAQARLTEV---GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1185 ALDNDSEKVVQHALDKARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELL 1241
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
386-611 |
7.33e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 85.24 E-value: 7.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPS--RPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFI-------MVDENDIRALN 456
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 457 VRHYRDHIGVVSQEPVLF--GTTISNNIKYGRDDVTDEEMERAA---------REANAYDFIMEFPNkfntlvgekgaQM 525
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYphRTVLDNLTEAIGLELPDELARMKAvitlkmvgfDEEKAEEILDKYPD-----------EL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 526 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTIRS-ADLIVTLKDGMLAE 602
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVK 508
|
....*....
gi 255708477 603 KGAHAELMA 611
Cdd:TIGR03269 509 IGDPEEIVE 517
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
390-581 |
7.35e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 81.67 E-value: 7.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 390 NVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHyrdhiGVVSQ 469
Cdd:PRK11248 6 HLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 470 -EPVLFGTTISNNIKYGrddVTDEEMERAAREANAYDFImefpnkfnTLVGEKGA------QMSGGQKQRIAIARALVRN 542
Cdd:PRK11248 78 nEGLLPWRNVQDNVAFG---LQLAGVEKMQRLEIAHQML--------KKVGLEGAekryiwQLSGGQRQRVGIARALAAN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 255708477 543 PKILILDEATSALDSESKSAVQAALEK--ASKGRTTIVVAH 581
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1033-1243 |
7.86e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.21 E-value: 7.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRsQIAIV------------PQEP 1100
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrsqlwwdlpAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1101 VLFNCSIaeniaYGdnsrvVPLDEIKEaanaaNIHSFIE--GLPEKYNTQVglkgAQLSGGQKQRLAIARALLQKPKILL 1178
Cdd:COG4586 117 FRLLKAI-----YR-----IPDAEYKK-----RLDELVEllDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1179 LDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
378-578 |
9.75e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 80.84 E-value: 9.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 378 KPESIEGTVEfknvSFNYPSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGfimvdenDIRALNV 457
Cdd:cd03267 15 KEPGLIGSLK----SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSG-------EVRVAGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 458 RHYRDHIGVVSQEPVLFG--TTISNNIK-----------YGRDDvtDEEMERAAREANAYDF--IMEFPNKfntlvgekg 522
Cdd:cd03267 84 VPWKRRKKFLRRIGVVFGqkTQLWWDLPvidsfyllaaiYDLPP--ARFKKRLDELSELLDLeeLLDTPVR--------- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 523 aQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIV 578
Cdd:cd03267 153 -QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTV 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1032-1241 |
1.02e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVL-FNCSIAEN 1110
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1111 IAYGDNSRvVPLDE--IKEAANAANIHSFIEGLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQKPKILLLDEATSALDn 1188
Cdd:PRK10253 102 VARGRYPH-QPLFTrwRKEDEEAVTKAMQATGITHLADQSVD----TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 1189 dsekvVQHALD--------KARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELL 1241
Cdd:PRK10253 176 -----ISHQIDllellselNREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1035-1243 |
1.04e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.83 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1035 GLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELN-VQWL--RSQIAIVPQEPVL-FN--CSIA 1108
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPLAsLNprMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1109 ENIA------YGDNSRvvplDEIKEAANAANihsfieglpekynTQVGLKGA-------QLSGGQKQRLAIARALLQKPK 1175
Cdd:PRK15079 119 EIIAeplrtyHPKLSR----QEVKDRVKAMM-------------LKVGLLPNlinryphEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 1176 ILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVNLLQQlqREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
382-611 |
1.10e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 81.76 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 382 IEGTVEFKNVS--FNYPS----RPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAL 455
Cdd:PRK15112 1 VETLLEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 456 NVRHYRDHIGVVSQEPvlfGTTISNNIKYGRD-DVT---DEEMERAAREANAY----------DFIMEFPNkfntlvgek 521
Cdd:PRK15112 81 DYSYRSQRIRMIFQDP---STSLNPRQRISQIlDFPlrlNTDLEPEQREKQIIetlrqvgllpDHASYYPH--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 522 gaQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSA-VQAALEKASK-GRTTIVVAHRLSTIRS-ADLIVTLKDG 598
Cdd:PRK15112 149 --MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQlINLMLELQEKqGISYIYVTQHLGMMKHiSDQVLVMHQG 226
|
250
....*....|...
gi 255708477 599 MLAEKGAHAELMA 611
Cdd:PRK15112 227 EVVERGSTADVLA 239
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
369-550 |
1.12e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 85.02 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 369 IDNFSTAGYKPESIEG-------TVEFKNVSFNYPSrPSIKiLKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPD 441
Cdd:PRK10522 299 LNKLALAPYKAEFPRPqafpdwqTLELRNVTFAYQD-NGFS-VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 442 DGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERaareanaydfiMEFPNKFnTLVGEK 521
Cdd:PRK10522 377 SGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPEGKPANPALVEKWLER-----------LKMAHKL-ELEDGR 444
|
170 180 190
....*....|....*....|....*....|.
gi 255708477 522 GA--QMSGGQKQRIAIARALVRNPKILILDE 550
Cdd:PRK10522 445 ISnlKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1015-1233 |
1.19e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 85.02 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPdvFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:PRK10522 323 LELRNVTFAYQDNG--FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLFncsiaeniaygdnSRVvpLDEIKEAANAANIHSFIE--GLPEKYNTQVG-LKGAQLSGGQKQRLAIARALL 1171
Cdd:PRK10522 401 AVFTDFHLF-------------DQL--LGPEGKPANPALVEKWLErlKMAHKLELEDGrISNLKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 1172 QKPKILLLDEAtsALDNDSE---KVVQHALDKAR-TGRTCLVVTHRLSAIQNADLIVVLHNGKIKE 1233
Cdd:PRK10522 466 EERDILLLDEW--AADQDPHfrrEFYQVLLPLLQeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
387-602 |
1.23e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.58 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPSrpsIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDH-IG 465
Cdd:PRK11288 6 SFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAgVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQE----PVLfgtTISNNIKYGRddvtdeemeraareanaydfimeFPNKF-----NTLVGEKGAQM----------- 525
Cdd:PRK11288 83 IIYQElhlvPEM---TVAENLYLGQ-----------------------LPHKGgivnrRLLNYEAREQLehlgvdidpdt 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 526 -----SGGQKQRIAIARALVRNPKILILDEATSAL---DSESKSAVQAALEkaSKGRTTIVVAHRLSTI-RSADLIVTLK 596
Cdd:PRK11288 137 plkylSIGQRQMVEIAKALARNARVIAFDEPTSSLsarEIEQLFRVIRELR--AEGRVILYVSHRMEEIfALCDAITVFK 214
|
....*.
gi 255708477 597 DGMLAE 602
Cdd:PRK11288 215 DGRYVA 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1032-1250 |
1.30e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.84 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTS----VQLLQrlydPVQGQVLFDGVDAKELNVqWLRSQ--IAIVPQEPVLF-N 1104
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTfymiVGLVK----PDSGRIFLDGEDITHLPM-HKRARlgIGYLPQEASIFrK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1105 CSIAENIAYGDNSRVVPLDEIKEAANAAnIHSF-IEGLPEKyntqvglKGAQLSGGQKQRLAIARALLQKPKILLLDEAT 1183
Cdd:COG1137 93 LTVEDNILAVLELRKLSKKEREERLEEL-LEEFgITHLRKS-------KAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1184 SALD----NDSEKVVQHALDKartG----------RTCLVVTHRlSAIqnadlivvLHNGKIKEQGTHQELLRN---RDI 1246
Cdd:COG1137 165 AGVDpiavADIQKIIRHLKER---GigvlitdhnvRETLGICDR-AYI--------ISEGKVLAEGTPEEILNNplvRKV 232
|
....*...
gi 255708477 1247 Y----FKL 1250
Cdd:COG1137 233 YlgedFRL 240
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1015-1243 |
1.38e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 80.69 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKEL-NVQWLRSQI 1093
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1094 AIVPQEPVLFN-CSIAENIAYGDnsrvVPLDEIKEAANAANIHSFIEGLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQ 1172
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGG----FFAERDQFQERIKWVYELFPRLHERRIQRAG----TMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 1173 KPKILLLDEATSALdndSEKVVQHALDKART----GRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:PRK11614 155 QPRLLLLDEPSLGL---APIIIQQIFDTIEQlreqGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
399-599 |
1.81e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.07 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 399 PSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYdPD---DGFIMVDEndiralNVRHYRD-----HIGVV--S 468
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDG------EVCRFKDirdseALGIViiH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 469 QE----PVLfgtTISNNI-------KYGrddVTD-EEMERAAREANAYDFIMEFPnkfNTLVGEKGAqmsgGQKQRIAIA 536
Cdd:NF040905 85 QElaliPYL---SIAENIflgneraKRG---VIDwNETNRRARELLAKVGLDESP---DTLVTDIGV----GKQQLVEIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 537 RALVRNPKILILDEATSAL-DSESKSAVQAALEKASKGRTTIVVAHRLSTIRS-ADLIVTLKDGM 599
Cdd:NF040905 152 KALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGR 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1032-1223 |
2.00e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 78.94 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRsQIAIVPQEPVLFN-CSIAEN 1110
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE-NILYLGHLPGLKPeLSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1111 IAYgdnsrvvpldeikeaanAANIHSFIEGLPEKYNTQVGLKG------AQLSGGQKQRLAIARALLQKPKILLLDEATS 1184
Cdd:TIGR01189 94 LHF-----------------WAAIHGGAQRTIEDALAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 255708477 1185 ALDNDSEKVVQHALDkARTGRTCLVV--THRLSAIQNADLI 1223
Cdd:TIGR01189 157 ALDKAGVALLAGLLR-AHLARGGIVLltTHQDLGLVEAREL 196
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
403-610 |
2.59e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.42 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 403 ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFG-TTISNN 481
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 482 IKYGRDD---------VTDEEMERAAREANAydfimefpnkFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEAT 552
Cdd:PRK10253 102 VARGRYPhqplftrwrKEDEEAVTKAMQATG----------ITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 553 SALDSESKSAVQAALEKAS--KGRTTIVVAHRLS-TIRSADLIVTLKDGMLAEKGAHAELM 610
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNreKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
386-616 |
2.80e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.44 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVS--FNYPSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDE-------------- 449
Cdd:PRK13631 22 LRVKNLYcvFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 450 --NDIRALNVRHYRDHIGVVSQEP--VLFGTTISNNIKYGRDDVTDEEmERAAREANAYDFIMEFPNKFntlVGEKGAQM 525
Cdd:PRK13631 102 npYSKKIKNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKK-SEAKKLAKFYLNKMGLDDSY---LERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 526 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSA-VQAALEKASKGRTTIVVAHRLSTI-RSADLIVTLKDGMLAEK 603
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKT 257
|
250
....*....|...
gi 255708477 604 GAHAELMAKRGLY 616
Cdd:PRK13631 258 GTPYEIFTDQHII 270
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
398-584 |
3.20e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.94 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 398 RPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPD---DGFIMVDEndiRALNVRHYRDHIGVVSQEPVLF 474
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNG---MPIDAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 475 GT-------TISNNIKYGRDDVTDEEMERAAREANAydfiMEFPNKFNTLVGEKGAQ--MSGGQKQRIAIARALVRNPKI 545
Cdd:TIGR00955 112 PTltvrehlMFQAHLRMPRRVTKKEKRERVDEVLQA----LGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 255708477 546 LILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLS 584
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPS 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1002-1237 |
3.22e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.42 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1002 SQEGKKPDTCegnLEFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDA 1081
Cdd:PRK13536 32 SIPGSMSTVA---IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1082 KElNVQWLRSQIAIVPQEPVL-FNCSIAEN-IAYGDNSRVvPLDEIKEAanaanIHSFIE--GLPEKYNTQVglkgAQLS 1157
Cdd:PRK13536 106 PA-RARLARARIGVVPQFDNLdLEFTVRENlLVFGRYFGM-STREIEAV-----IPSLLEfaRLESKADARV----SDLS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1158 GGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARtGRTCLVVTHRL-SAIQNADLIVVLHNG-KIKE 1233
Cdd:PRK13536 175 GGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMeEAERLCDRLCVLEAGrKIAE 253
|
....
gi 255708477 1234 QGTH 1237
Cdd:PRK13536 254 GRPH 257
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
102-337 |
3.56e-16 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 81.02 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 102 DMTLLTLY---YVGIGVAALIFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGI 178
Cdd:cd18564 49 PLALLLLAaaaLVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 179 GDKIALLFQNMSTFSIGLAVGLVKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIA 258
Cdd:cd18564 129 VSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 259 FRAQEKELQRY-TQNLKDAKDfGIK-RTIASKVS-----LGAVyffmnGTyGLAFWYGTSLILNGEpgYTIGTVLaVFFS 331
Cdd:cd18564 209 FGREEHEERRFaRENRKSLRA-GLRaARLQALLSpvvdvLVAV-----GT-ALVLWFGAWLVLAGR--LTPGDLL-VFLA 278
|
....*.
gi 255708477 332 VIHSSY 337
Cdd:cd18564 279 YLKNLY 284
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
403-628 |
4.16e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.14 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 403 ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRD------HIGVVSQEPVLFGT 476
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDvlefrrRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 477 TISNNIKYG---RDDVTDEEMERAAR----EANAYDFIMEfpnkfntLVGEKGAQMSGGQKQRIAIARALVRNPKILILD 549
Cdd:PRK14271 116 SIMDNVLAGvraHKLVPRKEFRGVAQarltEVGLWDAVKD-------RLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 550 EATSALDSESKSAVQAALEKASKGRTTIVVAHRLS-TIRSADLIVTLKDGMLAEKGAHAELMAK----RGLYYSLVMSQD 624
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSSpkhaETARYVAGLSGD 268
|
....
gi 255708477 625 IKKA 628
Cdd:PRK14271 269 VKDA 272
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
404-610 |
4.34e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.50 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 404 LKGLNLRIKSGETVALVGLNGSGKSTvvqLLQRLYD--PDDGFIMVDENDIRALNVRHYRDHIGVVSQE-PVLFGTTISN 480
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMAGllPGQGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 481 NIKYGRDDVTDEEMERAAREANAYDFIMEfpNKFNTLVGekgaQMSGGQKQRIAIARALVR-----NP--KILILDEATS 553
Cdd:COG4138 89 YLALHQPAGASSEAVEQLLAQLAEALGLE--DKLSRPLT----QLSGGEWQRVRLAAVLLQvwptiNPegQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 554 ALDseskSAVQAALEK-----ASKGRTTIVVAHRLS-TIRSADLIVTLKDGMLAEKGAHAELM 610
Cdd:COG4138 163 SLD----VAQQAALDRllrelCQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
382-598 |
4.72e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.91 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 382 IEGTVEFKNVSfnyPSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVR-HY 460
Cdd:PRK09700 2 ATPYISMAGIG---KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 461 RDHIGVVSQE-PVLFGTTISNNIKYGRD--------DVTD-EEM-ERAAreanaydfIMEFPNKFNTLVGEKGAQMSGGQ 529
Cdd:PRK09700 79 QLGIGIIYQElSVIDELTVLENLYIGRHltkkvcgvNIIDwREMrVRAA--------MMLLRVGLKVDLDEKVANLSISH 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 530 KQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASK-GRTTIVVAHRLSTIRS-ADLIVTLKDG 598
Cdd:PRK09700 151 KQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
397-598 |
4.92e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 82.74 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 397 SRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDH-IGVVSQEPVLFG 475
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 476 T-TISNNIKYGRDDVTD------EEMEraaREANAYDFIMEFPNKFNTLVGEkgaqMSGGQKQRIAIARALVRNPKILIL 548
Cdd:PRK10762 93 QlTIAENIFLGREFVNRfgridwKKMY---AEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 255708477 549 DEATSAL-DSESKSAVQAALEKASKGRTTIVVAHRLSTI-RSADLIVTLKDG 598
Cdd:PRK10762 166 DEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDG 217
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1042-1235 |
6.05e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.07 E-value: 6.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1042 RGKTVAFvGSSGCGKSTSVQLLQRLYDPVQG------QVLFDgvDAKELNVQWLRSQIAIVPQEPVLF-NCSIAENIAYG 1114
Cdd:PRK11144 24 QGITAIF-GRSGAGKTSLINAISGLTRPQKGrivlngRVLFD--AEKGICLPPEKRRIGYVFQDARLFpHYKVRGNLRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1115 -DNSRVVPLDEIKEAANaanihsfIEGLPEKYNtqvglkgAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKV 1193
Cdd:PRK11144 101 mAKSMVAQFDKIVALLG-------IEPLLDRYP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 255708477 1194 VQHALDK-ARTGRT-CLVVTHRLSAI-QNADLIVVLHNGKIKEQG 1235
Cdd:PRK11144 167 LLPYLERlAREINIpILYVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
400-598 |
7.31e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 82.18 E-value: 7.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 400 SIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYdPD---DGFIMVDENDIRALNVRHY-RDHIGVVSQEPVLF- 474
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 475 GTTISNNIKYGrDDVT-------DEEMERAAREANAYDFIMEFPNkfNTLVGEKGaqmsGGQKQRIAIARALVRNPKILI 547
Cdd:TIGR02633 92 ELSVAENIFLG-NEITlpggrmaYNAMYLRAKNLLRELQLDADNV--TRPVGDYG----GGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255708477 548 LDEATSAL-DSESKSAVQAALEKASKGRTTIVVAHRLSTIRS-ADLIVTLKDG 598
Cdd:TIGR02633 165 LDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
407-598 |
7.81e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.69 E-value: 7.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 407 LNLRIK-----SGETvALVGLNGSGKSTVVQLLQRLYDPDDGFI------MVD-ENDIralNVRHYRDHIGVVSQEPVLF 474
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvLFDaEKGI---CLPPEKRRIGYVFQDARLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 475 -GTTISNNIKYGRDDVTDEEmeraareanaydfimefpnkFNTLVGEKG---------AQMSGGQKQRIAIARALVRNPK 544
Cdd:PRK11144 89 pHYKVRGNLRYGMAKSMVAQ--------------------FDKIVALLGieplldrypGSLSGGEKQRVAIGRALLTAPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 545 ILILDEATSALDSESKSAVQAALEKASKG-RTTIV-VAHRLSTI-RSADLIVTLKDG 598
Cdd:PRK11144 149 LLLMDEPLASLDLPRKRELLPYLERLAREiNIPILyVSHSLDEIlRLADRVVVLEQG 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1023-1242 |
8.78e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 8.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1023 FYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDG----------VDAKELNVQWLR-- 1090
Cdd:PRK10261 22 FMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRhv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1091 --SQIAIVPQEPV-----LFNC--SIAENIAYGDN-SRVVPLDEIKEAANAANIhsfieglPEKyNTQVGLKGAQLSGGQ 1160
Cdd:PRK10261 102 rgADMAMIFQEPMtslnpVFTVgeQIAESIRLHQGaSREEAMVEAKRMLDQVRI-------PEA-QTILSRYPHQLSGGM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1161 KQRLAIARALLQKPKILLLDEATSALDNDSE-------KVVQHALDKArtgrtCLVVTHRLSAIQN-ADLIVVLHNGKIK 1232
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQGEAV 248
|
250
....*....|
gi 255708477 1233 EQGTHQELLR 1242
Cdd:PRK10261 249 ETGSVEQIFH 258
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
45-327 |
1.31e-15 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 79.05 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 45 ITLMILGILASLVNgaclplmPLVLGEMSDNLIsgclvqtnttnyqnctqsqekLNEDMTLLTLY---YVGIGVAALIFG 121
Cdd:cd18545 6 LLLMLLSTAASLAG-------PYLIKIAIDEYI---------------------PNGDLSGLLIIallFLALNLVNWVAS 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 122 YIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLV 201
Cdd:cd18545 58 RLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 202 KGWKLTLVTLSTSPLIMASAAACSR------MVISLTSKELSAYSkagavaEEVLSSIRTVIAFRAQEKELQRYTQNLKD 275
Cdd:cd18545 138 LNVRLALVTLAVLPLLVLVVFLLRRrarkawQRVRKKISNLNAYL------HESISGIRVIQSFAREDENEEIFDELNRE 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 276 AKDFGIKrtiASKVSlGAVYFFMNGTYGLA----FWYGTSLILNGEpgYTIGTVLA 327
Cdd:cd18545 212 NRKANMR---AVRLN-ALFWPLVELISALGtalvYWYGGKLVLGGA--ITVGVLVA 261
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
401-602 |
1.44e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.51 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 401 IKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMV--------DENDIRALNVRHyrdhIGVVSQEPV 472
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmDEEARAKLRAKH----VGFVFQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 473 LFGTTISnnikygRDDVTDEEMERAAREANAYDFIMEFPNKFNtlVGEK----GAQMSGGQKQRIAIARALVRNPKILIL 548
Cdd:PRK10584 99 LIPTLNA------LENVELPALLRGESSRQSRNGAKALLEQLG--LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 549 DEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTIRSADLIVTLKDGMLAE 602
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1029-1243 |
1.83e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.44 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1029 DVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELN---VQWLRSQIAIVPQEPVlfnC 1105
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY---A 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1106 SIAENIAYGDnSRVVPLdeikeaanaaNIHSFIEGLPEKYNT-----QVGLKGA-------QLSGGQKQRLAIARALLQK 1173
Cdd:PRK10261 413 SLDPRQTVGD-SIMEPL----------RVHGLLPGKAAAARVawlleRVGLLPEhawryphEFSGGQRQRICIARALALN 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 1174 PKILLLDEATSALD-NDSEKVVQHALDKART-GRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLRN 1243
Cdd:PRK10261 482 PKVIIADEAVSALDvSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFEN 554
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1027-1194 |
1.86e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.45 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1027 RPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVqwlRSQIAIV-PQEPVLFNC 1105
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACHYLgHRNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1106 SIAENIAYGDNSRVVPLDEIKEAANAANIHSfIEGLPEKYntqvglkgaqLSGGQKQRLAIARALLQKPKILLLDEATSA 1185
Cdd:PRK13539 89 TVAENLEFWAAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
....*....
gi 255708477 1186 LDNDSEKVV 1194
Cdd:PRK13539 158 LDAAAVALF 166
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
401-609 |
2.23e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 401 IKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN-VRHYRDHIGVVSQEPVLFGT-TI 478
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFPNlSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 479 SNNIKYGrddvtdeemerAAREANAYdfimefpNKFNTLVGEKGAQ----MSGG-----QKQRIAIARALVRNPKILILD 549
Cdd:PRK15439 104 KENILFG-----------LPKRQASM-------QKMKQLLAALGCQldldSSAGslevaDRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 550 EATSALD-SESKSAVQAALEKASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAEL 609
Cdd:PRK15439 166 EPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1032-1212 |
3.17e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 75.61 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENI 1111
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1112 AY--GDNSRvvplDEIKEAANAANIHSFiEGLPekyntqvglkGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDND 1189
Cdd:cd03231 95 RFwhADHSD----EQVEEALARVGLNGF-EDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|....
gi 255708477 1190 S-EKVVQHALDKARTGRTCLVVTH 1212
Cdd:cd03231 160 GvARFAEAMAGHCARGGMVVLTTH 183
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
385-598 |
3.90e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 77.46 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDEndiRALNVRHyRDHI 464
Cdd:COG4152 1 MLELKGLTKRFGDK---TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPED-RRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQEPVLF-GTTISNNIKY-----GrddvtdeeMERAAREANAyDFIMEfpnKFNtlVGEKGA----QMSGGQKQRIA 534
Cdd:COG4152 74 GYLPEERGLYpKMKVGEQLVYlarlkG--------LSKAEAKRRA-DEWLE---RLG--LGDRANkkveELSKGNQQKVQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 535 IARALVRNPKILILDEATSALDSESKSAVQAAL-EKASKGRTTIVVAHRLSTI-RSADLIVTLKDG 598
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIrELAAKGTTVIFSSHQMELVeELCDRIVIINKG 205
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
692-966 |
4.25e-15 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 77.46 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 692 VVLGTLASVLNGTVHPVFSIIFAKII-TMFGNNDKTTLKhdaeIYSMIFVILGVICFVSYFMQGLFYGRAGEILTMRLRH 770
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLdDIFVEKDLEALL----LVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 771 LAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGWEMTFLILSIAPVLAV 850
Cdd:cd18552 77 DLFDKLLRLPLSFFDR--NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 851 tgmietaAMTGFANK----DKQELKHAGKIAT---EALENIRTIVSLTREKAFEQMYEEMLQtQHRNTSKKAQIIGscyA 923
Cdd:cd18552 155 -------PIRRIGKRlrkiSRRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANE-RLRRLSMKIARAR---A 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 255708477 924 FSHAFIYFAYAAGF----RFGAYLIQAGRMTPeGMFIVFTAIAYGAM 966
Cdd:cd18552 224 LSSPLMELLGAIAIalvlWYGGYQVISGELTP-GEFISFITALLLLY 269
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
402-619 |
4.43e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.59 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 402 KILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPD---DGFIMVDENDIR-----ALNVRHYRDHIGVVSQEPVL 473
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGRTVQregrlARDIRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 474 FGT-TISNNIKYGRDDVT----------DEEMERAAREANAYDFIMEFPNkfntlvgEKGAQMSGGQKQRIAIARALVRN 542
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAH-------QRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 543 PKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLS-TIRSADLIVTLKDGMLAEKGAHAELMAKR--GLYY 617
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfdHLYR 250
|
..
gi 255708477 618 SL 619
Cdd:PRK09984 251 SI 252
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1033-1209 |
4.98e-15 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 75.93 E-value: 4.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFD----GVD-AKELNVQWL---RSQIAIVPQepvlFn 1104
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDlAQASPREILalrRRTIGYVSQ----F- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1105 csiaeniaygdnSRVVP----LDEIKEA------------ANAANIHSFIeGLPEKYntqVGLKGAQLSGGQKQRLAIAR 1168
Cdd:COG4778 102 ------------LRVIPrvsaLDVVAEPllergvdreearARARELLARL-NLPERL---WDLPPATFSGGEQQRVNIAR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 255708477 1169 ALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLV 1209
Cdd:COG4778 166 GFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
724-958 |
5.11e-15 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 76.97 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 724 DKTTLKHDAEIYSMIFVILGVICFVSYF---MQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTILAI 800
Cdd:cd18784 24 DGIVIEKSQDKFSRAIIIMGLLAIASSVaagIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDT--VKTGDITSRLTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 801 DIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGWEMTFLILSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKIATEA 880
Cdd:cd18784 102 DTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEET 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 881 LENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGScYAFSHAFIYFAYAAG-FRFGAYLIQAGRMTpEGMFIVF 958
Cdd:cd18784 182 ISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGG-YVWSNELTELALTVStLYYGGHLVITGQIS-GGNLISF 258
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
385-612 |
5.34e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.96 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFNYPSRpsIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHyRDhI 464
Cdd:PRK11650 3 GLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-RD-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQEPVLF-GTTISNNIKYG-------RDDVtDEEMERAAReanaydfIMEFpnkfNTLVGEKGAQMSGGQKQRIAIA 536
Cdd:PRK11650 79 AMVFQNYALYpHMSVRENMAYGlkirgmpKAEI-EERVAEAAR-------ILEL----EPLLDRKPRELSGGQRQRVAMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 537 RALVRNPKILILDEATSALDseSKSAVQAALE----KASKGRTTIVVAH-RLSTIRSADLIVTLKDGMLAEKGAHAELMA 611
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLD--AKLRVQMRLEiqrlHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEVYE 224
|
.
gi 255708477 612 K 612
Cdd:PRK11650 225 K 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
403-580 |
6.01e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.91 E-value: 6.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 403 ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVR---HYRDHIGVVsqEPVLfgtTIS 479
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeacHYLGHRNAM--KPAL---TVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 480 NNIKYGRDDV-TDEEMERAAREANAYDFIMEFPnkFNTLvgekgaqmSGGQKQRIAIARALVRNPKILILDEATSALDSE 558
Cdd:PRK13539 92 ENLEFWAAFLgGEELDIAAALEAVGLAPLAHLP--FGYL--------SAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180
....*....|....*....|..
gi 255708477 559 SKSAVQAALEKASKGRTTIVVA 580
Cdd:PRK13539 162 AVALFAELIRAHLAQGGIVIAA 183
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1015-1241 |
7.17e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.15 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKElNVQWLRSQIA 1094
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQ----EPvlfNCSIAENI-AYGdnsRVVPLdeikeaaNAANIHSFIEGLPE------KYNTQVGlkgaQLSGGQKQR 1163
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLlVFG---RYFGL-------SAAAARALVPPLLEfaklenKADAKVG----ELSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1164 LAIARALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARtGRTCLVVTHRL-SAIQNADLIVVLHNGKIKEQGTHQEL 1240
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMeEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
.
gi 255708477 1241 L 1241
Cdd:PRK13537 226 I 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1032-1234 |
7.35e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.20 E-value: 7.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQW---LRSQ-IAIVPQEPVLFNCSI 1107
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKhVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1108 A-ENIAY-----GDNSRvvpldEIKEAAnaanihsfIEGLpekynTQVGLKG------AQLSGGQKQRLAIARALLQKPK 1175
Cdd:PRK10584 105 AlENVELpallrGESSR-----QSRNGA--------KALL-----EQLGLGKrldhlpAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 1176 ILLLDEATSALDNDS-EKVVQHALDKARTGRTCLV-VTHRLSAIQNADLIVVLHNGKIKEQ 1234
Cdd:PRK10584 167 VLFADEPTGNLDRQTgDKIADLLFSLNREHGTTLIlVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
404-608 |
7.98e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.91 E-value: 7.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 404 LKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRH---YRDHIGVVSQE-PVLFGTTIS 479
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDhHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 480 NNIKYGR--DDVTDEEMERaaREANAYDFIMEFPNKFNTLVgekgaQMSGGQKQRIAIARALVRNPKILILDEATSALDS 557
Cdd:PRK10908 98 DNVAIPLiiAGASGDDIRR--RVSAALDKVGLLDKAKNFPI-----QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255708477 558 ESKSAVQAALEKASK-GRTTIVVAHRLSTI-RSADLIVTLKDGMLAEkGAHAE 608
Cdd:PRK10908 171 ALSEGILRLFEEFNRvGVTVLMATHDIGLIsRRSYRMLTLSDGHLHG-GVGGE 222
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
45-331 |
9.06e-15 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 76.39 E-value: 9.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 45 ITLMILGILASLVngaclplMPLVLGEMSDNLISGCLVQTNTtnyqnctqsqeklnEDMTLLTLYYVGIGVAALIFGYIQ 124
Cdd:cd18563 5 FLLMLLGTALGLV-------PPYLTKILIDDVLIQLGPGGNT--------------SLLLLLVLGLAGAYVLSALLGILR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 125 --ISLWIitAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKI----SDGIGDkialLFQNMSTFsIGLAV 198
Cdd:cd18563 64 grLLARL--GERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLqdflSDGLPD----FLTNILMI-IGIGV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 199 GL-VKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFrAQEK-ELQRYTQNLKDA 276
Cdd:cd18563 137 VLfSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAF-GQEKrEIKRFDEANQEL 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 277 KDFGIkRTIASKVSLGAVYFFMNGTYGLAFWY-GTSLILNGEpgYTIGTVLAvFFS 331
Cdd:cd18563 216 LDANI-RAEKLWATFFPLLTFLTSLGTLIVWYfGGRQVLSGT--MTLGTLVA-FLS 267
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1035-1242 |
9.17e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 78.69 E-value: 9.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1035 GLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLF----DGVDAKELNVQwLRSQ----IAIVPQEPVLF-NC 1105
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD-GRGRakryIGILHQEYDLYpHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1106 SIAENIaygdnSRVVPLDEIKEAANAANIHSF-IEGLPEKYNTQVGLK-GAQLSGGQKQRLAIARALLQKPKILLLDEAT 1183
Cdd:TIGR03269 381 TVLDNL-----TEAIGLELPDELARMKAVITLkMVGFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 1184 SALDNDSEKVVQHALDKART--GRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLR 1242
Cdd:TIGR03269 456 GTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
386-555 |
9.44e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.30 E-value: 9.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSrpsIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAL-NVRHYRDHI 464
Cdd:PRK11614 6 LSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQEPVLFG-TTISNNIKYGRDDVTDEEMERaaREANAYDFimeFPNKFNTLVGEKGAqMSGGQKQRIAIARALVRNP 543
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQP 156
|
170
....*....|..
gi 255708477 544 KILILDEATSAL 555
Cdd:PRK11614 157 RLLLLDEPSLGL 168
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1029-1240 |
9.75e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 78.69 E-value: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1029 DVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRL--YDPVQGQVLFdgvdakelNVQWLRSQIAIVPQEPVLFNCS 1106
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIY--------HVALCEKCGYVERPSKVGEPCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1107 IAEN------IAYGDNSRVVPLDEIKEAA-----------NAANIHSFIEGLPE-KYNTQVGLKGA-------------- 1154
Cdd:TIGR03269 84 VCGGtlepeeVDFWNLSDKLRRRIRKRIAimlqrtfalygDDTVLDNVLEALEEiGYEGKEAVGRAvdliemvqlshrit 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1155 ----QLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKA--RTGRTCLVVTHRLSAIQN-ADLIVVLH 1227
Cdd:TIGR03269 164 hiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLE 243
|
250
....*....|...
gi 255708477 1228 NGKIKEQGTHQEL 1240
Cdd:TIGR03269 244 NGEIKEEGTPDEV 256
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
402-614 |
1.03e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.61 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 402 KILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLY--DPDDGFIMVDENDIralnvrhYRDhigvvsqepvlfgTTIS 479
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF-------GRE-------------ASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 480 NNIkyGRDDVTDEEMER--AAREANAYDFIMEFpnkfntlvgekgAQMSGGQKQRIAIARALVRNPKILILDEATSALDS 557
Cdd:COG2401 104 DAI--GRKGDFKDAVELlnAVGLSDAVLWLRRF------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 558 ESKSAVQAALEKASK--GRTTIVVAHRlstirsADLIVTLKDGMLAEKGAHAELMAKRG 614
Cdd:COG2401 170 QTAKRVARNLQKLARraGITLVVATHH------YDVIDDLQPDLLIFVGYGGVPEEKRR 222
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
397-580 |
1.65e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.55 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 397 SRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIrALNVRHYRDHIGVVSQEPVLFGT 476
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-AEQRDEPHENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 477 -TISNNIKYGRDDVTDEEmeRAAREANAydfimefpnkfntLVGEKG------AQMSGGQKQRIAIARALVRNPKILILD 549
Cdd:TIGR01189 88 lSALENLHFWAAIHGGAQ--RTIEDALA-------------AVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|.
gi 255708477 550 EATSALDSESkSAVQAALEKASKGRTTIVVA 580
Cdd:TIGR01189 153 EPTTALDKAG-VALLAGLLRAHLARGGIVLL 182
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
49-327 |
2.54e-14 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 75.21 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 49 ILGILASLVNGACL-PLMPLVLGEMSDNLIsgclvqtnttnyqnctqsqekLNEDMTLLTLYYVG-IGVAAL--IFGYIQ 124
Cdd:cd18550 1 LALVLLLILLSALLgLLPPLLLREIIDDAL---------------------PQGDLGLLVLLALGmVAVAVAsaLLGVVQ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 125 ISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGW 204
Cdd:cd18550 60 TYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 205 KLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLS--SIRTVIAFRAQEKELQRYTQNLKDAKDFGIK 282
Cdd:cd18550 140 RLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARRSRELRDLGVR 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 255708477 283 RTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEPgyTIGTVLA 327
Cdd:cd18550 220 QALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGL--TIGTLVA 262
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
393-592 |
5.94e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 77.36 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 393 FNYPSRPSIKilkGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAlNVRHYRDHIGVVSQEPV 472
Cdd:TIGR01257 938 FEPSGRPAVD---RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 473 LFG-TTISNNIKY-----GRD-DVTDEEMERAAREANAYdfimefpNKFNtlvgEKGAQMSGGQKQRIAIARALVRNPKI 545
Cdd:TIGR01257 1014 LFHhLTVAEHILFyaqlkGRSwEEAQLEMEAMLEDTGLH-------HKRN----EEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255708477 546 LILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLStirSADLI 592
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EADLL 1126
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1033-1252 |
6.74e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.12 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTsvqLLQRLYDPVQGQ-------------VLFDGVDAKELNVQwlRSQIAIVPQE 1099
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKST---LLRHLSGLITGDksagshiellgrtVQREGRLARDIRKS--RANTGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1100 PVLFN-CSIAENIAYGDNSRVVPLDEIKEAANAANIHSFIEGLpekynTQVGL------KGAQLSGGQKQRLAIARALLQ 1172
Cdd:PRK09984 95 FNLVNrLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGMvhfahqRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1173 KPKILLLDEATSALDNDSEKVVQHAL-DKART-GRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELLRNR-DIYF 1248
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLrDINQNdGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfDHLY 249
|
....
gi 255708477 1249 KLVN 1252
Cdd:PRK09984 250 RSIN 253
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
100-327 |
8.27e-14 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 73.63 E-value: 8.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 100 NEDMTLLTLYYVGIGVAAL---IFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTdDIDKISD 176
Cdd:cd18570 35 SGDINLLNIISIGLILLYLfqsLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIRE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 177 GIGDKIALLFQNMSTFSIGLAVGLVKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTV 256
Cdd:cd18570 114 AISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 257 IAFRAQEKEL----QRYTQNLKDAKDFGIKRTIASKVSLGAVYFFMNgtygLAFWYGTSLILNGEpgYTIGTVLA 327
Cdd:cd18570 194 KSLNAEEQFLkkieKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSL----LILWIGSYLVIKGQ--LSLGQLIA 262
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1029-1230 |
8.95e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.63 E-value: 8.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1029 DVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLY--DPVQGQVLFDGVDAKELNVQWL-RSQIAIVPQEPVLF-N 1104
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1105 CSIAENIAYGdNSRVVPLDEIKEAANAANIHSFIEGLpEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATS 1184
Cdd:TIGR02633 93 LSVAENIFLG-NEITLPGGRMAYNAMYLRAKNLLREL-QLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 255708477 1185 AL-DNDSEKVVQHALDKARTGRTCLVVTHRLSAIQN-ADLIVVLHNGK 1230
Cdd:TIGR02633 171 SLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1027-1241 |
9.69e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.90 E-value: 9.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1027 RPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWlRSQ-IAIVPQEPvlfnc 1105
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-RSQrIRMIFQDP----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1106 SIAENiaygDNSRV-----VPLDEIKEAANAANIHSFIEGLpekynTQVGLKGAQ-------LSGGQKQRLAIARALLQK 1173
Cdd:PRK15112 97 STSLN----PRQRIsqildFPLRLNTDLEPEQREKQIIETL-----RQVGLLPDHasyyphmLAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 1174 PKILLLDEATSALDND-SEKVVQHALD-KARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELL 1241
Cdd:PRK15112 168 PKVIIADEALASLDMSmRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1033-1231 |
1.29e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.06 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNV-QWLRSQIAIVPQEP-----VLfNCS 1106
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPrERRRLGVAYIPEDRlgrglVP-DMS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1107 IAENIAygdnsrvvpLDEIKEAA-------NAANIHSFIEGLPEKYN---TQVGLKGAQLSGGQKQRLAIARALLQKPKI 1176
Cdd:COG3845 353 VAENLI---------LGRYRRPPfsrggflDRKAIRAFAEELIEEFDvrtPGPDTPARSLSGGNQQKVILARELSRDPKL 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 1177 LLLDEATSALDNDS-EKVVQHALDKARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKI 1231
Cdd:COG3845 424 LIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1028-1230 |
1.58e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.83 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1028 PDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYdP---VQGQVLFDGvdaKELNVQWLRSQ----IAIVPQE- 1099
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDG---EVCRFKDIRDSealgIVIIHQEl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1100 ---PVLfncSIAENIAYGDnsrvvpldEIKEAA----NAANIHSfIE-----GLPEKYNTQVGlkgaQLSGGQKQRLAIA 1167
Cdd:NF040905 88 aliPYL---SIAENIFLGN--------ERAKRGvidwNETNRRA-REllakvGLDESPDTLVT----DIGVGKQQLVEIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1168 RALLQKPKILLLDEATSAL-DNDSEKVVQHALDKARTGRTCLVVTHRLSAI-QNADLIVVLHNGK 1230
Cdd:NF040905 152 KALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGR 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1015-1230 |
1.74e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.56 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQ-WLRSQI 1093
Cdd:PRK11288 5 LSFDGIGKTFP---GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1094 AIVPQE----PVLfncSIAENIAYGD--NSRVVpldeIKEAANAANIHSFIEGLPEKYNTQVGLKgaQLSGGQKQRLAIA 1167
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGQlpHKGGI----VNRRLLNYEAREQLEHLGVDIDPDTPLK--YLSIGQRQMVEIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1168 RALLQKPKILLLDEATSALDNDSEKVVQHALDKART-GRTCLVVTHRLSAI-QNADLIVVLHNGK 1230
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAeGRVILYVSHRMEEIfALCDAITVFKDGR 217
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1032-1236 |
1.81e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.60 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLL--QRLYDPVQGQVLFDGVDAKELNVQwLRSQIAIVP--QEPVLFNCSI 1107
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPE-ERAHLGIFLafQYPIEIPGVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1108 AEN---IAYGDNSRVVPLDEIKEAanaanihSFIEGLPEKYNTqVGLKGAQL--------SGGQKQRLAIARALLQKPKI 1176
Cdd:CHL00131 101 NADflrLAYNSKRKFQGLPELDPL-------EFLEIINEKLKL-VGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 1177 LLLDEATSALDNDSEKVVQHALDKARTGRTCLV-VTH--RLSAIQNADLIVVLHNGKIKEQGT 1236
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1034-1212 |
2.38e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.22 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1034 RGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKEL------NVQWLRSQIAI----VPQEPVLF 1103
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGIktelTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1104 NCSIAEniaygdnsrvvPLDEikEAANAAnihsfiegLpekynTQVGLKG------AQLSGGQKQRLAIARALLQKPKIL 1177
Cdd:PRK13538 98 YQRLHG-----------PGDD--EALWEA--------L-----AQVGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 255708477 1178 LLDEATSALDNDSEKVVQHALDK-ARTGRTCLVVTH 1212
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
48-328 |
2.62e-13 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 72.05 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 48 MILGILASLVNGACLPLMPLVLGEMSDNLISGclvqtNTTNYqnctqsqeklnedMTLLTLYYVGIGVAALIFGYIQISL 127
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIAN-----GDLSY-------------ILRTGLLMLLLALLGLIAGILAGYF 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 128 WIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIgdkiaLLFQNMSTFSIGLAVG-----LVK 202
Cdd:cd18548 63 AAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFV-----MMLLRMLVRAPIMLIGaiimaFRI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 203 GWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIK 282
Cdd:cd18548 138 NPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLK 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 255708477 283 --RTIAskVSLGAVYFFMNGTYGLAFWYGTSLILNGEPgyTIGTVLAV 328
Cdd:cd18548 218 agRLMA--LLNPLMMLIMNLAIVAILWFGGHLINAGSL--QVGDLVAF 261
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
397-559 |
2.69e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 70.21 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 397 SRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVdENDIRALNVRHYRDHIGVVSQEPVLFGT 476
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL-NGGPLDFQRDSIARGLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 477 -TISNNIKYGRDDVTDEEMERAAREANaydfimefpnkFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSAL 555
Cdd:cd03231 88 lSVLENLRFWHADHSDEQVEEALARVG-----------LNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
....
gi 255708477 556 DSES 559
Cdd:cd03231 157 DKAG 160
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
400-600 |
2.92e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.61 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 400 SIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVR---HYRDH-IGVVSQ------ 469
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRNQkLGFIYQfhhllp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 470 ---------EPVLFGttisnnikygrdDVTDEEMERAAREanaydfiMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALV 540
Cdd:PRK11629 101 dftalenvaMPLLIG------------KKKPAEINSRALE-------MLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 541 RNPKILILDEATSALDSESKSAVQAALEK--ASKGRTTIVVAHRLSTIRSADLIVTLKDGML 600
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
691-958 |
4.28e-13 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 71.22 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 691 FVVLgTLAsVLNGTVHPVFSiifAKIITMFGNNDKttlkHDAEIYSMIFviLGVICFVSYFMQGL---FYGRAGEILTMR 767
Cdd:cd18590 2 FLFL-TLA-VICETFIPYYT---GRVIDILGGEYQ----HNAFTSAIGL--MCLFSLGSSLSAGLrggLFMCTLSRLNLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 768 LRHLAFKAMLYQDIAWFDekENSTGGLTTILAIDIAQIqgatgSRigVLTQNATNMglsvIISFIYGWEMTFLILSIAPV 847
Cdd:cd18590 71 LRHQLFSSLVQQDIGFFE--KTKTGDLTSRLSTDTTLM-----SR--SVALNANVL----LRSLVKTLGMLGFMLSLSWQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 848 LAVTGMIE---TAAMTGFANKDKQELK--------HAGKIATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQ 916
Cdd:cd18590 138 LTLLTLIEmplTAIAQKVYNTYHQKLSqavqdsiaKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDT 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 255708477 917 IIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRMTPEGM--FIVF 958
Cdd:cd18590 218 VRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLvsFILY 261
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1018-1231 |
4.51e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.13 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1018 REVSFFYPCRPD-----VFILRGL---------SLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKE 1083
Cdd:COG1129 239 RELEDLFPKRAAapgevVLEVEGLsvggvvrdvSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1084 LNV-QWLRSQIAIVP----QEPVLFNCSIAENI---AYGDNSRVVPLDEIKEAANAanihsfieglpEKYNTQVGLKGA- 1154
Cdd:COG1129 319 RSPrDAIRAGIAYVPedrkGEGLVLDLSIRENItlaSLDRLSRGGLLDRRRERALA-----------EEYIKRLRIKTPs 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1155 ------QLSGGQKQRLAIARALLQKPKILLLDEATSALDndsekV-----VQHALDK-ARTGRTCLVVTHRLS-AIQNAD 1221
Cdd:COG1129 388 peqpvgNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID-----VgakaeIYRLIRElAAEGKAVIVISSELPeLLGLSD 462
|
250
....*....|
gi 255708477 1222 LIVVLHNGKI 1231
Cdd:COG1129 463 RILVMREGRI 472
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
385-556 |
6.07e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFNYpSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFI-------------MVDEND 451
Cdd:PRK10261 14 AVENLNIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 452 IRALNVRHYRD-HIGVVSQEPVL-------FGTTISNNIKYGRDDVTDEEMERAAREANAydfiMEFPNKfNTLVGEKGA 523
Cdd:PRK10261 93 QSAAQMRHVRGaDMAMIFQEPMTslnpvftVGEQIAESIRLHQGASREEAMVEAKRMLDQ----VRIPEA-QTILSRYPH 167
|
170 180 190
....*....|....*....|....*....|...
gi 255708477 524 QMSGGQKQRIAIARALVRNPKILILDEATSALD 556
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALD 200
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
48-333 |
6.13e-13 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 70.97 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 48 MILGILASLVNGACLPLMPLVLGEMSDNLISGclvqtnttnyqnctQSQEKLnedmTLLTLYYVGIGVAALIFGYI---- 123
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAH--------------GDRSAL----WPLVLLLLALGVAEAVLSFLrryl 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 124 --QISLWIitaarQTkRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGdKIALLFQNMSTFSIGLAVGLV 201
Cdd:cd18543 63 agRLSLGV-----EH-DLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 202 KGWKLTLVTLSTSPLIMASAAACSRMVISLTskeLSAYSKAGAVA---EEVLSSIRTVIAFRAQEKELQRYTQNLKDakd 278
Cdd:cd18543 136 LSPPLALVALASLPPLVLVARRFRRRYFPAS---RRAQDQAGDLAtvvEESVTGIRVVKAFGRERRELDRFEAAARR--- 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 279 fgIKRTIASKVSLGAVYFFM-----NGTYGLAFWYGTSLILNGEpgYTIGTVLAvFFSVI 333
Cdd:cd18543 210 --LRATRLRAARLRARFWPLlealpELGLAAVLALGGWLVANGS--LTLGTLVA-FSAYL 264
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1023-1241 |
6.42e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.16 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1023 FYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTsvqLLQRL--YDP----VQGQVLFDG--VDAKELnvqwlRSQIA 1094
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTT---LMNALafRSPkgvkGSGSVLLNGmpIDAKEM-----RAISA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLFNCSIAEN----IAYGDNSRVVPLDEIKEAANAanihsFIE--GLPEKYNTQVGLKGAQ--LSGGQKQRLAI 1166
Cdd:TIGR00955 103 YVQQDDLFIPTLTVREhlmfQAHLRMPRRVTKKEKRERVDE-----VLQalGLRKCANTRIGVPGRVkgLSGGERKRLAF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1167 ARALLQKPKILLLDEATSALDNDS-EKVVQHALDKARTGRTCLVVTHRLSA--IQNADLIVVLHNGKIKEQGTHQELL 1241
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
399-1217 |
7.00e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.60 E-value: 7.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 399 PSIKILKGLNLRIKSGETVALVGLNGSGKSTvvqLLQRLYDPDDGFIMVDENDIR------ALNVRHYRDHIGVVSQEPV 472
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCST---LLKTIASNTDGFHIGVEGVITydgitpEEIKKHYRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 473 LFGT-TISNNIKYG--------RDDVTDEEmERAAREANAYDFIMEFPNKFNTLVGE---KGaqMSGGQKQRIAIARALV 540
Cdd:TIGR00956 149 HFPHlTVGETLDFAarcktpqnRPDGVSRE-EYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 541 RNPKILILDEATSALDSESksavqaALE--KASKGRTTIVVAHRLSTIRSA--------DLIVTLKDGmlaekgahaelm 610
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSAT------ALEfiRALKTSANILDTTPLVAIYQCsqdayelfDKVIVLYEG------------ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 611 akRGLYYSlvmsqDIKKADEQMESMTYST-ERKTNSLPLHSVKS-----IKSDFIDKAEESTQS---------------K 669
Cdd:TIGR00956 288 --YQIYFG-----PADKAKQYFEKMGFKCpDRQTTADFLTSLTSpaerqIKPGYEKKVPRTPQEfetywrnspeyaqlmK 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 670 EISLP--------------EVSLLKILKLNKPEWPFVV-------LGTLASVL----NGTVH--PVFSIIFAKII--TMF 720
Cdd:TIGR00956 361 EIDEYldrcsesdtkeayrESHVAKQSKRTRPSSPYTVsfsmqvkYCLARNFLrmkgNPSFTlfMVFGNIIMALIlsSVF 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 721 GNNDKTT------------------LKHDAEIYSMI------------------------------FVILGVICF--VSY 750
Cdd:TIGR00956 441 YNLPKNTsdfysrggalffailfnaFSSLLEIASMYearpivekhrkyalyhpsadaiasiiseipFKIIESVVFniILY 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 751 FMQGlFYGRAGEILTmrlrHLAFKAMLYQDIAWFDEkenSTGGLTTILaidiaqIQGATGSRIGVLtqnATNM--GLSVI 828
Cdd:TIGR00956 521 FMVN-FRRTAGRFFF----YLLILFICTLAMSHLFR---SIGAVTKTL------SEAMTPAAILLL---ALSIytGFAIP 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 829 ISFIYGWEMTflilsIAPVLAVTGMIETAAMTGFANK--DKQELKHAGKiATEALENIRTIVSLTREKAFEQMYE--EML 904
Cdd:TIGR00956 584 RPSMLGWSKW-----IYYVNPLAYAFESLMVNEFHGRrfECSQYVPSGG-GYDNLGVTNKVCTVVGAEPGQDYVDgdDYL 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 905 QTQHRntskkaqiigscYAFSHAFIYF----AYAAGFRFgayliqagrmtpegMFIVFTAIAYGAMAIGETLVLApeySK 980
Cdd:TIGR00956 658 KLSFQ------------YYNSHKWRNFgiiiGFTVFFFF--------------VYILLTEFNKGAKQKGEILVFR---RG 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 981 AKSGAAHLFALLEKKPN-IDSRSQEGKKPDTCEGNLEFREVSFFYPCRPDVFILRGLSLSI-----ER------------ 1042
Cdd:TIGR00956 709 SLKRAKKAGETSASNKNdIEAGEVLGSTDLTDESDDVNDEKDMEKESGEDIFHWRNLTYEVkikkeKRvilnnvdgwvkp 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1043 GKTVAFVGSSGCGKSTsvqLLQRLYDPVQGQVLFDG---VDAKELNVQWLRSqIAIVPQEPV-LFNCSIAENI---AYGD 1115
Cdd:TIGR00956 789 GTLTALMGASGAGKTT---LLNVLAERVTTGVITGGdrlVNGRPLDSSFQRS-IGYVQQQDLhLPTSTVRESLrfsAYLR 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1116 NSRVVPLDEIKEAanaanIHSFIEGLP-EKY-NTQVGLKGAQLSGGQKQRLAIARALLQKPKILL-LDEATSALDNDSEK 1192
Cdd:TIGR00956 865 QPKSVSKSEKMEY-----VEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAW 939
|
970 980
....*....|....*....|....*.
gi 255708477 1193 VVQHALDK-ARTGRTCLVVTHRLSAI 1217
Cdd:TIGR00956 940 SICKLMRKlADHGQAILCTIHQPSAI 965
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
404-598 |
7.68e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.36 E-value: 7.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 404 LKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRH-------Y----RDHIGVVSQEPV 472
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagiaYvpedRKGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 473 LFGTTISNNIKYGRDDVTDEEMERAAreanAYDFIMEF----PNKfNTLVGekgaQMSGGQKQRIAIARALVRNPKILIL 548
Cdd:COG1129 348 RENITLASLDRLSRGGLLDRRRERAL----AEEYIKRLriktPSP-EQPVG----NLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 549 DEATSALDSESKSAVQAALEK-ASKGRTTIVVahrlST-----IRSADLIVTLKDG 598
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRElAAEGKAVIVI----SSelpelLGLSDRILVMREG 470
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
386-612 |
1.04e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.14 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSrpsIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRL--YDPDDGFIM----------------- 446
Cdd:TIGR03269 1 IEVKNLTKKFDG---KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 447 ----------------VDENDIRALNVRHYRDHIGVVSQEP-VLFG--TTISNNIKygrddvTDEEMERAAREA--NAYD 505
Cdd:TIGR03269 78 vgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTfALYGddTVLDNVLE------ALEEIGYEGKEAvgRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 506 FIMEFpnKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRL 583
Cdd:TIGR03269 152 LIEMV--QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWP 229
|
250 260 270
....*....|....*....|....*....|
gi 255708477 584 STIRS-ADLIVTLKDGMLAEKGAHAELMAK 612
Cdd:TIGR03269 230 EVIEDlSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
388-604 |
1.10e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.57 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 388 FKNVSFN-YPsrpsikilkglnlriksGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNV--------R 458
Cdd:PRK11701 22 CRDVSFDlYP-----------------GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 459 H-YRDHIGVVSQEP-------VLFGTTISNNI------KYG--RDDVTD--EEMERAAreanayDFIMEFPNKFntlvge 520
Cdd:PRK11701 85 RlLRTEWGFVHQHPrdglrmqVSAGGNIGERLmavgarHYGdiRATAGDwlERVEIDA------ARIDDLPTTF------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 521 kgaqmSGGQKQRIAIARALVRNPKILILDEATSALDseskSAVQAALEKASKGRTT------IVVAHRLSTIRS-ADLIV 593
Cdd:PRK11701 153 -----SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD----VSVQARLLDLLRGLVRelglavVIVTHDLAVARLlAHRLL 223
|
250
....*....|.
gi 255708477 594 TLKDGMLAEKG 604
Cdd:PRK11701 224 VMKQGRVVESG 234
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1036-1242 |
1.31e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1036 LSLSIERGKTVAFVGSSGCGKSTsvqLLQRLYD--PVQGQVLFDGVD-----AKELNVQ--WLRSQIAIVPQEPVL--FN 1104
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPleawsAAELARHraYLSQQQTPPFAMPVFqyLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1105 CSIAENIAYGDNSRVvpLDEIKEAAnaanihsfieGLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQ-----KP--KIL 1177
Cdd:PRK03695 92 LHQPDKTRTEAVASA--LNEVAEAL----------GLDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 1178 LLDEATSALDndsekVVQH-ALDK-----ARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELLR 1242
Cdd:PRK03695 156 LLDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1015-1232 |
1.35e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 71.78 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYD-PVQGQVLFDGvdaKELNV----QWL 1089
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFING---KPVDIrnpaQAI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1090 RSQIAIVPQE-------PVLfncSIAENIAYGDNSRVVPLDEIKEAANAANIHSFIEGLPEKyNTQVGLKGAQLSGGQKQ 1162
Cdd:TIGR02633 335 RAGIAMVPEDrkrhgivPIL---GVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVK-TASPFLPIGRLSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 1163 RLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDK-ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIK 1232
Cdd:TIGR02633 411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLK 482
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1029-1215 |
1.91e-12 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 71.70 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1029 DVFILRgLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYdPVQGQVLFdgVDAKelnvqwlrSQIAIVPQEPVLFNCSIA 1108
Cdd:TIGR00954 465 DVLIES-LSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLT--KPAK--------GKLFYVPQRPYMTLGTLR 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1109 ENIAYGDNSrvvpLDEIKEAANAANIHSFIEGLPEKY--NTQVGLKGAQ-----LSGGQKQRLAIARALLQKPKILLLDE 1181
Cdd:TIGR00954 533 DQIIYPDSS----EDMKRRGLSDKDLEQILDNVQLTHilEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|....*
gi 255708477 1182 ATSALDNDSE-KVVQHALDKartGRTCLVVTHRLS 1215
Cdd:TIGR00954 609 CTSAVSVDVEgYMYRLCREF---GITLFSVSHRKS 640
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1036-1242 |
2.36e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.77 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1036 LSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYD---PVQGQVL-FDGVDAKELNVQWLR----SQIAIVPQEPVlfncsI 1107
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgRVMAEKLeFNGQDLQRISEKERRnlvgAEVAMIFQDPM-----T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1108 AENIAYGDNSRVVPLDEIKEAANAANIHS-FIEGLpekynTQVGLKGA---------QLSGGQKQRLAIARALLQKPKIL 1177
Cdd:PRK11022 101 SLNPCYTVGFQIMEAIKVHQGGNKKTRRQrAIDLL-----NQVGIPDPasrldvyphQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1178 LLDEATSALD-NDSEKVVQHALDKARTGRTCLV-VTHRLSAI-QNADLIVVLHNGKIKEQGTHQELLR 1242
Cdd:PRK11022 176 IADEPTTALDvTIQAQIIELLLELQQKENMALVlITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1032-1246 |
2.99e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.00 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNV-QWLRSQIAIVPQEPvlfncSIAEN 1110
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEA-----SIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1111 IAYGDNsrVVPLDEIKEAANAANIHSFIEGLPEKYNTQvGLK---GAQLSGGQKQRLAIARALLQKPKILLLDEATSALD 1187
Cdd:PRK10895 93 LSVYDN--LMAVLQIRDDLSAEQREDRANELMEEFHIE-HLRdsmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 1188 N----DSEKVVQHALDkarTGRTCLVVTHRL-SAIQNADLIVVLHNGKIKEQGTHQELLRNRDI 1246
Cdd:PRK10895 170 PisviDIKRIIEHLRD---SGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
386-556 |
3.02e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.22 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFImvdendiralnVRHYRDHIG 465
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLFGT---TISNNIKYgRDDVTDEEMERAAREANAYDFImEFPNKfntlvgekgaQMSGGQKQRIAIARALVRN 542
Cdd:PRK09544 71 YVPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLI-DAPMQ----------KLSGGETQRVLLARALLNR 138
|
170
....*....|....
gi 255708477 543 PKILILDEATSALD 556
Cdd:PRK09544 139 PQLLVLDEPTQGVD 152
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
734-960 |
3.25e-12 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 68.61 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 734 IYSMIFVILGVICFVSYFMQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDekENSTGGLTTILAIDIAQIQGATGSRI 813
Cdd:cd18542 40 LLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 814 GVLTQNATNMGLSVIISFIYGWEMTFLILSIAPVLAVTGMI-ETAAMTGFANKDKQElkhaGKIATEALENI---RTIVS 889
Cdd:cd18542 118 VELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVfFKKVRPAFEEIREQE----GELNTVLQENLtgvRVVKA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 890 LTREKA----FEQMYEEmlqtqHRNTSKKAQIIGSCY-AFSHAFIYFAYAAGFRFGAYLIQAGRMTPeGMFIVFTA 960
Cdd:cd18542 194 FAREDYeiekFDKENEE-----YRDLNIKLAKLLAKYwPLMDFLSGLQIVLVLWVGGYLVINGEITL-GELVAFIS 263
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1030-1231 |
3.67e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.46 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1030 VFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELN-VQWLRSQIAIVPQEPVLF-NCSI 1107
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFpNLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1108 AENIAYGdnsrvVPldeiKEAANAANIHSFIEGLpekyNTQVGL--KGAQLSGGQKQRLAIARALLQKPKILLLDEATSA 1185
Cdd:PRK15439 104 KENILFG-----LP----KRQASMQKMKQLLAAL----GCQLDLdsSAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 255708477 1186 LD-NDSEKVVQHALDKARTGRTCLVVTHRLSAI-QNADLIVVLHNGKI 1231
Cdd:PRK15439 171 LTpAETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTI 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1033-1240 |
3.78e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.03 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWL---------RSQIAIVPQEP--- 1100
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1101 VLFNCSIAENIA----------YGdNSRVVPLD-----EIKEAAnaanihsfIEGLPEKYntqvglkgaqlSGGQKQRLA 1165
Cdd:PRK11701 102 LRMQVSAGGNIGerlmavgarhYG-DIRATAGDwlervEIDAAR--------IDDLPTTF-----------SGGMQQRLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1166 IARALLQKPKILLLDEATSALDndsekV-VQ-HALDKART-----GRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQG-T 1236
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLD-----VsVQaRLLDLLRGlvrelGLAVVIVTHDLAvARLLAHRLLVMKQGRVVESGlT 236
|
....
gi 255708477 1237 HQEL 1240
Cdd:PRK11701 237 DQVL 240
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
407-635 |
3.97e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 407 LNLRIKSGETVALVGLNGSGKSTvvqLLQRLYD--PDDGFIMVDENDIRALNVR---HYRDHIgvVSQEPVLFGTTISNN 481
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAAelaRHRAYL--SQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 482 IKYGRDDVTDEEMERAAREANAYDFIMEfpNKFNTLVGekgaQMSGGQKQRIAIARALVR-----NP--KILILDEATSA 554
Cdd:PRK03695 90 LTLHQPDKTRTEAVASALNEVAEALGLD--DKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 555 LDseskSAVQAALEK-----ASKGRTTIVVAHRLS-TIRSADLIVTLKDGMLAEKGAHAELMAKRGLyySLVMSQDIKKA 628
Cdd:PRK03695 164 LD----VAQQAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENL--AQVFGVNFRRL 237
|
....*..
gi 255708477 629 DEQMESM 635
Cdd:PRK03695 238 DVEGHPM 244
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
413-592 |
5.88e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 64.70 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 413 SGETVALVGLNGSGKSTVVQLLQRLYDPDD-GFIMVDENDIRALNVRHYRdhigvvsqepvlfgttisnnikygrddvtd 491
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 492 eemeraareanaydfimefpnkfNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALE--- 568
Cdd:smart00382 51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180
....*....|....*....|....*...
gi 255708477 569 ----KASKGRTTIVVAHRLSTIRSADLI 592
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
414-556 |
6.89e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.88 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 414 GETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALN---VRHYRDHIGVVSQEPV-------LFGTTISNNIK 483
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYasldprqTVGDSIMEPLR 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 484 YGRDDVTDEEMERAA----REANAYDFIMEFPNKFntlvgekgaqmSGGQKQRIAIARALVRNPKILILDEATSALD 556
Cdd:PRK10261 430 VHGLLPGKAAAARVAwlleRVGLLPEHAWRYPHEF-----------SGGQRQRICIARALALNPKVIIADEAVSALD 495
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1032-1237 |
8.00e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.74 E-value: 8.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKST-SVQLLQRL-YDPVQGQVLFDGVDAKELNVQWLRSQ-IAIVPQEPV------- 1101
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLELSPEDRAGEgIFMAFQYPVeipgvsn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1102 --LFNCSIAENIAYGDNSrvvPLDEIkeaanaaNIHSFIE------GLPEKYNTQ---VGLkgaqlSGGQKQRLAIARAL 1170
Cdd:PRK09580 96 qfFLQTALNAVRSYRGQE---PLDRF-------DFQDLMEekiallKMPEDLLTRsvnVGF-----SGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1171 LQKPKILLLDEATSALDNDSEKVVQHALDKARTG-RTCLVVTH--RLSAIQNADLIVVLHNGKIKEQGTH 1237
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
397-598 |
9.27e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.99 E-value: 9.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 397 SRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDH-IGVVSQE-PVLF 474
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVHQElNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 475 GTTISNNIKYGRDD-----VTDEEMERAAREANAYDFIMEFPNkfntlvgEKGAQMSGGQKQRIAIARALVRNPKILILD 549
Cdd:PRK10982 87 QRSVMDNMWLGRYPtkgmfVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255708477 550 EATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDG 598
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKlKERGCGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
404-591 |
1.03e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.90 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 404 LKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDH-IGVVSQEPVLFGT----TI 478
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRLGRGLvpdmSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 479 SNNI--------KYGRDDVtdeeMERAAREANAYDFIMEF---PNKFNTLVGekgaQMSGGQKQRIAIARALVRNPKILI 547
Cdd:COG3845 354 AENLilgryrrpPFSRGGF----LDRKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLI 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 255708477 548 LDEATSALDSESKSAVQAAL-EKASKGRTTIVVahrlstirSADL 591
Cdd:COG3845 426 AAQPTRGLDVGAIEFIHQRLlELRDAGAAVLLI--------SEDL 462
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
385-598 |
1.47e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 64.98 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFNYP-SRPSIKILKGLNLRIKSGETVALVGLNGSGKSTvvqLLQRLYDPDDGFIMVdENDIR------ALNV 457
Cdd:cd03233 3 TLSWRNISFTTGkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCST---LLKALANRTEGNVSV-EGDIHyngipyKEFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 458 RHYRDHIGVVSQEPVLFGTtisnnikygrddVTDEEMERAAREANAYDFImefpnkfntlvgeKGaqMSGGQKQRIAIAR 537
Cdd:cd03233 79 EKYPGEIIYVSEEDVHFPT------------LTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAE 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 538 ALVRNPKILILDEATSALDSESksavqaALEKASKGRTtivVAH--RLSTIRSA-----------DLIVTLKDG 598
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSST------ALEILKCIRT---MADvlKTTTFVSLyqasdeiydlfDKVLVLYEG 196
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1028-1229 |
1.68e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1028 PDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwLRSQ--IAIVPQE-PVLFN 1104
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQlgIGIIYQElSVIDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1105 CSIAENIAYGD--NSRV--VPLDEIKEAANAANIHSFIEGLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQKPKILLLD 1180
Cdd:PRK09700 95 LTVLENLYIGRhlTKKVcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255708477 1181 EATSALDNDSEKVVQHALDKART-GRTCLVVTHRLSAIQN-ADLIVVLHNG 1229
Cdd:PRK09700 171 EPTSSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
411-581 |
1.74e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 65.89 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 411 IKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRalnvrhYR------DHIGVVSQepVLFGTT-ISNNIK 483
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------YKpqyikaDYEGTVRD--LLSSITkDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 484 YGRDDVTDE-EMERaareanaydfIMEfpNKFNTLvgekgaqmSGGQKQRIAIARALVRNPKILILDEATSALDSESKSA 562
Cdd:cd03237 94 YFKTEIAKPlQIEQ----------ILD--REVPEL--------SGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180
....*....|....*....|...
gi 255708477 563 VQAAL----EKASKgrTTIVVAH 581
Cdd:cd03237 154 ASKVIrrfaENNEK--TAFVVEH 174
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1020-1212 |
1.87e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 68.42 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1020 VSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTsvqLLQrlydpvqgqvLFDGVDAKELNVQWLRSQIAI--VP 1097
Cdd:TIGR03719 10 VSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKST---LLR----------IMAGVDKDFNGEARPQPGIKVgyLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1098 QEPVL-FNCSIAENI-------------------AYGDNS--------RVVPLDEIKEAANAANIHSFIE------GLPE 1143
Cdd:TIGR03719 75 QEPQLdPTKTVRENVeegvaeikdaldrfneisaKYAEPDadfdklaaEQAELQEIIDAADAWDLDSQLEiamdalRCPP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1144 KyNTQVglkgAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALdkARTGRTCLVVTH 1212
Cdd:TIGR03719 155 W-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL--QEYPGTVVAVTH 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
403-611 |
2.20e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.81 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 403 ILKGLNLRIKSGETVALVGLNGSGKS-TVVQLLQRLYDPDdgfIMVDENDIR----------ALNVRHYR-DHIGVVSQE 470
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPP---VVYPSGDIRfhgesllhasEQTLRGVRgNKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 471 PVlfgttISNNIKYGRDDVTDE--EMERAAREANAYDFIMEFPNKfntlVGEKGA---------QMSGGQKQRIAIARAL 539
Cdd:PRK15134 101 PM-----VSLNPLHTLEKQLYEvlSLHRGMRREAARGEILNCLDR----VGIRQAakrltdyphQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 540 VRNPKILILDEATSALDSESKSAVQAALE--KASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAELMA 611
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
386-615 |
2.56e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.61 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENdiraLNVRHY-RDHI 464
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN----ANIGYYaQDHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 465 GVVSQEPVLFgttisNNIKYGRDDVTDEEMERAA--ReanaydfiMEFPNKfntLVGEKGAQMSGGQKQRIAIARALVRN 542
Cdd:PRK15064 393 YDFENDLTLF-----DWMSQWRQEGDDEQAVRGTlgR--------LLFSQD---DIKKSVKVLSGGEKGRMLFGKLMMQK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 543 PKILILDEATSALDSESKSAVQAALEKaSKGrTTIVVAHRLSTIRS-ADLIVTLK-DGMLAEKGAHAELMAKRGL 615
Cdd:PRK15064 457 PNVLVMDEPTNHMDMESIESLNMALEK-YEG-TLIFVSHDREFVSSlATRIIEITpDGVVDFSGTYEEYLRSQGI 529
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1015-1240 |
2.71e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.65 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPV-QGQVLFDGvdaKELNV----QWL 1089
Cdd:PRK13549 260 LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDG---KPVKIrnpqQAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1090 RSQIAIVPQE-------PVLfncSIAENIAYGDNSRVVPLDEIKEAANAANIHSFIEGLPEKYNTqVGLKGAQLSGGQKQ 1162
Cdd:PRK13549 337 AQGIAMVPEDrkrdgivPVM---GVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTAS-PELAIARLSGGNQQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1163 RLAIARALLQKPKILLLDEATSALDNDSE----KVVqHALdkARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTH 1237
Cdd:PRK13549 413 KAVLAKCLLLNPKILILDEPTRGIDVGAKyeiyKLI-NQL--VQQGVAIIVISSELPEVLGlSDRVLVMHEGKLKGDLIN 489
|
...
gi 255708477 1238 QEL 1240
Cdd:PRK13549 490 HNL 492
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1029-1249 |
2.81e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 66.29 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1029 DVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDP---VQGQVLFDG-----VDAKELNVqwLRS-QIAIVPQE 1099
Cdd:PRK09473 28 DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGreilnLPEKELNK--LRAeQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1100 P----------------VLF---NCSIAEniAYGDNSRVvpLDEIKeaanaanihsfiegLPEKyNTQVGLKGAQLSGGQ 1160
Cdd:PRK09473 106 PmtslnpymrvgeqlmeVLMlhkGMSKAE--AFEESVRM--LDAVK--------------MPEA-RKRMKMYPHEFSGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1161 KQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALD--KARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTh 1237
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNelKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGN- 245
|
250
....*....|..
gi 255708477 1238 qellrNRDIYFK 1249
Cdd:PRK09473 246 -----ARDVFYQ 252
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
406-589 |
3.26e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.05 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 406 GLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRD------HIGVvsqEPVLfgTTIS 479
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllylghQPGI---KTEL--TALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 480 NNIKYGRD-DVTDEEMERAAREAnaydfimefpnkfntlVGEKG------AQMSGGQKQRIAIARALVRNPKILILDEAT 552
Cdd:PRK13538 94 NLRFYQRLhGPGDDEALWEALAQ----------------VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 255708477 553 SALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRSA 589
Cdd:PRK13538 158 TAIDKQGVARLEALLAQhAEQGGMVILTTHQDLPVASD 195
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
388-598 |
4.07e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 63.42 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 388 FKNVSFNYPSRPSIK-ILKGLNLRIKSGETVALVGLNGSGKSTVVQLL-QRlydPDDGFImvdENDIRA---LNVRHYRD 462
Cdd:cd03232 6 WKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGR---KTAGVI---TGEILIngrPLDKNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEPVLFGT-TIsnnikygrddvtdeemeraaREAnaydfiMEFPNKFNTLvgekgaqmSGGQKQRIAIARALVR 541
Cdd:cd03232 80 STGYVEQQDVHSPNlTV--------------------REA------LRFSALLRGL--------SVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 542 NPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLS--TIRSADLIVTLKDG 598
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
720-972 |
4.59e-11 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 65.20 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 720 FGNNDKTTLKHDAEIYSMIFVILGVICFVSYFmqglFYGRAGEILTMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTILA 799
Cdd:cd18575 27 FAAGNTALLNRAFLLLLAVALVLALASALRFY----LVSWLGERVVADLRKAVFAHLLRLSPSFFET--TRTGEVLSRLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 800 IDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGWEMTFLILSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKIATE 879
Cdd:cd18575 101 TDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 880 ALENIRTIVSLTREKA----FEQMYEEMLQTQHRNTSKKAQIIgscyAFSHAFIYFAYAAGFRFGAYLIQAGRMTPE--G 953
Cdd:cd18575 181 TLSAIKTVQAFTREDAerqrFATAVEAAFAAALRRIRARALLT----ALVIFLVFGAIVFVLWLGAHDVLAGRMSAGelS 256
|
250 260
....*....|....*....|
gi 255708477 954 MFIVFTAIAYGAMA-IGETL 972
Cdd:cd18575 257 QFVFYAVLAAGSVGaLSEVW 276
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1042-1223 |
5.50e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 62.01 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1042 RGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIvpqepvlfncsiaeniaygdnsrvvp 1121
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1122 ldeikeaanaanihsfieglpekyntqvGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALD-- 1199
Cdd:smart00382 55 ----------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180
....*....|....*....|....*....
gi 255708477 1200 -----KARTGRTCLVVTHRLSAIQNADLI 1223
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1032-1242 |
6.08e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.46 E-value: 6.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQ-RLYDP-------VQGQVLFDGVDAKELNVQWLRSQIAIVPQ--EPV 1101
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1102 lFNCSIAENIAYGDNSRVvpldeikEAANAANIHSfieglPEKYNTQVGLKGAQ---------LSGGQKQRLAIARALLQ 1172
Cdd:PRK13547 96 -FAFSAREIVLLGRYPHA-------RRAGALTHRD-----GEIAWQALALAGATalvgrdvttLSGGELARVQFARVLAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1173 ---------KPKILLLDEATSALDNDSekvvQHAL-----DKARTGRT-CLVVTHRLS-AIQNADLIVVLHNGKIKEQGT 1236
Cdd:PRK13547 163 lwpphdaaqPPRYLLLDEPTAALDLAH----QHRLldtvrRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
....*.
gi 255708477 1237 HQELLR 1242
Cdd:PRK13547 239 PADVLT 244
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
412-584 |
6.65e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 64.31 E-value: 6.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 412 KSGETVALVGLNGSGKSTVVQLLQ--------RLYDPDDG---------------FIMVDENDIRALNVRHYRDHIgvvs 468
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWdeildefrgselqnyFTKLLEGDVKVIVKPQYVDLI---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 469 qePVLFGTTISNNIKygrddvtdeemerAAREANAYDFIMEfPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILIL 548
Cdd:cd03236 100 --PKAVKGKVGELLK-------------KKDERGKLDELVD-QLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 255708477 549 DEATSALDSESK-SAVQAALEKASKGRTTIVVAHRLS 584
Cdd:cd03236 164 DEPSSYLDIKQRlNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
406-565 |
7.04e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 64.24 E-value: 7.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 406 GLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAL---------------NVRHYRDHIGV---- 466
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghqiarmgvvrtfqHVRLFREMTVIenll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 467 VSQEPVLFGTTISNNIK---YGRDDvtDEEMERAAREANAYDfIMEFPNKfntlvgEKGaQMSGGQKQRIAIARALVRNP 543
Cdd:PRK11300 103 VAQHQQLKTGLFSGLLKtpaFRRAE--SEALDRAATWLERVG-LLEHANR------QAG-NLAYGQQRRLEIARCMVTQP 172
|
170 180
....*....|....*....|..
gi 255708477 544 KILILDEATSALDSESKSAVQA 565
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDE 194
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1020-1212 |
8.59e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.30 E-value: 8.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1020 VSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFdgvdAKELNVQWLrsqiaivPQE 1099
Cdd:PRK11819 12 VSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP----APGIKVGYL-------PQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1100 PVL-----------------------FNcSIAENIAYGDN------SRVVPLDEIKEAANAANIHSFIE------GLPEK 1144
Cdd:PRK11819 79 PQLdpektvrenveegvaevkaaldrFN-EIYAAYAEPDAdfdalaAEQGELQEIIDAADAWDLDSQLEiamdalRCPPW 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 1145 yNTQVGlkgaQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALdKARTGrTCLVVTH 1212
Cdd:PRK11819 158 -DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL-HDYPG-TVVAVTH 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1035-1246 |
1.06e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.47 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1035 GLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwlrsQIA---IVP--QEPVLF-NCSIA 1108
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGH----QIArmgVVRtfQHVRLFrEMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1109 ENIAYGDNSRV----------VPLDEIKEAANAANIHSFIE--GLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQKPKI 1176
Cdd:PRK11300 99 ENLLVAQHQQLktglfsgllkTPAFRRAESEALDRAATWLErvGLLEHANRQAG----NLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 1177 LLLDEATSALDNDSEKVVQHALDKART--GRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLRNRDI 1246
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPDV 247
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
397-610 |
1.87e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.31 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 397 SRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQ-RLYDPDD-------GFIMVDENDIRALNVRHYRDHIGVVS 468
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 469 Q-----------EPVLFG----TTISNNIKYGRDDVTDEEMERAAREAnaydfimefpnkfntLVGEKGAQMSGGQKQRI 533
Cdd:PRK13547 90 QaaqpafafsarEIVLLGryphARRAGALTHRDGEIAWQALALAGATA---------------LVGRDVTTLSGGELARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 534 AIARAL---------VRNPKILILDEATSALDSESKSAVQAALEKASK----GRTTIVVAHRLSTiRSADLIVTLKDGML 600
Cdd:PRK13547 155 QFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwnlGVLAIVHDPNLAA-RHADRIAMLADGAI 233
|
250
....*....|
gi 255708477 601 AEKGAHAELM 610
Cdd:PRK13547 234 VAHGAPADVL 243
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
102-327 |
1.89e-10 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 63.38 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 102 DMTLLTLYYVGIGVAAL---IFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRmTDDIDKISDGI 178
Cdd:cd18782 37 DLATLYVIGVVMLVAALleaVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTR-ISELDTIRGFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 179 GDKIALLFQNmSTFSIG-LAVGLVKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVi 257
Cdd:cd18782 116 TGTALTTLLD-VLFSVIyIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTV- 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 258 afRAQEKELQ-------RYTQNLKdaKDFgikRTIASKVSLGAVYFFMNGTYGLAF-WYGTSLILNGEpgYTIGTVLA 327
Cdd:cd18782 194 --KAQNAELKarwrwqnRYARSLG--EGF---KLTVLGTTSGSLSQFLNKLSSLLVlWVGAYLVLRGE--LTLGQLIA 262
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
401-578 |
1.90e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.57 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 401 IKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVD-----ENDIRalnvrhYRDHIGVV----SQ-- 469
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgyvpfKRRKE------FARRIGVVfgqrSQlw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 470 --EPVLFGTTISNNIkYGrddVTDEEMERAAREanaYDFIMEFPNKFNTLVgekgAQMSGGQKQRIAIARALVRNPKILI 547
Cdd:COG4586 109 wdLPAIDSFRLLKAI-YR---IPDAEYKKRLDE---LVELLDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190
....*....|....*....|....*....|..
gi 255708477 548 LDEATSALDSESKSAVQAALEKASKGR-TTIV 578
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKEYNRERgTTIL 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
389-581 |
2.52e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.57 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 389 KNVSFNYPsrPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENdIRalnvrhyrdhIGVVS 468
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPG-IK----------VGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 469 QEPVLfgttisNNIKYGRDDVTD--EEMERAAREANA-YDFIMEFPNKFNTLVGEKG----------------------- 522
Cdd:TIGR03719 75 QEPQL------DPTKTVRENVEEgvAEIKDALDRFNEiSAKYAEPDADFDKLAAEQAelqeiidaadawdldsqleiamd 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 523 -----------AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKaSKGrTTIVVAH 581
Cdd:TIGR03719 149 alrcppwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE-YPG-TVVAVTH 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
409-600 |
2.95e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.59 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 409 LRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVdENDIralnvrhyrdhigVVS---QEP--VLFGTT---ISN 480
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDL-------------IVArlqQDPprNVEGTVydfVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 481 NIK--------YGR--DDVTDEEMERAARE----------ANAYdfimEFPNKFNTLVGEKG-------AQMSGGQKQRI 533
Cdd:PRK11147 90 GIEeqaeylkrYHDisHLVETDPSEKNLNElaklqeqldhHNLW----QLENRINEVLAQLGldpdaalSSLSGGWLRKA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 534 AIARALVRNPKILILDEATSALDSESKSAVQAALeKASKGrTTIVVAHRLSTIRS-ADLIVTLKDGML 600
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKL 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1033-1217 |
3.01e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.59 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLrsqIAIVPQE-------PVLfnc 1105
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVL--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1106 siAENIA----YGDNS---RVVPLD-EIKEAANAAnihsfiEGLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQKPKIL 1177
Cdd:PRK15056 97 --VEDVVmmgrYGHMGwlrRAKKRDrQIVTAALAR------VDMVEFRHRQIG----ELSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 255708477 1178 LLDEATSALDNDSEKVVQHALDKAR-TGRTCLVVTHRLSAI 1217
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1037-1244 |
4.68e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.38 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1037 SLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDG--VDAKELNVqwlRSQIAIVPQEPVLFN-CSIAENIA- 1112
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIAT---RRRVGYMSQAFSLYGeLTVRQNLEl 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1113 ----YGdnsrvVPLDEIKEAANAAnIHSF-----IEGLPEkyntqvglkgaQLSGGQKQRLAIARALLQKPKILLLDEAT 1183
Cdd:NF033858 363 harlFH-----LPAAEIAARVAEM-LERFdladvADALPD-----------SLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 1184 S-----ALDNdsekVVQHALDKART-GRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNR 1244
Cdd:NF033858 426 SgvdpvARDM----FWRLLIELSREdGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVAAR 488
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
403-607 |
4.94e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 61.35 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 403 ILKGLNLRIKSGETVALVGLNGSGKSTVVQLL--QRLYDPDDGFIMVDENDIRALNVRHYR-DHIGVVSQEPV------- 472
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAgEGIFMAFQYPVeipgvsn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 473 -LFGTTISNNIKYGRDdvtDEEMERAAREanayDFIME------FPNKFNTLVGEKGaqMSGGQKQRIAIARALVRNPKI 545
Cdd:PRK09580 96 qFFLQTALNAVRSYRG---QEPLDRFDFQ----DLMEEkiallkMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPEL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 546 LILDEATSALDSESKSAVQAALEKASKG-RTTIVVAH--RLSTIRSADLIVTLKDGMLAEKGAHA 607
Cdd:PRK09580 167 CILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFT 231
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1032-1249 |
4.96e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.36 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVG--SSGCG---KSTSVQLLQRLYDpVQGQVLFDGVDAKELnVQWLRSQIAIVPQEPVLF-NC 1105
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGrpGSGCStllKTIASNTDGFHIG-VEGVITYDGITPEEI-KKHYRGDVVYNAETDVHFpHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1106 SIAENIAY-----GDNSRVVPLDEIKEAANAANIHSFIEGLPEKYNTQVG---LKGaqLSGGQKQRLAIARALLQKPKIL 1177
Cdd:TIGR00956 154 TVGETLDFaarckTPQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGndfVRG--VSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1178 LLDEATSALDNDSekvvqhALDKARTGRTCLVVTHRLSAI------QNA----DLIVVLHNGKIKEQGTHQELLRnrdiY 1247
Cdd:TIGR00956 232 CWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFGPADKAKQ----Y 301
|
..
gi 255708477 1248 FK 1249
Cdd:TIGR00956 302 FE 303
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
104-327 |
6.45e-10 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 61.74 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 104 TLLTLYYVGIGVAALIFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIA 183
Cdd:cd18546 39 LLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 184 LLFQNMSTFSIGLAVGLVKGWKLTLVTLSTSPLImasaAACSRMVISLTSKelsAYSKA-GAVAE------EVLSSIRTV 256
Cdd:cd18546 119 QLVVSLLTLVGIAVVLLVLDPRLALVALAALPPL----ALATRWFRRRSSR---AYRRArERIAAvnadlqETLAGIRVV 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 257 IAFRAQEKELQRYTQnlkDAKDFGIKRTIASKVSlgAVYF-FM----NGTYGLAFWYGTSLILNGEpgYTIGTVLA 327
Cdd:cd18546 192 QAFRRERRNAERFAE---LSDDYRDARLRAQRLV--AIYFpGVellgNLATAAVLLVGAWRVAAGT--LTVGVLVA 260
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
386-587 |
6.59e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 63.61 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSrpSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDEndiralnvrhyRDHIG 465
Cdd:TIGR00954 452 IKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 466 VVSQEPVLFGTTISNNIKYgrDDVTDEEMERAAREANAYDFIMEFpnKFNTLVGEKGA---------QMSGGQKQRIAIA 536
Cdd:TIGR00954 519 YVPQRPYMTLGTLRDQIIY--PDSSEDMKRRGLSDKDLEQILDNV--QLTHILEREGGwsavqdwmdVLSGGEKQRIAMA 594
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255708477 537 RALVRNPKILILDEATSALDSESKSAVQAALEKAskGRTTIVVAHRLSTIR 587
Cdd:TIGR00954 595 RLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWK 643
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
404-593 |
9.71e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 59.26 E-value: 9.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 404 LKGLNLRIKSGETVALVGLNGSGKSTVVQllqrlydpdDGFIMVDENDIRALNVRHYRDHIGVVSQepvlFGTTISNNIK 483
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISFLPKFSRNKLIFIDQ----LQFLIDVGLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 484 YGRddvtdeemeraareanaydfimefpnkfntlVGEKGAQMSGGQKQRIAIARALVRNPK--ILILDEATSALDSESKS 561
Cdd:cd03238 78 YLT-------------------------------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|...
gi 255708477 562 AVQAALEK-ASKGRTTIVVAHRLSTIRSADLIV 593
Cdd:cd03238 127 QLLEVIKGlIDLGNTVILIEHNLDVLSSADWII 159
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
400-604 |
1.03e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.43 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 400 SIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLL--QRLYDPDDGFIMVDENDIRALNVRHyRDHIGV--VSQEPVlfg 475
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPEE-RAHLGIflAFQYPI--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 476 tTIS--NNIKYGRDDVTDEEMERAAREANAYDFiMEFPNKFNTLVGEKGAQM--------SGGQKQRIAIARALVRNPKI 545
Cdd:CHL00131 95 -EIPgvSNADFLRLAYNSKRKFQGLPELDPLEF-LEIINEKLKLVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 546 LILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAH--RLSTIRSADLIVTLKDGMLAEKG 604
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTG 234
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
380-586 |
1.18e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 380 ESIEGTVEFKNVSFNYP-SRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLL-QRLydpDDGFImvdENDIRALNV 457
Cdd:TIGR00956 754 ESGEDIFHWRNLTYEVKiKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERV---TTGVI---TGGDRLVNG 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 458 RHyRDH-----IGVVSQEPVLFGTTI-------------SNNI-KYGRDDVTDEEMEraareanaydfIMEFPNKFNTLV 518
Cdd:TIGR00956 828 RP-LDSsfqrsIGYVQQQDLHLPTSTvreslrfsaylrqPKSVsKSEKMEYVEEVIK-----------LLEMESYADAVV 895
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 519 GEKGAQMSGGQKQRIAIARALVRNPKILI-LDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTI 586
Cdd:TIGR00956 896 GVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPSAI 965
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
747-986 |
1.60e-09 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 60.64 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 747 FVSYFMQGLF---Y----GRAGEILTMRLRHLAFKAMLYQDIAWFDekENSTGGLTTILAIDIAQIQGATGSrigVLTQN 819
Cdd:cd18574 49 LGLYLLQSLLtfaYisllSVVGERVAARLRNDLFSSLLRQDIAFFD--THRTGELVNRLTADVQEFKSSFKQ---CVSQG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 820 ATNMGLSV--IISFIY-GWEMTFLILSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKAF 896
Cdd:cd18574 124 LRSVTQTVgcVVSLYLiSPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 897 EQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRMTPEGM--FIVFTAIAYGAMAigETLVL 974
Cdd:cd18574 204 LELYEEEVEKAAKLNEKLGLGIGIFQGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLmsFLVATQTIQRSLA--QLSVL 281
|
250
....*....|..
gi 255708477 975 APEYSKAKSGAA 986
Cdd:cd18574 282 FGQYVKGKSAGA 293
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
734-959 |
1.80e-09 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 60.48 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 734 IYSMIFVILGVICFVSYFMQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDekENSTGGLTTILAIDIAQIQGATGSRI 813
Cdd:cd18544 42 LLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSGL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 814 GVLTQNATNMGLSVIISFIYGWEMTFLILSIAPVLAVTGMI--------------ETAAMTGFANkdkqelkhagkiatE 879
Cdd:cd18544 120 VTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLfrkksrkayrevreKLSRLNAFLQ--------------E 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 880 ALENIRTIVSLTREKAFEQMYEEMLQtQHRNTSKKAQIIgscYAFSHAFIYFAYAAG----FRFGAYLIQAGRMTPeGMF 955
Cdd:cd18544 186 SISGMSVIQLFNREKREFEEFDEINQ-EYRKANLKSIKL---FALFRPLVELLSSLAlalvLWYGGGQVLSGAVTL-GVL 260
|
....
gi 255708477 956 IVFT 959
Cdd:cd18544 261 YAFI 264
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
404-601 |
3.21e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.51 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 404 LKGLNLRIKSGETVALVGLNGSGKSTVVQLLQrlydpddGFIMVDENDIRAL----NVRHYRDHIGVVSQE-------PV 472
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALM-------GFVRLASGKISILgqptRQALQKNLVAYVPQSeevdwsfPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 473 LFGTTISNNiKYG------RDDVTDEEMeraAREANAYDFIMEFPNKfntLVGEkgaqMSGGQKQRIAIARALVRNPKIL 546
Cdd:PRK15056 96 LVEDVVMMG-RYGhmgwlrRAKKRDRQI---VTAALARVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 547 ILDEATSALDSESKSAVQAAL-EKASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLA 601
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLrELRDEGKTMLVSTHNLGSVTEfCDYTVMVKGTVLA 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
387-558 |
4.08e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENdiraLNVRHYRDHIGV 466
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFDQHRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 467 VSQEpvlfgTTISNNIKYGRDDVTdeeMERAAREANAY--DFIMEfPNKFNTLVgekgAQMSGGQKQRIAIARALVRNPK 544
Cdd:PRK11147 394 LDPE-----KTVMDNLAEGKQEVM---VNGRPRHVLGYlqDFLFH-PKRAMTPV----KALSGGERNRLLLARLFLKPSN 460
|
170
....*....|....
gi 255708477 545 ILILDEATSALDSE 558
Cdd:PRK11147 461 LLILDEPTNDLDVE 474
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1005-1230 |
4.26e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1005 GKKPDTCEGNLEFREVSffypcrpdvfILRGLSLSIERGKTVAFVGSSGCGKSTsvqLLQRLYDPVQGQVLFDGV--DAK 1082
Cdd:PLN03211 66 GHKPKISDETRQIQERT----------ILNGVTGMASPGEILAVLGPSGSGKST---LLNALAGRIQGNNFTGTIlaNNR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1083 ELNVQWLRsQIAIVPQEPVLF-NCSIAENIAYGDNSRVVPLDEIKEAANAANihSFIE--GLPEKYNTQVG---LKGaqL 1156
Cdd:PLN03211 133 KPTKQILK-RTGFVTQDDILYpHLTVRETLVFCSLLRLPKSLTKQEKILVAE--SVISelGLTKCENTIIGnsfIRG--I 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 1157 SGGQKQRLAIARALLQKPKILLLDEATSALDNDSE-KVVQHALDKARTGRTCLVVTHRLSA--IQNADLIVVLHNGK 1230
Cdd:PLN03211 208 SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1032-1214 |
4.72e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.59 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGvdakELNVQWLRSQIAIVPQEPVLFncsiaeni 1111
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----KLRIGYVPQKLYLDTTLPLTV-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1112 aygdnSRVVPLdeiKEAANAANIHSFIEGLPEKYNTQVGLKgaQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSE 1191
Cdd:PRK09544 87 -----NRFLRL---RPGTKKEDILPALKRVQAGHLIDAPMQ--KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|....*
gi 255708477 1192 KVVQHALDKARTGRTC--LVVTHRL 1214
Cdd:PRK09544 157 VALYDLIDQLRRELDCavLMVSHDL 181
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1015-1221 |
6.57e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 1094
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQEPVLFNCSIAENIAYG--DNSRVVPLDEIKEAANAANIHSFIEGLpekyntqvglkgaqLSGGQKQRLAIARALLQ 1172
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDihFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 255708477 1173 KPKILLLDEATSALDNDSEKVVQHALDKART-GRTCLVVTHRLSAIQNAD 1221
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRAkGGAVLLTSHQDLPLNKAD 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1037-1241 |
6.73e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1037 SLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGvdaKELNV----QWLRSQIAIVP----QEPVLFNCSIA 1108
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIrsprDAIRAGIMLCPedrkAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1109 ENIAYGDNSRVVP----LDEIKEAANAAnihSFIEGLPEKY---NTQVGlkgaQLSGGQKQRLAIARALLQKPKILLLDE 1181
Cdd:PRK11288 350 DNINISARRHHLRagclINNRWEAENAD---RFIRSLNIKTpsrEQLIM----NLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 1182 ATSALDNDSEKVVQHAL-DKARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKI-----KEQGTHQELL 1241
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIagelaREQATERQAL 489
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
387-600 |
7.01e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.84 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPD-DGFIMVDEN--DIR--ALNVRHY- 460
Cdd:TIGR02633 259 EARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRnpAQAIRAGi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 461 ------RDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLvgekgAQMSGGQKQRIA 534
Cdd:TIGR02633 339 amvpedRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPI-----GRLSGGNQQKAV 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 535 IARALVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGML 600
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
411-592 |
9.26e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.80 E-value: 9.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 411 IKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFImvdENDIRalnvrhyrdhigvVSQEPvlfgttisnniKYGRDDvT 490
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLK-------------ISYKP-----------QYISPD-Y 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 491 DEEMERAAREANAYDFimeFPNKFNTLVGEK----------GAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESK 560
Cdd:COG1245 415 DGTVEEFLRSANTDDF---GSSYYKTEIIKPlgleklldknVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491
|
170 180 190
....*....|....*....|....*....|....
gi 255708477 561 SAVQAALEK--ASKGRTTIVVAHRLSTIrsaDLI 592
Cdd:COG1245 492 LAVAKAIRRfaENRGKTAMVVDHDIYLI---DYI 522
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
48-321 |
9.67e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 58.35 E-value: 9.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 48 MILGILASLVNGACLPLMPLVLGEMSDnlisgcLVQTNTTNYQNCTQSQEKLNEDMTLLTLY---YVGIGVAALIFGYIQ 124
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAID------AVFNGEASFLPLVPASLGPADPRGQLWLLgglTVAAFLLESLFQYLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 125 ISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGW 204
Cdd:cd18565 75 GVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 205 KLTLVTLSTSPLImasAAACSRMVISLTSKELSAYSKAGAVA---EEVLSSIRTVIAFRAQEKELQRYT---QNLKDAKd 278
Cdd:cd18565 155 QLALVALLPVPLI---IAGTYWFQRRIEPRYRAVREAVGDLNarlENNLSGIAVIKAFTAEDFERERVAdasEEYRDAN- 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 255708477 279 fgiKRTIasKVSLG---AVYFFMNGTYGLAFWYGTSLILNGEPGYT 321
Cdd:cd18565 231 ---WRAI--RLRAAffpVIRLVAGAGFVATFVVGGYWVLDGPPLFT 271
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
358-568 |
1.01e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.87 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 358 HIFQVIDKKPSIDNFSTAGYKPESieGTVEFKNVSFNYPSRPSIkiLKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRL 437
Cdd:PLN03073 483 HVDAVVNDPDYKFEFPTPDDRPGP--PIISFSDASFGYPGGPLL--FKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGE 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 438 YDPDDGFIMvdendiRALNVRhyrdhIGVVSQEPVLFGTTISNNIKYgrddvtdeeMERaareanAYDFIMEfpNKFNTL 517
Cdd:PLN03073 559 LQPSSGTVF------RSAKVR-----MAVFSQHHVDGLDLSSNPLLY---------MMR------CFPGVPE--QKLRAH 610
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 518 VGEKGAQ----------MSGGQKQRIAIARALVRNPKILILDEATSALDSEsksAVQAALE 568
Cdd:PLN03073 611 LGSFGVTgnlalqpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD---AVEALIQ 668
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
403-585 |
1.04e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 403 ILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQ-RLYDPD-DGFIMVDENDIRALNVRHyrdhIGVVSQEPVLF-GTTIS 479
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTKQILKR----TGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 480 NNIKYGRDDVTDEEMERAAREANAYDFIMEF--PNKFNTLVGEKGAQ-MSGGQKQRIAIARALVRNPKILILDEATSALD 556
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVISELglTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190
....*....|....*....|....*....|
gi 255708477 557 SESK-SAVQAALEKASKGRTTIVVAHRLST 585
Cdd:PLN03211 239 ATAAyRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
691-958 |
1.58e-08 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 57.41 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 691 FVVLGTLASVLngtvhpvFSIIFAKIITMFGNNDKTTLKHD-AEIYSMIFVILG--VICFVSYFMQGLFYGRAGEILTMR 767
Cdd:cd18547 7 LAIISTLLSVL-------GPYLLGKAIDLIIEGLGGGGGVDfSGLLRILLLLLGlyLLSALFSYLQNRLMARVSQRTVYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 768 LRHLAFKAMLYQDIAWFDekENSTGGLTTILAIDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGWEMTFLILSIAPV 847
Cdd:cd18547 80 LRKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 848 -LAVTGMI-------------ETAAMTGFANkdkqelkhagkiatEALENIRTIVSLTREKAFEQMYEEMLQTQhRNTSK 913
Cdd:cd18547 158 sLLVTKFIakrsqkyfrkqqkALGELNGYIE--------------EMISGQKVVKAFNREEEAIEEFDEINEEL-YKASF 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 255708477 914 KAQIIGSC-YAFSHAFIYFAYAAGFRFGAYLIQAGRMTPeGMFIVF 958
Cdd:cd18547 223 KAQFYSGLlMPIMNFINNLGYVLVAVVGGLLVINGALTV-GVIQAF 267
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
411-592 |
2.25e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 411 IKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDEndiralnvrhyrdhigvvsqepvlfgtTISNNIKYGRDD-- 488
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL---------------------------KISYKPQYIKPDyd 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 489 VTDEEMERAAreANAYD---FIMEFPNKFN--TLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAV 563
Cdd:PRK13409 415 GTVEDLLRSI--TDDLGssyYKSEIIKPLQleRLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 492
|
170 180 190
....*....|....*....|....*....|.
gi 255708477 564 QAALEK--ASKGRTTIVVAHRLSTIrsaDLI 592
Cdd:PRK13409 493 AKAIRRiaEEREATALVVDHDIYMI---DYI 520
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
407-565 |
2.44e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.43 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 407 LNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPD---DGFIMVDENDI-----RALNvRHYRDHIGVVSQEPVlfgTTI 478
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlnlpeKELN-KLRAEQISMIFQDPM---TSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 479 SNNIKYGrDDVTD--------------EE---MERAAREANAYDFIMEFPNKFntlvgekgaqmSGGQKQRIAIARALVR 541
Cdd:PRK09473 111 NPYMRVG-EQLMEvlmlhkgmskaeafEEsvrMLDAVKMPEARKRMKMYPHEF-----------SGGMRQRVMIAMALLC 178
|
170 180
....*....|....*....|....
gi 255708477 542 NPKILILDEATSALDseskSAVQA 565
Cdd:PRK09473 179 RPKLLIADEPTTALD----VTVQA 198
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
714-975 |
2.60e-08 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 57.02 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 714 AKII-TMFGNNDKTTLKHdaeiYSMIFVILGVICFVSYFMQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDEKenSTG 792
Cdd:cd18548 23 ADIIdEGIANGDLSYILR----TGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKF--GTS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 793 GLTTILAIDIAQIQgatgsrigvltqNATNMGL------------SVIISFIYGWEMTFLILSIAPVLAVT-GMIETAAM 859
Cdd:cd18548 97 SLITRLTNDVTQVQ------------NFVMMLLrmlvrapimligAIIMAFRINPKLALILLVAIPILALVvFLIMKKAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 860 TGFANKDKQeLKHAGKIATEALENIRTIVSLTREKA----FEQMYEEMlqtqhRNTSKKAQIIGSC-YAFSHAFIYFAYA 934
Cdd:cd18548 165 PLFKKVQKK-LDRLNRVVRENLTGIRVIRAFNREDYeeerFDKANDDL-----TDTSLKAGRLMALlNPLMMLIMNLAIV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 255708477 935 AGFRFGAYLIQAGRMTPeGMFIVFtaIAYGAMAIGETLVLA 975
Cdd:cd18548 239 AILWFGGHLINAGSLQV-GDLVAF--INYLMQILMSLMMLS 276
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1027-1212 |
2.63e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.63 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1027 RPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNvqwlRSQ-IAIVPQEPVL-FN 1104
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRfMAYLGHLPGLkAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1105 CSIAENIAY-----GDNSRVVPldeikeaANAANIhsfiEGLPEKYNTQVglkgAQLSGGQKQRLAIARALLQKPKILLL 1179
Cdd:PRK13543 97 LSTLENLHFlcglhGRRAKQMP-------GSALAI----VGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLL 161
|
170 180 190
....*....|....*....|....*....|....
gi 255708477 1180 DEATSALDNDSEKVVQHALD-KARTGRTCLVVTH 1212
Cdd:PRK13543 162 DEPYANLDLEGITLVNRMISaHLRGGGAALVTTH 195
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
386-611 |
2.69e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 56.70 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHY---RD 462
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 463 HIGVVSQEPVLF-GTTISNNIKYGRDDVTD--EEMERAAreanaydFIMEFpnkfnTLVGEKGA------QMSGGQKQRI 533
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAYPLREHTQlpAPLLHST-------VMMKL-----EAVGLRGAaklmpsELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 534 AIARALVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAELM 610
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQ 232
|
.
gi 255708477 611 A 611
Cdd:PRK11831 233 A 233
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1015-1195 |
2.81e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.33 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPDVFilRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLfdgvdakelnvqwlRS--- 1091
Cdd:PLN03073 509 ISFSDASFGYPGGPLLF--KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF--------------RSakv 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1092 QIAIVPQEPVlfncsiaeniaYGDNSRVVPLDEIkeaanaanIHSFiEGLPE-KYNTQVGLKGAQ----------LSGGQ 1160
Cdd:PLN03073 573 RMAVFSQHHV-----------DGLDLSSNPLLYM--------MRCF-PGVPEqKLRAHLGSFGVTgnlalqpmytLSGGQ 632
|
170 180 190
....*....|....*....|....*....|....*.
gi 255708477 1161 KQRLAIARALLQKPKILLLDEATSALDNDS-EKVVQ 1195
Cdd:PLN03073 633 KSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
397-558 |
2.97e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.63 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 397 SRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVD-ENDIRALNVRH--YRDHIGVVSQEPvl 473
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDgKTATRGDRSRFmaYLGHLPGLKADL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 474 fgTTISN----NIKYGRddvtdeemeRAAREANAYDFIMEFPNKFNTLVgekgAQMSGGQKQRIAIARALVRNPKILILD 549
Cdd:PRK13543 98 --STLENlhflCGLHGR---------RAKQMPGSALAIVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLD 162
|
....*....
gi 255708477 550 EATSALDSE 558
Cdd:PRK13543 163 EPYANLDLE 171
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
410-609 |
3.08e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.06 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 410 RIKSGETVALVGLNGSGKSTVVQLLQRLYD-PddGFIMVDE-----NDIRALNVRHYRDHIG----VVSQEPVL------ 473
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVMAEKlefngQDLQRISEKERRNLVGaevaMIFQDPMTslnpcy 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 474 -FGTTISNNIKygrddvTDEEMERAAREANAYDFImefpnkfnTLVGEKGA---------QMSGGQKQRIAIARALVRNP 543
Cdd:PRK11022 107 tVGFQIMEAIK------VHQGGNKKTRRQRAIDLL--------NQVGIPDPasrldvyphQLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 544 KILILDEATSALDseskSAVQAA-----LE-KASKGRTTIVVAHRLSTI-RSADLIVTLKDGMLAEKGAHAEL 609
Cdd:PRK11022 173 KLLIADEPTTALD----VTIQAQiiellLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
48-330 |
3.12e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 56.78 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 48 MILGILASLVNGACLPLMPLVLGEMSDNLisgclvqtnttnyqncTQSQEKLNEdmtLLTLYYVGIGVAAL--IFGYIQI 125
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLV----------------TIGSKSLGL---LLGLALLLLGAYLLraLLNFLRI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 126 SLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGWK 205
Cdd:cd18778 62 YLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 206 LTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYtqnlkDAKDFGIKRTI 285
Cdd:cd18778 142 LALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRF-----EALSRRYRKAQ 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 255708477 286 ASKVSLGAVYF-FMNGT----YGLAFWYGTSLILNGEpgYTIGTVLAVFF 330
Cdd:cd18778 217 LRAMKLWAIFHpLMEFLtslgTVLVLGFGGRLVLAGE--LTIGDLVAFLL 264
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
386-556 |
3.57e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 386 VEFKNVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRlyDPDDGFimvdENDIRALNVRH------ 459
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGY----SNDLTLFGRRRgsgeti 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 460 --YRDHIGVVSQEPVL---FGTTISNNIKYGRDD-------VTDEEMERA----------AREANAydfimefpnKFNTL 517
Cdd:PRK10938 332 wdIKKHIGYVSSSLHLdyrVSTSVRNVILSGFFDsigiyqaVSDRQQKLAqqwldilgidKRTADA---------PFHSL 402
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 255708477 518 vgekgaqmSGGQkQRIA-IARALVRNPKILILDEATSALD 556
Cdd:PRK10938 403 --------SWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
107-328 |
4.53e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 56.05 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 107 TLYYVGIGVAALIFGYI-------QISLWIitAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTdDIDKISDGIG 179
Cdd:cd18566 40 TLQVLVIGVVIAILLESllrllrsYILAWI--GARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLN-SLEQIREFLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 180 DKIALLFQNMSTFSIGLAVGLVKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAF 259
Cdd:cd18566 117 GQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAM 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 260 RAQEKELQRYTQNLKDAKDFGIKRTI--ASKVSLGAVyfFMNGTYGLAFWYGTSLILNGEpgYTIGTVLAV 328
Cdd:cd18566 197 AMEPQMLRRYERLQANAAYAGFKVAKinAVAQTLGQL--FSQVSMVAVVAFGALLVINGD--LTVGALIAC 263
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1028-1230 |
6.65e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1028 PDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGvdaKELNV----QWLRSQIAIVPQE-PVL 1102
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFksskEALENGISMVHQElNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1103 FNCSIAENIAYGDNSRVVP-LDEIKEAANAANIhsFIEgLPEKYNTQVglKGAQLSGGQKQRLAIARALLQKPKILLLDE 1181
Cdd:PRK10982 86 LQRSVMDNMWLGRYPTKGMfVDQDKMYRDTKAI--FDE-LDIDIDPRA--KVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1182 ATSALdndSEKVVQH---ALDKARTgRTCLVV--THRLSAI-QNADLIVVLHNGK 1230
Cdd:PRK10982 161 PTSSL---TEKEVNHlftIIRKLKE-RGCGIVyiSHKMEEIfQLCDEITILRDGQ 211
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
387-556 |
8.31e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.34 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 387 EFKNVSFNYPSRPSIKILKGLNLRIKSGETVALVGLNGSGKS-TVVQLLQRLYDPD-DGFIMVDENDIRALNVRH----- 459
Cdd:NF040905 259 EVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRNiSGTVFKDGKEVDVSTVSDaidag 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 460 --Y----RDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREanaydfimEFPNKFNTL---VGEKGAQMSGGQK 530
Cdd:NF040905 339 laYvtedRKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAE--------EYRKKMNIKtpsVFQKVGNLSGGNQ 410
|
170 180
....*....|....*....|....*.
gi 255708477 531 QRIAIARALVRNPKILILDEATSALD 556
Cdd:NF040905 411 QKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1034-1231 |
8.89e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1034 RGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNV-QWLRSQIAIVP---QEPVLF-NCSIA 1108
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaQRLARGLVYLPedrQSSGLYlDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1109 ENI-AYGDNSRVVPLDEIKEAAnaanihsfiegLPEKYNTQVGLKGAQ-------LSGGQKQRLAIARALLQKPKILLLD 1180
Cdd:PRK15439 360 WNVcALTHNRRGFWIKPARENA-----------VLERYRRALNIKFNHaeqaartLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 1181 EATSALD----NDSEKVVQHAldkARTGRTCLVVTHRLSAI-QNADLIVVLHNGKI 1231
Cdd:PRK15439 429 EPTRGVDvsarNDIYQLIRSI---AAQNVAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
734-960 |
1.09e-07 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 55.11 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 734 IYSMIFVILGVICFV-SYFMQGLFYGrAGEILTMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQGATGsr 812
Cdd:cd18541 41 RYALLILLLALLIGIfRFLWRYLIFG-ASRRIEYDLRNDLFAHLLTLSPSFYQK--NRTGDLMARATNDLNAVRMALG-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 813 IGVLTQ-NATNMGLSVIISFIY-GWEMTFLILSIAPVLAVTGM-IETAAMTGFanKDKQElkHAGKIATEALEN---IRT 886
Cdd:cd18541 116 PGILYLvDALFLGVLVLVMMFTiSPKLTLIALLPLPLLALLVYrLGKKIHKRF--RKVQE--AFSDLSDRVQESfsgIRV 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 887 IVSLTREKAFEQMYEEMLQtQHRNTSKK-AQIIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRMTPeGMFIVFTA 960
Cdd:cd18541 192 IKAFVQEEAEIERFDKLNE-EYVEKNLRlARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITL-GDLVAFNS 264
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1032-1190 |
1.13e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.42 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTsvqLLQRL------YDPVQGQVLFDGVDAKELNVQWlRSQIAIVPQEPVLF-N 1104
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCST---LLKALanrtegNVSVEGDIHYNGIPYKEFAEKY-PGEIIYVSEEDVHFpT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1105 CSIAENIaygdnsrvvpldeikEAANAANIHSFIEGLpekyntqvglkgaqlSGGQKQRLAIARALLQKPKILLLDEATS 1184
Cdd:cd03233 98 LTVRETL---------------DFALRCKGNEFVRGI---------------SGGERKRVSIAEALVSRASVLCWDNSTR 147
|
....*.
gi 255708477 1185 ALDNDS 1190
Cdd:cd03233 148 GLDSST 153
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
390-590 |
1.32e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 390 NVSFNYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRAlNVRHYRDHIGVVSQ 469
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 470 EpvlfgTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGekgaQMSGGQKQRIAIARALVRNPKILILD 549
Cdd:PRK13540 82 R-----SGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 255708477 550 EATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRSAD 590
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEhRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
377-560 |
1.45e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 377 YKPESI-EGTVEFKNVSFNYPSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYdPD--DGFIMVDEndiR 453
Cdd:PRK13549 250 REPHTIgEVILEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGrwEGEIFIDG---K 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 454 ALNVRHYRDHI--------------GVVSQEPVLFGTTISNNIKYGRDDVTDEemerAAREANAYDFIMEFPNKFNTLVg 519
Cdd:PRK13549 326 PVKIRNPQQAIaqgiamvpedrkrdGIVPVMGVGKNITLAALDRFTGGSRIDD----AAELKTILESIQRLKVKTASPE- 400
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 255708477 520 EKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESK 560
Cdd:PRK13549 401 LAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAK 441
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
691-960 |
1.57e-07 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 54.40 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 691 FVVLGTLASVLNgtvhPVFSiifaKIITmfgnnDKTTLKHDAE---IYSMIFVILGVICFVSYFMQGLFYGRAGEILTMR 767
Cdd:cd18545 8 LMLLSTAASLAG----PYLI----KIAI-----DEYIPNGDLSgllIIALLFLALNLVNWVASRLRIYLMAKVGQRILYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 768 LRHLAFKAMLYQDIAWFDEKEnsTGGLTTILAIDIAQIQGA-TGSRIGVLTQNATNMGLsVIISFIYGWEMTFLILSIAP 846
Cdd:cd18545 75 LRQDLFSHLQKLSFSFFDSRP--VGKILSRVINDVNSLSDLlSNGLINLIPDLLTLVGI-VIIMFSLNVRLALVTLAVLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 847 VL-AVTGMIETAAMTGFankdkQELKHagKIAT------EALENIRTIVSLTREKAFEQMYEEmLQTQHRNTSKKAQ--- 916
Cdd:cd18545 152 LLvLVVFLLRRRARKAW-----QRVRK--KISNlnaylhESISGIRVIQSFAREDENEEIFDE-LNRENRKANMRAVrln 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 255708477 917 -----IIGSCYAFSHAFIYFayaagfrFGAYLIQAGRMTPeGMFIVFTA 960
Cdd:cd18545 224 alfwpLVELISALGTALVYW-------YGGKLVLGGAITV-GVLVAFIG 264
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
411-593 |
2.50e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 411 IKSGETVALVGLNGSGKSTVV-----QLLQRLYDPDDG------------------FIMVDENDIRALNVRHYRDHIgvv 467
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVkilsgELIPNLGDYEEEpswdevlkrfrgtelqnyFKKLYNGEIKVVHKPQYVDLI--- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 468 sqeP-VLFGTTisnnikygrddvtdEEMERAAREANAYDFIMEFPNkFNTLVGEKGAQMSGGQKQRIAIARALVRNPKIL 546
Cdd:PRK13409 173 ---PkVFKGKV--------------RELLKKVDERGKLDEVVERLG-LENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255708477 547 ILDEATSALDSESKSAVQAALEKASKGRTTIVVAHrlstirsaDLIV 593
Cdd:PRK13409 235 FFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEH--------DLAV 273
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
385-611 |
3.08e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.16 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 385 TVEFKNVSFnYPSRPsikILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPD----DGFIMVDENDIRALNVRHy 460
Cdd:PRK10418 4 QIELRNIAL-QAAQP---LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCALRG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 461 rDHIGVVSQEP-VLFG----------TTISNNIKYGRDDVTDEEM-----ERAAREANAYDFimefpnkfntlvgekgaQ 524
Cdd:PRK10418 79 -RKIATIMQNPrSAFNplhtmhtharETCLALGKPADDATLTAALeavglENAARVLKLYPF-----------------E 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 525 MSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK--ASKGRTTIVVAHRLSTI-RSADLIVTLKDGMLA 601
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIV 220
|
250
....*....|
gi 255708477 602 EKGAHAELMA 611
Cdd:PRK10418 221 EQGDVETLFN 230
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
389-559 |
3.12e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 389 KNVSFNYPsrPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENdiralnvrhYRdhIGVVS 468
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG---------IK--VGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 469 QEPVLfgttisNNIKYGRDDVtdEEMERAAREA-NAYDFIM----EFPNKFNTLVGEKG--------------------- 522
Cdd:PRK11819 77 QEPQL------DPEKTVRENV--EEGVAEVKAAlDRFNEIYaayaEPDADFDALAAEQGelqeiidaadawdldsqleia 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 255708477 523 -------------AQMSGGQKQRIAIARALVRNPKILILDEATSALDSES 559
Cdd:PRK11819 149 mdalrcppwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
412-585 |
3.24e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.79 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 412 KSGETVALVGLNGSGKSTVVQLLQ-----RLYDPDDGfimVDENDIralnVRHYRdhigvvsqepvlfGTTISNNIKygr 486
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSgelkpNLGDYDEE---PSWDEV----LKRFR-------------GTELQDYFK--- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 487 dDVTDEEMeRAAREANAYDFI-MEFPNKFNTL---VGEKGA-------------------QMSGGQKQRIAIARALVRNP 543
Cdd:COG1245 154 -KLANGEI-KVAHKPQYVDLIpKVFKGTVRELlekVDERGKldelaeklglenildrdisELSGGELQRVAIAAALLRDA 231
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255708477 544 KILILDEATSALD-SESKSAVQAALEKASKGRTTIVVAHRLST 585
Cdd:COG1245 232 DFYFFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAI 274
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
738-960 |
5.29e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 52.90 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 738 IFVILGVICFVSYFMQGLFyGRAGEILTMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQGATGSRIGVLT 817
Cdd:cd18564 60 LVGIALLRGLASYAGTYLT-ALVGQRVVLDLRRDLFAHLQRLSLSFHDR--RRTGDLLSRLTGDVGAIQDLLVSGVLPLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 818 QNATNMGLSVIISFIYGWEMTFLILSIAPVLAVTGMIETAAMTGFAnkdKQELKHAGKIAT---EALENIRTIVSLTREK 894
Cdd:cd18564 137 TNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEAS---REQRRREGALASvaqESLSAIRVVQAFGREE 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 895 AFEQMYEEmLQTQHRNTSKKAQIIGSCY--------AFSHAFIYFayaagfrFGAYLIQAGRMTPeGMFIVFTA 960
Cdd:cd18564 214 HEERRFAR-ENRKSLRAGLRAARLQALLspvvdvlvAVGTALVLW-------FGAWLVLAGRLTP-GDLLVFLA 278
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
393-608 |
6.81e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 393 FNYPSRP------SIKILKGLNLR------IKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDEndiRALNVRHY 460
Cdd:PRK11288 246 YGYRPRPlgevrlRLDGLKGPGLRepisfsVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSP 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 461 RDHI--GVV------SQEPVLFGTTISNNIKYG--RDDVTDEEMERAAREA-NAYDFI----MEFPNKfNTLVGekgaQM 525
Cdd:PRK11288 323 RDAIraGIMlcpedrKAEGIIPVHSVADNINISarRHHLRAGCLINNRWEAeNADRFIrslnIKTPSR-EQLIM----NL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 526 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL-EKASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEK 603
Cdd:PRK11288 398 SGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGE 477
|
....*
gi 255708477 604 GAHAE 608
Cdd:PRK11288 478 LAREQ 482
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1028-1227 |
7.81e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.98 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1028 PDVFILRGLSlSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQ---------VL--FDGVDAKELNVQWLRSQI--A 1094
Cdd:cd03236 12 PNSFKLHRLP-VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeILdeFRGSELQNYFTKLLEGDVkvI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 IVPQE----PVLFNCSIAENIAYGDNSRVvpLDEIKEAANaanihsfIEGLPEKyntqvglKGAQLSGGQKQRLAIARAL 1170
Cdd:cd03236 91 VKPQYvdliPKAVKGKVGELLKKKDERGK--LDELVDQLE-------LRHVLDR-------NIDQLSGGELQRVAIAAAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1171 LQKPKILLLDEATSALDndsekvVQHALDKART-------GRTCLVVTHRLSAIQN-ADLIVVLH 1227
Cdd:cd03236 155 ARDADFYFFDEPSSYLD------IKQRLNAARLirelaedDNYVLVVEHDLAVLDYlSDYIHCLY 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
407-601 |
9.07e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 407 LNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHyRDHIGVV-----SQEPVLF------- 474
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylpedRQSSGLYldaplaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 475 ---GTTISNN---IKYGRDDVTdeeMERAAREANAydfimefpnKFNTLvgEKGAQ-MSGGQKQRIAIARALVRNPKILI 547
Cdd:PRK15439 361 nvcALTHNRRgfwIKPARENAV---LERYRRALNI---------KFNHA--EQAARtLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 548 LDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLA 601
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRSiAAQNVAVLFISSDLEEIEQmADRVLVMHQGEIS 482
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
369-588 |
9.30e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 369 IDN-FSTAGYKPESIEGTV-EFKNVSFNYPSRpsiKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIM 446
Cdd:PRK10636 294 VDNpFHFSFRAPESLPNPLlKMEKVSAGYGDR---IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 447 VdendirALNVRhyrdhIGVVSQepvlfgttisNNIKYGRDD---------VTDEEMERAAReanayDFIMEFPNKFNTl 517
Cdd:PRK10636 371 L------AKGIK-----LGYFAQ----------HQLEFLRADesplqhlarLAPQELEQKLR-----DYLGGFGFQGDK- 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 518 VGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL---EKAskgrtTIVVAHRLSTIRS 588
Cdd:PRK10636 424 VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALidfEGA-----LVVVSHDRHLLRS 492
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
45-331 |
1.12e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 51.71 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 45 ITLMILGILASLVNGaclpLMPLVLGEMSDNLISGclvqtnttnyqnctqsqeKLNEDMTLLTLYYVGIGV--AALIFGY 122
Cdd:cd18540 5 ILLIILMLLVALLDA----VFPLLTKYAIDHFITP------------------GTLDGLTGFILLYLGLILiqALSVFLF 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 123 IQISLWIitAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISD----GIGDkialLFQNMSTFSIGLAV 198
Cdd:cd18540 63 IRLAGKI--EMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEiiswGLVD----LVWGITYMIGILIV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 199 GLVKGWKLTLVTLSTSPLIMASAA-------ACSRMVISLTSKELSAYSkagavaeEVLSSIRTVIAFRAQEK---ELQR 268
Cdd:cd18540 137 MLILNWKLALIVLAVVPVLAVVSIyfqkkilKAYRKVRKINSRITGAFN-------EGITGAKTTKTLVREEKnlrEFKE 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 269 YTQNLKDAkdfGIKRTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGepGYTIGTvLAVFFS 331
Cdd:cd18540 210 LTEEMRRA---SVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAG--AITIGT-LVAFIS 266
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
404-595 |
1.15e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 51.46 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 404 LKGLNLRIKSGETVALVGLNGSGKSTVVQ------LLQRLYDPDDGFIMVDEndIRALNvrhYRDHIGVVSQEPVlfGTT 477
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLHLKKEQPGNHDR--IEGLE---HIDKVIVIDQSPI--GRT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 478 ISNN------------------------------IKY-GR--DDVTDEEMEraareaNAYDFIMEFP---NKFNTLV--- 518
Cdd:cd03271 84 PRSNpatytgvfdeirelfcevckgkrynretleVRYkGKsiADVLDMTVE------EALEFFENIPkiaRKLQTLCdvg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 519 ------GEKGAQMSGGQKQRIAIARALVR---NPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRS 588
Cdd:cd03271 158 lgyiklGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNLDVIKC 237
|
....*..
gi 255708477 589 ADLIVTL 595
Cdd:cd03271 238 ADWIIDL 244
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
411-586 |
1.24e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.88 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 411 IKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDendiralnvrhyrdhigvvsqepvlfGTTISNNIKYgrddvt 490
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD--------------------------GITPVYKPQY------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 491 deemeraareanaydfimefpnkfntlvgekgAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKA 570
Cdd:cd03222 70 --------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170
....*....|....*...
gi 255708477 571 SK--GRTTIVVAHRLSTI 586
Cdd:cd03222 118 SEegKKTALVVEHDLAVL 135
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
739-958 |
1.42e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 51.80 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 739 FVILGVICFVSYFMQGLF---YGRAGEILTMRLRHL----AFKAMLYQDIAWFDEKenSTGGLTTILAIDIAQIQGATGS 811
Cdd:cd18565 53 LWLLGGLTVAAFLLESLFqylSGVLWRRFAQRVQHDlrtdTYDHVQRLDMAFFEDR--QTGDLMSVLNNDVNQLERFLDD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 812 RIGVLTQNATNMGLSVIISFIYGWEMTFLILSIAPVLAVTGMIetaamtgFANK------DKQElkHAGKIATeALEN-- 883
Cdd:cd18565 131 GANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYW-------FQRRiepryrAVRE--AVGDLNA-RLENnl 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 884 --IRTIVSLTREkAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFShafIYFAYAAGFR----FGAYLIQAGRMTPE----- 952
Cdd:cd18565 201 sgIAVIKAFTAE-DFERERVADASEEYRDANWRAIRLRAAFFPV---IRLVAGAGFVatfvVGGYWVLDGPPLFTgtltv 276
|
....*.
gi 255708477 953 GMFIVF 958
Cdd:cd18565 277 GTLVTF 282
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1038-1190 |
1.64e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1038 LSIERGKTVAFVGSSGCGKSTSVQLLQRlydpvqGQVLFDG--VDAKELNVQWLRsqiaivpQEP------VLFNcSIAE 1109
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNG------EVLLDDGriIYEQDLIVARLQ-------QDPprnvegTVYD-FVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1110 NIA--------YGDNSRVVPLD-------------EIKEAANAANIHSFIEGLPEkyntQVGLKG----AQLSGGQKQRL 1164
Cdd:PRK11147 90 GIEeqaeylkrYHDISHLVETDpseknlnelaklqEQLDHHNLWQLENRINEVLA----QLGLDPdaalSSLSGGWLRKA 165
|
170 180
....*....|....*....|....*.
gi 255708477 1165 AIARALLQKPKILLLDEATSALDNDS 1190
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1156-1240 |
1.75e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.71 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1156 LSGGQKQRLAIARALLQK---PKILLLDEATSALDNDSEK----VVQHALDKartGRTCLVVTHRLSAIQNADLIVVL-- 1226
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLVDK---GNTVVVIEHNLDVIKTADYIIDLgp 906
|
90
....*....|....*...
gi 255708477 1227 ----HNGKIKEQGTHQEL 1240
Cdd:TIGR00630 907 eggdGGGTVVASGTPEEV 924
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1032-1215 |
1.80e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1032 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLL--QRLYDPVQGQVLFDGVDAKE---LNVQWLRSQIAI-VPQ----EPV 1101
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKKQetfARISGYCEQNDIhSPQvtvrESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1102 LFNCSIAENIAYGDNSRVVPLDEIKEAANAANIHSFIEGLPekyntqvGLKGaqLSGGQKQRLAIARALLQKPKILLLDE 1181
Cdd:PLN03140 975 IYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPSIIFMDE 1045
|
170 180 190
....*....|....*....|....*....|....*
gi 255708477 1182 ATSALDNDSEKVVQHAL-DKARTGRTCLVVTHRLS 1215
Cdd:PLN03140 1046 PTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
99-327 |
1.89e-06 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 51.30 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 99 LNEDMTLLTLYYVGIGVAALIFGYI--QISLWIIT------AARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDD 170
Cdd:cd18549 29 IDDLLPSKNLRLILIIGAILLALYIlrTLLNYFVTywghvmGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITND 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 171 IDKISD----GIGDkialLFQNMSTFSIGLAVGLVKGWKLTLVTLSTSPLIMASAAACSR--MVISLTSKElsAYSKAGA 244
Cdd:cd18549 109 LFDISElahhGPED----LFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKkmKKAFRRVRE--KIGEINA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 245 VAEEVLSSIRTVIAFRAQEKELQRY---TQNLKDAKDFGIKrtiASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEpgYT 321
Cdd:cd18549 183 QLEDSLSGIRVVKAFANEEYEIEKFdegNDRFLESKKKAYK---AMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGE--IT 257
|
....*.
gi 255708477 322 IGTVLA 327
Cdd:cd18549 258 LGDLVA 263
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1039-1212 |
2.03e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 50.48 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1039 SIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDakelnvqwlrsqIAIVPQEpvlfncsiaenIAYGDNSR 1118
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT------------VSYKPQY-----------IKADYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1119 VVPLdeIKEAANAANIHSF----------IEGLpekYNTQVglkgAQLSGGQKQRLAIARALLQKPKILLLDEATSALDN 1188
Cdd:cd03237 78 VRDL--LSSITKDFYTHPYfkteiakplqIEQI---LDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180
....*....|....*....|....*...
gi 255708477 1189 DSE----KVVQHALDKARtgRTCLVVTH 1212
Cdd:cd03237 149 EQRlmasKVIRRFAENNE--KTAFVVEH 174
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
404-595 |
2.13e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.32 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 404 LKGLNLRIKSGETVALVGLNGSGKSTVVQ------LLQRLYDPDDGFIMVDenDIRALNvrhYRDHIGVVSQEPV----- 472
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypaLANRLNGAKTVPGRYT--SIEGLE---HLDKVIHIDQSPIgrtpr 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 473 ---------------LFGTT------------ISNNIKYGR------DDVTDEEM---------------ERAAREA--- 501
Cdd:TIGR00630 699 snpatytgvfdeireLFAETpeakvrgytpgrFSFNVKGGRceacqgDGVIKIEMhflpdvyvpcevckgKRYNRETlev 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 502 ----------------NAYDFIMEFPN---KFNTLV---------GEKGAQMSGGQKQRIAIARALVR---NPKILILDE 550
Cdd:TIGR00630 779 kykgkniadvldmtveEAYEFFEAVPSisrKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDE 858
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 255708477 551 ATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRSADLIVTL 595
Cdd:TIGR00630 859 PTTGLHFDDIKKLLEVLQRlVDKGNTVVVIEHNLDVIKTADYIIDL 904
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
100-337 |
2.82e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 50.59 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 100 NEDMTLLTLYYVGIGVAALIFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMtDDIDKISDGIG 179
Cdd:cd18555 38 LNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 180 DKIALLFQNMSTFSIGLAVGLVKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAF 259
Cdd:cd18555 117 NQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSL 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 260 RAQEKELQRYTQNLKDAKDFGIKRTIASKVsLGAVYFFMNGTYGLA-FWYGTSLILNGEpgYTIGTVLAvfFSVIHSSY 337
Cdd:cd18555 197 GSEKNIYKKWENLFKKQLKAFKKKERLSNI-LNSISSSIQFIAPLLiLWIGAYLVINGE--LTLGELIA--FSSLAGSF 270
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
401-607 |
2.94e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.77 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 401 IKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRlyDPDDGFImvdENDIRALNVRHYRDHIGVVS------------ 468
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI---EGDIRISGFPKKQETFARISgyceqndihspq 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 469 ---QEPVLFGTTISNNIKYGRDD---VTDEEMEraareanaydfIMEFPNKFNTLVGEKGAQ-MSGGQKQRIAIARALVR 541
Cdd:PLN03140 968 vtvRESLIYSAFLRLPKEVSKEEkmmFVDEVME-----------LVELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVA 1036
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708477 542 NPKILILDEATSALDSESKSAVQAALEKA-SKGRTTIVVAHRlstiRSADLIVTLKDGMLAEKGAHA 607
Cdd:PLN03140 1037 NPSIIFMDEPTSGLDARAAAIVMRTVRNTvDTGRTVVCTIHQ----PSIDIFEAFDELLLMKRGGQV 1099
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1156-1241 |
3.08e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.16 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1156 LSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALD--KARTGRTCLVVTHRLSAIQNADLIVVLHNGKI-- 1231
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINqfKAEGLSIILVSSEMPEVLGMSDRILVMHEGRIsg 475
|
90
....*....|...
gi 255708477 1232 ---KEQGTHQELL 1241
Cdd:PRK10762 476 eftREQATQEKLM 488
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
737-915 |
3.15e-06 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 50.55 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 737 MIFVILGVICFVSYFMQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDekENSTGGLTTILAIDIAQIQGATGSRIGVL 816
Cdd:cd18589 40 TVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 817 TQNATNMGLSVIISFIYGWEMTFLILSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKAF 896
Cdd:cd18589 118 MWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGE 197
|
170
....*....|....*....
gi 255708477 897 EQMYEEMLQTQHRNTSKKA 915
Cdd:cd18589 198 AQRYRQRLQKTYRLNKKEA 216
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
400-557 |
3.74e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 50.77 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 400 SIKI-----LKGLNLRIKSGETVaLVGLNGSGKSTVVQLLQRLYDPDDGfIMVDENDI-RALNVRHYRDHIGVVsqepvl 473
Cdd:COG3593 5 KIKIknfrsIKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSS-RKFDEEDFyLGDDPDLPEIEIELT------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 474 FGTTISNNIKYGRDDVTDEEMERAAREANAyDFIMEFpNKFNTLVGEKGAQMSGGQKQRIAIA----RALVRNPKILILD 549
Cdd:COG3593 77 FGSLLSRLLRLLLKEEDKEELEEALEELNE-ELKEAL-KALNELLSEYLKELLDGLDLELELSldelEDLLKSLSLRIED 154
|
....*...
gi 255708477 550 EATSALDS 557
Cdd:COG3593 155 GKELPLDR 162
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1033-1242 |
5.18e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKST------SVQLLQrlydpvQGQV-LFDG--VDAKELNVqwLRSQIAIVPQ----- 1098
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSllsliaGARKIQ------QGRVeVLGGdmADARHRRA--VCPRIAYMPQglgkn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1099 -EPVLfncSIAENIA-----YGDNSRvvpldE----IKEAANAANIHSFIEGLPEKyntqvglkgaqLSGGQKQRLAIAR 1168
Cdd:NF033858 89 lYPTL---SVFENLDffgrlFGQDAA-----ErrrrIDELLRATGLAPFADRPAGK-----------LSGGMKQKLGLCC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1169 ALLQKPKILLLDEATSALDNDSEKvvQ-----HALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLR 1242
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSRR--QfweliDRIRAERPGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLA 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1029-1231 |
7.59e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1029 DVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQV-LFDGVDA---KELNVQWLRSqiaivpqepvlfn 1104
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLgyfAQHQLEFLRA------------- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1105 csiaeniaygDNSRVVPLDEIKEAANAANIHSFIEGLPEKyNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATS 1184
Cdd:PRK10636 391 ----------DESPLQHLARLAPQELEQKLRDYLGGFGFQ-GDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255708477 1185 ALDNDSEKVVQHAL---DKArtgrtCLVVTHRLSAIQN-ADLIVVLHNGKI 1231
Cdd:PRK10636 460 HLDLDMRQALTEALidfEGA-----LVVVSHDRHLLRStTDDLYLVHDGKV 505
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
93-273 |
7.84e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 49.04 E-value: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 93 TQSQEKLNEDMTLLTLYYVGIGVAALIFGYIQISLWIITAARQT-KRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDI 171
Cdd:cd18580 27 SDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRAsRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 172 DKISDGIGDKIALLFQNMSTFSIGLAvglvkgwkltlVTLSTSPLIMASAAACSRMVISL------TSKEL--------- 236
Cdd:cd18580 107 GLIDEELPLALLDFLQSLFSVLGSLI-----------VIAIVSPYFLIVLPPLLVVYYLLqryylrTSRQLrrlesesrs 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 255708477 237 ---SAYSkagavaeEVLSSIRTVIAFRAQEKELQRYTQNL 273
Cdd:cd18580 176 plySHFS-------ETLSGLSTIRAFGWQERFIEENLRLL 208
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1015-1246 |
8.88e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1015 LEFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVlfdgvdakelnvQWlrsqia 1094
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KW------ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1095 ivpqepvlfncsiAENIAYGdnsrVVPLDEIKEAANAANIHSFIEGL-PEKYNTQV--GLKGAQL-------------SG 1158
Cdd:PRK15064 379 -------------SENANIG----YYAQDHAYDFENDLTLFDWMSQWrQEGDDEQAvrGTLGRLLfsqddikksvkvlSG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1159 GQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKArTGrTCLVVTH-R--LSAIQNAdLIVVLHNGKIKEQG 1235
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdRefVSSLATR-IIEITPDGVVDFSG 518
|
250
....*....|.
gi 255708477 1236 THQELLRNRDI 1246
Cdd:PRK15064 519 TYEEYLRSQGI 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
411-560 |
1.19e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.62 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 411 IKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIralNVRHYRDHI--GVV------SQEPVLFGTTISNNI 482
Cdd:PRK10762 275 LRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV---VTRSPQDGLanGIVyisedrKRDGLVLGMSVKENM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 483 ----------KYGRDDVTDEEMEraareanAYDFIMEF----PNKfNTLVGEkgaqMSGGQKQRIAIARALVRNPKILIL 548
Cdd:PRK10762 352 sltalryfsrAGGSLKHADEQQA-------VSDFIRLFniktPSM-EQAIGL----LSGGNQQKVAIARGLMTRPKVLIL 419
|
170
....*....|..
gi 255708477 549 DEATSALDSESK 560
Cdd:PRK10762 420 DEPTRGVDVGAK 431
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
767-975 |
1.38e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 48.35 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 767 RLRHLAFKAMLYQDIAWFdEKENSTGGLTTILAIDiaQIQGATGSRIGVLTQNATNMGLSVIISFIYGWEMTFLILSIAP 846
Cdd:cd18566 76 RLSNAAFEHLLSLPLSFF-EREPSGAHLERLNSLE--QIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 847 VLAVTGMI------ETAAMTGFANKDKQELkhagkiATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGS 920
Cdd:cd18566 153 LFVLVAILlgpilrRALKERSRADERRQNF------LIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAV 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 921 CYAFSHAFIYFAYAAGFRFGAYLIQAGRMTpEGMFIVFTAIAYGAMAIGETLVLA 975
Cdd:cd18566 227 AQTLGQLFSQVSMVAVVAFGALLVINGDLT-VGALIACTMLSGRVLQPLQRAFGL 280
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
408-611 |
1.56e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 408 NLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHY---------RDHIGVVSQEPVLFGTTI 478
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLqklvsdewqRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 479 SNNIKygrDDVTDEEmeRAAREAnAYDFIMefpnkfnTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSE 558
Cdd:PRK10938 103 AEIIQ---DEVKDPA--RCEQLA-QQFGIT-------ALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 559 SKSAVQAALEK-ASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLAEKGAHAELMA 611
Cdd:PRK10938 170 SRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1155-1227 |
1.64e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.01 E-value: 1.64e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 1155 QLSGGQKQRLAIARALLQKPKILLLDEATSALD-NDSEKVVQHALDKARTGRTCLVVTHRLsAIQN--ADLIVVLH 1227
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDL-AILDylADYVHILY 286
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
734-958 |
1.93e-05 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 47.81 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 734 IYSMIFVILGVIcFVSYFMQGL-FY--GRAGEILTMRLRHLAFKAMLYQDIAWFDekENSTGGLTTILAIDIAQIQGATG 810
Cdd:cd18551 35 SGGLLALLVALF-LLQAVLSALsSYllGRTGERVVLDLRRRLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLRELIT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 811 SRIGVLTQNATNMGLSVIISFIYGWEMTFLILSIAPVLAVtGMIETAAMTGFANKDKQE-LKHAGKIATEALENIRTI-V 888
Cdd:cd18551 112 SGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFL-IILPLGRRIRKASKRAQDaLGELSAALERALSAIRTVkA 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 889 SLTREKAFEQMYEEMlqTQHRNTSKKAQIIGSCYA-FSHAFIYFAYAAGFRFGAYLIQAGRMTPeGMFIVF 958
Cdd:cd18551 191 SNAEERETKRGGEAA--ERLYRAGLKAAKIEALIGpLMGLAVQLALLVVLGVGGARVASGALTV-GTLVAF 258
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1037-1241 |
2.03e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1037 SLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSqiaIVPQEPVLFN---CSIAENiAY 1113
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK---LVSDEWQRNNtdmLSPGED-DT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1114 GDNSRVVPLDEIKEAAnaanihsfiegLPEKYNTQVGLKG------AQLSGGQKQRLAIARALLQKPKILLLDEATSALD 1187
Cdd:PRK10938 99 GRTTAEIIQDEVKDPA-----------RCEQLAQQFGITAlldrrfKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255708477 1188 NDSEKVVQHALDK-ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELL 1241
Cdd:PRK10938 168 VASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEIL 223
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
421-596 |
2.19e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.79 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 421 GLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNvRHYRDHIGvvSQEPVLFGTTISNNIKYGRDDVTDEEMERAAre 500
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-KPYCTYIG--HNLGLKLEMTVFENLKFWSEIYNSAETLYAA-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 501 anaydfIMEFpnKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALE-KASKGRTTIVV 579
Cdd:PRK13541 108 ------IHYF--KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLLS 179
|
170
....*....|....*..
gi 255708477 580 AHRLSTIRSAdLIVTLK 596
Cdd:PRK13541 180 SHLESSIKSA-QILQLD 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1028-1187 |
2.65e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1028 PDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQV---------LFDGVDAkELNvqwlrsqiaivPQ 1098
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklevaYFDQHRA-ELD-----------PE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1099 EPVLfncsiaENIAYGDNSRVVpldeikeaaNAANIH--SFIEGL---PEKYNTQVglkgAQLSGGQKQRLAIARALLQK 1173
Cdd:PRK11147 398 KTVM------DNLAEGKQEVMV---------NGRPRHvlGYLQDFlfhPKRAMTPV----KALSGGERNRLLLARLFLKP 458
|
170
....*....|....
gi 255708477 1174 PKILLLDEATSALD 1187
Cdd:PRK11147 459 SNLLILDEPTNDLD 472
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1040-1223 |
3.06e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1040 IERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDgvdakeLNV----QWLRSQIAiVPQEPVLFncSIAENIA--Y 1113
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKIsykpQYIKPDYD-GTVEDLLR--SITDDLGssY 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1114 GDNSRVVPLdeikeaanaanihsfieGLPEKYNTQVGlkgaQLSGGQKQRLAIARALLQKPKILLLDEATSALdnDSE-- 1191
Cdd:PRK13409 433 YKSEIIKPL-----------------QLERLLDKNVK----DLSGGELQRVAIAACLSRDADLYLLDEPSAHL--DVEqr 489
|
170 180 190
....*....|....*....|....*....|....*.
gi 255708477 1192 ----KVVQHALDKarTGRTCLVVTHRLSAIqnaDLI 1223
Cdd:PRK13409 490 lavaKAIRRIAEE--REATALVVDHDIYMI---DYI 520
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
397-593 |
3.54e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.06 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 397 SRPSIKILKGLNLriksgetvaLVGLNGSGKSTVVQLL-------------QRLYDPDdgfiMVDENDIRA---LNVRHY 460
Cdd:cd03240 14 ERSEIEFFSPLTL---------IVGQNGAGKTTIIEALkyaltgelppnskGGAHDPK----LIREGEVRAqvkLAFENA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 461 RDHIGVVSQEPVLFgttisNNIKYgrddVTDEEMeraareanaydfimefpnkfNTLVGEKGAQMSGGQKQ------RIA 534
Cdd:cd03240 81 NGKKYTITRSLAIL-----ENVIF----CHQGES--------------------NWPLLDMRGRCSGGEKVlasliiRLA 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255708477 535 IARALVRNPKILILDEATSALDSESKSAVQAAL---EKASKGRTTIVVAHRLSTIRSADLIV 593
Cdd:cd03240 132 LAETFGSNCGILALDEPTTNLDEENIEESLAEIieeRKSQKNFQLIVITHDEELVDAADHIY 193
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1125-1236 |
3.58e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.84 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1125 IKEA----ANAANIHSFIEGLpekynTQVGL-------KGAQLSGGQKQRLAIARALLQK---PKILLLDEATSALDNDS 1190
Cdd:cd03271 133 VEEAleffENIPKIARKLQTL-----CDVGLgyiklgqPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHD 207
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 255708477 1191 EKVVQHALDK-ARTGRTCLVVTHRLSAIQNADLIVVL------HNGKIKEQGT 1236
Cdd:cd03271 208 VKKLLEVLQRlVDKGNTVVVIEHNLDVIKCADWIIDLgpeggdGGGQVVASGT 260
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1005-1240 |
3.62e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 48.47 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1005 GKKPDTcegnLEFREVSFFYPCRPDVFILRgLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGvDAKEL 1084
Cdd:TIGR01257 1932 GNKTDI----LRLNELTKVYSGTSSPAVDR-LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG-KSILT 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1085 NVQWLRSQIAIVPQEPVLFNCSIA-ENIAYGDNSRVVPLDEIKEAANAAnIHSFieGLPEKYNTQVGlkgaQLSGGQKQR 1163
Cdd:TIGR01257 2006 NISDVHQNMGYCPQFDAIDDLLTGrEHLYLYARLRGVPAEEIEKVANWS-IQSL--GLSLYADRLAG----TYSGGNKRK 2078
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1164 LAIARALLQKPKILLLDEATSALDNDSEKVVQHAL-DKARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQEL 1240
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1034-1245 |
4.08e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.86 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1034 RGLSLSIERGKTVAFVGSSGCGKStsvQLLQRLY--DPVQ-GQVLFDGVDAKELN-VQWLRSQIAIVPQ---EPVLF-NC 1105
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFpNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1106 SIAENIAYgdnSRVVPLDEIKEAANAANiHSFIEGLPEKYNTQVGLKGA-------QLSGGQKQRLAIARALLQKPKILL 1178
Cdd:PRK09700 357 SIAQNMAI---SRSLKDGGYKGAMGLFH-EVDEQRTAENQRELLALKCHsvnqnitELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708477 1179 LDEATSALDNDSEKVVQHALDK-ARTGRTCLVVTHRLSAIQNA-DLIVVLHNGKIkeqgthQELLRNRD 1245
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRL------TQILTNRD 495
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
110-273 |
4.39e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 47.08 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 110 YVGIGVAALIFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNM 189
Cdd:cd18604 49 YALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLEST 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 190 STFSIGLAVGLVKGWKLTLVTLstspLIMASAAACSRMVISlTSKEL----SA-----YSKAGavaeEVLSSIRTVIAFR 260
Cdd:cd18604 129 LSLLVILIAIVVVSPAFLLPAV----VLAALYVYIGRLYLR-ASRELkrleSVarspiLSHFG----ETLAGLVTIRAFG 199
|
170
....*....|...
gi 255708477 261 AQEkelqRYTQNL 273
Cdd:cd18604 200 AEE----RFIEEM 208
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1150-1240 |
4.66e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1150 GLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSE-KVVQHALDKARTGRTCLVVTHRL-SAIQNADLIVVLH 1227
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMeEAEQLAHELTVID 218
|
90
....*....|...
gi 255708477 1228 NGKIKEQGTHQEL 1240
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
524-602 |
4.89e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.47 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 524 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRSA-DLIVTLKDGMLA 601
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLT 488
|
.
gi 255708477 602 E 602
Cdd:PRK09700 489 Q 489
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1156-1249 |
5.28e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.26 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1156 LSGGQKQRLAIARALLQKPKILLLDEATSALDND----SEKVVQHALDKARtgRTCLVVTHRLSAIQN-ADLIVVLH--- 1227
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGK--KTALVVEHDLAVLDYlSDRIHVFEgep 149
|
90 100
....*....|....*....|....*...
gi 255708477 1228 --NGK-IKEQGTHQ---ELLRNRDIYFK 1249
Cdd:cd03222 150 gvYGIaSQPKGTREginRFLRGYLITFR 177
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
524-581 |
5.83e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 5.83e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 524 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKgrTTIVVAH 581
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK--TFIVVSH 399
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1155-1226 |
5.90e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1155 QLSGGQKQRLAIARALLQKPKILLLDEATSALDndsekVVQHaLDKART------GRTCLVVTHRLsAIQN--ADLIVVL 1226
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD-----IRQR-LNVARLirelaeGKYVLVVEHDL-AVLDylADNVHIA 284
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1033-1235 |
1.07e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.24 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1033 LRGLSLSIERGKTVAFVGSSGCGKSTsvqllqrlydpvqgqVLFDGVDAKELNVqwLRSQIAIVPQEPVLFNCSIAENIA 1112
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKST---------------LVNEGLYASGKAR--LISFLPKFSRNKLIFIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1113 YGdnsrvvpldeikeaanaanihsfIEGLPekyntqVGLKGAQLSGGQKQRLAIARALLQKPK--ILLLDEATSALDNDS 1190
Cdd:cd03238 74 VG-----------------------LGYLT------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1191 ekvVQHALDKART----GRTCLVVTHRLSAIQNADLIVVL------HNGKIKEQG 1235
Cdd:cd03238 125 ---INQLLEVIKGlidlGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1145-1242 |
1.09e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1145 YNTQVGlkgaQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSE-KVVQHALDKARTGRTCLVVTHRLSAIQN-ADL 1222
Cdd:PRK10982 385 HRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDR 460
|
90 100
....*....|....*....|....*
gi 255708477 1223 IVVLHNGKI-----KEQGTHQELLR 1242
Cdd:PRK10982 461 ILVMSNGLVagivdTKTTTQNEILR 485
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
404-593 |
1.12e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.94 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 404 LKGLNLRIKSGETVALVGLNGSGKSTVV---------------------QLLQRLYDPD----DGF---IMVDENDIRal 455
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDvdsiEGLspaIAIDQKTTS-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 456 nvRHYRDHIGVVsqepvlfgTTISNNIK--YGRDDVTdeemeraareaNAYDFIMEFPNKFNTLVGEKGAqMSGGQKQRI 533
Cdd:cd03270 89 --RNPRSTVGTV--------TEIYDYLRllFARVGIR-----------ERLGFLVDVGLGYLTLSRSAPT-LSGGEAQRI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255708477 534 AIARALVRNPK--ILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRSADLIV 593
Cdd:cd03270 147 RLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRlRDLGNTVLVVEHDEDTIRAADHVI 209
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
524-596 |
1.57e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.50 E-value: 1.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 524 QMSGGQKQRIAIARAL----VRNPKILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRSADLIVTLK 596
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1156-1223 |
1.78e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.93 E-value: 1.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 1156 LSGGQKQRLAIARALLQKPKILLLDEATSALdnDSE------KVVQHALDKarTGRTCLVVTHRLSAIqnaDLI 1223
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHL--DVEqrlavaKAIRRFAEN--RGKTAMVVDHDIYLI---DYI 522
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
110-201 |
2.16e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 44.77 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 110 YVGIGVAALIFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNM 189
Cdd:cd18606 41 YAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTL 120
|
90
....*....|..
gi 255708477 190 StfSIGLAVGLV 201
Cdd:cd18606 121 S--SIIGTFILI 130
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
383-601 |
2.74e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 383 EGTVEFKNV-SFNYPSrpsikiLKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFI------MVDENDIRAL 455
Cdd:PRK10982 248 EVILEVRNLtSLRQPS------IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTItlhgkkINNHNANEAI 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 456 N-----VRHYRDHIGVVSQEPVLFGTTISNNIKY-GRDDVTDEEMERAAREANAYDFIMEFPNKfNTLVGekgaQMSGGQ 529
Cdd:PRK10982 322 NhgfalVTEERRSTGIYAYLDIGFNSLISNIRNYkNKVGLLDNSRMKSDTQWVIDSMRVKTPGH-RTQIG----SLSGGN 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708477 530 KQRIAIARALVRNPKILILDEATSALDSESKSAV-QAALEKASKGRTTIVVAHRLSTIRS-ADLIVTLKDGMLA 601
Cdd:PRK10982 397 QQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLVA 470
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1156-1221 |
3.54e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1156 LSGGQkQRLA-IARALLQKPKILLLDEATSALDNDSEKVVQHALDK-ARTGRTCLV------------VTHRLSAIQNAD 1221
Cdd:PRK10938 402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapacITHRLEFVPDGD 480
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
401-602 |
4.31e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 401 IKILKGLNLRIKSGETVALVGLNGSGKSTVVqLLQRLYDPDDGfimvdENDIR----ALNVRHYRDHIGVvsQEPVLFGT 476
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAG-----RRPWRf*twCANRRALRRTIG*--HRPVR*GR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 477 TISNNikyGRDDV----TDEEMERAAREANAYDFIMEFpnKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEAT 552
Cdd:NF000106 98 RESFS---GRENLymigR*LDLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708477 553 SALDSESKSAVQAALEKASKGRTTIV-----------VAHRLSTIRSADLIVtlkDGMLAE 602
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRDGATVLlttqymeeaeqLAHELTVIDRGRVIA---DGKVDE 230
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1155-1241 |
4.48e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.02 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1155 QLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAI-QNADLIVVLHNGKI 1231
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRlnQNNNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|
gi 255708477 1232 KEQGTHQELL 1241
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1035-1199 |
5.09e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 44.16 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1035 GLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLF-DGVdakelnvqwlrsQIAIVPQ--EPVLFNCSIAENI 1111
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV------------KLAYVDQsrDALDPNKTVWEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1112 AYGdnsrvvpLDEIK----EAANAANIHSFieglpekyntqvGLKGA-------QLSGGQKQRLAIARALLQKPKILLLD 1180
Cdd:TIGR03719 408 SGG-------LDIIKlgkrEIPSRAYVGRF------------NFKGSdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLD 468
|
170
....*....|....*....
gi 255708477 1181 EATSALDNDSEKVVQHALD 1199
Cdd:TIGR03719 469 EPTNDLDVETLRALEEALL 487
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
518-598 |
5.83e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 518 VGEKGAQMSGGQKQRIAIARALVRNPK---ILILDEATSALDSESKSAVQAALEK-ASKGRTTIVVAHRLSTIRSADLIV 593
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
|
....*
gi 255708477 594 TLKDG 598
Cdd:PRK00635 1773 EMGPG 1777
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1122-1245 |
7.61e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1122 LDEIKEAANAANIHSFIEGLPEKYNTQVGlKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKa 1201
Cdd:PLN03073 312 LELIDAYTAEARAASILAGLSFTPEMQVK-ATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK- 389
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 255708477 1202 rTGRTCLVVTHR---LSAIQNAdlIVVLHNGKIKE-QGTHQELLRNRD 1245
Cdd:PLN03073 390 -WPKTFIVVSHArefLNTVVTD--ILHLHGQKLVTyKGDYDTFERTRE 434
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
711-963 |
1.13e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 42.47 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 711 IIFAKIITMFGNNDKTTLkhdAEIYSMIFVILGVICFVSYFMQGLFYGraGEILTMRLRhLAFKAMLYQ---DIAWFDEK 787
Cdd:cd18579 18 LLLGLLISYLSSYPDEPL---SEGYLLALALFLVSLLQSLLLHQYFFL--SFRLGMRVR-SALSSLIYRkalRLSSSARQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 788 ENSTGGLTTILAIDIAQIQGATgsrigVLTQNATNMGLSVIISFIY-----GWEMTFLILSIAPVLAVTGMIetAAMTGF 862
Cdd:cd18579 92 ETSTGEIVNLMSVDVQRIEDFF-----LFLHYLWSAPLQIIVALYLlyrllGWAALAGLGVLLLLIPLQAFL--AKLISK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 863 ANKDKQELKHA-GKIATEALENIRTIvsltreK--AFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFA--YAAGF 937
Cdd:cd18579 165 LRKKLMKATDErVKLTNEILSGIKVI------KlyAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTpvLVSLA 238
|
250 260
....*....|....*....|....*.
gi 255708477 938 RFGAYLIQAGRMTPEgmfIVFTAIAY 963
Cdd:cd18579 239 TFATYVLLGNPLTAA---KVFTALSL 261
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
408-556 |
1.14e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 408 NLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIM-----VDENDIRAlnvrhyRDHIGVVSQEPVLFGT-TISNN 481
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIAT------RRRVGYMSQAFSLYGElTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 482 IK-----YgrdDVTDEEmeRAAReanaydfIMEFPNKFN--TLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSA 554
Cdd:NF033858 360 LElharlF---HLPAAE--IAAR-------VAEMLERFDlaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSG 427
|
..
gi 255708477 555 LD 556
Cdd:NF033858 428 VD 429
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1149-1248 |
1.30e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1149 VGLKGAQLSGGQKQRLAIARALLQKPK---ILLLDEATSALDNDSEkvvQHALDKART----GRTCLVVTHRLSAIQNAD 1221
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQK---SALLVQLRTlvslGHSVIYIDHDPALLKQAD 1769
|
90 100 110
....*....|....*....|....*....|
gi 255708477 1222 LIVVLHNGKIKEQGthqELL---RNRDIYF 1248
Cdd:PRK00635 1770 YLIEMGPGSGKTGG---KILfsgPPKDISA 1796
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
710-962 |
1.32e-03 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 42.43 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 710 SIIFAKII-TMFGNNDKTTLKhdaeIYSMIFVILGVICFVSYFMQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDEKE 788
Cdd:cd18570 22 SFFFQILIdDIIPSGDINLLN----IISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 789 nsTGGLTTILaIDIAQIQGAtgsrigvLTQNATNMGLSVIIS-------FIYGWEMTFLILSIAPVLAVTGMIetaAMTG 861
Cdd:cd18570 98 --TGEIISRF-NDANKIREA-------ISSTTISLFLDLLMViisgiilFFYNWKLFLITLLIIPLYILIILL---FNKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 862 FANKDKQELKHAGKIAT---EALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFAYAAGFR 938
Cdd:cd18570 165 FKKKNREVMESNAELNSyliESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILW 244
|
250 260
....*....|....*....|....
gi 255708477 939 FGAYLIQAGRMTPeGMFIVFTAIA 962
Cdd:cd18570 245 IGSYLVIKGQLSL-GQLIAFNALL 267
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
482-595 |
1.55e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 482 IKYGRDDVTDEeMERAAREANayDFIMEFP---NKFNTL---------VGEKGAQMSGGQKQRIAIARAL---VRNPKIL 546
Cdd:PRK00635 758 VRYKGKNIADI-LEMTAYEAE--KFFLDEPsihEKIHALcslgldylpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLY 834
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 255708477 547 ILDEATSALDSES-KSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTL 595
Cdd:PRK00635 835 VLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
48-329 |
1.60e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 42.02 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 48 MILGILASLVNGACLPLMPLVLGEMSDNLISGclvqtnttnyqNCTQSQEKLnedmtllTLYYVGIGVAALIFGYIQISL 127
Cdd:cd18554 1 IIITIVIGLVRFGIPLLLPLILKYIVDDVIQG-----------SSLTLDEKV-------YKLFTIIGIMFFIFLILRPPV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 128 WII-------TAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGL 200
Cdd:cd18554 63 EYYrqyfaqwIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIML 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 201 VKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFG 280
Cdd:cd18554 143 VLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRA 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 255708477 281 IKRTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEpgYTIGTVLAVF 329
Cdd:cd18554 223 LKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGN--LTVGTLVAFV 269
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
738-962 |
1.87e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 41.70 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 738 IFVILGVICFVSYFMQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDekENSTGGLTTILAIDIAQIQGATgSRIGVLT 817
Cdd:cd18543 44 LLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRFL-AFGPFLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 818 QNATNMGLSVIISFIYGWEMTFLILSIAPVLAVTGMIETAAMTGfANKDKQElkHAGKIATEALEN---IRTIVSLTREK 894
Cdd:cd18543 121 GNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFP-ASRRAQD--QAGDLATVVEESvtgIRVVKAFGRER 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708477 895 AFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRMTPeGMFIVFTAIA 962
Cdd:cd18543 198 RELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTL-GTLVAFSAYL 264
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
816-962 |
1.88e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 41.78 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 816 LTQNATNMGLSVIISFIYG-------WEMTFLILSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKIATEALENIRTIV 888
Cdd:cd18568 115 LTRSALTTILDLLMVFIYLglmfyynLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIK 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 889 SLTREKAF----EQMYEEMLQTQHR--NTSKKAQIIGScyAFSH---AFIYFayaagfrFGAYLIQAGRMTPeGMFIVFT 959
Cdd:cd18568 195 ALAAERPIrwrwENKFAKALNTRFRgqKLSIVLQLISS--LINHlgtIAVLW-------YGAYLVISGQLTI-GQLVAFN 264
|
...
gi 255708477 960 AIA 962
Cdd:cd18568 265 MLF 267
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
105-335 |
2.18e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 41.78 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 105 LLTLYYVGIGVaaLIFGYIQIslwIITAARQ------TKRIR----KQFFHSVLAQDIGWFDSCDIGELNTRMTDDiDKI 174
Cdd:cd18568 38 ISLLNLILIGL--LIVGIFQI---LLSAVRQylldyfANRIDlsllSDFYKHLLSLPLSFFASRKVGDIITRFQEN-QKI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 175 SDGIGDKIALLFQNMSTFSIGLAVGLVKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIR 254
Cdd:cd18568 112 RRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 255 TVIAFrAQEKELQ-----RYTQNLKdaKDF-GIKRTIasKVSLGAVYFFMNGTYGLaFWYGTSLILNGEpgYTIGTVLA- 327
Cdd:cd18568 192 TIKAL-AAERPIRwrwenKFAKALN--TRFrGQKLSI--VLQLISSLINHLGTIAV-LWYGAYLVISGQ--LTIGQLVAf 263
|
250
....*....|
gi 255708477 328 --VFFSVIHS 335
Cdd:cd18568 264 nmLFGSVINP 273
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1156-1226 |
2.59e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 2.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708477 1156 LSGGQKQRLAIARALL---QKPKILLLDEATSAL-DNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVL 1226
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLhTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
524-611 |
4.09e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.94 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 524 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASK--GRTTIVVAHRLSTIRS-ADLIVTLKDGML 600
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|.
gi 255708477 601 AEKGAHAELMA 611
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1156-1235 |
8.22e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.16 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708477 1156 LSGGQKQRLAIARALLQKPK--ILLLDEATSAL-DNDSEKVVqHALDKART-GRTCLVVTHRLSAIQNADLIVVL----- 1226
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLhPRDNDRLI-ETLKRLRDlGNTVLVVEHDEDTIRAADHVIDIgpgag 216
|
90
....*....|
gi 255708477 1227 -HNGKIKEQG 1235
Cdd:cd03270 217 vHGGEIVAQG 226
|
|
| |
