|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
33-608 |
8.76e-171 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 519.72 E-value: 8.76e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 33 LFSLFRYAdRLDVLLMVVGTVGALGNGISQPLMTVLFGNVINSFganTSGSVLRSVTKVVLNFIYLGIGTSVASFLQVSC 112
Cdd:COG1132 9 LRRLLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDAL---LAGGDLSALLLLLLLLLGLALLRALLSYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 113 WTMAGERQSARIRSLYLKAVLRQDITFFDTEmTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTRGWLL 192
Cdd:COG1132 85 LARLAQRVVADLRRDLFEHLLRLPLSFFDRR-RTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 193 TLVMLTSLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGII 272
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 273 TGFGMGSVMCVVFGSYGLAFWYGGKLIIEKGYTGGKIMTILFAVLTGASSLGNATPAVAAVVEGQSAAYNLFKTIERKPE 352
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 353 IDsDDNNGMVLEDMNGDIELKDVYFRYParPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLID 432
Cdd:COG1132 324 IP-DPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 433 GISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGG 512
Cdd:COG1132 401 GVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 513 QKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDA 592
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEE 560
|
570
....*....|....*.
gi 1443040382 593 LVKDpDGAYSQLIRLQ 608
Cdd:COG1132 561 LLAR-GGLYARLYRLQ 575
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
679-1292 |
6.33e-167 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 509.32 E-value: 6.33e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 679 KTPFGRLFNLNKPEVPVLLLGSIAASVHGVILPLYGIIMPGVLKSFYEPPDQlrkdSRFWALMSVVLGVACLISI--PAE 756
Cdd:COG1132 6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDL----SALLLLLLLLLGLALLRALlsYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 757 YFLFGIAGGKLIQRVRTLSFQRIMHQEVAWFDKPSnsrcatlmyfcyfifykkiftfkpmlrghlisySGALGTRLSVDA 836
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRR---------------------------------TGDLLSRLTNDV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 837 LNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVG 916
Cdd:COG1132 129 DAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 917 SIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGKTTFSDVFKVFFALV 996
Cdd:COG1132 209 GIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 997 LAAVGVSQSSALSTNATKARDSAISIFSIIDRKSRIDSSSDEGAImENVTGSIDFNNVSFKYPsrPDVQIFSDFTLHIPS 1076
Cdd:COG1132 289 RLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPL-PPVRGEIEFENVSFSYP--GDRPVLKDISLTIPP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1077 QKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFNDTIRANITYGKhSEVTEE 1156
Cdd:COG1132 366 GETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGR-PDATDE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1157 EITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMV 1236
Cdd:COG1132 445 EVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK 524
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 1237 NRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRiKDGAYASLVQLRSNSE 1292
Cdd:COG1132 525 GRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA-RGGLYARLYRLQFGEE 579
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
29-1287 |
1.81e-166 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 535.38 E-value: 1.81e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 29 KKVPLFSLFRYADRLDVLLMVVGTVGALGNGISQPLMTVLFGNVINSFgantsgSVLRSVTKVVLNFIYLGIGTSVASFL 108
Cdd:PTZ00265 43 QKIPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFVSVFGVIMKNM------NLGENVNDIIFSLVLIGIFQFILSFI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 109 QVSCWTMAGERQSARIRSLYLKAVLRQDITFFDTEmttgeAVSRMSSDTLL----IQGALGEKGGKLVELLSSFIGGFII 184
Cdd:PTZ00265 117 SSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNN-----PGSKLTSDLDFyleqVNAGIGTKFITIFTYASAFLGLYIW 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 185 AFTRGWLLTLVMLTSLPLIAIASAVSAQaltRVSSKRQTSYSDAGDT---VEQTIGSIRTVVSFNGEKKAIAMYrNFIKK 261
Cdd:PTZ00265 192 SLFKNARLTLCITCVFPLIYICGVICNK---KVKINKKTSLLYNNNTmsiIEEALVGIRTVVSYCGEKTILKKF-NLSEK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 262 SY-KATIEEGIITGFGMGSVMCVVFGSYGLAFWYGGKLIIE--------KGYTGGKIMTILFAVLTGASSLGNATPAVAA 332
Cdd:PTZ00265 268 LYsKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 333 VVEGQSAAYNLFKTIERKPEIDsDDNNGMVLEDMNgDIELKDVYFRYPARPEQLILDGLSLQVASGTTMAIVGESGSGKS 412
Cdd:PTZ00265 348 YMKSLEATNSLYEIINRKPLVE-NNDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKS 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 413 TVISLVERFYDPQSGEVLI-DGISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNIIY----------------------- 468
Cdd:PTZ00265 426 TILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsq 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 469 -GKKDATLEEIKRAAELANAAN---------------------------------FIDKLPNGYDTLVGQRGTQLSGGQK 514
Cdd:PTZ00265 506 eNKNKRNSCRAKCAGDLNDMSNttdsneliemrknyqtikdsevvdvskkvlihdFVSALPDKYETLVGSNASKLSGGQK 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 515 QRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMM--VERTTLVVAHRLSTVRNVDCITVV------------- 579
Cdd:PTZ00265 586 QRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdi 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 580 -----------------RKGK-----------------IVEQGPHDALVKDPDGAYSQLIRLQE-THRDERHKLPDSRSK 624
Cdd:PTZ00265 666 igedptkdnkennnknnKDDNnnnnnnnnnkinnagsyIIEQGTHDALMKNKNGIYYTMINNQKvSSKKSSNNDNDKDSD 745
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 625 STSLSFRRSRTKDFLSKSNRYSfksplglpvdIHEDGMTSEQQKVDHSDSKAIK-----KTPFGRLFNLNKPEVPVLL-- 697
Cdd:PTZ00265 746 MKSSAYKDSERGYDPDEMNGNS----------KHENESASNKKSCKMSDENASEnnaggKLPFLRNLFKRKPKAPNNLri 815
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 698 -----------LGSIAAS--VHGVILPLYGIIMPGVLKSFYEPPDqLRKDSRFWALMSVVLGVACLISIPAEYFLFGIAG 764
Cdd:PTZ00265 816 vyreifsykkdVTIIALSilVAGGLYPVFALLYAKYVSTLFDFAN-LEANSNKYSLYILVIAIAMFISETLKNYYNNVIG 894
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 765 GKLIQRVRTLSFQRIMHQEVAWFDKPSNSRCATLMYfcyfiFYKKIFTFKPMLRGHLISYSGALGTRLsvdalnVRRLVG 844
Cdd:PTZ00265 895 EKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAH-----INRDVHLLKTGLVNNIVIFTHFIVLFL------VSMVMS 963
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 845 DNLALIVQAVATLITG-FAIAFAADWRLAliitcVIPLVGAQGYAQVKFLKGFSEESkEMYEDANQVAADAVGSIRTVAS 923
Cdd:PTZ00265 964 FYFCPIVAAVLTGTYFiFMRVFAIRARLT-----ANKDVEKKEINQPGTVFAYNSDD-EIFKDPSFLIQEAFYNMNTVII 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 924 FCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGKTTFSDVFKVFFALVLAAVGVS 1003
Cdd:PTZ00265 1038 YGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAG 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1004 QSSALSTNATKARDSAISIFSIIDRKSRIDSSSDEGAIMEN---VTGSIDFNNVSFKYPSRPDVQIFSDFTLHIPSQKTI 1080
Cdd:PTZ00265 1118 KLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTT 1197
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1081 ALVGESGSGKSTIIALLERFYD------------------------------------------------------PDSG 1106
Cdd:PTZ00265 1198 AIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSG 1277
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1107 NISLDGVEIRSLKVSWLRDQMGLVGQEPVLFNDTIRANITYGKHsEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKG 1186
Cdd:PTZ00265 1278 KILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE-DATREDVKRACKFAAIDEFIESLPNKYDTNVGPYG 1356
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1187 VQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQ----DALDRvmVNRTTIVVAHRLSTIKGADMIAVL--- 1259
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEktivDIKDK--ADKTIITIAHRIASIKRSDKIVVFnnp 1434
|
1450 1460 1470
....*....|....*....|....*....|
gi 1443040382 1260 -KEGKIAE-KGKHEALLRIKDGAYASLVQL 1287
Cdd:PTZ00265 1435 dRTGSFVQaHGTHEELLSVQDGVYKKYVKL 1464
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
370-608 |
6.99e-135 |
|
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: 411.93 E-value: 6.99e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIG 449
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKI 529
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 530 LLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKdPDGAYSQLIRLQ 608
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1049-1287 |
5.97e-133 |
|
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: 406.54 E-value: 5.97e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMG 1128
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLFNDTIRANITYGKHSeVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPK 1208
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPD-ATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1209 ILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRiKDGAYASLVQL 1287
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKLVKA 237
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
95-608 |
5.78e-131 |
|
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: 414.48 E-value: 5.78e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 95 FIYLGIGTSVASFLQVSCWTMAGERQSARIRSLYLKAVLRQDITFFDTeMTTGEAVSRMSSDTLLIQGALGEKGGKLVEL 174
Cdd:TIGR02204 64 LLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDK-NRSGEVVSRLTTDTTLLQSVIGSSLSMALRN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 175 LSSFIGGFIIAFTRGWLLTLVMLTSLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAM 254
Cdd:TIGR02204 143 ALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 255 YRNFIKKSYKATIEEGIITGFGMGSVMCVVFGSYGLAFWYGGKLIIEKGYTGGKIMTILFAVLTGASSLGNATPAVAAVV 334
Cdd:TIGR02204 223 FGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQ 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 335 EGQSAAYNLFKTIERKPEIDSDDNNGMVLEDMNGDIELKDVYFRYPARPEQLILDGLSLQVASGTTMAIVGESGSGKSTV 414
Cdd:TIGR02204 303 RAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 415 ISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKL 494
Cdd:TIGR02204 383 FQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISAL 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 495 PNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVD 574
Cdd:TIGR02204 463 PEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKAD 542
|
490 500 510
....*....|....*....|....*....|....
gi 1443040382 575 CITVVRKGKIVEQGPHDALVKDpDGAYSQLIRLQ 608
Cdd:TIGR02204 543 RIVVMDQGRIVAQGTHAELIAK-GGLYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
29-608 |
1.01e-128 |
|
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: 1.01e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 29 KKVPLFSLFRYADRLDVLLMVVGTVGALGN--GISQPLMT-VLFGNVInsfgantSGSVLRSVTKVVLNFIYLGIGTSVA 105
Cdd:COG2274 140 KPFGLRWFLRLLRRYRRLLLQVLLASLLINllALATPLFTqVVIDRVL-------PNQDLSTLWVLAIGLLLALLFEGLL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 106 SFLQVSCWTMAGERQSARIRSLYLKAVLRQDITFFDTeMTTGEAVSRMSsDTLLIQGAL-GEKGGKLVELLSSFIGGFII 184
Cdd:COG2274 213 RLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFES-RSVGDLASRFR-DVESIREFLtGSLLTALLDLLFVLIFLIVL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 185 AFTrGWLLTLVMLTSLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYK 264
Cdd:COG2274 291 FFY-SPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLN 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 265 ATIEEGIITGFGMGSVMCVVFGSYGLAFWYGGKLIIEKGYTGGKIMTILFAVltgasslGNATPAVAAVVEGQSAAYNLF 344
Cdd:COG2274 370 ARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILS-------GRFLAPVAQLIGLLQRFQDAK 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 345 KTIER-------KPEIDSDDNNgMVLEDMNGDIELKDVYFRYPARpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISL 417
Cdd:COG2274 443 IALERlddildlPPEREEGRSK-LSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 418 VERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNG 497
Cdd:COG2274 521 LLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMG 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 498 YDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCIT 577
Cdd:COG2274 601 YDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRII 680
|
570 580 590
....*....|....*....|....*....|.
gi 1443040382 578 VVRKGKIVEQGPHDALVKdPDGAYSQLIRLQ 608
Cdd:COG2274 681 VLDKGRIVEDGTHEELLA-RKGLYAELVQQQ 710
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
682-1284 |
9.46e-124 |
|
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: 395.24 E-value: 9.46e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 682 FGRLFNLNKPEVPVLLLGSIAASVHGVILPlygiIMPGVLKSFYEPPDQLRKDSRFWALMSVVLGVACLISIP---AEYF 758
Cdd:TIGR02203 2 FRRLWSYVRPYKAGLVLAGVAMILVAATES----TLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICsfvSTYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 759 LfGIAGGKLIQRVRTLSFQRIMHQEVAWFDKPSNsrcatlmyfcyfifykkiftfkpmlrGHLISysgalgtRLSVDALN 838
Cdd:TIGR02203 78 L-SWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPT--------------------------GTLLS-------RITFDSEQ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 839 VRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSI 918
Cdd:TIGR02203 124 VASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 919 RTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVgAKFVSQ-GKTTFSDVFKVFFALVL 997
Cdd:TIGR02203 204 RVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFI-ALFQAQaGSLTAGDFTAFITAMIA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 998 AAVGVSQSSALSTNATKARDSAISIFSIIDRKSRIDsssDEGAIMENVTGSIDFNNVSFKYPSRpDVQIFSDFTLHIPSQ 1077
Cdd:TIGR02203 283 LIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1078 KTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFNDTIRANITYGKHSEVTEEE 1157
Cdd:TIGR02203 359 ETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1158 ITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVN 1237
Cdd:TIGR02203 439 IERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQG 518
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1443040382 1238 RTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRiKDGAYASL 1284
Cdd:TIGR02203 519 RTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLA-RNGLYAQL 564
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
28-605 |
2.74e-123 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 398.71 E-value: 2.74e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 28 GKKVPLFSLFRYADRlDVLLMVVG----TVGALGnGISQPLMTvlfGNVINSFGANTSgsvLRSVTKVVLNFIYLGIGTS 103
Cdd:TIGR00958 144 ETADLLFRLLGLSGR-DWPWLISAfvflTLSSLG-EMFIPFYT---GRVIDTLGGDKG---PPALASAIFFMCLLSIASS 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 104 VASFLQVSCWTMAGERQSARIRSLYLKAVLRQDITFFDtEMTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFI 183
Cdd:TIGR00958 216 VSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFD-ENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 184 IAFTRGWLLTLVMLTSLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSY 263
Cdd:TIGR00958 295 FMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 264 KATIEEGIITG--------FGMGSVMCVVfgsyglafWYGGKLIIEKGYTGGKIMTILFAVLTGASSLGNATPAVAAVVE 335
Cdd:TIGR00958 375 QLNKRKALAYAgylwttsvLGMLIQVLVL--------YYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQ 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 336 GQSAAYNLFKTIERKPEIDsddNNGMVL-EDMNGDIELKDVYFRYPARPEQLILDGLSLQVASGTTMAIVGESGSGKSTV 414
Cdd:TIGR00958 447 AVGASEKVFEYLDRKPNIP---LTGTLApLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTV 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 415 ISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKL 494
Cdd:TIGR00958 524 AALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEF 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 495 PNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMmvERTTLVVAHRLSTVRNVD 574
Cdd:TIGR00958 604 PNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRA--SRTVLLIAHRLSTVERAD 681
|
570 580 590
....*....|....*....|....*....|.
gi 1443040382 575 CITVVRKGKIVEQGPHDALVKDPDgAYSQLI 605
Cdd:TIGR00958 682 QILVLKKGSVVEMGTHKQLMEDQG-CYKHLV 711
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
673-1286 |
6.54e-121 |
|
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: 392.27 E-value: 6.54e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 673 DSKAIKKTPFGRLFNLNKPEVPVL---LLGSIAASVHGVILPLY-GIIMPGVLKSfyeppdqlrKDSRFWALMSVVLGVA 748
Cdd:COG2274 135 DKRGEKPFGLRWFLRLLRRYRRLLlqvLLASLLINLLALATPLFtQVVIDRVLPN---------QDLSTLWVLAIGLLLA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 749 CLISIPAEY---FLFGIAGGKLIQRVRTLSFQRIMHQEVAWFDKpsnsrcatlmyfcyfifykkiftfkpmlrghliSYS 825
Cdd:COG2274 206 LLFEGLLRLlrsYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFES---------------------------------RSV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 826 GALGTRLSvDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAqvkFLKGFSEESKEMYE 905
Cdd:COG2274 253 GDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLL---FQPRLRRLSREESE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 906 DANQVAA---DAVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGK 982
Cdd:COG2274 329 ASAKRQSllvETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQ 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 983 TTFSDvfkvFFALVLAAVGVSQS-SALSTNATKARDSAIS---IFSIIDRKsrIDSSSDEGAI-MENVTGSIDFNNVSFK 1057
Cdd:COG2274 409 LTLGQ----LIAFNILSGRFLAPvAQLIGLLQRFQDAKIAlerLDDILDLP--PEREEGRSKLsLPRLKGDIELENVSFR 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1058 YPSRpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLF 1137
Cdd:COG2274 483 YPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLF 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1138 NDTIRANITYGkHSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATS 1217
Cdd:COG2274 562 SGTIRENITLG-DPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATS 640
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1218 ALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRiKDGAYASLVQ 1286
Cdd:COG2274 641 ALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLA-RKGLYAELVQ 708
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
686-1032 |
6.40e-117 |
|
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: 367.16 E-value: 6.40e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 686 FNLNKPEVPVLLLGSIAASVHGVILPLYGIIMPGVLKSFYEP-PDQLRKDSRFWALMSVVLGVACLISIPAEYFLFGIAG 764
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPdDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 765 GKLIQRVRTLSFQRIMHQEVAWFDKPSNSrcatlmyfcyfifykkiftfkpmlrghlisySGALGTRLSVDALNVRRLVG 844
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENS-------------------------------TGALTSRLSTDASDVRGLVG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 845 DNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSIRTVASF 924
Cdd:cd18578 130 DRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 925 CSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGKTTFSDVFKVFFALVLAAVGVSQ 1004
Cdd:cd18578 210 TLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQ 289
|
330 340
....*....|....*....|....*...
gi 1443040382 1005 SSALSTNATKARDSAISIFSIIDRKSRI 1032
Cdd:cd18578 290 AFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
684-1285 |
1.35e-115 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 377.91 E-value: 1.35e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 684 RLFNLNKPEVPVLLLG---SIAASVHGVILPLY-GIIMPGVLKSFyePPDQLRKDSRFWALMSVV--LGVACLISIpaey 757
Cdd:TIGR00958 151 RLLGLSGRDWPWLISAfvfLTLSSLGEMFIPFYtGRVIDTLGGDK--GPPALASAIFFMCLLSIAssVSAGLRGGS---- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 758 flFGIAGGKLIQRVRTLSFQRIMHQEVAWFDKpsnsrcatlmyfcyfifykkiftfkpmlrghliSYSGALGTRLSVDAL 837
Cdd:TIGR00958 225 --FNYTMARINLRIREDLFRSLLRQDLGFFDE---------------------------------NKTGELTSRLSSDTQ 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 838 NVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGS 917
Cdd:TIGR00958 270 TMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSG 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 918 IRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGKTTFSDVfkVFFALVL 997
Cdd:TIGR00958 350 MRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNL--VSFLLYQ 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 998 AAVG--VSQSSALSTNATKARDSAISIFSIIDRKSRIDSSsdeGAIM-ENVTGSIDFNNVSFKYPSRPDVQIFSDFTLHI 1074
Cdd:TIGR00958 428 EQLGeaVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLT---GTLApLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTL 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1075 PSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFNDTIRANITYGKhSEVT 1154
Cdd:TIGR00958 505 HPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGL-TDTP 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1155 EEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDalDRV 1234
Cdd:TIGR00958 584 DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRS 661
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 1235 MVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEAlLRIKDGAYASLV 1285
Cdd:TIGR00958 662 RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQ-LMEDQGCYKHLV 711
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1049-1284 |
1.61e-114 |
|
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: 357.31 E-value: 1.61e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPDvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMG 1128
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLFNDTIRANITYGKHsEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPK 1208
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRP-GATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 1209 ILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRiKDGAYASL 1284
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA-QGGVYAKL 233
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
825-1288 |
7.44e-114 |
|
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: 368.64 E-value: 7.44e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 825 SGALGTRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMY 904
Cdd:TIGR02204 114 SGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 905 EDANQVAADAVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGKTT 984
Cdd:TIGR02204 194 ADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 985 FSDVFKVFFALVLAAVGVSQSSALSTNATKARDSAISIFSIIDRKSRIDSSSDEGAIMENVTGSIDFNNVSFKYPSRPDV 1064
Cdd:TIGR02204 274 AGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQ 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1065 QIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFNDTIRAN 1144
Cdd:TIGR02204 354 PALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMEN 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1145 ITYGKhSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESE 1224
Cdd:TIGR02204 434 IRYGR-PDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESE 512
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1225 RVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRiKDGAYASLVQLR 1288
Cdd:TIGR02204 513 QLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA-KGGLYARLARLQ 575
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
48-343 |
9.18e-114 |
|
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: 357.94 E-value: 9.18e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 48 MVVGTVGALGNGISQPLMTVLFGNVINSFGANTSGSV-----LRSVTKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSA 122
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESspdefLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 123 RIRSLYLKAVLRQDITFFDTeMTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTRGWLLTLVMLTSLPL 202
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDK-NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 203 IAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFGMGSVMC 282
Cdd:cd18577 160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFF 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 283 VVFGSYGLAFWYGGKLIIEKGYTGGKIMTILFAVLTGASSLGNATPAVAAVVEGQSAAYNL 343
Cdd:cd18577 240 IIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
47-608 |
2.58e-112 |
|
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: 364.42 E-value: 2.58e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 47 LMVVGTVGALGNGISQPLMTVLFGNVIN-SFGANTSGSVLRSVTKVVLNFIYLGIgtsvASFLQVSCWTMAGERQSARIR 125
Cdd:TIGR02203 15 GLVLAGVAMILVAATESTLAALLKPLLDdGFGGRDRSVLWWVPLVVIGLAVLRGI----CSFVSTYLLSWVSNKVVRDIR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 126 SLYLKAVLRQDITFFDTEmTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTRGWLLTLVMLTSLPLIAI 205
Cdd:TIGR02203 91 VRMFEKLLGLPVSFFDRQ-PTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 206 ASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMY-------RNFIKKSYKATieegiitgfGMG 278
Cdd:TIGR02203 170 LMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFdavsnrnRRLAMKMTSAG---------SIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 279 SVMCVVFGSYGLAF--WYGGKLIIEKGYTGGKIMTILFAVLTGASSLGNATPAVAAVVEGQSAAYNLFKTIERKPEIDSd 356
Cdd:TIGR02203 241 SPITQLIASLALAVvlFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDT- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 357 dnNGMVLEDMNGDIELKDVYFRYPARpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISI 436
Cdd:TIGR02203 320 --GTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 437 KKLRLDWIRGKIGLVSQEPLLFMASIKDNIIYGK-KDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQ 515
Cdd:TIGR02203 397 ADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 516 RIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVk 595
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL- 555
|
570
....*....|...
gi 1443040382 596 DPDGAYSQLIRLQ 608
Cdd:TIGR02203 556 ARNGLYAQLHNMQ 568
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
817-1292 |
2.97e-112 |
|
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: 365.30 E-value: 2.97e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 817 LRGHLISYSGAL------GTRlSVDALnVRRLVGDNLALIVQAVATLITgFAIAFaaDWRLALIiTCVIplVGAQGYAQV 890
Cdd:COG5265 126 LRFHLERQTGGLsrdierGTK-GIEFL-LRFLLFNILPTLLEIALVAGI-LLVKY--DWWFALI-TLVT--VVLYIAFTV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 891 KFLK---GFSEESKEMYEDANQVAADAVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIvggiGLSFSN----LML 963
Cdd:COG5265 198 VVTEwrtKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYERAAVKSQT----SLALLNfgqaLII 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 964 YLTYGLCFYVGAKFVSQGKTTFSDvfkvfFALVLA-AVGVSQS-SALSTNATKARDSAISI---FSIIDRKSRIDSSsdE 1038
Cdd:COG5265 274 ALGLTAMMLMAAQGVVAGTMTVGD-----FVLVNAyLIQLYIPlNFLGFVYREIRQALADMermFDLLDQPPEVADA--P 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1039 GAIMENVT-GSIDFNNVSFKYpsRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRS 1117
Cdd:COG5265 347 DAPPLVVGgGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1118 LKVSWLRDQMGLVGQEPVLFNDTIRANITYGKHsEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRV 1197
Cdd:COG5265 425 VTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP-DASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRV 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1198 AIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRiK 1277
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLA-Q 582
|
490
....*....|....*
gi 1443040382 1278 DGAYASLVQLRSNSE 1292
Cdd:COG5265 583 GGLYAQMWARQQEEE 597
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
370-604 |
1.21e-105 |
|
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: 333.43 E-value: 1.21e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEqLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIG 449
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKI 529
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 530 LLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKDpDGAYSQL 604
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1049-1284 |
4.50e-105 |
|
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: 331.89 E-value: 4.50e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPsrPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMG 1128
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLFNDTIRANITYGKHSeVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPK 1208
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD-ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 1209 ILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRiKDGAYASL 1284
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAEM 232
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
734-1284 |
2.11e-104 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 343.15 E-value: 2.11e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 734 DSRFWALMSVVL-------GVACLISipaEYFLFGIAGgKLIQRVRTLSFQRIMHQEVAWFDKPSnsrcatlmyfcyfif 806
Cdd:PRK11176 60 DRSVLKWMPLVViglmilrGITSFIS---SYCISWVSG-KVVMTMRRRLFGHMMGMPVSFFDKQS--------------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 807 ykkiftfkpmlrghlisySGALGTRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVgAQG 886
Cdd:PRK11176 121 ------------------TGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIV-SIA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 887 YAQVKflKGFSEESKEMYEDANQVAADAVGSI---RTVASFCSEKRVVAIYNKKCEALRKQGIR----SGIVGGI----- 954
Cdd:PRK11176 182 IRVVS--KRFRNISKNMQNTMGQVTTSAEQMLkghKEVLIFGGQEVETKRFDKVSNRMRQQGMKmvsaSSISDPIiqlia 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 955 ---------GLSFSNLMLYLTYGlcfyvgakfvsqgktTFSDVFKVFFALVLAAvgvsqSSALSTNATKARDSAI--SIF 1023
Cdd:PRK11176 260 slalafvlyAASFPSVMDTLTAG---------------TITVVFSSMIALMRPL-----KSLTNVNAQFQRGMAAcqTLF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1024 SIIDrksrIDSSSDEGAI-MENVTGSIDFNNVSFKYPSRpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYD 1102
Cdd:PRK11176 320 AILD----LEQEKDEGKRvIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1103 PDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFNDTIRANITYGKHSEVTEEEITAVAKAANAHEFVSSLPQGYDTVV 1182
Cdd:PRK11176 395 IDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVI 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1183 GEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEG 1262
Cdd:PRK11176 475 GENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDG 554
|
570 580
....*....|....*....|..
gi 1443040382 1263 KIAEKGKHEALLRiKDGAYASL 1284
Cdd:PRK11176 555 EIVERGTHAELLA-QNGVYAQL 575
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
342-620 |
4.67e-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: 340.26 E-value: 4.67e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 342 NLFKTIERKPEI-DSDDNNGMVLEDmnGDIELKDVYFRY-PARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVE 419
Cdd:COG5265 331 RMFDLLDQPPEVaDAPDAPPLVVGG--GEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 420 RFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYD 499
Cdd:COG5265 406 RFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYD 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 500 TLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVV 579
Cdd:COG5265 486 TRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVL 565
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1443040382 580 RKGKIVEQGPHDALVKDpDGAYSQLIRLQETHRDERHKLPD 620
Cdd:COG5265 566 EAGRIVERGTHAELLAQ-GGLYAQMWARQQEEEEAEEALAA 605
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
48-608 |
1.51e-101 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 335.45 E-value: 1.51e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 48 MVVGTVGALGNGISQPLMTVLFGNVI-NSFGaNTSGSVLRSVTKVVLNFIYL-GIGTSVASFlqvsCWTMAGERQSARIR 125
Cdd:PRK11176 27 LIVAGVALILNAASDTFMLSLLKPLLdDGFG-KADRSVLKWMPLVVIGLMILrGITSFISSY----CISWVSGKVVMTMR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 126 SLYLKAVLRQDITFFDTEmTTGEAVSRMSSDTLLIQGAlgeKGGKLVELL---SSFIGGFIIAFTRGWLLTLVMLTSLPL 202
Cdd:PRK11176 102 RRLFGHMMGMPVSFFDKQ-STGTLLSRITYDSEQVASS---SSGALITVVregASIIGLFIMMFYYSWQLSLILIVIAPI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 203 IAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNG---EKKAIAMYRNFIK-KSYK----ATIEEGIITg 274
Cdd:PRK11176 178 VSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGqevETKRFDKVSNRMRqQGMKmvsaSSISDPIIQ- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 275 fgmgsvmcvVFGSYGLAF-WYGGKL--IIEKgYTGGKIMTI---LFAVLTGASSLGNATpavAAVVEGQSAAYNLFKTIE 348
Cdd:PRK11176 257 ---------LIASLALAFvLYAASFpsVMDT-LTAGTITVVfssMIALMRPLKSLTNVN---AQFQRGMAACQTLFAILD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 349 RKPEidsDDNNGMVLEDMNGDIELKDVYFRYPARpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGE 428
Cdd:PRK11176 324 LEQE---KDEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 429 VLIDGISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNIIYGKKDA-TLEEIKRAAELANAANFIDKLPNGYDTLVGQRGT 507
Cdd:PRK11176 400 ILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 508 QLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQ 587
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVER 559
|
570 580
....*....|....*....|.
gi 1443040382 588 GPHDALVKDpDGAYSQLIRLQ 608
Cdd:PRK11176 560 GTHAELLAQ-NGVYAQLHKMQ 579
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
370-608 |
1.07e-96 |
|
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: 309.16 E-value: 1.07e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYParPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIG 449
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKI 529
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 530 LLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVkDPDGAYSQLIRLQ 608
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1047-1278 |
6.42e-96 |
|
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: 306.46 E-value: 6.42e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1047 GSIDFNNVSFKYpsRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQ 1126
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1127 MGLVGQEPVLFNDTIRANITYGkHSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKD 1206
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1207 PKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRIKD 1278
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
368-595 |
2.94e-94 |
|
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: 302.22 E-value: 2.94e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 368 GDIELKDVYFRYpaRPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGK 447
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 448 IGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDP 527
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 528 KILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVK 595
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
826-1287 |
6.93e-94 |
|
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: 313.63 E-value: 6.93e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 826 GALGTRLSVDALNvrRLVGD-----NLALIV---QAVATLITGFAIAFAA--DWRLALIITC-------VIPLVGAqgya 888
Cdd:COG4987 104 AGLARLRSGDLLN--RLVADvdaldNLYLRVllpLLVALLVILAAVAFLAffSPALALVLALglllaglLLPLLAA---- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 889 qvKFLKGFSEESKEMYEDANQVAADAVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYG 968
Cdd:COG4987 178 --RLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 969 LCFYVGAKFVSQGktTFSDVFKVFFAL-VLAAVGVSQS-SALSTNATKARDSAISIFSIIDRKSRIDSSSDEGAImeNVT 1046
Cdd:COG4987 256 AVLWLAAPLVAAG--ALSGPLLALLVLaALALFEALAPlPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPA--PGG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1047 GSIDFNNVSFKYPSRPDvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQ 1126
Cdd:COG4987 332 PSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1127 MGLVGQEPVLFNDTIRANITYGKhSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKD 1206
Cdd:COG4987 411 IAVVPQRPHLFDTTLRENLRLAR-PDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRD 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1207 PKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRiKDGAYASLVQ 1286
Cdd:COG4987 490 APILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA-QNGRYRQLYQ 568
|
.
gi 1443040382 1287 L 1287
Cdd:COG4987 569 R 569
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
848-1275 |
1.41e-93 |
|
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: 312.46 E-value: 1.41e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 848 ALIVQAVATLITgFAIAFAADWRLALIITCVIPLV---------GAQGYAQVKFLKgfseeskemYEDANQVAADAVGSI 918
Cdd:COG4988 138 QLFLAALVPLLI-LVAVFPLDWLSGLILLVTAPLIplfmilvgkGAAKASRRQWRA---------LARLSGHFLDRLRGL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 919 RTVASFCSEKRVVAIYNKKCEALRKQGIR-------SGIV------GGIGLsfsnLMLYLTYGLcfyvgakfvSQGKTTF 985
Cdd:COG4988 208 TTLKLFGRAKAEAERIAEASEDFRKRTMKvlrvaflSSAVleffasLSIAL----VAVYIGFRL---------LGGSLTL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 986 sdvFKVFFALVLA--------AVGvsqsSA--LSTNATKARDSaisIFSIIDRKSRIDSSSDEGAIMENvTGSIDFNNVS 1055
Cdd:COG4988 275 ---FAALFVLLLApefflplrDLG----SFyhARANGIAAAEK---IFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVS 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1056 FKYPSRPdvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPV 1135
Cdd:COG4988 344 FSYPGGR--PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPY 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1136 LFNDTIRANITYGKHsEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEA 1215
Cdd:COG4988 422 LFAGTIRENLRLGRP-DASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEP 500
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1216 TSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLR 1275
Cdd:COG4988 501 TAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLA 560
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
335-595 |
5.08e-92 |
|
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: 308.23 E-value: 5.08e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 335 EGQSAAYNLFKTIERKPEIDSDDNNGMVLEDmNGDIELKDVYFRYPARPEqlILDGLSLQVASGTTMAIVGESGSGKSTV 414
Cdd:COG4988 303 NGIAAAEKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYPGGRP--ALDGLSLTIPPGERVALVGPSGAGKSTL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 415 ISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKL 494
Cdd:COG4988 380 LNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 495 PNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVD 574
Cdd:COG4988 460 PDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQAD 539
|
250 260
....*....|....*....|.
gi 1443040382 575 CITVVRKGKIVEQGPHDALVK 595
Cdd:COG4988 540 RILVLDDGRIVEQGTHEELLA 560
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
845-1285 |
4.04e-90 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 303.81 E-value: 4.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 845 DNLALIVqAVATLItgfAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSIRTVASF 924
Cdd:PRK13657 136 EHLATLV-ALVVLL---PLALFMNWRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSY 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 925 cseKRVVAiynkkcealRKQGIRS----------------GIVGGIGLSFSNL-MLYLtyglcFYVGAKFVSQGKTTFSD 987
Cdd:PRK13657 212 ---NRIEA---------ETQALRDiadnllaaqmpvlswwALASVLNRAASTItMLAI-----LVLGAALVQKGQLRVGE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 988 VFK-VFFALVLAAvGVSQSSALSTNATKARDSAISIFSIIDRKSRIDSSSDEGAImENVTGSIDFNNVSFKYPSRPdvQI 1066
Cdd:PRK13657 275 VVAfVGFATLLIG-RLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDL-GRVKGAVEFDDVSFSYDNSR--QG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1067 FSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFNDTIRANIT 1146
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1147 YGKhSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERV 1226
Cdd:PRK13657 431 VGR-PDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAK 509
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1227 VQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRiKDGAYASLV 1285
Cdd:PRK13657 510 VKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVA-RGGRFAALL 567
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
363-608 |
9.19e-89 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 299.95 E-value: 9.19e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 363 LEDMNGDIELKDVYFRYPARPEQLilDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLD 442
Cdd:PRK13657 328 LGRVKGAVEFDDVSFSYDNSRQGV--EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 443 WIRGKIGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARA 522
Cdd:PRK13657 406 SLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 523 ILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVkDPDGAYS 602
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELV-ARGGRFA 564
|
....*.
gi 1443040382 603 QLIRLQ 608
Cdd:PRK13657 565 ALLRAQ 570
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
171-607 |
1.52e-87 |
|
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: 295.91 E-value: 1.52e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 171 LVELLSSFIGGFIIAF---TRGWLLTLVMLTSLPLIAIASAVSAQALTR-VSSKRQTSYSDAGDTVEqtigSIRTVVSFN 246
Cdd:COG4987 137 LVALLVILAAVAFLAFfspALALVLALGLLLAGLLLPLLAARLGRRAGRrLAAARAALRARLTDLLQ----GAAELAAYG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 247 GEKKAIAMYRNFIKKSYKATIEEGIITGFGMGSVMCVVFGSYGLAFWYGGKLIIEKGYTGGKIMTILFAVLTGASSLGNA 326
Cdd:COG4987 213 ALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 327 TPAVAAVVEGQSAAYNLFKTIERKPEIdSDDNNGMVLEDmNGDIELKDVYFRYPARPeQLILDGLSLQVASGTTMAIVGE 406
Cdd:COG4987 293 PAAAQHLGRVRAAARRLNELLDAPPAV-TEPAEPAPAPG-GPSLELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGP 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 407 SGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELAN 486
Cdd:COG4987 370 SGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVG 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 487 AANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHR 566
Cdd:COG4987 450 LGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHR 529
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1443040382 567 LSTVRNVDCITVVRKGKIVEQGPHDALVKDPdGAYSQLIRL 607
Cdd:COG4987 530 LAGLERMDRILVLEDGRIVEQGTHEELLAQN-GRYRQLYQR 569
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
370-608 |
1.08e-81 |
|
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: 267.43 E-value: 1.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPArPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIG 449
Cdd:cd03252 1 ITFEHVRFRYKP-DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKI 529
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 530 LLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVkDPDGAYSQLIRLQ 608
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL-AENGLYAYLYQLQ 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1044-1264 |
6.75e-81 |
|
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: 264.72 E-value: 6.75e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1044 NVTGSIDFNNVSFKYPSRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWL 1123
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1124 RDQMGLVGQEPVLFNDTIRANITYGKHSeVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAI 1203
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAYGLQS-CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 1204 LKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKI 1264
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1049-1288 |
2.13e-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: 263.96 E-value: 2.13e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYpsRPD-VQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQM 1127
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1128 GLVGQEPVLFNDTIRANITYGKHSeVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDP 1207
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG-MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1208 KILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRiKDGAYASLVQL 1287
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA-ENGLYAYLYQL 236
|
.
gi 1443040382 1288 R 1288
Cdd:cd03252 237 Q 237
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
46-353 |
3.04e-80 |
|
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: 266.63 E-value: 3.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 46 LLMVVGTVGALGNGISQPLMTVLFGNVINSFGANTSGSVLRSVTKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSARIR 125
Cdd:cd18578 9 PLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 126 SLYLKAVLRQDITFFD-TEMTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTRGWLLTLVMLTSLPLIA 204
Cdd:cd18578 89 KLAFRAILRQDIAWFDdPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 205 IASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFGMGSVMCVV 284
Cdd:cd18578 169 LAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLT 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 285 FGSYGLAFWYGGKLIIEKGYTGGKIMTILFAVLTGASSLGNATPAVAAVVEGQSAAYNLFKTIERKPEI 353
Cdd:cd18578 249 FFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1049-1263 |
1.39e-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: 256.16 E-value: 1.39e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPdVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMG 1128
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLFNDTIRANItygkhsevteeeitavakaanahefvsslpqgydtvvgekgvqLSGGQKQRVAIARAILKDPK 1208
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1209 ILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGK 1263
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
365-584 |
3.34e-78 |
|
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: 257.40 E-value: 3.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 365 DMNGDIELKDVYFRYPARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWI 444
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 445 RGKIGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAIL 524
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 525 KDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKI 584
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
370-583 |
5.84e-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: 251.53 E-value: 5.84e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIG 449
Cdd:cd03228 1 IEFKNVSFSYPGRPKP-VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMASIKDNIiygkkdatleeikraaelanaanfidklpngydtlvgqrgtqLSGGQKQRIAIARAILKDPKI 529
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 530 LLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGK 583
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
137-608 |
6.79e-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: 263.53 E-value: 6.79e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 137 ITFFdTEMTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIggFI-IAFTRGWLLTLVMLTSLPL-IAIASAVSAQAL 214
Cdd:TIGR01846 227 LGYF-ESRRVGDTVARVRELEQIRNFLTGSALTVVLDLLFVVV--FLaVMFFYSPTLTGVVIGSLVCyALLSVFVGPILR 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 215 TRVSSKRQTSYSDAGDTVE-----QTIGSIRTVVSFNGE-KKAIAMYrnfIKKSYKATiEEGIITGFGMGSVMCVVFGsy 288
Cdd:TIGR01846 304 KRVEDKFERSAAATSFLVEsvtgiETIKATATEPQFQNRwDRQLAAY---VAASFRVT-NLGNIAGQAIELIQKLTFA-- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 289 gLAFWYGGKLIIEKGYTGGKImtILFAVLTGAsslgnatpaVAAVVEGQSAAYNLFK----TIERKPEI-DSDDNNG--- 360
Cdd:TIGR01846 378 -ILLWFGAHLVIGGALSPGQL--VAFNMLAGR---------VTQPVLRLAQLWQDFQqtgiALERLGDIlNSPTEPRsag 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 361 -MVLEDMNGDIELKDVYFRY-PARPEqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKK 438
Cdd:TIGR01846 446 lAALPELRGAITFENIRFRYaPDSPE--VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAI 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 439 LRLDWIRGKIGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIA 518
Cdd:TIGR01846 524 ADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIA 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 519 IARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKDpD 598
Cdd:TIGR01846 604 IARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLAL-Q 682
|
490
....*....|
gi 1443040382 599 GAYSQLIRLQ 608
Cdd:TIGR01846 683 GLYARLWQQQ 692
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
368-588 |
6.69e-72 |
|
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: 239.03 E-value: 6.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 368 GDIELKDVYFRYPARpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGK 447
Cdd:cd03245 1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 448 IGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDP 527
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 528 KILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQG 588
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
28-608 |
1.88e-69 |
|
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: 247.56 E-value: 1.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 28 GKKVPLFSLFRYADRL---DVL-LMVVGTVGALGnGISQPLMT-VLFGNVINS---------FGANTSGSVLRSVTKVVL 93
Cdd:TIGR03797 118 DKALGLRDLLRFALRGarrDLLaILAMGLLGTLL-GMLVPIATgILIGTAIPDadrsllvqiALALLAAAVGAAAFQLAQ 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 94 NFIYLGIGTSVASFLQVSCWTmagerqsariRSLYLKAvlrqdiTFFdTEMTTGEAVSRMSSDTLlIQGALGekGGKLVE 173
Cdd:TIGR03797 197 SLAVLRLETRMDASLQAAVWD----------RLLRLPV------SFF-RQYSTGDLASRAMGISQ-IRRILS--GSTLTT 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 174 LLSSFIGGFIIA--FTRGWLLTLVmltslpliAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIrTVVSFNG---- 247
Cdd:TIGR03797 257 LLSGIFALLNLGlmFYYSWKLALV--------AVALALVAIAVTLVLGLLQVRKERRLLELSGKISGL-TVQLINGiskl 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 248 -----EKKAIAMY-RNF---IKKSYKATIEEGIITGFGmgSVMCVVFGsyGLAFWYGGKLIIEKGYTGGKIM---TILFA 315
Cdd:TIGR03797 328 rvagaENRAFARWaKLFsrqRKLELSAQRIENLLTVFN--AVLPVLTS--AALFAAAISLLGGAGLSLGSFLafnTAFGS 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 316 VLTGASSLGNATPAVAAVVegqsAAYNLFKTI-ERKPEIDSDDNNGMVLedmNGDIELKDVYFRYpaRPEQ-LILDGLSL 393
Cdd:TIGR03797 404 FSGAVTQLSNTLISILAVI----PLWERAKPIlEALPEVDEAKTDPGKL---SGAIEVDRVTFRY--RPDGpLILDDVSL 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 394 QVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNIIyGKKDA 473
Cdd:TIGR03797 475 QIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAPL 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 474 TLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNR 553
Cdd:TIGR03797 554 TLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLER 633
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 554 MMVERttLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKDPdGAYSQLIRLQ 608
Cdd:TIGR03797 634 LKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMARE-GLFAQLARRQ 685
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
848-1259 |
1.43e-67 |
|
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: 237.96 E-value: 1.43e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 848 ALIVQAVATLITGFAIaFAADWRLALIITCVIPLV---------GAQGYAQvKFLKGFSEESKEMyedanqvaADAVGSI 918
Cdd:TIGR02857 124 QLVLAVIVPLAILAAV-FPQDWISGLILLLTAPLIpifmiligwAAQAAAR-KQWAALSRLSGHF--------LDRLRGL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 919 RTVASFCSEKRVVAIYNKKCEALRKQGIRSgivggIGLSF-SNLMLYL-----TYGLCFYVGAKFVSqGKTTFsdvFKVF 992
Cdd:TIGR02857 194 PTLKLFGRAKAQAAAIRRSSEEYRERTMRV-----LRIAFlSSAVLELfatlsVALVAVYIGFRLLA-GDLDL---ATGL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 993 FALVLAA---VGVSQSSALSTNATKARDSAISIFSIIDRKSRIDSSSDEgaIMENVTGSIDFNNVSFKYPSRPDVqiFSD 1069
Cdd:TIGR02857 265 FVLLLAPefyLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAP--VTAAPASSLEFSGVSVAYPGRRPA--LRP 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1070 FTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFNDTIRANITYGK 1149
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1150 hSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQD 1229
Cdd:TIGR02857 421 -PDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLE 499
|
410 420 430
....*....|....*....|....*....|
gi 1443040382 1230 ALDRVMVNRTTIVVAHRLSTIKGADMIAVL 1259
Cdd:TIGR02857 500 ALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
696-1022 |
1.86e-66 |
|
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: 226.97 E-value: 1.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 696 LLLGSIAASVHGVILPLYGIIMPGVLKSF------YEPPDQLRKDSRFWALMSVVLGVACLISIPAEYFLFGIAGGKLIQ 769
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 770 RVRTLSFQRIMHQEVAWFDKPSnsrcatlmyfcyfifykkiftfkpmlrghlisySGALGTRLSVDALNVRRLVGDNLAL 849
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNG---------------------------------AGELTSRLTSDTNLIQDGIGEKLGL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 850 IVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSIRTVASFCSEKR 929
Cdd:cd18577 128 LIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 930 VVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGKTTFSDVFKVFFALVLAAVGVSQSSALS 1009
Cdd:cd18577 208 EIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNL 287
|
330
....*....|...
gi 1443040382 1010 TNATKARDSAISI 1022
Cdd:cd18577 288 QAFAKARAAAAKI 300
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
363-606 |
2.73e-65 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 232.86 E-value: 2.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 363 LEDMNGDIELKDVYFRYPaRPEQLILDgLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLD 442
Cdd:TIGR01192 328 LPNVKGAVEFRHITFEFA-NSSQGVFD-VSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 443 WIRGKIGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARA 522
Cdd:TIGR01192 406 SLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 523 ILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKDpDGAYS 602
Cdd:TIGR01192 486 ILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK-DGRFY 564
|
....
gi 1443040382 603 QLIR 606
Cdd:TIGR01192 565 KLLR 568
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
48-343 |
3.06e-65 |
|
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: 223.69 E-value: 3.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 48 MVVGTVGALGNGISQPLMTVLFGNVINSF--GANTSGSVLRS---------------VTKVVLNFIYLGIGTSVASFLQV 110
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFtnGGMTNITGNSSglnssagpfekleeeMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 111 SCWTMAGERQSARIRSLYLKAVLRQDITFFDTEmTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTRGW 190
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVN-DTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 191 LLTLVMLTSLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEG 270
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 271 IITGFGMGSVMCVVFGSYGLAFWYGGKLIIEKGYTGGKIMTILFAVLTGASSLGNATPAVAAVVEGQSAAYNL 343
Cdd:cd18558 240 ITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1047-1264 |
5.05e-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: 219.38 E-value: 5.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1047 GSIDFNNVSFKYPS--RPDVQIFSdFTLHiPSQKtIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLR 1124
Cdd:cd03245 1 GRIEFRNVSFSYPNqeIPALDNVS-LTIR-AGEK-VAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1125 DQMGLVGQEPVLFNDTIRANITYGkHSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAIL 1204
Cdd:cd03245 78 RNIGYVPQDVTLFYGTLRDNITLG-APLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1205 KDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKI 1264
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
825-1286 |
1.28e-64 |
|
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: 233.31 E-value: 1.28e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 825 SGALGTRlsVDALN-VRRLVGDNLALIVQAVATLITGFAIAFAADWRLAL----IITCVIPLVGAQGYAQVKFLKGFSEE 899
Cdd:TIGR03797 232 TGDLASR--AMGISqIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKLALvavaLALVAIAVTLVLGLLQVRKERRLLEL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 900 SKEMYEDANQVAAdAVGSIRTVASfcsEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVS 979
Cdd:TIGR03797 310 SGKISGLTVQLIN-GISKLRVAGA---ENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAVLPVLTSAALFAAAISLLG 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 980 QGKTTFSD--VFKVFFALVLAAVGVSQSSALSTNAtkardsAISIFS----IIDRKSRIDS-SSDEGAImenvTGSIDFN 1052
Cdd:TIGR03797 386 GAGLSLGSflAFNTAFGSFSGAVTQLSNTLISILA------VIPLWErakpILEALPEVDEaKTDPGKL----SGAIEVD 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1053 NVSFKYpsRPD-VQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVG 1131
Cdd:TIGR03797 456 RVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVL 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1132 QEPVLFNDTIRANITYGkhSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILL 1211
Cdd:TIGR03797 534 QNGRLMSGSIFENIAGG--APLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILL 611
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1212 LDEATSALDAESERVVQDALDRVMVNRttIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRiKDGAYASLVQ 1286
Cdd:TIGR03797 612 FDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA-REGLFAQLAR 683
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
346-1274 |
2.40e-64 |
|
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: 241.00 E-value: 2.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 346 TIERKPEIDSDDNNgmvledmngdIELKDVYFRYpARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQ 425
Cdd:TIGR00957 623 SIERRTIKPGEGNS----------ITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKV 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 426 SGEVLIdgisikklrldwiRGKIGLVSQEPLLFMASIKDNIIYGKKdatLEEIKRAAELANAANFID--KLPNGYDTLVG 503
Cdd:TIGR00957 692 EGHVHM-------------KGSVAYVPQQAWIQNDSLRENILFGKA---LNEKYYQQVLEACALLPDleILPSGDRTEIG 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 504 QRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEAL---NRMMVERTTLVVAHRLSTVRNVDCITVVR 580
Cdd:TIGR00957 756 EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMS 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 581 KGKIVEQGPHDALVkDPDGAYSQLIRLQETHRDERHkLPDSRSKSTSLSFRRSR-TKDFLSKSNRYSFKSPLGLPVDIHE 659
Cdd:TIGR00957 836 GGKISEMGSYQELL-QRDGAFAEFLRTYAPDEQQGH-LEDSWTALVSGEGKEAKlIENGMLVTDVVGKQLQRQLSASSSD 913
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 660 DGMTSEQQKVDHSDSKAIKKTPFGRLFNLNKPEVpvlllGSIAASVH-------GVILPLYGIIM-----PGVLKSFY-- 725
Cdd:TIGR00957 914 SGDQSRHHGSSAELQKAEAKEETWKLMEADKAQT-----GQVELSVYwdymkaiGLFITFLSIFLfvcnhVSALASNYwl 988
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 726 -----EPPDQLRKDSRfwalmSVVLGVACLISIPAEYFLFGIA-----GGKLIQRVRTLSF-QRIMHQEVAWFDKPSNSR 794
Cdd:TIGR00957 989 slwtdDPMVNGTQNNT-----SLRLSVYGALGILQGFAVFGYSmavsiGGIQASRVLHQDLlHNKLRSPMSFFERTPSGN 1063
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 795 CATLmyfcyfiFYKKIFTFKPMLRGHLISYSGALGTRLSvdalnvrrlvgdnlALIVQAVATLITGFAIAfaadwRLALI 874
Cdd:TIGR00957 1064 LVNR-------FSKELDTVDSMIPPVIKMFMGSLFNVIG--------------ALIVILLATPIAAVIIP-----PLGLL 1117
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 875 ITCVIPLVGAQGyAQVKFLKGFSEESkeMYEDANQvaadAVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSgIVGGI 954
Cdd:TIGR00957 1118 YFFVQRFYVASS-RQLKRLESVSRSP--VYSHFNE----TLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPS-IVANR 1189
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 955 GLSfsnlmlyltyglcfyVGAKFVSQGKTTFSDVFKVFFALVLAAVGVSQSSALSTNATKARDSAISIFS-------IID 1027
Cdd:TIGR00957 1190 WLA---------------VRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSemetnivAVE 1254
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1028 RKSRIDSSSDEG--AIMENV-------TGSIDFNNVSFKYpsRPDVQ-IFSDFTLHIPSQKTIALVGESGSGKSTIIALL 1097
Cdd:TIGR00957 1255 RLKEYSETEKEApwQIQETAppsgwppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGL 1332
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1098 ERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFNDTIRANITygKHSEVTEEEITAVAKAANAHEFVSSLPQG 1177
Cdd:TIGR00957 1333 FRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD--PFSQYSDEEVWWALELAHLKTFVSALPDK 1410
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1178 YDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIA 1257
Cdd:TIGR00957 1411 LDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVI 1490
|
970
....*....|....*..
gi 1443040382 1258 VLKEGKIAEKGKHEALL 1274
Cdd:TIGR00957 1491 VLDKGEVAEFGAPSNLL 1507
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1047-1268 |
2.68e-64 |
|
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: 217.36 E-value: 2.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1047 GSIDFNNVSFKYpsRPDVQ-IFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRD 1125
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 QMGLVGQEPVLFNDTIRANItyGKHSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILK 1205
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL--DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 1206 DPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKG 1268
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
368-589 |
3.25e-64 |
|
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: 217.36 E-value: 3.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 368 GDIELKDVYFRYpaRPE-QLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRG 446
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 KIGLVSQEPLLFMASIKDNI-IYGKkdATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILK 525
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLdPFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 526 DPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGP 589
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
146-609 |
4.99e-64 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 228.83 E-value: 4.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 146 TGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTR-GWLLTLVMLTSLPLIAIASAVSAQALTRVSSKRQTS 224
Cdd:PRK10789 92 TGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTQiSWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 225 YSDAGDTVEQTIGSIRTVVSFNGEKK------AIA-------MYRNFIKKSYKATIEEGI----ITGFGMGSVMcVVFGS 287
Cdd:PRK10789 172 FSSLNDRTQESLTSIRMIKAFGLEDRqsalfaADAedtgkknMRVARIDARFDPTIYIAIgmanLLAIGGGSWM-VVNGS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 288 YGLafwygGKLIIEKGYTGGKIMTILfavltgasslgnATPAVAAVVEGQSAAYNLFKT-IERKPEIDsdDNNGMVLEDm 366
Cdd:PRK10789 251 LTL-----GQLTSFVMYLGLMIWPML------------ALAWMFNIVERGSAAYSRIRAmLAEAPVVK--DGSEPVPEG- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 367 NGDIELKDVYFRYPARpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRG 446
Cdd:PRK10789 311 RGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 KIGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKD 526
Cdd:PRK10789 390 RLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLN 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 527 PKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKDPdGAYSQLIR 606
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS-GWYRDMYR 548
|
...
gi 1443040382 607 LQE 609
Cdd:PRK10789 549 YQQ 551
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1022-1292 |
2.53e-63 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 227.29 E-value: 2.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1022 IFSIIDRkSRIDSSSDEGAIMenvTGSIDFNNVSFKYpsRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFY 1101
Cdd:PRK10790 318 VFELMDG-PRQQYGNDDRPLQ---SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1102 DPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFNDTIRANITYGKHseVTEEEITAVAKAANAHEFVSSLPQGYDTV 1181
Cdd:PRK10790 392 PLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD--ISEEQVWQALETVQLAELARSLPDGLYTP 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1182 VGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKE 1261
Cdd:PRK10790 470 LGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHR 549
|
250 260 270
....*....|....*....|....*....|.
gi 1443040382 1262 GKIAEKGKHEALLRiKDGAYASLVQLRSNSE 1292
Cdd:PRK10790 550 GQAVEQGTHQQLLA-AQGRYWQMYQLQLAGE 579
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
91-605 |
7.71e-63 |
|
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: 228.47 E-value: 7.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 91 VVLNFIYLGIGTSVASFLQVSCWTMAGERQSARIRSLYLKAVLRQDITFFDTEmTTGEAVSRMSsDTLLIQGALGEKggk 170
Cdd:TIGR01193 198 ISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTR-RTGEIVSRFT-DASSIIDALAST--- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 171 lveLLSSF-------IGGFIIAFtRGWLLTLVMLTSLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVV 243
Cdd:TIGR01193 273 ---ILSLFldmwilvIVGLFLVR-QNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 244 SFNGE----KKAIAMYRNFIKKSYKATIEEGIITGFGMGS--VMCVVFgsyglaFWYGGKLIIEKGYTGGKIMT---ILF 314
Cdd:TIGR01193 349 SLTSEaerySKIDSEFGDYLNKSFKYQKADQGQQAIKAVTklILNVVI------LWTGAYLVMRGKLTLGQLITfnaLLS 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 315 AVLTGASSLGNATPAVAAVvegqSAAYNLFKTIERKPEIDSDDNNGMVLEDMNGDIELKDVYFRYPARPEqlILDGLSLQ 394
Cdd:TIGR01193 423 YFLTPLENIINLQPKLQAA----RVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSN--ILSDISLT 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 395 VASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNIIYG-KKDA 473
Cdd:TIGR01193 497 IKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENV 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 474 TLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESE-RIVQEALN 552
Cdd:TIGR01193 577 SQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEkKIVNNLLN 656
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 553 rmMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKDpDGAYSQLI 605
Cdd:TIGR01193 657 --LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDR-NGFYASLI 706
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
335-579 |
4.00e-61 |
|
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: 219.08 E-value: 4.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 335 EGQSAAYNLFKTIERKPEIDSDDnnGMVLEDMNGDIELKDVYFRYPARPEqlILDGLSLQVASGTTMAIVGESGSGKSTV 414
Cdd:TIGR02857 289 DGVAAAEALFAVLDAAPRPLAGK--APVTAAPASSLEFSGVSVAYPGRRP--ALRPVSFTVPPGERVALVGPSGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 415 ISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKL 494
Cdd:TIGR02857 365 LNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAAL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 495 PNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVD 574
Cdd:TIGR02857 445 PQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALAD 524
|
....*
gi 1443040382 575 CITVV 579
Cdd:TIGR02857 525 RIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1018-1286 |
6.08e-61 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 219.70 E-value: 6.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1018 SAISIFSIIDRKSRIDSSSDEGAimENVTGSIDFNNVSFKYPSRPDvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALL 1097
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTA--AADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1098 ERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFNDTIRANITYGKHsEVTEEEITAVAKAANAHEFVSSlPQG 1177
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAP-NASDEALIEVLQQVGLEKLLED-DKG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1178 YDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIA 1257
Cdd:PRK11160 465 LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRIC 544
|
250 260
....*....|....*....|....*....
gi 1443040382 1258 VLKEGKIAEKGKHEALLRiKDGAYASLVQ 1286
Cdd:PRK11160 545 VMDNGQIIEQGTHQELLA-QQGRYYQLKQ 572
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
338-606 |
4.64e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 214.30 E-value: 4.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 338 SAAYNLFKTIERKPEIDSDDNNGMVLEdmNGDIELKDVYFRYPARPeQLILDGLSLQVASGTTMAIVGESGSGKSTVISL 417
Cdd:PRK11160 309 ASARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQP-QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 418 VERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKlPNG 497
Cdd:PRK11160 386 LTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 498 YDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCIT 577
Cdd:PRK11160 465 LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRIC 544
|
250 260
....*....|....*....|....*....
gi 1443040382 578 VVRKGKIVEQGPHDALVKDpDGAYSQLIR 606
Cdd:PRK11160 545 VMDNGQIIEQGTHQELLAQ-QGRYYQLKQ 572
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
385-606 |
5.12e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 214.32 E-value: 5.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 385 QLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYdPQSGEVLIDGISIKKLRL-DWiRGKIGLVSQEPLLFMASIK 463
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPeSW-RKHLSWVGQNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 464 DNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVES 543
Cdd:PRK11174 441 DNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 544 ERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKDPdGAYSQLIR 606
Cdd:PRK11174 521 EQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG-GLFATLLA 582
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1022-1274 |
1.94e-58 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 212.27 E-value: 1.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1022 IFSIIDRKS----RIDSSSDEGAIMENVT-------GSIDFNNVSFKYPSRpDVQIFSDFTLHIPSQKTIALVGESGSGK 1090
Cdd:PRK10789 276 MFNIVERGSaaysRIRAMLAEAPVVKDGSepvpegrGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1091 STIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFNDTIRANITYGKhSEVTEEEITAVAKAANAHEF 1170
Cdd:PRK10789 355 STLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGR-PDATQQEIEHVARLASVHDD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1171 VSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTI 1250
Cdd:PRK10789 434 ILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSAL 513
|
250 260
....*....|....*....|....
gi 1443040382 1251 KGADMIAVLKEGKIAEKGKHEALL 1274
Cdd:PRK10789 514 TEASEILVMQHGHIAQRGNHDQLA 537
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1071-1291 |
5.11e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 211.63 E-value: 5.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1071 TLHIPSQKTIALVGESGSGKSTIIALLERFYdPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFNDTIRANITYGKH 1150
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNP 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1151 sEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDA 1230
Cdd:PRK11174 449 -DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 1231 LDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRiKDGAYASLVQLRSNS 1291
Cdd:PRK11174 528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQ-AGGLFATLLAHRQEE 587
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
370-1286 |
2.57e-56 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 215.23 E-value: 2.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIdgisikklrldwIRGKIG 449
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMASIKDNIIYGKkDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKI 529
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFGS-DFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDI 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 530 LLLDEATSALDVE-SERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKDpdgaySQLIRlq 608
Cdd:PLN03232 762 YIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS-----GSLFK-- 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 609 ethrderhKLPDSRSKSTSlsfrrsrTKDFLSKSNRYSFKSPlGLPVDIHEDGMTSEQQKvDHSDSKAIKKTPFGR-LFN 687
Cdd:PLN03232 835 --------KLMENAGKMDA-------TQEVNTNDENILKLGP-TVTIDVSERNLGSTKQG-KRGRSVLVKQEERETgIIS 897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 688 LNkpevpVLLLGSIAasvhgvilpLYGIIMPGVLKSFYEPPDQLRKDSRFWalMSVVLGVACLISIPAEYFLF--GIAGG 765
Cdd:PLN03232 898 WN-----VLMRYNKA---------VGGLWVVMILLVCYLTTEVLRVSSSTW--LSIWTDQSTPKSYSPGFYIVvyALLGF 961
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 766 KLIQRVRTLSFQRI---MHQEVAWFDKPSNSRCATLMYFcyfifykkiFTFKPmlrghlisySGALGTRLSVDALNVRRL 842
Cdd:PLN03232 962 GQVAVTFTNSFWLIsssLHAAKRLHDAMLNSILRAPMLF---------FHTNP---------TGRVINRFSKDIGDIDRN 1023
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 843 VGDNLALIVQAVATLITGFA-IAFAADWRLALIITCVIPLVGAQGYAQ-----VKFLKGFSEESkeMYEDANQvAADAVG 916
Cdd:PLN03232 1024 VANLMNMFMNQLWQLLSTFAlIGTVSTISLWAIMPLLILFYAAYLYYQstsreVRRLDSVTRSP--IYAQFGE-ALNGLS 1100
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 917 SIRTVASFcseKRVVAIYNKKCE-----------ALRKQGIRSGIVGGIglsfsnlMLYLTyglcfyvgAKF--VSQGKT 983
Cdd:PLN03232 1101 SIRAYKAY---DRMAKINGKSMDnnirftlantsSNRWLTIRLETLGGV-------MIWLT--------ATFavLRNGNA 1162
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 984 TFSDVFKVFFALVLAAVgVSQSSALSTNATKARDSAISIFSIIDRKSRIDSSSDEGAIMEN--------VTGSIDFNNVS 1055
Cdd:PLN03232 1163 ENQAGFASTMGLLLSYT-LNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENnrpvsgwpSRGSIKFEDVH 1241
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1056 FKY-PSRPDVQIFSDFTLHiPSQKtIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEP 1134
Cdd:PLN03232 1242 LRYrPGLPPVLHGLSFFVS-PSEK-VGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSP 1319
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1135 VLFNDTIRANITygKHSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDE 1214
Cdd:PLN03232 1320 VLFSGTVRFNID--PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1215 ATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRIKDGAYASLVQ 1286
Cdd:PLN03232 1398 ATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
370-1286 |
7.49e-56 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 213.83 E-value: 7.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIdgisikklrldwIRGKIG 449
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMASIKDNIIYGKK-DAtlEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPK 528
Cdd:PLN03130 683 YVPQVSWIFNATVRDNILFGSPfDP--ERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 529 ILLLDEATSALDVESERIV-QEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKDPDgAYSQLI-- 605
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGP-LFQKLMen 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 606 --RLQETHRDE-RHKLPDSRSKSTSLSFRRSRTKDFLSKSNRYSFKSPLgLPVDIHEDGMTSEQQKVDHSDSkaikktpf 682
Cdd:PLN03130 840 agKMEEYVEENgEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKSVL-IKQEERETGVVSWKVLERYKNA-------- 910
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 683 grlfnlnkpevpvlllgsiaasvhgvilpLYGIIMPGVLKSFYEPPDQLRKDSRFWalMSVVLGVACLISIPAEYFLFGI 762
Cdd:PLN03130 911 -----------------------------LGGAWVVMILFLCYVLTEVFRVSSSTW--LSEWTDQGTPKTHGPLFYNLIY 959
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 763 AGGKLIQRVRTL--SFQRIMHQEVA---WFDKPSNSRCATLMYFcyfifykkiFTFKPMlrGHLISysgalgtRLSVDAL 837
Cdd:PLN03130 960 ALLSFGQVLVTLlnSYWLIMSSLYAakrLHDAMLGSILRAPMSF---------FHTNPL--GRIIN-------RFAKDLG 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 838 NVRRLVGDNLALIVQAVATLITGFA-IAFAADWRLALIITCVIPLVGAQGYAQVKflkgfSEESKEMyeDA---NQVAA- 912
Cdd:PLN03130 1022 DIDRNVAVFVNMFLGQIFQLLSTFVlIGIVSTISLWAIMPLLVLFYGAYLYYQST-----AREVKRL--DSitrSPVYAq 1094
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 913 --DAVGSIRTVASFCSEKRVVAIYNKKCE-----------ALRKQGIRSGIVGGiglsfsnLMLYLTyglcfyvgAKFVS 979
Cdd:PLN03130 1095 fgEALNGLSTIRAYKAYDRMAEINGRSMDnnirftlvnmsSNRWLAIRLETLGG-------LMIWLT--------ASFAV 1159
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 980 QGKTTFSDvfKVFFAlvlAAVGVSQSSALS-TN--------ATKARDSaisiFSIIDR-KSRIDSSSDEGAIMEN----- 1044
Cdd:PLN03130 1160 MQNGRAEN--QAAFA---STMGLLLSYALNiTSlltavlrlASLAENS----LNAVERvGTYIDLPSEAPLVIENnrppp 1230
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1045 ---VTGSIDFNNVSFKY-PSRPDVQIFSDFTLHiPSQKtIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKV 1120
Cdd:PLN03130 1231 gwpSSGSIKFEDVVLRYrPELPPVLHGLSFEIS-PSEK-VGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGL 1308
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1121 SWLRDQMGLVGQEPVLFNDTIRANIT-YGKHSEVteeEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAI 1199
Cdd:PLN03130 1309 MDLRKVLGIIPQAPVLFSGTVRFNLDpFNEHNDA---DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSL 1385
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1200 ARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRIKDG 1279
Cdd:PLN03130 1386 ARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGS 1465
|
....*..
gi 1443040382 1280 AYASLVQ 1286
Cdd:PLN03130 1466 AFSKMVQ 1472
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
123-608 |
3.01e-55 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 203.41 E-value: 3.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 123 RIRSLYLKAVLRQDITFFDTEmTTGEAVSRMSSDTLLIQGALgekggklVELLSS------FIGGFIIA-FTRGWLLTLV 195
Cdd:PRK10790 99 QLRTDVMDAALRQPLSAFDTQ-PVGQLISRVTNDTEVIRDLY-------VTVVATvlrsaaLIGAMLVAmFSLDWRMALV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 196 MLTSLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFN-----GEKKAIAMYRNFIKKS-------- 262
Cdd:PRK10790 171 AIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRqqarfGERMGEASRSHYMARMqtlrldgf 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 263 --------YKATIEEGIITGFGMGSVmcvvfGSYGL----AFW-YGGKL---IIEkgytggkimtilfavLTGASSLGNA 326
Cdd:PRK10790 251 llrpllslFSALILCGLLMLFGFSAS-----GTIEVgvlyAFIsYLGRLnepLIE---------------LTTQQSMLQQ 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 327 tpavaAVVEGQsaayNLFKTIERKPEIDSDDNNGMvledMNGDIELKDVYFRYpaRPEQLILDGLSLQVASGTTMAIVGE 406
Cdd:PRK10790 311 -----AVVAGE----RVFELMDGPRQQYGNDDRPL----QSGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGH 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 407 SGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNIIYGKkDATLEEIKRAAELAN 486
Cdd:PRK10790 376 TGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQ 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 487 AANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALnRMMVERTTLVV-AH 565
Cdd:PRK10790 455 LAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLVViAH 533
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1443040382 566 RLSTVRNVDCITVVRKGKIVEQGPHDALVKDpDGAYSQLIRLQ 608
Cdd:PRK10790 534 RLSTIVEADTILVLHRGQAVEQGTHQQLLAA-QGRYWQMYQLQ 575
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
48-320 |
4.16e-54 |
|
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: 190.55 E-value: 4.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 48 MVVGTVGALGNGISQPLMTVLFGNVINSFGANTSGSVlRSVTKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSARIRSL 127
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPET-QALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 128 YLKAVLRQDITFFDTeMTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTRGWLLTLVMLTSLPLIAIAS 207
Cdd:pfam00664 80 LFKKILRQPMSFFDT-NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 208 AVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFGMGSVMCVVFGS 287
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1443040382 288 YGLAFWYGGKLIIEKGYTGGKIMTI--LFAVLTGA 320
Cdd:pfam00664 239 YALALWFGAYLVISGELSVGDLVAFlsLFAQLFGP 273
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1046-1275 |
8.08e-54 |
|
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: 198.43 E-value: 8.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1046 TGSIDFNNVSFKYPSRpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSlkvsWLRD 1125
Cdd:COG4618 328 KGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ----WDRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 QMG-LVG---QEPVLFNDTIRANItyGKHSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIAR 1201
Cdd:COG4618 403 ELGrHIGylpQDVELFDGTIAENI--ARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1202 AILKDPKILLLDEATSALDAESERVVQDALDRV-MVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLR 1275
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
144-567 |
4.34e-53 |
|
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: 195.66 E-value: 4.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 144 MTTGEAVSRMSSDTLLIQG----ALGEKGGKLVELLSSFIGGFIIAFTRGWLLTLVMLTSL---PLIAIASAVSA-QALT 215
Cdd:TIGR02868 107 LRRGDLLGRLGADVDALQDlyvrVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGfvaPLVSLRAARAAeQALA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 216 RVSSKRqtsYSDAGDTVEqtigSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFGMGSVMCVVFGSYGLAFWYG 295
Cdd:TIGR02868 187 RLRGEL---AAQLTDALD----GAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 296 GKLIIEKGYTGGKIMTILFAVLTGASSLGNATPAVAAVVEGQSAAYNLFKTIERKPEI-DSDDNNGMVLEDMNGDIELKD 374
Cdd:TIGR02868 260 GPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVaEGSAPAAGAVGLGKPTLELRD 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 375 VYFRYPARPEqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQE 454
Cdd:TIGR02868 340 LSAGYPGAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQD 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 455 PLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDE 534
Cdd:TIGR02868 418 AHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDE 497
|
410 420 430
....*....|....*....|....*....|...
gi 1443040382 535 ATSALDVESERIVQEALNRMMVERTTLVVAHRL 567
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
696-1022 |
2.24e-50 |
|
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: 180.94 E-value: 2.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 696 LLLGSIAASVHGVILPLYGIIMPGVLKSF------------------YEPPDQLRKDSRFWALMSVVLGVACLISIPAEY 757
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFtnggmtnitgnssglnssAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 758 FLFGIAGGKLIQRVRTLSFQRIMHQEVAWFDKPSnsrcatlmyfcyfifykkiftfkpmlrghlisySGALGTRLSVDAL 837
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVND---------------------------------TGELNTRLADDVS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 838 NVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGS 917
Cdd:cd18558 128 KINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 918 IRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGKTTFSDVFKVFF-ALV 996
Cdd:cd18558 208 FRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFsVLI 287
|
330 340
....*....|....*....|....*.
gi 1443040382 997 LAAVGVSQSSALSTNAtKARDSAISI 1022
Cdd:cd18558 288 GAFSAGQQVPSIEAFA-NARGAAYHI 312
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1043-1285 |
3.88e-50 |
|
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: 190.34 E-value: 3.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1043 ENVTGSIDFNNVSFKYPSrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSW 1122
Cdd:TIGR01193 468 NNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1123 LRDQMGLVGQEPVLFNDTIRANITYGKHSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARA 1202
Cdd:TIGR01193 546 LRQFINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARA 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1203 ILKDPKILLLDEATSALDAESERVVQDALDRvMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRiKDGAYA 1282
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLD-RNGFYA 703
|
...
gi 1443040382 1283 SLV 1285
Cdd:TIGR01193 704 SLI 706
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
825-1247 |
8.49e-50 |
|
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: 185.64 E-value: 8.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 825 SGALGTRLS--VDALN---VRRLVGDNLALIVQAVATLITG-----FAIAFAAdwrLALIITCVIPLVGAqgyaqvkfLK 894
Cdd:TIGR02868 109 RGDLLGRLGadVDALQdlyVRVIVPAGVALVVGAAAVAAIAvlsvpAALILAA---GLLLAGFVAPLVSL--------RA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 895 GFSEESKEMyEDANQVAADAVGSIRTVAS---FCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCF 971
Cdd:TIGR02868 178 ARAAEQALA-RLRGELAAQLTDALDGAAElvaSGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGAL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 972 YVGAKFVSQGKTTfSDVFKVFFALVLAAVGVSqsSALSTNA---TKARDSAISIFSIIDRKSRIDSSSDEGAIMENVTG- 1047
Cdd:TIGR02868 257 WAGGPAVADGRLA-PVTLAVLVLLPLAAFEAF--AALPAAAqqlTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKp 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1048 SIDFNNVSFKYPSRPDVqiFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQM 1127
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRV 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1128 GLVGQEPVLFNDTIRANITYGKhSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDP 1207
Cdd:TIGR02868 412 SVCAQDAHLFDTTVRENLRLAR-PDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADA 490
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1443040382 1208 KILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRL 1247
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
360-591 |
1.97e-49 |
|
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: 185.34 E-value: 1.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 360 GMVLEDMNGDIELKDVYFRYPARpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKL 439
Cdd:COG4618 321 RMPLPRPKGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQW 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 440 RLDWIRGKIGLVSQEPLLFMASIKDNII-YGkkDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIA 518
Cdd:COG4618 400 DREELGRHIGYLPQDVELFDGTIAENIArFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 519 IARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTT-LVVAHRLSTVRNVDCITVVRKGKIVEQGPHD 591
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATvVVITHRPSLLAAVDKLLVLRDGRVQAFGPRD 551
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
370-598 |
2.52e-48 |
|
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: 172.13 E-value: 2.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYParPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIG 449
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPL--LFMASIKDNIIYG------KKDATLEEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIAR 521
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenlglPREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 522 AILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVA-HRLSTV-RNVDCITVVRKGKIVEQGPHDALVKDPD 598
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
370-603 |
2.62e-48 |
|
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: 180.87 E-value: 2.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARP--EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKL---RLDWI 444
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 445 RGKIGLVSQEPL--LF-MASIKDNI-----IYGKKDATlEEIKRAAELANA----ANFIDKLPNgydtlvgqrgtQLSGG 512
Cdd:COG1123 341 RRRVQMVFQDPYssLNpRMTVGDIIaeplrLHGLLSRA-ERRERVAELLERvglpPDLADRYPH-----------ELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 513 QKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRNV-DCITVVRKGKIVEQGP 589
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGP 488
|
250
....*....|....
gi 1443040382 590 HDALVKDPDGAYSQ 603
Cdd:COG1123 489 TEEVFANPQHPYTR 502
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
370-603 |
8.02e-48 |
|
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: 171.14 E-value: 8.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQL-ILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKI 448
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 449 GLVSQEPllfMAS------IKDNI-----IYGKKDATlEEIKRAAELAN-AANFIDKLPNgydtlvgqrgtQLSGGQKQR 516
Cdd:COG1124 82 QMVFQDP---YASlhprhtVDRILaeplrIHGLPDRE-ERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 517 IAIARAILKDPKILLLDEATSALDVeserIVQ----EALNRMMVER--TTLVVAHRLSTVRNV-DCITVVRKGKIVEQGP 589
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDV----SVQaeilNLLKDLREERglTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELT 222
|
250
....*....|....
gi 1443040382 590 HDALVKDPDGAYSQ 603
Cdd:COG1124 223 VADLLAGPKHPYTR 236
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
51-341 |
2.55e-47 |
|
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: 171.20 E-value: 2.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 51 GTVGALGNGISQPLMTVLFGNVINSFGANTSGSVLRSVTKVvlnFIYLGIGTSVASFLQVSCWTMAGERQSARIRSLYLK 130
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALI---LLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 131 AVLRQDITFFDTEmTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTRGWLLTLVMLTSLPLIAIASAVS 210
Cdd:cd18557 78 SLLRQEIAFFDKH-KTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 211 AQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFGMGSVMCVVFGSYGL 290
Cdd:cd18557 157 GRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 291 AFWYGGKLIIEKGYTGGKIMTILFAVLTGASSLGNATPAVAAVVEGQSAAY 341
Cdd:cd18557 237 VLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASE 287
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
370-584 |
1.11e-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: 1.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIG 449
Cdd:cd03246 1 LEVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMASIKDNIiygkkdatleeikraaelanaanfidklpngydtlvgqrgtqLSGGQKQRIAIARAILKDPKI 529
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 530 LLLDEATSALDVESERIVQEALNRM-MVERTTLVVAHRLSTVRNVDCITVVRKGKI 584
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
51-324 |
8.71e-46 |
|
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: 167.04 E-value: 8.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 51 GTVGALGNGISQPLMTVLFGNVINSFGANTSGSV---LRSVTKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSARIRSL 127
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGeeaLRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 128 YLKAVLRQDITFFDTeMTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTRGWLLTLVMLTSLPLIAIAS 207
Cdd:cd18780 81 LFSAIIAQEIAFFDV-TRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 208 AVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFGMGSVMCVVFGS 287
Cdd:cd18780 160 VIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLA 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 1443040382 288 YGLAFWYGGKLIIEKGYTGGKIMTILFAVLTGASSLG 324
Cdd:cd18780 240 IVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFA 276
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1049-1268 |
2.32e-45 |
|
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: 161.71 E-value: 2.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSwLRDQMG 1128
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLFNDTIRANItygkhsevteeeitavakaanahefvsslpqgydtvvgekGVQLSGGQKQRVAIARAILKDPK 1208
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1209 ILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKG 1268
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
370-588 |
4.94e-45 |
|
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: 160.56 E-value: 4.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRlDWIRGKIG 449
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMASIKDNIiygkkdatleeikraaelanaanfidklpngydtlvgqrGTQLSGGQKQRIAIARAILKDPKI 529
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 530 LLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQG 588
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1044-1274 |
6.66e-45 |
|
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: 171.76 E-value: 6.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1044 NVTGSIDFNNVSFKYPSrPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSlkvsWL 1123
Cdd:TIGR01842 312 EPEGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQ----WD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1124 RDQMG-LVG---QEPVLFNDTIRANIT-YGKhsEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVA 1198
Cdd:TIGR01842 387 RETFGkHIGylpQDVELFPGTVAENIArFGE--NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIA 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1199 IARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNR-TTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALL 1274
Cdd:TIGR01842 465 LARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1046-1268 |
7.83e-45 |
|
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: 161.04 E-value: 7.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1046 TGSIDFNNVSFKYpsRPDV-QIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLR 1124
Cdd:cd03369 4 HGEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1125 DQMGLVGQEPVLFNDTIRANITygKHSEVTEEEITAVAKaanahefvsslpqgydtvVGEKGVQLSGGQKQRVAIARAIL 1204
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNLD--PFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1205 KDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKG 1268
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
368-588 |
9.31e-45 |
|
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: 161.04 E-value: 9.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 368 GDIELKDVYFRY-PARPEqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRG 446
Cdd:cd03369 5 GEIEVENLSVRYaPDLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 KIGLVSQEPLLFMASIKDNI-IYGKKDAtlEEIKRAAElanaanfidklpngydtlVGQRGTQLSGGQKQRIAIARAILK 525
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEYSD--EEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 526 DPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQG 588
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
370-565 |
9.40e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 161.14 E-value: 9.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIG 449
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMASIKDNII----YGKKDATLEEIKRAAELANaanfidkLPngyDTLVGQRGTQLSGGQKQRIAIARAILK 525
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPfpfqLRERKFDRERALELLERLG-------LP---PDILDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1443040382 526 DPKILLLDEATSALDVESERIVQEALNRMMVE--RTTLVVAH 565
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEegRAVLWVSH 189
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1049-1245 |
1.11e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 160.75 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMG 1128
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLFNDTIRANITYG---KHSEVTEEEITAVAKAANahefvssLPQGY-DTVVGEkgvqLSGGQKQRVAIARAIL 1204
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPfqlRERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1443040382 1205 KDPKILLLDEATSALDAESERVVQDALDRVM--VNRTTIVVAH 1245
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSH 189
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
370-588 |
2.55e-44 |
|
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: 160.36 E-value: 2.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQL-ILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKL---RLDWIR 445
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 446 GKIGLVSQEPllfMAS------IKDNI-----IYGKKDATLEEIKRAAELA----NAANFIDKLPNgydtlvgqrgtQLS 510
Cdd:cd03257 82 KEIQMVFQDP---MSSlnprmtIGEQIaeplrIHGKLSKKEARKEAVLLLLvgvgLPEEVLNRYPH-----------ELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 511 GGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRNV-DCITVVRKGKIVEQ 587
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIaDRVAVMYAGKIVEE 227
|
.
gi 1443040382 588 G 588
Cdd:cd03257 228 G 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
366-587 |
6.96e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 159.05 E-value: 6.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 366 MNGDIELKDVYFRYPARPEQL-ILDGLSLQVASGTTMAIVGESGSGKST---VISLVERfydPQSGEVLIDGISIKKL-- 439
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGEVtALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLse 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 440 -RLDWIRG-KIGLVSQEP-LLFMASIKDNI----IYGKKDATlEEIKRAAELANA---ANFIDKLPNgydtlvgqrgtQL 509
Cdd:COG1136 78 rELARLRRrHIGFVFQFFnLLPELTALENValplLLAGVSRK-ERRERARELLERvglGDRLDHRPS-----------QL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 510 SGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVE--RTTLVVAHRLSTVRNVDCITVVRKGKIVEQ 587
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
370-593 |
6.96e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.46 E-value: 6.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDwIRGKIG 449
Cdd:COG1131 1 IEVRGLTKRYGDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMA-SIKDNI-----IYGKKDATLEEikRAAELANAANFIDKLpngyDTLVGQrgtqLSGGQKQRIAIARAI 523
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARE--RIDELLELFGLTDAA----DRKVGT----LSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 524 LKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVA-HRLSTVRNV-DCITVVRKGKIVEQGPHDAL 593
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERLcDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
371-583 |
8.60e-44 |
|
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: 158.40 E-value: 8.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 371 ELKDVYFRYPARPEQlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGL 450
Cdd:cd03225 1 ELKNLSFSYPDGARP-ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 451 VSQEP--LLFMASIKDNIIYG------KKDATLEEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIARA 522
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGlenlglPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 523 ILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVA-HRLSTVRNV-DCITVVRKGK 583
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
388-537 |
1.20e-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: 155.50 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLF-MASIKDNI 466
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 467 IYGKKDATLEEIKRAAELANAANFIDkLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATS 537
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
370-593 |
1.41e-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: 158.50 E-value: 1.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYD-----PQSGEVLIDGISIKKLRLD-- 442
Cdd:cd03260 1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 443 WIRGKIGLVSQEPLLFMASIKDNIIYGKK----------DATLEEIKRAAELANAANfiDKLpngydtlvgqRGTQLSGG 512
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgiklkeelDERVEEALRKAALWDEVK--DRL----------HALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 513 QKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHD 591
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTE 225
|
..
gi 1443040382 592 AL 593
Cdd:cd03260 226 QI 227
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
361-595 |
1.54e-43 |
|
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: 167.52 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 361 MVLEDMNGDIELKDVYFRyPARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR 440
Cdd:TIGR01842 308 MPLPEPEGHLSVENVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 441 LDWIRGKIGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIA 520
Cdd:TIGR01842 387 RETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALA 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 521 RAILKDPKILLLDEATSALDVESERIVQEALNRMMVER-TTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVK 595
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1049-1273 |
2.33e-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: 157.73 E-value: 2.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPsrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYD-----PDSGNISLDGVEIRSLK--VS 1121
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDvdVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1122 WLRDQMGLVGQEPVLFNDTIRANITYG------KHSEVTEEEITAVAKAANAHEFVSSLPQGYDtvvgekgvqLSGGQKQ 1195
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1196 RVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEAL 1273
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1049-1275 |
3.21e-43 |
|
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: 157.49 E-value: 3.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPsrPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMG 1128
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPV--LFNDTIRANITYG-KHSEVTEEEITAVAKAA----NAHEFVSSLPQgydtvvgekgvQLSGGQKQRVAIAR 1201
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpENLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 1202 AILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTI-KGADMIAVLKEGKIAEKGKHEALLR 1275
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFS 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
366-599 |
3.34e-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: 165.85 E-value: 3.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 366 MNGDIELKDVYFRYPARPEQlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQ---SGEVLIDGISIKKLRLD 442
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 443 WIRGKIGLVSQEPL--LFMASIKDNIIYG--KKDATLEEIK-RAAELANAAnfidklpnGYDTLVGQRGTQLSGGQKQRI 517
Cdd:COG1123 80 LRGRRIGMVFQDPMtqLNPVTVGDQIAEAleNLGLSRAEARaRVLELLEAV--------GLERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 518 AIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTV-RNVDCITVVRKGKIVEQGPHDALV 594
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEIL 231
|
....*
gi 1443040382 595 KDPDG 599
Cdd:COG1123 232 AAPQA 236
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
370-584 |
9.70e-43 |
|
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: 155.73 E-value: 9.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQL-ILDGLSLQVASGTTMAIVGESGSGKST---VISLVERfydPQSGEVLIDGISIKKL---RLD 442
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLsekELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 443 WIRGK-IGLVSQEP-LLFMASIKDNI-----IYGKKDATLEEikRAAELANAANFIDKLpngydtlvGQRGTQLSGGQKQ 515
Cdd:cd03255 78 AFRRRhIGFVFQSFnLLPDLTALENVelpllLAGVPKKERRE--RAEELLERVGLGDRL--------NHYPSELSGGQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 516 RIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRNVDCITVVRKGKI 584
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
370-597 |
2.37e-42 |
|
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: 157.91 E-value: 2.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQL-ILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQ---SGEVLIDGISIKKL---RLD 442
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLsekELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 443 WIRGK-IGLVSQEPllfMAS------IKDNII--------YGKKDAtleeIKRAAE------LANAANFIDKLPNgydtl 501
Cdd:COG0444 82 KIRGReIQMIFQDP---MTSlnpvmtVGDQIAeplrihggLSKAEA----RERAIEllervgLPDPERRLDRYPH----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 502 vgqrgtQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRNV-DCITV 578
Cdd:COG0444 150 ------ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEIaDRVAV 223
|
250
....*....|....*....
gi 1443040382 579 VRKGKIVEQGPHDALVKDP 597
Cdd:COG0444 224 MYAGRIVEEGPVEELFENP 242
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
370-641 |
5.26e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 154.38 E-value: 5.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISI--KKLRLDWIRGK 447
Cdd:COG1126 2 IEIENLHKSFGDLE---VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 448 IGLVSQEPLLF--MaSIKDNIIYG--------KKDATleeiKRAAELANA---ANFIDKLPNgydtlvgqrgtQLSGGQK 514
Cdd:COG1126 79 VGMVFQQFNLFphL-TVLENVTLApikvkkmsKAEAE----ERAMELLERvglADKADAYPA-----------QLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 515 QRIAIARAILKDPKILLLDEATSALDVEserIVQEALNrMMVE-----RTTLVVAHRLSTVRNV-DCITVVRKGKIVEQG 588
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLD-VMRDlakegMTMVVVTHEMGFAREVaDRVVFMDGGRIVEEG 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 589 PHDALVKDPdgaysqlirlqethRDErhklpdsrskstslsfrrsRTKDFLSK 641
Cdd:COG1126 219 PPEEFFENP--------------QHE-------------------RTRAFLSK 238
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1053-1264 |
1.09e-41 |
|
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: 150.83 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1053 NVSFKYP--SRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLV 1130
Cdd:cd03246 5 NVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1131 GQEPVLFNDTIRANItygkhsevteeeitavakaanahefvsslpqgydtvvgekgvqLSGGQKQRVAIARAILKDPKIL 1210
Cdd:cd03246 82 PQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1211 LLDEATSALDAESERVVQDALDRV-MVNRTTIVVAHRLSTIKGADMIAVLKEGKI 1264
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1049-1263 |
1.90e-41 |
|
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: 151.47 E-value: 1.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPDVQ--IFSDFTLHIPSQKTIALVGESGSGKSTII-ALL-ErfYDPDSGNISLDGveirslkvswlr 1124
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLsALLgE--LEKLSGSVSVPG------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1125 dQMGLVGQEPVLFNDTIRANITYGKhsEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAIL 1204
Cdd:cd03250 67 -SIAYVSQEPWIQNGTIRENILFGK--PFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1205 KDPKILLLDEATSALDAES-----ERVVQDALdrvMVNRTTIVVAHRLSTIKGADMIAVLKEGK 1263
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
80-606 |
5.66e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 165.53 E-value: 5.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 80 TSGSVLRSVTKVVLNFIY--LGIGtSVASFLQVSCWTMAGERQSA-RIRSLYLKAVLRQDITFFDTEmTTGEAVSRMSSD 156
Cdd:PLN03232 939 TDQSTPKSYSPGFYIVVYalLGFG-QVAVTFTNSFWLISSSLHAAkRLHDAMLNSILRAPMLFFHTN-PTGRVINRFSKD 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 157 TLLIQGALGEKGGKLVELLSSFIGGFIIAftrGWLLTLVMLTSLPLIAI--ASAVSAQALTRV-----SSKRQTSYSDAG 229
Cdd:PLN03232 1017 IGDIDRNVANLMNMFMNQLWQLLSTFALI---GTVSTISLWAIMPLLILfyAAYLYYQSTSREvrrldSVTRSPIYAQFG 1093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 230 DTVeQTIGSIRtvvsfngekkaiamyrnfikkSYKATIEEGIITGFGMGSVMCVVFGSYGLAFWyggkLIIEKGYTGGKI 309
Cdd:PLN03232 1094 EAL-NGLSSIR---------------------AYKAYDRMAKINGKSMDNNIRFTLANTSSNRW----LTIRLETLGGVM 1147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 310 --MTILFAVLTG---------ASSLG-------NATPAVAAVVEGQSAAYNLFKTIER--------KPEIDSDDNNGMVL 363
Cdd:PLN03232 1148 iwLTATFAVLRNgnaenqagfASTMGlllsytlNITTLLSGVLRQASKAENSLNSVERvgnyidlpSEATAIIENNRPVS 1227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 364 E-DMNGDIELKDVYFRYpaRPE-QLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRL 441
Cdd:PLN03232 1228 GwPSRGSIKFEDVHLRY--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGL 1305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 442 DWIRGKIGLVSQEPLLFMASIKDNI--IYGKKDATLEEikrAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAI 519
Cdd:PLN03232 1306 TDLRRVLSIIPQSPVLFSGTVRFNIdpFSEHNDADLWE---ALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSL 1382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 520 ARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKDPDG 599
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTS 1462
|
....*..
gi 1443040382 600 AYSQLIR 606
Cdd:PLN03232 1463 AFFRMVH 1469
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
370-589 |
9.10e-41 |
|
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: 150.42 E-value: 9.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQLI-LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR---LDWIR 445
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 446 GKIGLVSQEPLLFMA-SIKDNI-----IYGKKDATLEE-IKRAAELANAANFIDKLPngydtlvgqrgTQLSGGQKQRIA 518
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENValpleIAGVPKAEIEErVLELLELVGLEDKADAYP-----------AQLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 519 IARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRNV-DCITVVRKGKIVEQGP 589
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGT 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
370-583 |
1.25e-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: 149.16 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQ--LILDGLSLQVASGTTMAIVGESGSGKSTVIS--LVErfYDPQSGEVlidgisikklrldWIR 445
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSalLGE--LEKLSGSV-------------SVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 446 GKIGLVSQEPLLFMASIKDNIIYGKK--DATLEEIKRAAELANAanfIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAI 523
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENILFGKPfdEERYEKVIKACALEPD---LEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 524 LKDPKILLLDEATSALDVE-SERIVQEALNRMMVE-RTTLVVAHRLSTVRNVDCITVVRKGK 583
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHvGRHIFENCILGLLLNnKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1051-1263 |
1.34e-40 |
|
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: 149.15 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1051 FNNVSFKYPSRpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLV 1130
Cdd:cd03225 2 LKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1131 GQEP--VLFNDTIRANITYG-KHSEVTEEEITAVAKAANAhefvsslpqgydtVVGEKGV------QLSGGQKQRVAIAR 1201
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGlENLGLPEEEIEERVEEALE-------------LVGLEGLrdrspfTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1202 AILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTIKG-ADMIAVLKEGK 1263
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
370-598 |
4.03e-40 |
|
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: 148.80 E-value: 4.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKL---RLDWIRG 446
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 KIGLVSQEPLLFMA-SIKDNI---IYGKKDATLEEIKRAAELanaanfidKLpngydTLVGQRGT------QLSGGQKQR 516
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVafpLREHTRLSEEEIREIVLE--------KL-----EAVGLRGAedlypaELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 517 IAIARAILKDPKILLLDEATSALD-VESERIVQEALN-RMMVERTTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDAL 593
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEEL 224
|
....*
gi 1443040382 594 VKDPD 598
Cdd:cd03261 225 RASDD 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
370-598 |
4.63e-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: 148.59 E-value: 4.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR---LDWIRG 446
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 KIGLVSQEPLLF--MaSIKDNIIYG---KKDATLEEIKRAA----ELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRI 517
Cdd:COG1127 83 RIGMLFQGGALFdsL-TVFENVAFPlreHTDLSEAEIRELVleklELVGLPGAADKMPS-----------ELSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 518 AIARAILKDPKILLLDEATSALD-VESERIV------QEALNrmmveRTTLVVAHRLSTVRNV-DCITVVRKGKIVEQGP 589
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDpITSAVIDelirelRDELG-----LTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGT 225
|
....*....
gi 1443040382 590 HDALVKDPD 598
Cdd:COG1127 226 PEELLASDD 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1049-1278 |
6.05e-40 |
|
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: 148.03 E-value: 6.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRpdvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWL---RD 1125
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 QMGLVGQEPVLFND-TIRANITYG--KHSEVTEEEITAVAK----AANAHEFVSSLPQgydtvvgekgvQLSGGQKQRVA 1198
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlrEHTRLSEEEIREIVLekleAVGLRGAEDLYPA-----------ELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1199 IARAILKDPKILLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEALLR 1275
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
...
gi 1443040382 1276 IKD 1278
Cdd:cd03261 227 SDD 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1049-1275 |
6.51e-40 |
|
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: 155.83 E-value: 6.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRP--DVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLK---VSWL 1123
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1124 RDQMGLVGQEPVL-FN--DTIRANITYG--KHSEVTEEEITA-VAKAANA----HEFVSSLPQgydtvvgekgvQLSGGQ 1193
Cdd:COG1123 341 RRRVQMVFQDPYSsLNprMTVGDIIAEPlrLHGLLSRAERRErVAELLERvglpPDLADRYPH-----------ELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1194 KQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKH 1270
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
....*
gi 1443040382 1271 EALLR 1275
Cdd:COG1123 490 EEVFA 494
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
370-565 |
9.53e-40 |
|
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: 146.85 E-value: 9.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYP-ARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDwirgkI 448
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 449 GLVSQEPLLF-MASIKDNIIYG------KKDATLEEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIAR 521
Cdd:cd03293 76 GYVFQQDALLpWLTVLDNVALGlelqgvPKAEARERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1443040382 522 AILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAH 565
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTH 190
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
696-1000 |
6.13e-39 |
|
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: 146.63 E-value: 6.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 696 LLLGSIAASVHGVILPLYGIIMPGVLKSFYEPPDQLRKDSRFWALMSVVLGVACLISIPAEYFLFGIAGGKLIQRVRTLS 775
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 776 FQRIMHQEVAWFDKPSnsrcatlmyfcyfifykkiftfkpmlrghlisySGALGTRLSVDALNVRRLVGDNLALIVQAVA 855
Cdd:pfam00664 81 FKKILRQPMSFFDTNS---------------------------------VGELLSRLTNDTSKIRDGLGEKLGLLFQSLA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 856 TLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSIRTVASFCSEKRVVAIYN 935
Cdd:pfam00664 128 TIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYD 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 936 KKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGKTTFSD--VFKVFFALVLAAV 1000
Cdd:pfam00664 208 KALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
370-593 |
8.45e-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: 145.00 E-value: 8.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRlDWIRGKIG 449
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMA-SIKDNI-----IYGKKDATLEeiKRAAELANAANFIDKLpngyDTLVGQrgtqLSGGQKQRIAIARAI 523
Cdd:COG4555 78 VLPDERGLYDRlTVRENIryfaeLYGLFDEELK--KRIEELIELLGLEEFL----DRRVGE----LSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 524 LKDPKILLLDEATSALDVESERIVQEALNRMMVE-RTTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDAL 593
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDEL 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1042-1266 |
1.02e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 144.42 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1042 MENVtgsIDFNNVSFKYPS-RPDVQIFSDFTLHIPSQKTIALVGESGSGKST---IIALLERfydPDSGNISLDGVEIRS 1117
Cdd:COG1136 1 MSPL---LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1118 LK----VSWLRDQMGLVGQEPVLFND-TIRANITY-----GKHSEVTEEEITAVAKAANAHEFVSSLPQgydtvvgekgv 1187
Cdd:COG1136 75 LSerelARLRRRHIGFVFQFFNLLPElTALENVALplllaGVSRKERRERARELLERVGLGDRLDHRPS----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1188 QLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLSTIKGADMIAVLKEGKIA 1265
Cdd:COG1136 144 QLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
.
gi 1443040382 1266 E 1266
Cdd:COG1136 224 S 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1067-1217 |
1.33e-38 |
|
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: 141.25 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1067 FSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFND-TIRANI 1145
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1146 TYGkhseVTEEEITAVAKAANAHEFVSSLPQGY--DTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATS 1217
Cdd:pfam00005 81 RLG----LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1049-1268 |
1.46e-38 |
|
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: 143.43 E-value: 1.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSrpdVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVsWLRDqMG 1128
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP-ERRN-IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLF-NDTIRANITYG-KHSEVTEEEITAVAKAANAHefvsslpQGYDTVVGEKGVQLSGGQKQRVAIARAILKD 1206
Cdd:cd03259 76 MVFQDYALFpHLTVAENIAFGlKLRGVPKAEIRARVRELLEL-------VGLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1207 PKILLLDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRLS---TIkgADMIAVLKEGKIAEKG 1268
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEealAL--ADRIAVMNEGRIVQVG 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
94-606 |
1.98e-38 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 157.21 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 94 NFIYlgigtSVASFLQV------SCW-TMAGERQSARIRSLYLKAVLRQDITFFDTEmTTGEAVSRMSSDTLLIQGALGE 166
Cdd:PLN03130 956 NLIY-----ALLSFGQVlvtllnSYWlIMSSLYAAKRLHDAMLGSILRAPMSFFHTN-PLGRIINRFAKDLGDIDRNVAV 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 167 KG----GKLVELLSSFiggFIIAFTRgwllTLVMLTSLPL-IAIASAV-----SAQALTRVSS-KRQTSYSDAGDTVeQT 235
Cdd:PLN03130 1030 FVnmflGQIFQLLSTF---VLIGIVS----TISLWAIMPLlVLFYGAYlyyqsTAREVKRLDSiTRSPVYAQFGEAL-NG 1101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 236 IGSIRtvvsfngekkaiamyrnfikkSYKATIEEGIITGFGMGSVMCVVFGSYGLAFWYGGKLIiekgyTGGKIM---TI 312
Cdd:PLN03130 1102 LSTIR---------------------AYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLE-----TLGGLMiwlTA 1155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 313 LFAVLTG---------ASSLG-------NATPAVAAVVEGQSAAYNLFKTIERKPE-IDSDDNNGMVLED--------MN 367
Cdd:PLN03130 1156 SFAVMQNgraenqaafASTMGlllsyalNITSLLTAVLRLASLAENSLNAVERVGTyIDLPSEAPLVIENnrpppgwpSS 1235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 368 GDIELKDVYFRYpaRPE-QLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRG 446
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 KIGLVSQEPLLFMASIKDNI--IYGKKDATLEEikrAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAIL 524
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLdpFNEHNDADLWE---SLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 525 KDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKDPDGAYSQL 604
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM 1470
|
..
gi 1443040382 605 IR 606
Cdd:PLN03130 1471 VQ 1472
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1049-1275 |
2.39e-38 |
|
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: 143.98 E-value: 2.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYP-SRPDVqifSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQM 1127
Cdd:cd03295 1 IEFENVTKRYGgGKKAV---NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1128 GLVGQEPVLF-NDTIRANI-TYGKHSEVTEEEITavAKAANAHEFVSSLPQGYdtvVGEKGVQLSGGQKQRVAIARAILK 1205
Cdd:cd03295 78 GYVIQQIGLFpHMTVEENIaLVPKLLKWPKEKIR--ERADELLALVGLDPAEF---ADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 1206 DPKILLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRL-STIKGADMIAVLKEGKIAEKGKHEALLR 1275
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1049-1268 |
3.19e-38 |
|
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: 143.03 E-value: 3.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPD-VQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRD-- 1125
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 -QMGLVGQEPVL-FND--TIRANIT-----YGKHSEVTEEEITAVAKAA---NAHEFVSSLPQgydtvvgekgvQLSGGQ 1193
Cdd:cd03257 82 kEIQMVFQDPMSsLNPrmTIGEQIAeplriHGKLSKKEARKEAVLLLLVgvgLPEEVLNRYPH-----------ELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1194 KQRVAIARAILKDPKILLLDEATSALDAESERVVQDALD--RVMVNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKG 1268
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
370-565 |
3.67e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 143.69 E-value: 3.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARP-EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDwirgkI 448
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 449 GLVSQEPLLF-MASIKDNIIYG------KKDATLEEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIAR 521
Cdd:COG1116 83 GVVFQEPALLpWLTVLDNVALGlelrgvPKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1443040382 522 AILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAH 565
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTH 197
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
370-588 |
3.80e-38 |
|
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: 142.27 E-value: 3.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYParpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDwiRGKIG 449
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLF--MaSIKDNIIYG------KKDATLEEIKRAAELANAANFIDKLPngydtlvgqrgTQLSGGQKQRIAIAR 521
Cdd:cd03259 76 MVFQDYALFphL-TVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 522 AILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAH------RLStvrnvDCITVVRKGKIVEQG 588
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHdqeealALA-----DRIAVMNEGRIVQVG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1049-1263 |
4.05e-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: 140.79 E-value: 4.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPsrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSL--KVSWLRDQ 1126
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1127 MGLVGQEPVLF-NDTIRANITYGkhsevteeeitavakaanahefvsslpqgydtvvgekgvqLSGGQKQRVAIARAILK 1205
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG----------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 1206 DPKILLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLS-TIKGADMIAVLKEGK 1263
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
378-1292 |
5.05e-38 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 156.09 E-value: 5.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 378 RYPARPEQLILDgLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVlidgisikklrldWIRGKIGLVSQEPLL 457
Cdd:PTZ00243 667 FFELEPKVLLRD-VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 458 FMASIKDNIIYGKkdatlEEikRAAELANAANF------IDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILL 531
Cdd:PTZ00243 733 MNATVRGNILFFD-----EE--DAARLADAVRVsqleadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYL 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 532 LDEATSALDVE-SERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKDPdgaysqlirLQET 610
Cdd:PTZ00243 806 LDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS---------LYAT 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 611 HRDERHKLPDSRSKSTSLSFRRSRTKDflsksnrysfksplGLPVDIheDGMTSEQQKVDHSDSKAIKKTPFGRLFNLNK 690
Cdd:PTZ00243 877 LAAELKENKDSKEGDADAEVAEVDAAP--------------GGAVDH--EPPVAKQEGNAEGGDGAALDAAAGRLMTREE 940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 691 PEVpvlllGSIAASVHGVILPLYGiimpGVLKsfyeppdqlrkdsrfWALMSVVLGVACLISIPAEYFLFGIAGGKLiqr 770
Cdd:PTZ00243 941 KAS-----GSVPWSTYVAYLRFCG----GLHA---------------AGFVLATFAVTELVTVSSGVWLSMWSTRSF--- 993
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 771 vrtlsfqrimhqevawfdKPSNSRCATLMYFCYF--IF---YKKIFTFKPMLRG----H---LISYSGA---------LG 829
Cdd:PTZ00243 994 ------------------KLSAATYLYVYLGIVLlgTFsvpLRFFLSYEAMRRGsrnmHrdlLRSVSRGtmsffdttpLG 1055
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 830 ---TRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADwrlALIITCVIPLvgaqGYAQVKFLKGFSEESKEMYED 906
Cdd:PTZ00243 1056 rilNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQ---PFVLVALVPC----GYLYYRLMQFYNSANREIRRI 1128
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 907 ANQVAA-------DAVGSIRTVASFCSEKRVVAiynkkcEALRKQ-----------------GIR--------------S 948
Cdd:PTZ00243 1129 KSVAKSpvftlleEALQGSATITAYGKAHLVMQ------EALRRLdvvyscsylenvanrwlGVRveflsnivvtvialI 1202
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 949 GIVGG--------IGL-SFSNLM-LYLTYGLCFYVgaKFVSQGKTTFSDVFKVFF--------------ALVlaavgvsq 1004
Cdd:PTZ00243 1203 GVIGTmlratsqeIGLvSLSLTMaMQTTATLNWLV--RQVATVEADMNSVERLLYytdevphedmpeldEEV-------- 1272
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1005 sSALSTNATKARDSAISIFsiidrksrIDSSSDEGAIMENV-TGSIDFNNVSFKY-PSRPDVQIFSDFTLHiPSQKtIAL 1082
Cdd:PTZ00243 1273 -DALERRTGMAADVTGTVV--------IEPASPTSAAPHPVqAGSLVFEGVQMRYrEGLPLVLRGVSFRIA-PREK-VGI 1341
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1083 VGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFNDTIRANITygKHSEVTEEEITAVA 1162
Cdd:PTZ00243 1342 VGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD--PFLEASSAEVWAAL 1419
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1163 KAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILK-DPKILLLDEATSALDAESERVVQDALDRVMVNRTTI 1241
Cdd:PTZ00243 1420 ELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVI 1499
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 1242 VVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRIKDGAYASLVQLRSNSE 1292
Cdd:PTZ00243 1500 TIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEALGRSE 1550
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1048-1275 |
6.10e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 146.06 E-value: 6.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1048 SIDFNNVSFKYPSRpdvQIFSDFTLHIPSQKTIALVGESGSGKST---IIALLERfydPDSGNISLDGVEIRS-LKVswl 1123
Cdd:COG1118 2 SIEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTllrIIAGLET---PDSGRIVLNGRDLFTnLPP--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1124 RD-QMGLVGQEPVLF-NDTIRANITYG-KHSEVTEEEITAVA----KAANAHEFVSSLPQgydtvvgekgvQLSGGQKQR 1196
Cdd:COG1118 73 RErRVGFVFQHYALFpHMTVAENIAFGlRVRPPSKAEIRARVeellELVQLEGLADRYPS-----------QLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1197 VAIARAILKDPKILLLDEATSALDA----ESERVVQDALDRvmVNRTTIVVAH------RLstikgADMIAVLKEGKIAE 1266
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDE--LGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQ 214
|
....*....
gi 1443040382 1267 KGKHEALLR 1275
Cdd:COG1118 215 VGTPDEVYD 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1049-1274 |
6.85e-38 |
|
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: 142.33 E-value: 6.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRP-DVQIFSDFTLHIPSQKTIALVGESGSGKST---IIALLERfydPDSGNISLDGVEIRSLKVSWLR 1124
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLER---PTSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1125 D---QMGLVGQEPVLFND-TIRANITYG-KHSEVTEEEITAvaKAANAHEFV--SSLPQGYDTvvgekgvQLSGGQKQRV 1197
Cdd:cd03258 79 KarrRIGMIFQHFNLLSSrTVFENVALPlEIAGVPKAEIEE--RVLELLELVglEDKADAYPA-------QLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1198 AIARAILKDPKILLLDEATSALDAESERVVQDALDRvmVNR----TTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEA 1272
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRD--INRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
..
gi 1443040382 1273 LL 1274
Cdd:cd03258 228 VF 229
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
370-583 |
8.20e-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: 8.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYParpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDW--IRGK 447
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 448 IGLVSQEPLLF--MaSIKDNIIYGkkdatleeikraaelanaanfidklpngydtlvgqrgtqLSGGQKQRIAIARAILK 525
Cdd:cd03229 78 IGMVFQDFALFphL-TVLENIALG---------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 526 DPKILLLDEATSALDVESERIVQEALNRM--MVERTTLVVAHRLSTVRNV-DCITVVRKGK 583
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1032-1286 |
1.02e-37 |
|
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: 142.74 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1032 IDSSSDEGAImeNVTGSIDFNNVSFKYPS--RPdvqIFSDFTLHI-PSQKtIALVGESGSGKSTIIALLERFYDPDSGNI 1108
Cdd:cd03288 5 ISGSSNSGLV--GLGGEIKIHDLCVRYENnlKP---VLKHVKAYIkPGQK-VGICGRTGSGKSSLSLAFFRMVDIFDGKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1109 SLDGVEIRSLKVSWLRDQMGLVGQEPVLFNDTIRANITygKHSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQ 1188
Cdd:cd03288 79 VIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLD--PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1189 LSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKG 1268
Cdd:cd03288 157 FSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECD 236
|
250
....*....|....*...
gi 1443040382 1269 KHEALLRIKDGAYASLVQ 1286
Cdd:cd03288 237 TPENLLAQEDGVFASLVR 254
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
370-584 |
1.14e-37 |
|
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: 139.46 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDwIRGKIG 449
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPllfmasikdniiygkkdatleeikraaelanaaNFIDKLpNGYDTLvgqrgtQLSGGQKQRIAIARAILKDPKI 529
Cdd:cd03230 77 YLPEEP---------------------------------SLYENL-TVRENL------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 530 LLLDEATSALDVESERIVQEALNRMMVERTTLVVA-HRLSTVRNV-DCITVVRKGKI 584
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERLcDRVAILNNGRI 173
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
353-606 |
1.35e-37 |
|
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: 142.36 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 353 IDSDDNNGMVleDMNGDIELKDVYFRYPA--RPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVL 430
Cdd:cd03288 5 ISGSSNSGLV--GLGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 431 IDGISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNIIYGKK--DATLEEikrAAELANAANFIDKLPNGYDTLVGQRGTQ 508
Cdd:cd03288 80 IDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKctDDRLWE---ALEIAQLKNMVKSLPGGLDAVVTEGGEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 509 LSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQG 588
Cdd:cd03288 157 FSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECD 236
|
250
....*....|....*...
gi 1443040382 589 PHDALVKDPDGAYSQLIR 606
Cdd:cd03288 237 TPENLLAQEDGVFASLVR 254
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
370-589 |
1.40e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 144.84 E-value: 1.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQLI-LDGLSLQVASGTTMAIVGESGSGKST---VISLVERfydPQSGEVLIDGISI-----KKLR 440
Cdd:COG1135 2 IELENLSKTFPTKGGPVTaLDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLtalseRELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 441 LdwIRGKIGLVSQEPLLFMA-SIKDNIIY-----GKKDAtleEI-KRAAELANaanfidklpngydtLVGQRG------T 507
Cdd:COG1135 79 A--ARRKIGMIFQHFNLLSSrTVAENVALpleiaGVPKA---EIrKRVAELLE--------------LVGLSDkadaypS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 508 QLSGGQKQRIAIARAILKDPKILLLDEATSALDVES--------ERIVQEaLNrmmveRTTLVVAHRLSTVRNV-DCITV 578
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsildllKDINRE-LG-----LTIVLITHEMDVVRRIcDRVAV 213
|
250
....*....|.
gi 1443040382 579 VRKGKIVEQGP 589
Cdd:COG1135 214 LENGRIVEQGP 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-593 |
1.65e-37 |
|
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: 154.33 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 29 KKVPLFSLFryadrLDVLLMVVGTVGALGNGISQPLMTVlfGNVINSFGANTSgsVLRSVtkvvlnFIYLGIGTSVASFL 108
Cdd:TIGR00957 960 KAIGLFITF-----LSIFLFVCNHVSALASNYWLSLWTD--DPMVNGTQNNTS--LRLSV------YGALGILQGFAVFG 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 109 QVSCWTMAGERQSARIRSLYLKAVLRQDITFFDTeMTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTR 188
Cdd:TIGR00957 1025 YSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFER-TPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLA 1103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 189 GWLLTLVMLtslPLIAIASAV------SAQALTRVSS-KRQTSYSDAGDTVEqtigSIRTVVSFNGEKKAIAMYRNFIKK 261
Cdd:TIGR00957 1104 TPIAAVIIP---PLGLLYFFVqrfyvaSSRQLKRLESvSRSPVYSHFNETLL----GVSVIRAFEEQERFIHQSDLKVDE 1176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 262 SYKATIEEGIITGFGMGSVMCVvfgsyglafwygGKLIIekgytggkIMTILFAVLtGASSLGnatpavAAVVeGQSAAY 341
Cdd:TIGR00957 1177 NQKAYYPSIVANRWLAVRLECV------------GNCIV--------LFAALFAVI-SRHSLS------AGLV-GLSVSY 1228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 342 NLFKT-------------------IERKPEIDSDDNNG-MVLEDM--------NGDIELKDVYFRYpaRPE-QLILDGLS 392
Cdd:TIGR00957 1229 SLQVTfylnwlvrmssemetnivaVERLKEYSETEKEApWQIQETappsgwppRGRVEFRNYCLRY--REDlDLVLRHIN 1306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 393 LQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNI-IYGKK 471
Cdd:TIGR00957 1307 VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQY 1386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 472 DAtlEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEAL 551
Cdd:TIGR00957 1387 SD--EEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI 1464
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1443040382 552 NRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQG-PHDAL 593
Cdd:TIGR00957 1465 RTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGaPSNLL 1507
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1049-1268 |
2.06e-37 |
|
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: 141.15 E-value: 2.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSrpdVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSlKVSWLRDQMG 1128
Cdd:COG4555 2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLF-NDTIRANITY-----GKHSEVTEEEITAVAKAANahefvssLPQGYDTVVGEkgvqLSGGQKQRVAIARA 1202
Cdd:COG4555 78 VLPDERGLYdRLTVRENIRYfaelyGLFDEELKKRIEELIELLG-------LEEFLDRRVGE----LSTGMKKKVALARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1203 ILKDPKILLLDEATSALDAESERVVQDALDRVM-VNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKG 1268
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQG 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1049-1275 |
2.24e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 140.58 E-value: 2.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPsrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRdQMG 1128
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLFND-TIRANIT-----YGKHSEVTEEEITAVAKAANahefvssLPQGYDTVVGekgvQLSGGQKQRVAIARA 1202
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRffarlYGLPRKEARERIDELLELFG-------LTDAADRKVG----TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1203 ILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTI-KGADMIAVLKEGKIAEKGKHEALLR 1275
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
370-593 |
2.74e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 140.99 E-value: 2.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRldwirGKIG 449
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-----RRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLL---FMASIKDNI------------IYGKKDAtlEEIKRAAELANAANFIDKLpngydtlVGQrgtqLSGGQK 514
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgrygrrglfrRPSRADR--EAVDEALERVGLEDLADRP-------IGE----LSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 515 QRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTT-LVVAHRLSTVR-NVDCITVVRKGKIVEQGPHDA 592
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTiLVVTHDLGAVReYFDRVLLLNRGLVAHGPPEEV 225
|
.
gi 1443040382 593 L 593
Cdd:COG1121 226 L 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1049-1264 |
2.77e-37 |
|
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: 139.93 E-value: 2.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPD-VQIFSDFTLHIPSQKTIALVGESGSGKST---IIALLERfydPDSGNISLDGVEIRSLKVSWL- 1123
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1124 ---RDQMGLVGQEPVLFND-TIRANITY-----GKHSEVTEEEITAVAK----AANAHEFVSslpqgydtvvgekgvQLS 1190
Cdd:cd03255 78 afrRRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRERAEELLErvglGDRLNHYPS---------------ELS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 1191 GGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLSTIKGADMIAVLKEGKI 1264
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
370-589 |
4.94e-37 |
|
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: 141.03 E-value: 4.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDW-IRGKI 448
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 449 GLVSQEPllfmasikDNIIYGkkdATLEE-------------------IKRAAELANAANFIDKLPNgydtlvgqrgtQL 509
Cdd:TIGR04520 80 GMVFQNP--------DNQFVG---ATVEDdvafglenlgvpreemrkrVDEALKLVGMEDFRDREPH-----------LL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 510 SGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRNVDCITVVRKGKIVEQ 587
Cdd:TIGR04520 138 SGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
..
gi 1443040382 588 GP 589
Cdd:TIGR04520 218 GT 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1048-1268 |
5.60e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 143.31 E-value: 5.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1048 SIDFNNVSFKYPsrpDVQIFSDFTLHIPSQKTIALVGESGSGKST---IIALLERfydPDSGNISLDGVEIRSLKVSwlR 1124
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTllrMIAGFET---PDSGRILLDGRDVTGLPPE--K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1125 DQMGLVGQEPVLF-NDTIRANITYG-KHSEVTEEEITAvaKAANAHEFVSsLpQGYdtvvGEKGV-QLSGGQKQRVAIAR 1201
Cdd:COG3842 77 RNVGMVFQDYALFpHLTVAENVAFGlRMRGVPKAEIRA--RVAELLELVG-L-EGL----ADRYPhQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1202 AILKDPKILLLDEATSALDAESERVVQDALDRVM--VNRTTIVVAHRLS---TIkgADMIAVLKEGKIAEKG 1268
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQreLGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVG 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
370-596 |
5.92e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 140.90 E-value: 5.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIG 449
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEP--LLFMASIKDNIIYG--KKDATLEEIKR----AAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIAR 521
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGleNKKVPPKKMKDiiddLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 522 AILKDPKILLLDEATSALDVESERIVQEALNRMMVERT-TLV-VAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKD 596
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1042-1266 |
6.73e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 140.22 E-value: 6.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1042 MENVTGSIDFNNVSFKYPSRP-DVQIFSDFTLHIPSQKTIALVGESGSGKST---IIALLERfydPDSGNISLDGVEIRS 1117
Cdd:COG1116 1 MSAAAPALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTllrLIAGLEK---PTSGEVLVDGKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1118 LkvswlRDQMGLVGQEPVLFN-DTIRANITYG-KHSEVTEEEITAVAKAANAH----EFVSSLPQgydtvvgekgvQLSG 1191
Cdd:COG1116 78 P-----GPDRGVVFQEPALLPwLTVLDNVALGlELRGVPKAERRERARELLELvglaGFEDAYPH-----------QLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1192 GQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRV-MVNRTTIV-VAH------RLstikgADMIAVLKE-- 1261
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLfVTHdvdeavFL-----ADRVVVLSArp 216
|
....*
gi 1443040382 1262 GKIAE 1266
Cdd:COG1116 217 GRIVE 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1049-1282 |
6.99e-37 |
|
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: 139.94 E-value: 6.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRP-DVQIFSDFTLHIPSQKTIALVGESGSGKSTI---IALLERfydPDSGNISLDGVEIRSLKVSWLR 1124
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLlraLAGLER---PWSGEVTFDGRPVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1125 DQMGLVGQEPVL-FND--TIRANItygkhSEV--------TEEEITAVAKAAN-AHEFVSSLPQgydtvvgekgvQLSGG 1192
Cdd:COG1124 79 RRVQMVFQDPYAsLHPrhTVDRIL-----AEPlrihglpdREERIAELLEQVGlPPSFLDRYPH-----------QLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1193 QKQRVAIARAILKDPKILLLDEATSALDAeserVVQ----DALDRVMVNR--TTIVVAHRLSTI-KGADMIAVLKEGKIA 1265
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDV----SVQaeilNLLKDLREERglTYLFVSHDLAVVaHLCDRVAVMQNGRIV 218
|
250
....*....|....*..
gi 1443040382 1266 EKGKHEALLRIKDGAYA 1282
Cdd:COG1124 219 EELTVADLLAGPKHPYT 235
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1049-1278 |
7.62e-37 |
|
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: 139.34 E-value: 7.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVS---WLRD 1125
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 QMGLVGQEPVLFND-TIRANITYG--KHSEVTEEEITAVAKAANAHefvsslpqgydtvVGEKGV------QLSGGQKQR 1196
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlrEHTDLSEAEIRELVLEKLEL-------------VGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1197 VAIARAILKDPKILLLDEATSALDAESERVV-------QDALdrvmvNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKG 1268
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIdelirelRDEL-----GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
250
....*....|
gi 1443040382 1269 KHEALLRIKD 1278
Cdd:COG1127 225 TPEELLASDD 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
370-586 |
8.58e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 138.65 E-value: 8.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYParPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR---LDWIRG 446
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 KIGLVSQE-PLLFMASIKDNI-----IYGKKDAtleEIKRAAELA----NAANFIDKLPNgydtlvgqrgtQLSGGQKQR 516
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENValplrVTGKSRK---EIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 517 IAIARAILKDPKILLLDEATSALDVE-SERIVQ--EALNRMmveRTTLVVA-HRLSTVRNVDCITVV-RKGKIVE 586
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPEtSWEIMEllEEINRR---GTTVLIAtHDLELVDRMPKRVLElEDGRLVR 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
371-583 |
8.75e-37 |
|
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: 136.22 E-value: 8.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 371 ELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGL 450
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 451 VSQepllfmasikdniiygkkdatleeikraaelanaanfidklpngydtlvgqrgtqLSGGQKQRIAIARAILKDPKIL 530
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 531 LLDEATSALDVESERIVQEALNRMMVE-RTTLVVAHRLSTVRNV-DCITVVRKGK 583
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
366-589 |
9.17e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 142.54 E-value: 9.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 366 MNG-DIELKDVYFRYParpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKL----R 440
Cdd:COG3842 1 MAMpALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppekR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 441 ldwirgKIGLVSQEPLLF--MaSIKDNIIYG------KKDATLEEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGG 512
Cdd:COG3842 78 ------NVGMVFQDYALFphL-TVAENVAFGlrmrgvPKAEIRARVAELLELVGLEGLADRYPH-----------QLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 513 QKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAH------RLStvrnvDCITVVRKGKI 584
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHdqeealALA-----DRIAVMNDGRI 214
|
....*
gi 1443040382 585 VEQGP 589
Cdd:COG3842 215 EQVGT 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1049-1274 |
1.56e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 138.59 E-value: 1.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPsrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTI---IALLERfydPDSGNISLDGVEIRSLKVSW--L 1123
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLTDSKKDInkL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1124 RDQMGLVGQEPVLFND-TIRANITYG--KHSEVTEEEITAVAKA----------ANAHefvsslPQgydtvvgekgvQLS 1190
Cdd:COG1126 76 RRKVGMVFQQFNLFPHlTVLENVTLApiKVKKMSKAEAEERAMEllervgladkADAY------PA-----------QLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1191 GGQKQRVAIARAILKDPKILLLDEATSALDAEserVVQDALDrVMVN-----RTTIVVAHRLSTIKG-ADMIAVLKEGKI 1264
Cdd:COG1126 139 GGQQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLD-VMRDlakegMTMVVVTHEMGFAREvADRVVFMDGGRI 214
|
250
....*....|
gi 1443040382 1265 AEKGKHEALL 1274
Cdd:COG1126 215 VEEGPPEEFF 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
388-603 |
2.01e-36 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 141.02 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR---LDWIRGKIGLVSQEPllfMAS--- 461
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP---YASlnp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 462 ---IKDNI-----IYGKKDATlEEIKRAAELANA----ANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIARAILKDPKI 529
Cdd:COG4608 111 rmtVGDIIaeplrIHGLASKA-ERRERVAELLELvglrPEHADRYPH-----------EFSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 530 LLLDEATSALDVeSeriVQ-EALNRMM--VER---TTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKDPDGAYS 602
Cdd:COG4608 179 IVCDEPVSALDV-S---IQaQVLNLLEdlQDElglTYLFISHDLSVVRHIsDRVAVMYLGKIVEIAPRDELYARPLHPYT 254
|
.
gi 1443040382 603 Q 603
Cdd:COG4608 255 Q 255
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1051-1263 |
2.54e-36 |
|
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: 135.06 E-value: 2.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1051 FNNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLV 1130
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1131 GQepvlfndtiranitygkhsevteeeitavakaanahefvsslpqgydtvvgekgvqLSGGQKQRVAIARAILKDPKIL 1210
Cdd:cd00267 79 PQ--------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1211 LLDEATSALDAESERVVQDALDRVMV-NRTTIVVAHRLSTI-KGADMIAVLKEGK 1263
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
370-593 |
2.88e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 137.88 E-value: 2.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARpeQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR---LDWIRG 446
Cdd:COG3638 3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 KIGLVSQEPLLFM-ASIKDNIIYGK-----------KDATLEEIKRAAELANAANFIDKLpngydtlvGQRGTQLSGGQK 514
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVLAGRlgrtstwrsllGLFPPEDRERALEALERVGLADKA--------YQRADQLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 515 QRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRN-VDCITVVRKGKIVEQGPHD 591
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRyADRIIGLRDGRVVFDGPPA 232
|
..
gi 1443040382 592 AL 593
Cdd:COG3638 233 EL 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
370-589 |
3.95e-36 |
|
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: 137.87 E-value: 3.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIG 449
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLL-FMASIKDNIIYG------------KKDatLEEIKRAAELANAANFIDKLpngYDTLvgqrgtqlSGGQKQR 516
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlglfgrpsAED--REAVEEALERTGLEHLADRP---VDEL--------SGGERQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 517 IAIARAILKDPKILLLDEATSALD----VESERIVQEaLNRMMvERTTLVVAHRLSTVRNV-DCITVVRKGKIVEQGP 589
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRR-LARER-GRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGP 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
365-589 |
6.68e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 137.84 E-value: 6.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 365 DMNGDIELKDVYFRYPaRPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWI 444
Cdd:PRK13635 1 MKEEIIRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 445 RGKIGLVSQEP--LLFMASIKDNIIYG------KKDATLEEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQR 516
Cdd:PRK13635 80 RRQVGMVFQNPdnQFVGATVQDDVAFGlenigvPREEMVERVDQALRQVGMEDFLNREPH-----------RLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 517 IAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRNVDCITVVRKGKIVEQGP 589
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
370-597 |
1.14e-35 |
|
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: 136.28 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIG 449
Cdd:cd03295 1 IEFENVTKRYGGGKK--AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLF-MASIKDNI-----IYGKKDATLEEikRAAEL-----ANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIA 518
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIalvpkLLKWPKEKIRE--RADELlalvgLDPAEFADRYPH-----------ELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 519 IARAILKDPKILLLDEATSALDVESERIVQEALNRMMVE--RTTLVVAHRL-STVRNVDCITVVRKGKIVEQGPHDALVK 595
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
..
gi 1443040382 596 DP 597
Cdd:cd03295 226 SP 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1049-1268 |
1.26e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 139.06 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRP-DVQIFSDFTLHIPSQKTIALVGESGSGKST---IIALLERfydPDSGNISLDGVEIRSLKVSWLR 1124
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1125 D---QMGLVGQEPVLFND-TIRANITYG-KHSEVTEEEITavAKAANAHEFV------SSLPQgydtvvgekgvQLSGGQ 1193
Cdd:COG1135 79 AarrKIGMIFQHFNLLSSrTVAENVALPlEIAGVPKAEIR--KRVAELLELVglsdkaDAYPS-----------QLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1194 KQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRvmVNRT---TIVVA-HRLSTIKG-ADMIAVLKEGKIAEKG 1268
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKD--INRElglTIVLItHEMDVVRRiCDRVAVLENGRIVEQG 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
371-588 |
1.86e-35 |
|
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: 133.33 E-value: 1.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 371 ELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGL 450
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 451 VSQepllfmasikdniiygkkdatleeikrAAELANAANFIDKlpnGYDTLvgqrgtqlSGGQKQRIAIARAILKDPKIL 530
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADR---PFNEL--------SGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 531 LLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLS-TVRNVDCITVVRKGKIVEQG 588
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1049-1266 |
2.00e-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: 134.52 E-value: 2.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPS-RPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLkvswlRDQM 1127
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1128 GLVGQEPVLFN-DTIRANITYG-KHSEVTEEEITAVAKAANA----HEFVSSLPQgydtvvgekgvQLSGGQKQRVAIAR 1201
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlELQGVPKAEARERAEELLElvglSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1202 AILKDPKILLLDEATSALDAESERVVQDALDRVMV-NRTTIV-VAHRLS-TIKGADMIAVLKE--GKIAE 1266
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWReTGKTVLlVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
68-340 |
2.04e-35 |
|
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: 136.88 E-value: 2.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 68 LFGNVINSFGANTSGSVLRSVTKVVLNFIYLGIGT--SVASFLQVSCWTMAGERQSARIRSLYLKAVLRQDITFFDTEMT 145
Cdd:cd18573 18 AIGKLIDVASKESGDIEIFGLSLKTFALALLGVFVvgAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 146 tGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTRGWLLTLVMLTSLPLIAIASAVSAQALTRVSSKRQTSY 225
Cdd:cd18573 98 -GELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 226 SDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFGMGSVMCVVFGSYGLAFWYGGKLIIEKGYT 305
Cdd:cd18573 177 ADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELT 256
|
250 260 270
....*....|....*....|....*....|....*..
gi 1443040382 306 GGKiMT--ILFAVLTGaSSLGNATPAVAAVVEGQSAA 340
Cdd:cd18573 257 VGD-LTsfLMYAVYVG-SSVSGLSSFYSELMKGLGAS 291
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
370-593 |
2.49e-35 |
|
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: 135.00 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR---LDWIRG 446
Cdd:cd03256 1 IEVENLSKTYPNGKK--ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 KIGLVSQE-PLLFMASIKDNIIYGKKDA-----------TLEEIKRAAELanaanfIDKLpnGYDTLVGQRGTQLSGGQK 514
Cdd:cd03256 79 QIGMIFQQfNLIERLSVLENVLSGRLGRrstwrslfglfPKEEKQRALAA------LERV--GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 515 QRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVR-NVDCITVVRKGKIVEQGPHD 591
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230
|
..
gi 1443040382 592 AL 593
Cdd:cd03256 231 EL 232
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1049-1273 |
1.28e-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: 133.08 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRD--- 1125
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 QMGLVGQEPVLFND-TIRANITYGKHSE----------VTEEEItavAKAANAHEFVsslpqGYDTVVGEKGVQLSGGQK 1194
Cdd:cd03256 79 QIGMIFQQFNLIERlSVLENVLSGRLGRrstwrslfglFPKEEK---QRALAALERV-----GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1195 QRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHE 1271
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPA 230
|
..
gi 1443040382 1272 AL 1273
Cdd:cd03256 231 EL 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1049-1274 |
1.62e-34 |
|
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: 133.25 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMG 1128
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVL-FNDTIRANITYGKH------SEVTEEEITAVAKA---ANAHEFVSslpQGYDTvvgekgvqLSGGQKQRVA 1198
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRYphlglfGRPSAEDREAVEEAlerTGLEHLAD---RPVDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1199 IARAILKDPKILLLDEATSALD----AESERVVQD-ALDRvmvNRTTIVVAHRLS-TIKGADMIAVLKEGKIAEKGKHEA 1272
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRlARER---GRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEE 224
|
..
gi 1443040382 1273 LL 1274
Cdd:COG1120 225 VL 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1042-1275 |
2.01e-34 |
|
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: 139.65 E-value: 2.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1042 MENVtgsIDFNNVSFKYPSRpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPD---SGNISLDGVEIRSL 1118
Cdd:COG1123 1 MTPL---LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1119 KVSWLRDQMGLVGQEP--VLFNDTIRANITYG-KHSEVTEEEITAvaKAANAHEFVsslpqGYDTVVGEKGVQLSGGQKQ 1195
Cdd:COG1123 77 SEALRGRRIGMVFQDPmtQLNPVTVGDQIAEAlENLGLSRAEARA--RVLELLEAV-----GLERRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1196 RVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEA 1272
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEE 229
|
...
gi 1443040382 1273 LLR 1275
Cdd:COG1123 230 ILA 232
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
70-334 |
2.01e-34 |
|
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: 133.82 E-value: 2.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 70 GNVINSFGANTSGSVLRsvtKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSARIRSLYLKAVLRQDITFFDtEMTTGEA 149
Cdd:cd18572 20 GAVIDAVVADGSREAFY---RAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD-ATKTGEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 150 VSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTRGWLLTLVMLTSLPLIAIASAVSAQALTRVSSKRQTSYSDAG 229
Cdd:cd18572 96 TSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEAN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 230 DTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFGMGSVMCVVFGSYGLAFWYGGKLIIEKGYTGGKI 309
Cdd:cd18572 176 QVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQL 255
|
250 260
....*....|....*....|....*
gi 1443040382 310 MTILFAVLtgasSLGNATPAVAAVV 334
Cdd:cd18572 256 VTFMLYQQ----QLGEAFQSLGDVF 276
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1042-1269 |
3.23e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.81 E-value: 3.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1042 MENVTGSIDFNNVSFKYPSRpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVS 1121
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1122 WLRDQMGLVGQEPvlfnD------TIRANITYG-KHSEVTEEE----ITAVAKAANAHEFVSSLPQgydtvvgekgvQLS 1190
Cdd:PRK13632 80 EIRKKIGIIFQNP----DnqfigaTVEDDIAFGlENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQ-----------NLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1191 GGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALD--RVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKG 1268
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQG 224
|
.
gi 1443040382 1269 K 1269
Cdd:PRK13632 225 K 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
370-584 |
3.83e-34 |
|
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: 130.73 E-value: 3.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYParpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISI--KKLRLDWIRGK 447
Cdd:cd03262 1 IEIKNLHKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 448 IGLVSQEPLLF--MaSIKDNIIYG-------KKDATLEEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIA 518
Cdd:cd03262 78 VGMVFQQFNLFphL-TVLENITLApikvkgmSKAEAEERALELLEKVGLADKADAYPA-----------QLSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 519 IARAILKDPKILLLDEATSALDVEserIVQEALNrMMVE-----RTTLVVAHRLSTVRNV-DCITVVRKGKI 584
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPE---LVGEVLD-VMKDlaeegMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
371-572 |
5.10e-34 |
|
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: 130.35 E-value: 5.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 371 ELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKlrldwIRGKIGL 450
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 451 VSQEPLL---FMASIKDNI------------IYGKKDAtlEEIKRAAELANAANFIDklpngydtlvgQRGTQLSGGQKQ 515
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVlmglyghkglfrRLSKADK--AKVDEALERVGLSELAD-----------RQIGELSGGQQQ 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 516 RIAIARAILKDPKILLLDEATSALDVESERIVQEALNRM-MVERTTLVVAHRLSTVRN 572
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLE 197
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
370-589 |
7.68e-34 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 133.77 E-value: 7.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQLI-LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISI-----KKLRLdw 443
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalseKELRK-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 444 IRGKIGLVSQE-PLLFMASIKDNI-----IYGKKDAtleEIK-RAAELANaanfidklpngydtLVG---QRGT---QLS 510
Cdd:PRK11153 80 ARRQIGMIFQHfNLLSSRTVFDNValpleLAGTPKA---EIKaRVTELLE--------------LVGlsdKADRypaQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 511 GGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEAL---NRMMvERTTLVVAHRLSTVRNV-DCITVVRKGKIVE 586
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLkdiNREL-GLTIVLITHEMDVVKRIcDRVAVIDAGRLVE 221
|
...
gi 1443040382 587 QGP 589
Cdd:PRK11153 222 QGT 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
370-597 |
2.73e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 129.77 E-value: 2.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYParpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYD--PQ---SGEVLIDGISI--KKLRLD 442
Cdd:COG1117 12 IEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 443 WIRGKIGLVSQEPLLFMASIKDNIIYG------KKDATLEEI-----KRAA---ELAnaanfiDKLpngydtlvGQRGTQ 508
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIveeslRKAAlwdEVK------DRL--------KKSALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 509 LSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAH------RLStvrnvDCITVVRKG 582
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYLG 229
|
250
....*....|....*
gi 1443040382 583 KIVEQGPHDALVKDP 597
Cdd:COG1117 230 ELVEFGPTEQIFTNP 244
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1049-1276 |
2.80e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 128.72 E-value: 2.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPsrpdVQIFSdFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLkvswlrdqmg 1128
Cdd:COG3840 2 LRLDDLTYRYG----DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPV--LFND-------TIRANITYGKHS--EVTEEEITAVAKAA---NAHEFVSSLPQgydtvvgekgvQLSGGQK 1194
Cdd:COG3840 67 PPAERPVsmLFQEnnlfphlTVAQNIGLGLRPglKLTAEQRAQVEQALervGLAGLLDRLPG-----------QLSGGQR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1195 QRVAIARAILKDPKILLLDEATSALD----AESERVVQDALDRvmVNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGK 1269
Cdd:COG3840 136 QRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGP 213
|
....*..
gi 1443040382 1270 HEALLRI 1276
Cdd:COG3840 214 TAALLDG 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
356-1274 |
3.89e-33 |
|
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: 140.05 E-value: 3.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 356 DDNNGMVledmNGDIELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEvlidgis 435
Cdd:TIGR01271 417 NKARKQP----NGDDGLFFSNFSLYVTP---VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK------- 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 436 IKKlrldwiRGKIGLVSQEPLLFMASIKDNIIYGkkdATLEEIkRAAELANAANF---IDKLPNGYDTLVGQRGTQLSGG 512
Cdd:TIGR01271 483 IKH------SGRISFSPQTSWIMPGTIKDNIIFG---LSYDEY-RYTSVIKACQLeedIALFPEKDKTVLGEGGITLSGG 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 513 QKQRIAIARAILKDPKILLLDEATSALDVESER-IVQEALNRMMVERTTLVVAHRLSTVRNVD---------C------- 575
Cdd:TIGR01271 553 QRARISLARAVYKDADLYLLDSPFTHLDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADkilllhegvCyfygtfs 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 576 ----------------------------------------------------------------------------ITVV 579
Cdd:TIGR01271 633 elqakrpdfsslllgleafdnfsaerrnsiltetlrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpIASA 712
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 580 RKGKIVEQGPHDALVKDPDGAYSQLI--RLQETHRDERHK--LPDSRSKSTSLSF---RRSRTKDFLSKSNR-------- 644
Cdd:TIGR01271 713 RKFSFVQMGPQKAQATTIEDAVREPSerKFSLVPEDEQGEesLPRGNQYHHGLQHqaqRRQSVLQLMTHSNRgenrreql 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 645 -YSFKSPLGLP--------VDIH-----EDGMTSEQQKVDHSDSK------------AIKKTPFGRLFNLNKPEVPVLL- 697
Cdd:TIGR01271 793 qTSFRKKSSITqqnelaseLDIYsrrlsKDSVYEISEEINEEDLKecfaderenvfeTTTWNTYLRYITTNRNLVFVLIf 872
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 698 -----LGSIAASVHGVILPLYGIIMPGVLKSfyEPPDQLRKDSRFwalmsvvlgvACLISIPAEYFLFGIAGGkLIQRVR 772
Cdd:TIGR01271 873 clvifLAEVAASLLGLWLITDNPSAPNYVDQ--QHANASSPDVQK----------PVIITPTSAYYIFYIYVG-TADSVL 939
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 773 TLSFQR---IMHqevawfdkpsnsrcaTLMYFCYfIFYKKIFTfkPMLRGHLISY----SGALGTRLSVDALNVRRLVGD 845
Cdd:TIGR01271 940 ALGFFRglpLVH---------------TLLTVSK-RLHEQMLH--SVLQAPMAVLntmkAGRILNRFTKDMAIIDDMLPL 1001
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 846 NLALIVQAvaTLITGFAIAFAADWRlALIITCVIPLVGAQGYAQVKFLKGfSEESKEMYEDANQ-VAADAVGSIR---TV 921
Cdd:TIGR01271 1002 TLFDFIQL--TLIVLGAIFVVSVLQ-PYIFIAAIPVAVIFIMLRAYFLRT-SQQLKQLESEARSpIFSHLITSLKglwTI 1077
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 922 ASFCSEKRVVAIYNKkcealrkqgirsgivgGIGLSFSNLMLYLTYGLCFYVGAKFVsqgkttfsdvFKVFF-ALVLAAV 1000
Cdd:TIGR01271 1078 RAFGRQSYFETLFHK----------------ALNLHTANWFLYLSTLRWFQMRIDII----------FVFFFiAVTFIAI 1131
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1001 GVSQSS--------ALSTNATK----ARDSAISIFSIIDRKSR----IDSSSDEGA--------------IMEN------ 1044
Cdd:TIGR01271 1132 GTNQDGegevgiilTLAMNILStlqwAVNSSIDVDGLMRSVSRvfkfIDLPQEEPRpsggggkyqlstvlVIENphaqkc 1211
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1045 --VTGSIDFNNVSFKYPSRPDvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDsGNISLDGVEIRSLKVSW 1122
Cdd:TIGR01271 1212 wpSGGQMDVQGLTAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQT 1289
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1123 LRDQMGLVGQEPVLFNDTIRANITygKHSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARA 1202
Cdd:TIGR01271 1290 WRKAFGVIPQKVFIFSGTFRKNLD--PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARS 1367
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1203 ILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALL 1274
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
370-597 |
4.92e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.81 E-value: 4.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLV---ERfydPQSGEVLIDG------ISIKKLR 440
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIaglET---PDSGRIVLNGrdlftnLPPRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 441 ldwirgkIGLVSQEPLLF--MaSIKDNIIYG--KKDATLEEIKRAA----ELANAANFIDKLPNgydtlvgqrgtQLSGG 512
Cdd:COG1118 77 -------VGFVFQHYALFphM-TVAENIAFGlrVRPPSKAEIRARVeellELVQLEGLADRYPS-----------QLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 513 QKQRIAIARAILKDPKILLLDEATSALDV----ESERIVQEALNRmmVERTTLVVAH------RLStvrnvDCITVVRKG 582
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDE--LGGTTVFVTHdqeealELA-----DRVVVMNQG 210
|
250
....*....|....*
gi 1443040382 583 KIVEQGPHDALVKDP 597
Cdd:COG1118 211 RIEQVGTPDEVYDRP 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1049-1269 |
5.68e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 127.48 E-value: 5.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPsrPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLK---VSWLRD 1125
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 QMGLVGQEPVLFND-TIRANITY-----GKHSEVTEEEITAV------AKAANAhefvssLPQgydtvvgekgvQLSGGQ 1193
Cdd:COG2884 80 RIGVVFQDFRLLPDrTVYENVALplrvtGKSRKEIRRRVREVldlvglSDKAKA------LPH-----------ELSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1194 KQRVAIARAILKDPKILLLDEATSALDAE-SERVVqDALDRvmVNR--TTIVVA-HRLSTIKGADM-IAVLKEGKIAEKG 1268
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEE--INRrgTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
.
gi 1443040382 1269 K 1269
Cdd:COG2884 220 A 220
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
45-325 |
6.58e-33 |
|
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: 129.53 E-value: 6.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 45 VLLMVVGTVGALgngisqpLMTVLFGNVINSFGANTSGSVLRsvtKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSARI 124
Cdd:cd18576 2 LILLLLSSAIGL-------VFPLLAGQLIDAALGGGDTASLN---QIALLLLGLFLLQAVFSFFRIYLFARVGERVVADL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 125 RSLYLKAVLRQDITFFDtEMTTGEAVSRMSSDTLLIQGALGekgGKLVELLSS---FIGGFIIAFTRGWLLTLVMLTSLP 201
Cdd:cd18576 72 RKDLYRHLQRLPLSFFH-ERRVGELTSRLSNDVTQIQDTLT---TTLAEFLRQiltLIGGVVLLFFISWKLTLLMLATVP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 202 LIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFGMGSVM 281
Cdd:cd18576 148 VVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFII 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1443040382 282 CVVFGSYGLAFWYGGKLIIEKGYTGGKIMT-ILFAVLTGAS--SLGN 325
Cdd:cd18576 228 FLLFGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAGSigSLAD 274
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
366-584 |
1.60e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 128.31 E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 366 MNGDIELKDVYFRYPARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGisiKKLRLD--W 443
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEEnvW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 444 -IRGKIGLVSQEP--LLFMASIKDNIIYG--KKDATLEEIK----RAAELANAANFIDKLPngydtlvgqrgTQLSGGQK 514
Cdd:PRK13650 78 dIRHKIGMVFQNPdnQFVGATVEDDVAFGleNKGIPHEEMKervnEALELVGMQDFKEREP-----------ARLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 515 QRIAIARAILKDPKILLLDEATSALDVESE----RIVQEAlnRMMVERTTLVVAHRLSTVRNVDCITVVRKGKI 584
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEGRleliKTIKGI--RDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1049-1264 |
2.43e-32 |
|
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: 124.05 E-value: 2.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRdQMG 1128
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLFND-TIRANItygkhsevteeeitavakaanahefvsslpqgydtvvgekgvQLSGGQKQRVAIARAILKDP 1207
Cdd:cd03230 77 YLPEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1208 KILLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTI-KGADMIAVLKEGKI 1264
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAeRLCDRVAILNNGRI 173
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
370-618 |
3.21e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 128.54 E-value: 3.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVY--FRYPARPEQLI--LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISI-------KK 438
Cdd:PRK11308 9 IDLKKHYpvKRGLFKPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpeaQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 439 LRldwiRGKIGLVSQEPllfmasikdniiYG------KKDATLEE-------IKRAAELANAANFIDKlpngydtlVGQR 505
Cdd:PRK11308 89 LL----RQKIQIVFQNP------------YGslnprkKVGQILEEpllintsLSAAERREKALAMMAK--------VGLR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 506 GTQ-------LSGGQKQRIAIARAILKDPKILLLDEATSALDVEserIVQEALNRMM-----VERTTLVVAHRLSTVRNV 573
Cdd:PRK11308 145 PEHydryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVS---VQAQVLNLMMdlqqeLGLSYVFISHDLSVVEHI 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 574 -DCITVVRKGKIVEQGPHDALVKDPDGAYSQLI-----RLQETHRDERHKL 618
Cdd:PRK11308 222 aDEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALlsatpRLNPDDRRERIKL 272
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
370-588 |
6.63e-32 |
|
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: 125.04 E-value: 6.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYParpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIkkLRLDWIRGKIG 449
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLF--MaSIKDNIIYG------KKDATLEEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIAR 521
Cdd:cd03300 76 TVFQNYALFphL-TVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 522 AILKDPKILLLDEATSALDVESERIVQEALNRM--MVERTTLVVAHRLSTVRNV-DCITVVRKGKIVEQG 588
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQEEALTMsDRIAVMNKGKIQQIG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1052-1268 |
8.00e-32 |
|
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: 122.93 E-value: 8.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1052 NNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVG 1131
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1132 QepVLfndtIRANITYGKHSEVTEeeitavakaanahefvsslpqgydtvvgekgvqLSGGQKQRVAIARAILKDPKILL 1211
Cdd:cd03214 80 Q--AL----ELLGLAHLADRPFNE---------------------------------LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1212 LDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLS-TIKGADMIAVLKEGKIAEKG 1268
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1047-1264 |
8.71e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 128.27 E-value: 8.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1047 GSIDFNNVSFKYPsrpDVQIFSDFTLHIPSQKTIALVGESGSGKST---IIALLErfyDPDSGNISLDGVEirslkVSWL 1123
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTllrMIAGLE---DPTSGEILIGGRD-----VTDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1124 ----RDqMGLVGQEPVLF-NDTIRANITYG-KHSEVTEEEITA-VAKAANA---HEFVSSLPQgydtvvgekgvQLSGGQ 1193
Cdd:COG3839 71 ppkdRN-IAMVFQSYALYpHMTVYENIAFPlKLRKVPKAEIDRrVREAAELlglEDLLDRKPK-----------QLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1194 KQRVAIARAILKDPKILLLDEATSALDAESeRV--------VQDALdrvmvNRTTIVVAHRLS---TIkgADMIAVLKEG 1262
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDAKL-RVemraeikrLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDG 210
|
..
gi 1443040382 1263 KI 1264
Cdd:COG3839 211 RI 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1068-1274 |
1.35e-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: 123.99 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1068 SDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSwlRDQMGLVGQEPVLF-NDTIRANIT 1146
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1147 YG-KHSEVTEEEItavakAANAHEFVSSLpqGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESER 1225
Cdd:cd03299 94 YGlKKRKVDKKEI-----ERKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1226 VVQDALDRVM--VNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEALL 1274
Cdd:cd03299 167 KLREELKKIRkeFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
388-597 |
2.14e-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: 123.60 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDwiRGKIGLVSQEPLLF--MaSIKDN 465
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFphM-TVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 466 IIYGKKDATLEEIKRAAELANAANFIdklpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESER 545
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 546 IVQEALNRMMVERTTLV--VAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKDP 597
Cdd:cd03299 167 KLREELKKIRKEFGVTVlhVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
385-597 |
2.27e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 124.09 E-value: 2.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 385 QLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSG-----EVLIDG---ISIKKLRLDWIRGKIGLVSQEPL 456
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTarsLSQQKGLIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 457 LF-MASIKDNIIYG----KKDATLEEIKRAAELANAANFidklpNGYDTLVGQRgtqLSGGQKQRIAIARAILKDPKILL 531
Cdd:PRK11264 96 LFpHRTVLENIIEGpvivKGEPKEEATARARELLAKVGL-----AGKETSYPRR---LSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 532 LDEATSALDVEserIVQEALN--RMMVE--RTTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKDP 597
Cdd:PRK11264 168 FDEPTSALDPE---LVGEVLNtiRQLAQekRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALFADP 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
366-596 |
3.05e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 124.46 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 366 MNGDIELKDVYFRYPARPEQLilDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIR 445
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTKAL--KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 446 GKIGLVSQEP--LLFMASIKDNIIYGKKDATL--EEIKRAAELANAA----NFIDKLPNgydtlvgqrgtQLSGGQKQRI 517
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFGPVNMGLdkDEVERRVEEALKAvrmwDFRDKPPY-----------HLSYGQKKRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 518 AIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVA-HRLSTVRN-VDCITVVRKGKIVEQGPHDALVK 595
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTD 227
|
.
gi 1443040382 596 D 596
Cdd:PRK13647 228 E 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
392-601 |
3.12e-31 |
|
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: 124.29 E-value: 3.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 392 SLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKL---RLDWIRGK-IGLVSQEPLLF-MASIKDNI 466
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkELRELRRKkISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 467 IYG------KKDATLEEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIARAILKDPKILLLDEATSALD 540
Cdd:cd03294 124 AFGlevqgvPRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 541 VESERIVQEALNRM--MVERTTLVVAHRLS-TVRNVDCITVVRKGKIVEQGPHDALVKDPDGAY 601
Cdd:cd03294 193 PLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1049-1264 |
3.70e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 123.24 E-value: 3.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRD--- 1125
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 QMG-------LVGQEPVLFN---------DTIRANItygkhSEVTEEEItavAKAANAHEFVSSLPQGYdtvvgEKGVQL 1189
Cdd:COG3638 81 RIGmifqqfnLVPRLSVLTNvlagrlgrtSTWRSLL-----GLFPPEDR---ERALEALERVGLADKAY-----QRADQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1190 SGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRvmVNR----TTIVVAHRLSTIKG-ADMIAVLKEGKI 1264
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRR--IARedgiTVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1082-1275 |
4.99e-31 |
|
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: 123.52 E-value: 4.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1082 LVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWL----RDQMGLVGQEPVLF-NDTIRANITYGKhsevtee 1156
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLENVAFGL------- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1157 EITAVAKAANAHEFVSSLPQgydtvVGEKGV------QLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDA 1230
Cdd:cd03294 128 EVQGVPRAEREERAAEALEL-----VGLEGWehkypdELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1443040382 1231 LDRV--MVNRTTIVVAHRLS-TIKGADMIAVLKEGKIAEKGKHEALLR 1275
Cdd:cd03294 203 LLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1049-1269 |
7.81e-31 |
|
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: 122.92 E-value: 7.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSW-LRDQM 1127
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1128 GLVGQEPvlfnD------TIRANITYG------KHSEVtEEEITAVAKAANAHEFVSSLPQgydtvvgekgvQLSGGQKQ 1195
Cdd:TIGR04520 80 GMVFQNP----DnqfvgaTVEDDVAFGlenlgvPREEM-RKRVDEALKLVGMEDFRDREPH-----------LLSGGQKQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 1196 RVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVM--VNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGK 1269
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1048-1268 |
1.06e-30 |
|
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: 121.68 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1048 SIDFNNVSFKYPSRPDVQifsDFTLHIPSQKTIALVGESGSGKST---IIALLERfydPDSGNISLDGVEIRSLKVSwlR 1124
Cdd:cd03296 2 SIEVRNVSKRFGDFVALD---DVSLDIPSGELVALLGPSGSGKTTllrLIAGLER---PDSGTILFGGEDATDVPVQ--E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1125 DQMGLVGQEPVLFND-TIRANITYG---KHSEVTEEEITAVAKAANAHEFV--SSLPQGYDTvvgekgvQLSGGQKQRVA 1198
Cdd:cd03296 74 RNVGFVFQHYALFRHmTVFDNVAFGlrvKPRSERPPEAEIRAKVHELLKLVqlDWLADRYPA-------QLSGGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 1199 IARAILKDPKILLLDEATSALDAESERVVQDALDRVM--VNRTTIVVAHRLS-TIKGADMIAVLKEGKIAEKG 1268
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVG 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1049-1264 |
1.14e-30 |
|
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: 120.71 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRpdvQIFSDFTLHIPSQKTIALVGESGSGKSTI---IALLERfydPDSGNISLDGVEI--RSLKVSWL 1123
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTIIIDGLKLtdDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1124 RDQMGLVGQEPVLF-NDTIRANITYG--KHSEVTEEEitAVAKAANAHEFVsslpqGYDTVVGEKGVQLSGGQKQRVAIA 1200
Cdd:cd03262 75 RQKVGMVFQQFNLFpHLTVLENITLApiKVKGMSKAE--AEERALELLEKV-----GLADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1201 RAILKDPKILLLDEATSALDAEserVVQDALDrVMVN-----RTTIVVAHRLSTIKG-ADMIAVLKEGKI 1264
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPE---LVGEVLD-VMKDlaeegMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
370-609 |
1.74e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.97 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLD--WIRGK 447
Cdd:PRK09493 2 IEFKNVSKHFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 448 IGLVSQEPLLF--MASIkDNIIYG--------KKDATleeiKRAAELanaanfIDKLpnGYDTLVGQRGTQLSGGQKQRI 517
Cdd:PRK09493 79 AGMVFQQFYLFphLTAL-ENVMFGplrvrgasKEEAE----KQAREL------LAKV--GLAERAHHYPSELSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 518 AIARAILKDPKILLLDEATSALDVEserIVQEALNRM--MVER--TTLVVAHRLSTVRNVDC-ITVVRKGKIVEQGPHDA 592
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPE---LRHEVLKVMqdLAEEgmTMVIVTHEIGFAEKVASrLIFIDKGRIAEDGDPQV 222
|
250
....*....|....*..
gi 1443040382 593 LVKDPDgaySQliRLQE 609
Cdd:PRK09493 223 LIKNPP---SQ--RLQE 234
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
70-340 |
1.75e-30 |
|
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: 122.42 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 70 GNVINSFGANTSGSvlrSVTKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSARIRSLYLKAVLRQDITFFDTeMTTGEA 149
Cdd:cd18784 20 GQVIDGIVIEKSQD---KFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDT-VKTGDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 150 VSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTRGWLLTLVMLTSLPLIAIASAVSAQALTRVSSKRQTSYSDAG 229
Cdd:cd18784 96 TSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKAN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 230 DTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFGMGSVMCVVFGSYGLAFWYGGKLIIEKGYTGGKI 309
Cdd:cd18784 176 EVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGNL 255
|
250 260 270
....*....|....*....|....*....|.
gi 1443040382 310 MTILFAVLTGASSLGNATPAVAAVVEGQSAA 340
Cdd:cd18784 256 ISFILYQLELGSCLESVGSVYTGLMQAVGAA 286
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
370-593 |
2.00e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 120.63 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQLildglSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDwiRGKIG 449
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF-----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMA-SIKDNIIYG-----KKDAT-LEEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIARA 522
Cdd:COG3840 75 MLFQENNLFPHlTVAQNIGLGlrpglKLTAEqRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 523 ILKDPKILLLDEATSALDveserivqEALNRMMVE----------RTTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHD 591
Cdd:COG3840 144 LVRKRPILLLDEPFSALD--------PALRQEMLDlvdelcrergLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTA 215
|
..
gi 1443040382 592 AL 593
Cdd:COG3840 216 AL 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1048-1292 |
2.49e-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: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1048 SIDFNNVSFKYpSRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGveirslkvswlrdQM 1127
Cdd:TIGR00957 636 SITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SV 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1128 GLVGQEPVLFNDTIRANITYGKhsEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDP 1207
Cdd:TIGR00957 702 AYVPQQAWIQNDSLRENILFGK--ALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1208 KILLLDEATSALDAESERVVQDAL---DRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLRiKDGAYASL 1284
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQ-RDGAFAEF 858
|
....*...
gi 1443040382 1285 VQLRSNSE 1292
Cdd:TIGR00957 859 LRTYAPDE 866
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
371-564 |
2.94e-30 |
|
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: 119.28 E-value: 2.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 371 ELKDVYFRYpaRPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLdwiRGKIGL 450
Cdd:cd03226 1 RIENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER---RKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 451 VSQEP--LLFMASIKDNIIYGKKDAtleeikrAAELANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPK 528
Cdd:cd03226 76 VMQDVdyQLFTDSVREELLLGLKEL-------DAGNEQAETVLKDL--DLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 1443040382 529 ILLLDEATSALDVESERIVQEALNRMMVERTTLVVA 564
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVI 182
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1049-1268 |
3.21e-30 |
|
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: 120.03 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPsrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSwlRDQMG 1128
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLFND-TIRANITYG-KHSEVTEEEITAvaKAANAHEFVSSLPQGYdtvvgEKGVQLSGGQKQRVAIARAILKD 1206
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGlRLKKLPKAEIKE--RVAEALDLVQLEGYAN-----RKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1207 PKILLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLS-TIKGADMIAVLKEGKIAEKG 1268
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIG 213
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
48-316 |
3.92e-30 |
|
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: 121.50 E-value: 3.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 48 MVVGTVGALGNGISQPLMTVLFGNVINSFGANTsgsVLRSVTKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSARIRSL 127
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAG---DLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 128 YLKAVLRQDITFFDtEMTTGEAVSRMSSDTLLIQGALGekgGKLVELLSS---FIGGFIIAFTRGWLLTLVMLTSLPLIA 204
Cdd:cd07346 78 LFRHLQRLSLSFFD-RNRTGDLMSRLTSDVDAVQNLVS---SGLLQLLSDvltLIGALVILFYLNWKLTLVALLLLPLYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 205 IASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFGMGSVMCVV 284
Cdd:cd07346 154 LILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLT 233
|
250 260 270
....*....|....*....|....*....|..
gi 1443040382 285 FGSYGLAFWYGGKLIIEKGYTGGKIMTILFAV 316
Cdd:cd07346 234 ALGTALVLLYGGYLVLQGSLTIGELVAFLAYL 265
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
368-597 |
5.21e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 122.87 E-value: 5.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 368 GDIELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDG-----ISIKKlrld 442
Cdd:COG3839 2 ASLELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvtdLPPKD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 443 wiRGkIGLVSQEPLLF--MaSIKDNIIYG------KKDATLEEIKRAAELANAANFIDKLPngydtlvgqrgTQLSGGQK 514
Cdd:COG3839 75 --RN-IAMVFQSYALYphM-TVYENIAFPlklrkvPKAEIDRRVREAAELLGLEDLLDRKP-----------KQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 515 QRIAIARAILKDPKILLLDEATSALDVES-----ERI--VQEALNrmmveRTTLVVAH------RLStvrnvDCITVVRK 581
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDAKLrvemrAEIkrLHRRLG-----TTTIYVTHdqveamTLA-----DRIAVMND 209
|
250
....*....|....*.
gi 1443040382 582 GKIVEQGPHDALVKDP 597
Cdd:COG3839 210 GRIQQVGTPEELYDRP 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
370-564 |
7.04e-30 |
|
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: 118.28 E-value: 7.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYParPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR---LDWIRG 446
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 KIGLVSQE-PLLFMASIKDN------IIYGKKDATLEEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAI 519
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENvafaleVTGVPPREIRKRVPAALELVGLSHKHRALPA-----------ELSGGEQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1443040382 520 ARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVA 564
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
46-325 |
8.52e-30 |
|
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: 120.67 E-value: 8.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 46 LLMVVGTVGALGNGIsqplmtvlfGNVINS-FGANTSGSVLRSVtkvvLNFIYLGIGTSVASFLQVSCWTMAGERQSARI 124
Cdd:cd18575 5 LLIAAAATLALGQGL---------RLLIDQgFAAGNTALLNRAF----LLLLAVALVLALASALRFYLVSWLGERVVADL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 125 RSLYLKAVLRQDITFFDTEMTtGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTRGWLLTLVMLTSLPLIA 204
Cdd:cd18575 72 RKAVFAHLLRLSPSFFETTRT-GEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 205 IASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFGMGSVMCVV 284
Cdd:cd18575 151 LPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLV 230
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1443040382 285 FGSYGLAFWYGGKLIIEKGYTGGKIMTILFAVLTGASSLGN 325
Cdd:cd18575 231 FGAIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGA 271
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1049-1273 |
9.43e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.04 E-value: 9.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIR--SLKVSWL--- 1123
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRraRRRIGYVpqr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1124 -----------RD--QMGLVGQEPVLfndtiranityGKHSEVTEEEITAVAKAANAHEFVsslpqgyDTVVGEkgvqLS 1190
Cdd:COG1121 84 aevdwdfpitvRDvvLMGRYGRRGLF-----------RRPSRADREAVDEALERVGLEDLA-------DRPIGE----LS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1191 GGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDR-VMVNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKG 1268
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAHGP 221
|
....*
gi 1443040382 1269 KHEAL 1273
Cdd:COG1121 222 PEEVL 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
370-589 |
1.07e-29 |
|
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: 119.03 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSG-EVLIDGISIKKLRLDWIRGKI 448
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 449 GLVS---QEPLLFMASIKDNIIYGK-------KDATLEEIKRAAELANAAnfidklpnGYDTLVGQRGTQLSGGQKQRIA 518
Cdd:COG1119 81 GLVSpalQLRFPRDETVLDVVLSGFfdsiglyREPTDEQRERARELLELL--------GLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 519 IARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER-TTLV-VAHRLSTVrnVDCIT---VVRKGKIVEQGP 589
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVlVTHHVEEI--PPGIThvlLLKDGRVVAAGP 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
375-603 |
1.09e-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: 125.57 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 375 VYFRYPARpEQLILDGLSLQVASGTTMAIVGESGSGKS----TVISLVERFYDPQSGEVLIDGISIKKL---RLDWIRG- 446
Cdd:COG4172 14 VAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLserELRRIRGn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 KIGLVSQEPllfMAS------IKDNII--------YGKKDATleeiKRAAEL------ANAANFIDKLPNgydtlvgqrg 506
Cdd:COG4172 93 RIAMIFQEP---MTSlnplhtIGKQIAevlrlhrgLSGAAAR----ARALELlervgiPDPERRLDAYPH---------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 507 tQLSGGQKQRIAIARAILKDPKILLLDEATSALDVeserIVQ----EALNRMMVERTT--LVVAHRLSTVRNV-DCITVV 579
Cdd:COG4172 156 -QLSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaqilDLLKDLQRELGMalLLITHDLGVVRRFaDRVAVM 230
|
250 260
....*....|....*....|....
gi 1443040382 580 RKGKIVEQGPHDALVKDPDGAYSQ 603
Cdd:COG4172 231 RQGEIVEQGPTAELFAAPQHPYTR 254
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
370-598 |
2.05e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.38 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRY-PARP-EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISI--KKLRLDWIR 445
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 446 GKIGLVSQEP--LLFMASIKDNIIYGKKDATLEE------IKRAAELAnaanfidKLPngYDTLVGQRGTQLSGGQKQRI 517
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEeeienrVKRAMNIV-------GLD--YEDYKDKSPFELSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 518 AIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTV-RNVDCITVVRKGKIVEQGPHDALV 594
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVF 233
|
....
gi 1443040382 595 KDPD 598
Cdd:PRK13637 234 KEVE 237
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1049-1273 |
2.89e-29 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 117.78 E-value: 2.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRD--- 1125
Cdd:TIGR02315 2 LEVENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 QMGLVGQEPVLF-NDTIRANITYGK---HSEV-------TEEEItavAKAANAHEFVSSLPQGYdtvvgEKGVQLSGGQK 1194
Cdd:TIGR02315 80 RIGMIFQHYNLIeRLTVLENVLHGRlgyKPTWrsllgrfSEEDK---ERALSALERVGLADKAY-----QRADQLSGGQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1195 QRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHE 1271
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKyADRIVGLKAGEIVFDGAPS 231
|
..
gi 1443040382 1272 AL 1273
Cdd:TIGR02315 232 EL 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1049-1268 |
3.62e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 120.29 E-value: 3.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYP-SRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIA---LLERfydPDSGNISLDGVEIRSLKVSWL- 1123
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRcinLLER---PTSGRVLVDGQDLTALSEKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1124 --RDQMGLVGQEpvlFN----DTIRANITYG-KHSEVTEEEITA--------VAKAANAHEFVSslpqgydtvvgekgvQ 1188
Cdd:PRK11153 79 kaRRQIGMIFQH---FNllssRTVFDNVALPlELAGTPKAEIKArvtellelVGLSDKADRYPA---------------Q 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1189 LSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRvmVNRT---TIV-VAHRLSTIKG-ADMIAVLKEGK 1263
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKD--INRElglTIVlITHEMDVVKRiCDRVAVIDAGR 218
|
....*
gi 1443040382 1264 IAEKG 1268
Cdd:PRK11153 219 LVEQG 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
370-588 |
5.11e-29 |
|
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: 115.75 E-value: 5.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYParpEQLILDGLSLQVASGTTmAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRlDWIRGKIG 449
Cdd:cd03264 1 LQLENLTKRYG---KKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEP-----------LLFMASIKDnIIYGKKDAtleEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIA 518
Cdd:cd03264 76 YLPQEFgvypnftvrefLDYIAWLKG-IPSKEVKA---RVDEVLELVNLGDRAKKKIG-----------SLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 519 IARAILKDPKILLLDEATSALDVEsERI-VQEALNRMMVERTTLVVAHRLSTVRNV-DCITVVRKGKIVEQG 588
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPE-ERIrFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1049-1258 |
6.09e-29 |
|
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: 115.27 E-value: 6.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKST---IIALLERfydPDSGNISLDGVEIRSLKVSWlRD 1125
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTllrILAGLLP---PSAGEVLWNGEPIRDAREDY-RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 QMGLVGQEPVLFND-TIRANITY---GKHSEVTEEEITAVAKAAN----AHEFVSslpqgydtvvgekgvQLSGGQKQRV 1197
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRFwaaLYGLRADREAIDEALEAVGlaglADLPVR---------------QLSAGQKRRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1198 AIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTIKGADMIAV 1258
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
388-588 |
6.20e-29 |
|
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: 115.86 E-value: 6.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVA---SGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGI----SIKKLRLDWIRGKIGLVSQEPLLF-M 459
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 460 ASIKDNIIYGKKDATLEEIK-RAAELanaanfIDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSA 538
Cdd:cd03297 90 LNVRENLAFGLKRKRNREDRiSVDEL------LDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 539 LDVESERIVQEALNRMMVE--RTTLVVAHRLSTV-RNVDCITVVRKGKIVEQG 588
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1053-1275 |
9.04e-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: 118.23 E-value: 9.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1053 NVSFKYPSRPdVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDP---DSGNISLDGVEIRSLKVSWLRD---- 1125
Cdd:COG0444 8 KVYFPTRRGV-VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 QMGLVGQE------PVLfndTIRANITYG--KHSEVTEEEITAVAKAA-------NAHEFVSSLPQgydtvvgekgvQLS 1190
Cdd:COG0444 87 EIQMIFQDpmtslnPVM---TVGDQIAEPlrIHGGLSKAEARERAIELlervglpDPERRLDRYPH-----------ELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1191 GGQKQRVAIARAILKDPKILLLDEATSALDAeserVVQ----DALDRVMVNR-TTIV-VAHRLSTIKG-ADMIAVLKEGK 1263
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaqilNLLKDLQRELgLAILfITHDLGVVAEiADRVAVMYAGR 228
|
250
....*....|..
gi 1443040382 1264 IAEKGKHEALLR 1275
Cdd:COG0444 229 IVEEGPVEELFE 240
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
370-588 |
9.21e-29 |
|
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: 115.04 E-value: 9.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYParpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDwIRGkIG 449
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRD-IA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLF--MaSIKDNIIYG------KKDATLEEIKRAAELANAANFIDKLPngydtlvgqrgTQLSGGQKQRIAIAR 521
Cdd:cd03301 76 MVFQNYALYphM-TVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 522 AILKDPKILLLDEATSALDVESERIVQEALNRMM--VERTTLVVAHRLSTVRNV-DCITVVRKGKIVEQG 588
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQqrLGTTTIYVTHDQVEAMTMaDRIAVMNDGQIQQIG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
370-578 |
9.38e-29 |
|
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: 114.88 E-value: 9.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRypaRPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWiRGKIG 449
Cdd:COG4133 3 LEAENLSCR---RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMA-SIKDNI-----IYGKkDATLEEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIARAI 523
Cdd:COG4133 79 YLGHADGLKPElTVRENLrfwaaLYGL-RADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 524 LKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVA-HRLSTVRNVDCITV 578
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1049-1269 |
1.44e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 115.90 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRpdvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYD--PD---SGNISLDGVEIRSLKVS-- 1121
Cdd:COG1117 12 IEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIYDPDVDvv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1122 WLRDQMGLVGQEPVLFNDTIRANITYG-----KHSEVTEEEI--TAVAKAAnahefvssLpqgYDTV---VGEKGVQLSG 1191
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgIKSKSELDEIveESLRKAA--------L---WDEVkdrLKKSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1192 GQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAH------RLStikgaDMIAVLKEGKIA 1265
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYLGELV 232
|
....
gi 1443040382 1266 EKGK 1269
Cdd:COG1117 233 EFGP 236
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1048-1269 |
1.83e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 116.69 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1048 SIDFNNVSFKY-PSRP-DVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEI--RSLKVSWL 1123
Cdd:PRK13637 2 SIKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1124 RDQMGLVGQEP--VLFNDTIRANITYG-KHSEVTEEEI-TAVAKAANAhefvSSLPqgYDTVVGEKGVQLSGGQKQRVAI 1199
Cdd:PRK13637 82 RKKVGLVFQYPeyQLFEETIEKDIAFGpINLGLSEEEIeNRVKRAMNI----VGLD--YEDYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 1200 ARAILKDPKILLLDEATSALDAESErvvQDALDRVM-----VNRTTIVVAHRLSTI-KGADMIAVLKEGKIAEKGK 1269
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGR---DEILNKIKelhkeYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
729-1015 |
2.63e-28 |
|
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: 116.12 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 729 DQLRKDSRF-----WALMSVVLGVACLISIPAEYFLFGIAGGKLIQRVRTLSFQRIMHQEVAWFDKpsnsrcatlmyfcy 803
Cdd:cd18557 24 DTIIKGGDLdvlneLALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDK-------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 804 fifYKkiftfkpmlrghlisySGALGTRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVG 883
Cdd:cd18557 90 ---HK----------------TGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 884 AQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLML 963
Cdd:cd18557 151 IASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLI 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 964 YLTYGLCFYVGAKFVSQGKTTFSDVFKVFFALVLAAVGVSQSSALSTNATKA 1015
Cdd:cd18557 231 YLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKA 282
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
370-588 |
3.51e-28 |
|
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: 113.36 E-value: 3.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQLILdglslQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKlrLDWIRGKIG 449
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDL-----TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFM-ASIKDNIIYGKKDA-TLEEIKRAAELANAANFidklpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDP 527
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSPGlKLTAEDRQAIEVALARV------GLAGLEKRLPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 528 KILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRNVDC-ITVVRKGKIVEQG 588
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
396-598 |
4.52e-28 |
|
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: 117.14 E-value: 4.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 396 ASGTTmAIVGESGSGKSTVISLVERFYDPQSGEVLIDGI----SIKKLRLDWIRGKIGLVSQEPLLF-MASIKDNIIYGK 470
Cdd:TIGR02142 22 GQGVT-AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdSRKGIFLPPEKRRIGYVFQEARLFpHLSVRGNLRYGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 471 KDATLEEIKraaelANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEA 550
Cdd:TIGR02142 101 KRARPSERR-----ISFERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 551 LNRMMVERT--TLVVAHRLSTV-RNVDCITVVRKGKIVEQGPHDALVKDPD 598
Cdd:TIGR02142 174 LERLHAEFGipILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
370-588 |
4.70e-28 |
|
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: 113.23 E-value: 4.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRY-PARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDwIRGKI 448
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 449 GLVSQEPLLF-MASIKDNIIYGkkdATLEEIKRAAELANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDP 527
Cdd:cd03266 81 GFVSDSTGLYdRLTARENLEYF---AGLYGLKGDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 528 KILLLDEATSALDVESERIVQEALNRMMVERTTLVVA-HRLSTVRNV-DCITVVRKGKIVEQG 588
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1049-1268 |
4.90e-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: 113.06 E-value: 4.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRpdvQIFSDFTLHIPSqKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSwLRDQMG 1128
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLF-NDTIRANITY-----GKHSEVTEEEITAVAKAANAHEFVSSLPQgydtvvgekgvQLSGGQKQRVAIARA 1202
Cdd:cd03264 76 YLPQEFGVYpNFTVREFLDYiawlkGIPSKEVKARVDEVLELVNLGDRAKKKIG-----------SLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1203 ILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKG 1268
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
370-565 |
4.99e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 113.66 E-value: 4.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIG 449
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMASIKDNII--YGKKDATLEEIKRAAELANAAnfidkLPngyDTLVGQRGTQLSGGQKQRIAIARAILKDP 527
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIfpWQIRNQQPDPAIFLDDLERFA-----LP---DTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1443040382 528 KILLLDEATSALDVESERIVQEALNRMMVERTTLV--VAH 565
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTH 196
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
370-597 |
5.08e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 117.13 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPArpeQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDwiRGKIG 449
Cdd:PRK11432 7 VVLKNITKRFGS---NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLF--MaSIKDNIIYG------KKDATLEEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIAR 521
Cdd:PRK11432 82 MVFQSYALFphM-SLGENVGYGlkmlgvPKEERKQRVKEALELVDLAGFEDRYVD-----------QISGGQQQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 522 AILKDPKILLLDEATSALDVESERIVQEALnRMMVER---TTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKDP 597
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDANLRRSMREKI-RELQQQfniTSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
370-592 |
8.32e-28 |
|
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: 112.91 E-value: 8.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQL-ILDGLSLQVASGTTMAIVGESGSGKSTVISLV---ERfydPQSGEVLIDGISIKKL----RL 441
Cdd:COG4181 9 IELRGLTKTVGTGAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLaglDR---PTSGTVRLAGQDLFALdedaRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 442 DWIRGKIGLVSQ-EPLLFMASIKDNI-----IYGKKDATleeiKRAAELANAANfidklpngydtlVGQRGT----QLSG 511
Cdd:COG4181 86 RLRARHVGFVFQsFQLLPTLTALENVmlpleLAGRRDAR----ARARALLERVG------------LGHRLDhypaQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 512 GQKQRIAIARAILKDPKILLLDEATSALD-VESERIVQ--EALNRmmvER-TTLV-VAHRLSTVRNVDCITVVRKGKIVE 586
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDaATGEQIIDllFELNR---ERgTTLVlVTHDPALAARCDRVLRLRAGRLVE 226
|
....*.
gi 1443040382 587 QGPHDA 592
Cdd:COG4181 227 DTAATA 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1067-1268 |
8.98e-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: 8.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1067 FSDFTLHIP---SQKTIALVGESGSGKSTI---IALLERfydPDSGNISLDGVEI----RSLKVSWLRDQMGLVGQEPVL 1136
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLlrcIAGLEK---PDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1137 F-NDTIRANITYG-KHSEVTEEEITAvakaanaHEFVSSLpqGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDE 1214
Cdd:cd03297 87 FpHLNVRENLAFGlKRKRNREDRISV-------DELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1215 ATSALDAESERVVQDALDRVM--VNRTTIVVAHRLSTI-KGADMIAVLKEGKIAEKG 1268
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKknLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
45-296 |
9.40e-28 |
|
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: 114.45 E-value: 9.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 45 VLLMVVGTVGALgngiSQPLMTvlfGNVINSFGANtsgsvlRSVTKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSARI 124
Cdd:cd18551 5 LLLSLLGTAASL----AQPLLV---KNLIDALSAG------GSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 125 RSLYLKAVLRQDITFFDTEmTTGEAVSRMSSDTLLIQGALGEKggkLVELLSS---FIGGFIIAFTRGWLLTLVMLTSLP 201
Cdd:cd18551 72 RRRLWRRLLRLPVSFFDRR-RSGDLVSRVTNDTTLLRELITSG---LPQLVTGvltVVGAVVLMFLLDWVLTLVTLAVVP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 202 LIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFGMGSVM 281
Cdd:cd18551 148 LAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMG 227
|
250
....*....|....*
gi 1443040382 282 CVVFGSYGLAFWYGG 296
Cdd:cd18551 228 LAVQLALLVVLGVGG 242
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1049-1244 |
9.68e-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: 112.12 E-value: 9.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPsrPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLK---VSWLRD 1125
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 QMGLVGQE-PVLFNDTIRAN------ITYGKHSEVTEEEITAVAKAANAHEfVSSLPQgydtvvgekgvQLSGGQKQRVA 1198
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENvafaleVTGVPPREIRKRVPAALELVGLSHK-HRALPA-----------ELSGGEQQRVA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1443040382 1199 IARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVA 1244
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1042-1276 |
1.10e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.96 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1042 MENVtgsIDFNNVSFKYP--SRPDVQifsDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLK 1119
Cdd:PRK13635 2 KEEI---IRVEHISFRYPdaATYALK---DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1120 VSWLRDQMGLVGQEPvlfnD------TIRANITYG-KHSEVTEEEITAVAKAA----NAHEFVSSLPQgydtvvgekgvQ 1188
Cdd:PRK13635 76 VWDVRRQVGMVFQNP----DnqfvgaTVQDDVAFGlENIGVPREEMVERVDQAlrqvGMEDFLNREPH-----------R 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1189 LSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALdRVMVNRTTIVV---AHRLSTIKGADMIAVLKEGKIA 1265
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETV-RQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEIL 219
|
250
....*....|....*...
gi 1443040382 1266 EKG------KH-EALLRI 1276
Cdd:PRK13635 220 EEGtpeeifKSgHMLQEI 237
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
388-603 |
1.82e-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: 118.63 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKST----VISLVerfydPQSGEVLIDGISI-----KKLRLdwIRGKIGLVSQ----- 453
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLdglsrRALRP--LRRRMQVVFQdpfgs 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 454 ------------EPLLFMAsikdniIYGKKDATLEEIKRA-AELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIA 520
Cdd:COG4172 375 lsprmtvgqiiaEGLRVHG------PGLSAAERRARVAEAlEEVGLDPAARHRYPH-----------EFSGGQRQRIAIA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 521 RAILKDPKILLLDEATSALDVeserIVQ----EALNRMMVER--TTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDAL 593
Cdd:COG4172 438 RALILEPKLLVLDEPTSALDV----SVQaqilDLLRDLQREHglAYLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQV 513
|
250
....*....|
gi 1443040382 594 VKDPDGAYSQ 603
Cdd:COG4172 514 FDAPQHPYTR 523
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
695-996 |
2.02e-27 |
|
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: 113.80 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 695 VLLLGSIAASVHGVILPLY-GIIMPGVLksfyeppdqLRKDSRFWALMSVVLGVACLISIPAEYF---LFGIAGGKLIQR 770
Cdd:cd07346 3 LALLLLLLATALGLALPLLtKLLIDDVI---------PAGDLSLLLWIALLLLLLALLRALLSYLrryLAARLGQRVVFD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 771 VRTLSFQRIMHQEVAWFDKPSnsrcatlmyfcyfifykkiftfkpmlrghlisySGALGTRLSVDALNVRRLVGDNLALI 850
Cdd:cd07346 74 LRRDLFRHLQRLSLSFFDRNR---------------------------------TGDLMSRLTSDVDAVQNLVSSGLLQL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 851 VQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSIRTVASFCSEKRV 930
Cdd:cd07346 121 LSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEERE 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 931 VAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGKTTFSDVFkVFFALV 996
Cdd:cd07346 201 IERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELV-AFLAYL 265
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1042-1264 |
2.19e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 113.29 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1042 MENVtgsIDFNNVSFKYPSRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVS 1121
Cdd:PRK13650 1 MSNI---IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1122 WLRDQMGLVGQEP--VLFNDTIRANITYGKHSE-VTEEEItaVAKAANAHEFVsslpqGYDTVVGEKGVQLSGGQKQRVA 1198
Cdd:PRK13650 78 DIRHKIGMVFQNPdnQFVGATVEDDVAFGLENKgIPHEEM--KERVNEALELV-----GMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1199 IARAILKDPKILLLDEATSALDAESE----RVVQDALDRvmVNRTTIVVAHRLSTIKGADMIAVLKEGKI 1264
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRleliKTIKGIRDD--YQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
697-982 |
2.23e-27 |
|
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: 113.41 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 697 LLGSIAASVHGVILPLY-GIIMPGVLKSfyEPPDQLRKDSRFWALMSVVLGVACLISipaeYFLFGIAGGKLIQRVRTLS 775
Cdd:cd18572 2 FVFLVVAALSELAIPHYtGAVIDAVVAD--GSREAFYRAVLLLLLLSVLSGLFSGLR----GGCFSYAGTRLVRRLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 776 FQRIMHQEVAWFDKPSnsrcatlmyfcyfifykkiftfkpmlrghlisySGALGTRLSVDALNVRRLVGDNLALIVQAVA 855
Cdd:cd18572 76 FRSLLRQDIAFFDATK---------------------------------TGELTSRLTSDCQKVSDPLSTNLNVFLRNLV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 856 TLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSIRTVASFCSEKRVVAIYN 935
Cdd:cd18572 123 QLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYE 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1443040382 936 KKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGK 982
Cdd:cd18572 203 RALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGR 249
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1049-1269 |
2.51e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 113.36 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPdVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGN---ISLDGVEIRSLKVSWLRD 1125
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 QMGLVGQEP--VLFNDTIRANITYG-KHSEVTEEE-ITAVAKAAN---AHEFVSSLPQgydtvvgekgvQLSGGQKQRVA 1198
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGlENRAVPRPEmIKIVRDVLAdvgMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 1199 IARAILKDPKILLLDEATSALDAESERVVQDALDRVMV--NRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGK 1269
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1049-1268 |
3.67e-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: 110.66 E-value: 3.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPdvqifSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSwlRDQMG 1128
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLFND-TIRANITYG-----KHSEVTEEEITAVAKAANAHEFVSSLPQgydtvvgekgvQLSGGQKQRVAIARA 1202
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGlspglKLTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1203 ILKDPKILLLDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRLSTIKG-ADMIAVLKEGKIAEKG 1268
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
370-620 |
4.26e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 112.57 E-value: 4.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRY-PARP-EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISI----KKLRLDW 443
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 444 IRGKIGLVSQ--EPLLFMASIKDNIIYGKKD--ATLEEIKRAA-----ELANAANFIDKLPngydtlvgqrgTQLSGGQK 514
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNfkMNLDEVKNYAhrllmDLGFSRDVMSQSP-----------FQMSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 515 QRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVE--RTTLVVAHRLSTV-RNVDCITVVRKGKIVEQGphd 591
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVaRYADEVIVMKEGSIVSQT--- 228
|
250 260
....*....|....*....|....*....
gi 1443040382 592 alvkDPDGAYSQLIRLQETHRDerhkLPD 620
Cdd:PRK13646 229 ----SPKELFKDKKKLADWHIG----LPE 249
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
48-317 |
4.37e-27 |
|
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: 112.90 E-value: 4.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 48 MVVGTVGALGNGISQPLMTVLFGNVINSFGANTSGSVLRSVTKVVLnFIYLGIGtsVASFLQVSCWTMAGERQSARIRSL 127
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAII-GLFLLRG--LASYLQTYLMAYVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 128 YLKAVLRQDITFFDTEmTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTRGWLLTLVMLTSLPLIAIAS 207
Cdd:cd18552 78 LFDKLLRLPLSFFDRN-SSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 208 AVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEK-------KAIAMYRNFIKKSYKAT------IEegIITG 274
Cdd:cd18552 157 RRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDyeikrfrKANERLRRLSMKIARARalssplME--LLGA 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1443040382 275 FGMGSVMcvvfgsyglafWYGGKLIIEKGYTGGKIMTILFAVL 317
Cdd:cd18552 235 IAIALVL-----------WYGGYQVISGELTPGEFISFITALL 266
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1049-1274 |
4.75e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.95 E-value: 4.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPsrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVS--WLRDQ 1126
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1127 MGLVGQEPVLFND-TIRANITYG----------KHSEVTEEEITAVAKAANAHEFVSslpqgydtvvgekgvQLSGGQKQ 1195
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFGplrvrgaskeEAEKQARELLAKVGLAERAHHYPS---------------ELSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1196 RVAIARAILKDPKILLLDEATSALDAESE----RVVQDALDRVMvnrTTIVVAHRLSTIK--GADMIAVLKeGKIAEKGK 1269
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALDPELRhevlKVMQDLAEEGM---TMVIVTHEIGFAEkvASRLIFIDK-GRIAEDGD 219
|
....*
gi 1443040382 1270 HEALL 1274
Cdd:PRK09493 220 PQVLI 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1051-1265 |
6.31e-27 |
|
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: 109.93 E-value: 6.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1051 FNNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGveirsLKVSWLRDQMGLV 1130
Cdd:cd03235 2 VEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1131 GQE-------PVLFNDTIRANITY--GKHSEVTEEEItavAKAANAHEFVsslpqgydtvvGEKGV------QLSGGQKQ 1195
Cdd:cd03235 74 PQRrsidrdfPISVRDVVLMGLYGhkGLFRRLSKADK---AKVDEALERV-----------GLSELadrqigELSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1196 RVAIARAILKDPKILLLDEATSALDAESERVVQDALDRV-MVNRTTIVVAHRLSTIKG-ADMIAVLKEGKIA 1265
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1042-1269 |
7.97e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.38 E-value: 7.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1042 MENVTGSIDFNNVSFKYPSRPDVQIfSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVS 1121
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1122 WLRDQMGLVGQEP--VLFNDTIRANITYG--KHSEVTEEEITAVAKA---ANAHEFVSSLPQGydtvvgekgvqLSGGQK 1194
Cdd:PRK13648 80 KLRKHIGIVFQNPdnQFVGSIVKYDVAFGleNHAVPYDEMHRRVSEAlkqVDMLERADYEPNA-----------LSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1195 QRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRLSTIKGADMIAVLKEGKIAEKGK 1269
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
366-598 |
9.84e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 111.34 E-value: 9.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 366 MNGDIELKDVYFRYPARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIR 445
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 446 GKIGLVSQEP--LLFMASIKDNIIYGKKDATL---EEIKRAAELANAANFIDklpngydtLVGQRGTQLSGGQKQRIAIA 520
Cdd:PRK13642 81 RKIGMVFQNPdnQFVGATVEDDVAFGMENQGIpreEMIKRVDEALLAVNMLD--------FKTREPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 521 RAILKDPKILLLDEATSALD----VESERIVQEALNRMMVerTTLVVAHRLSTVRNVDCITVVRKGKIV-EQGPHDALVK 595
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIkEAAPSELFAT 230
|
...
gi 1443040382 596 DPD 598
Cdd:PRK13642 231 SED 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1048-1275 |
1.31e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 112.87 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1048 SIDFNNVSfKYPSRpdVQIFSDFTLHIPSQKTIALVGESGSGKST---IIALLERFydpDSGNISLDGVEIRSLKVswlR 1124
Cdd:PRK10851 2 SIEIANIK-KSFGR--TQVLNDISLDIPSGQMVALLGPSGSGKTTllrIIAGLEHQ---TSGHIRFHGTDVSRLHA---R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1125 D-QMGLVGQEPVLFND-TIRANITYG-----KHSEVTEEEITAvaKAANAHEFV--SSLPQGYDTvvgekgvQLSGGQKQ 1195
Cdd:PRK10851 73 DrKVGFVFQHYALFRHmTVFDNIAFGltvlpRRERPNAAAIKA--KVTQLLEMVqlAHLADRYPA-------QLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1196 RVAIARAILKDPKILLLDEATSALDAEservVQDALDRVM------VNRTTIVVAH-RLSTIKGADMIAVLKEGKIAEKG 1268
Cdd:PRK10851 144 RVALARALAVEPQILLLDEPFGALDAQ----VRKELRRWLrqlheeLKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAG 219
|
....*..
gi 1443040382 1269 KHEALLR 1275
Cdd:PRK10851 220 TPDQVWR 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1062-1262 |
1.33e-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: 109.34 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1062 PDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNI----SLDGVEIRSLKVSWLRDQMGLVGQEPVLF 1137
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1138 NDTIRANITYGkhSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATS 1217
Cdd:cd03290 92 NATVEENITFG--SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1443040382 1218 ALDAE-SERVVQDALDRVMVN--RTTIVVAHRLSTIKGADMIAVLKEG 1262
Cdd:cd03290 170 ALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1062-1268 |
1.64e-26 |
|
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: 108.88 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1062 PDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSwLRDqMGLVGQEPVLF-NDT 1140
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRD-IAMVFQNYALYpHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1141 IRANITYG-KHSEVTEEEITA-VAKAANAhefvsslpQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSA 1218
Cdd:cd03301 89 VYDNIAFGlKLRKVPKDEIDErVREVAEL--------LQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 1219 LDAESERVVQDALDRVM--VNRTTIVVAH-RLSTIKGADMIAVLKEGKIAEKG 1268
Cdd:cd03301 161 LDAKLRVQMRAELKRLQqrLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
385-618 |
2.01e-26 |
|
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: 112.50 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 385 QLILDGLSLQVA-----SGTTmAIVGESGSGKSTVISLV---ERfydPQSGEVLIDGisikKLRLD-----WI---RGKI 448
Cdd:COG4148 8 RLRRGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAIaglER---PDSGRIRLGG----EVLQDsargiFLpphRRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 449 GLVSQEPLLF--MaSIKDNIIYGkkdatleeIKRAAELANAANF---IDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAI 523
Cdd:COG4148 80 GYVFQEARLFphL-SVRGNLLYG--------RKRAPRAERRISFdevVELL--GIGHLLDRRPATLSGGERQRVAIGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 524 LKDPKILLLDEATSALDVES--------ERIVQEAlnRMMVerttLVVAH------RLStvrnvDCITVVRKGKIVEQGP 589
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLARkaeilpylERLRDEL--DIPI----LYVSHsldevaRLA-----DHVVLLEQGRVVASGP 217
|
250 260 270
....*....|....*....|....*....|....*..
gi 1443040382 590 HDALVKDPD--------GAYSqLIRLQETHRDERHKL 618
Cdd:COG4148 218 LAEVLSRPDllplaggeEAGS-VLEATVAAHDPDYGL 253
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
370-585 |
2.59e-26 |
|
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: 106.36 E-value: 2.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPArpeQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKL-RLDWIRGKI 448
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 449 GLVSQepllfmasikdniiygkkdatleeikraaelanaanfidklpngydtlvgqrgtqLSGGQKQRIAIARAILKDPK 528
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 529 ILLLDEATSALDVESERIVQEALNRMMVE-RTTLVVAHRLSTVRNV-DCITVVRKGKIV 585
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
370-594 |
2.90e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 108.95 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDG--------ISIKKLRL 441
Cdd:COG4161 3 IQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 442 dwIRGKIGLVSQE----PLLfmaSIKDNII--------YGKKDAtleeIKRAAELANA---ANFIDKLPNgydtlvgqrg 506
Cdd:COG4161 80 --LRQKVGMVFQQynlwPHL---TVMENLIeapckvlgLSKEQA----REKAMKLLARlrlTDKADRFPL---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 507 tQLSGGQKQRIAIARAILKDPKILLLDEATSALDVE-SERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITV-VRKGKI 584
Cdd:COG4161 141 -HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVyMEKGRI 219
|
250
....*....|
gi 1443040382 585 VEQGPHDALV 594
Cdd:COG4161 220 IEQGDASHFT 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
370-607 |
3.12e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 114.35 E-value: 3.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGisiKKLRLDWIR---- 445
Cdd:COG1129 5 LEMRGISKSFGGVK---ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSPRdaqa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 446 -GkIGLVSQEPLLF--MaSIKDNIIYGKKDATLEEIKRAAELANAANFIDKL-----PngyDTLVGQrgtqLSGGQKQRI 517
Cdd:COG1129 79 aG-IAIIHQELNLVpnL-SVAENIFLGREPRRGGLIDWRAMRRRARELLARLgldidP---DTPVGD----LSVAQQQLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 518 AIARAILKDPKILLLDEATSALDvESERivqEALNRMMVE-----RTTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHD 591
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLT-EREV---ERLFRIIRRlkaqgVAIIYISHRLDEVFEIaDRVTVLRDGRLVGTGPVA 225
|
250
....*....|....*.
gi 1443040382 592 ALVKDpdgaysQLIRL 607
Cdd:COG1129 226 ELTED------ELVRL 235
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
387-597 |
5.31e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 108.46 E-value: 5.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 387 ILDGLSLQVASGTTMAIVGESGSGKSTVIS----LVERFYDPQ-SGEVLIDGISIKKLRLDWIRGKIGLVSQEP-LLFMA 460
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEARvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 461 SIKDNIIYG-------KKDATLEEikRAAELANAANFIDKLPNGYDTLVGQrgtqLSGGQKQRIAIARAILKDPKILLLD 533
Cdd:PRK14247 98 SIFENVALGlklnrlvKSKKELQE--RVRWALEKAQLWDEVKDRLDAPAGK----LSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 534 EATSALDVESERIVQEALNRMMVERTTLVVAH-RLSTVRNVDCITVVRKGKIVEQGPHDALVKDP 597
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1042-1275 |
6.47e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.67 E-value: 6.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1042 MENVtgsIDFNNVSFKYPSrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVS 1121
Cdd:PRK13647 1 MDNI---IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1122 WLRDQMGLVGQEP--VLFNDTIRANITYG------KHSEVtEEEITAVAKAANAHEFVSSLPQgydtvvgekgvQLSGGQ 1193
Cdd:PRK13647 76 WVRSKVGLVFQDPddQVFSSTVWDDVAFGpvnmglDKDEV-ERRVEEALKAVRMWDFRDKPPY-----------HLSYGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1194 KQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLS-TIKGADMIAVLKEGKIAEKGKHE 1271
Cdd:PRK13647 144 KKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKS 223
|
....
gi 1443040382 1272 ALLR 1275
Cdd:PRK13647 224 LLTD 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
387-596 |
1.03e-25 |
|
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: 106.75 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 387 ILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWI-RGKIGLVSQEPLLF--MaSIK 463
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaRAGIGYVPEGRRIFpeL-TVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 464 DNIIYG-------KKDATLEEIkraaelanaanfIDKLPNGYDTLvGQRGTQLSGGQKQRIAIARAILKDPKILLLDEAT 536
Cdd:cd03224 94 ENLLLGayarrraKRKARLERV------------YELFPRLKERR-KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 537 SALdveSERIVQE---ALNRMMVERTT-LVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKD 596
Cdd:cd03224 161 EGL---APKIVEEifeAIRELRDEGVTiLLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLAD 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
363-591 |
1.11e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.91 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 363 LEDMNGDIELKDVYFRYPArPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLD 442
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 443 WIRGKIGLVSQEPL-LFMASI-KDNIIYGKK------DATLEEIKRAAELANAANFIDKLPNGydtlvgqrgtqLSGGQK 514
Cdd:PRK13648 80 KLRKHIGIVFQNPDnQFVGSIvKYDVAFGLEnhavpyDEMHRRVSEALKQVDMLERADYEPNA-----------LSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 515 QRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRNVDCITVVRKGKIVEQG-PHD 591
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGtPTE 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
370-589 |
1.18e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.42 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDwiRGKIG 449
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLF--MaSIKDNIIYG---KKDATlEEIKR----AAELANAANFIDKLPngydtlvgqrgTQLSGGQKQRIAIA 520
Cdd:PRK09452 90 TVFQSYALFphM-TVFENVAFGlrmQKTPA-AEITPrvmeALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 521 RAILKDPKILLLDEATSALDVESERIVQEALNRMmvERT---TLV-VAH------RLStvrnvDCITVVRKGKIVEQGP 589
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNELKAL--QRKlgiTFVfVTHdqeealTMS-----DRIVVMRDGRIEQDGT 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
370-597 |
1.20e-25 |
|
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: 107.04 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEqliLDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDG--ISIKKLRldwiRGK 447
Cdd:cd03296 3 IEVRNVSKRFGDFVA---LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedATDVPVQ----ERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 448 IGLVSQEPLLF--MaSIKDNIIYGKKdatleeIKRAAELANAANFIDKLPN-----GYDTLVGQRGTQLSGGQKQRIAIA 520
Cdd:cd03296 76 VGFVFQHYALFrhM-TVFDNVAFGLR------VKPRSERPPEAEIRAKVHEllklvQLDWLADRYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 521 RAILKDPKILLLDEATSALDV----ESERIVQEALNRMMVerTTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVK 595
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHV--TTVFVTHDQEEALEVaDRVVVMNKGRIEQVGTPDEVYD 226
|
..
gi 1443040382 596 DP 597
Cdd:cd03296 227 HP 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
369-603 |
1.37e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 112.88 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 369 DIELKDVYFRYpARPEQLILDGLSLQVASGTTMAIVGESGSGKS-TVISLVERFYDPQ----SGEVLIDGISIKKL---R 440
Cdd:PRK15134 7 AIENLSVAFRQ-QQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHAseqT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 441 LDWIRG-KIGLVSQEPllfMASIK--DNI---IYG--------KKDATLEEIKRAAE---LANAANFIDKLPNgydtlvg 503
Cdd:PRK15134 86 LRGVRGnKIAMIFQEP---MVSLNplHTLekqLYEvlslhrgmRREAARGEILNCLDrvgIRQAAKRLTDYPH------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 504 qrgtQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESE-------RIVQEALNRMMverttLVVAHRLSTVRNV-DC 575
Cdd:PRK15134 156 ----QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQaqilqllRELQQELNMGL-----LFITHNLSIVRKLaDR 226
|
250 260
....*....|....*....|....*...
gi 1443040382 576 ITVVRKGKIVEQGPHDALVKDPDGAYSQ 603
Cdd:PRK15134 227 VAVMQNGRCVEQNRAATLFSAPTHPYTQ 254
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1048-1275 |
1.93e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 107.94 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1048 SIDFNNVSFKY-PSRP-DVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEI----RSLKVS 1121
Cdd:PRK13646 2 TIRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1122 WLRDQMGLVGQ--EPVLFNDTIRANITYG-KHSEVTEEEITAvakaaNAHEFVSSLpqGYDTVVGEKG-VQLSGGQKQRV 1197
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGpKNFKMNLDEVKN-----YAHRLLMDL--GFSRDVMSQSpFQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1198 AIARAILKDPKILLLDEATSALDAESERVVQDALDRVMV--NRTTIVVAHRLSTI-KGADMIAVLKEGKIAEKGKHEALL 1274
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELF 234
|
.
gi 1443040382 1275 R 1275
Cdd:PRK13646 235 K 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
370-596 |
2.01e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 107.04 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPArpeQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQsGEVLIDG--------ISIKKLRL 441
Cdd:PRK14258 8 IKVNNLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnqnIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 442 DWIRGKIGLVSQEPLLFMASIKDNIIYGKK----------DATLEEIKRAAELAnaanfiDKLPNGydtlVGQRGTQLSG 511
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrpkleiDDIVESALKDADLW------DEIKHK----IHKSALDLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 512 GQKQRIAIARAILKDPKILLLDEATSALD----VESERIVQEAlnRMMVERTTLVVAHRLSTVRNVDCITVV------RK 581
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSL--RLRSELTMVIVSHNLHQVSRLSDFTAFfkgnenRI 231
|
250 260
....*....|....*....|...
gi 1443040382 582 GKIVEQG--------PHDALVKD 596
Cdd:PRK14258 232 GQLVEFGltkkifnsPHDSRTRE 254
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1063-1268 |
3.05e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 109.27 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1063 DVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRslKVSWLRDQMGLVGQEPVLF-NDTI 1141
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVNTVFQSYALFpHMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1142 RANITYG-KHSEVTEEEITAVAKAANA----HEFVSSLPQgydtvvgekgvQLSGGQKQRVAIARAILKDPKILLLDEAT 1216
Cdd:PRK09452 104 FENVAFGlRMQKTPAAEITPRVMEALRmvqlEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1217 SALDAESERVVQDALDRVM--VNRTTIVVAH-RLSTIKGADMIAVLKEGKIAEKG 1268
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQrkLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1042-1262 |
3.88e-25 |
|
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: 113.85 E-value: 3.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1042 MENVTGSID------F-----NNVSFKYPSRPDVQIFSDFTLHI-PSQKTI----------ALVGESGSGKSTIIALLER 1099
Cdd:TIGR01271 395 MVNVTASWDegigelFekikqNNKARKQPNGDDGLFFSNFSLYVtPVLKNIsfklekgqllAVAGSTGSGKSSLLMMIMG 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1100 FYDPDSGNISLDGVEIRSLKVSWLrdqmglvgqepvlFNDTIRANITYGKHSEvtEEEITAVAKAANAHEFVSSLPQGYD 1179
Cdd:TIGR01271 475 ELEPSEGKIKHSGRISFSPQTSWI-------------MPGTIKDNIIFGLSYD--EYRYTSVIKACQLEEDIALFPEKDK 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1180 TVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESER-VVQDALDRVMVNRTTIVVAHRLSTIKGADMIAV 1258
Cdd:TIGR01271 540 TVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILL 619
|
....
gi 1443040382 1259 LKEG 1262
Cdd:TIGR01271 620 LHEG 623
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
388-598 |
4.43e-25 |
|
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: 105.21 E-value: 4.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWI-RGKIGLVSQEPLLFMA-SIKDN 465
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 466 II----YGKKDATL---------EEIKRAAELANAANFIDKLpngyDTLVGqrgtQLSGGQKQRIAIARAILKDPKILLL 532
Cdd:cd03219 96 VMvaaqARTGSGLLlararreerEARERAEELLERVGLADLA----DRPAG----ELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 533 DEATSAL-DVESERIVQ--EALNRMmvERTTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKDPD 598
Cdd:cd03219 168 DEPAAGLnPEETEELAEliRELRER--GITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1071-1273 |
5.00e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 107.51 E-value: 5.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1071 TLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVS---WLRDQMGLVGQEP---------VlfN 1138
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRelrPLRRRMQMVFQDPyaslnprmtV--G 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1139 DTIRANITYgkHSEVTEEEITAVAKAA-------------NAHEFvsslpqgydtvvgekgvqlSGGQKQRVAIARAILK 1205
Cdd:COG4608 116 DIIAEPLRI--HGLASKAERRERVAELlelvglrpehadrYPHEF-------------------SGGQRQRIGIARALAL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1206 DPKILLLDEATSALD----AEserVV------QDALdrvmvNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEAL 1273
Cdd:COG4608 175 NPKLIVCDEPVSALDvsiqAQ---VLnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1039-1262 |
5.25e-25 |
|
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: 106.48 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1039 GAIMENVTGSID-----------FNNVSFKYPSRPDVQIFSDFTLHI-PSQKTI----------ALVGESGSGKSTIIAL 1096
Cdd:cd03291 3 GVIMENVTAFWDegfgellekakQENNDRKHSSDDNNLFFSNLCLVGaPVLKNInlkiekgemlAITGSTGSGKTSLLML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1097 LERFYDPDSGNISLDGVEIRSLKVSWLrdqmglvgqepvlFNDTIRANITYGKHSEvtEEEITAVAKAANAHEFVSSLPQ 1176
Cdd:cd03291 83 ILGELEPSEGKIKHSGRISFSSQFSWI-------------MPGTIKENIIFGVSYD--EYRYKSVVKACQLEEDITKFPE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1177 GYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESER-VVQDALDRVMVNRTTIVVAHRLSTIKGADM 1255
Cdd:cd03291 148 KDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADK 227
|
....*..
gi 1443040382 1256 IAVLKEG 1262
Cdd:cd03291 228 ILILHEG 234
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
367-566 |
6.09e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 111.05 E-value: 6.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 367 NGDIELKDVYFRYPArpEQLILDGLSLQVASGTTMAIVGESGSGKSTVIslveRfydpqsgevLIDGISikklrlDWIRG 446
Cdd:COG4178 360 DGALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSGSGKSTLL----R---------AIAGLW------PYGSG 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 KIGLVSQEPLLFMA--------SIKDNIIY--GKKDATLEEIKRAAELANAANFIDKLpngyDTlVGQRGTQLSGGQKQR 516
Cdd:COG4178 419 RIARPAGARVLFLPqrpylplgTLREALLYpaTAEAFSDAELREALEAVGLGHLAERL----DE-EADWDQVLSLGEQQR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1443040382 517 IAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHR 566
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
367-609 |
6.97e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 105.44 E-value: 6.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 367 NGDIELKDVYFRYParpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR------ 440
Cdd:PRK10619 3 ENKLNVIDLHKRYG---EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRdkdgql 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 441 -------LDWIRGKIGLVSQE-PLLFMASIKDNIIygKKDATLEEIKRAAELANAANFIDKLpnGYDTLV-GQRGTQLSG 511
Cdd:PRK10619 80 kvadknqLRLLRTRLTMVFQHfNLWSHMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKV--GIDERAqGKYPVHLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 512 GQKQRIAIARAILKDPKILLLDEATSALDVEserIVQEALnRMMVE-----RTTLVVAHRLSTVRNVDC-ITVVRKGKIV 585
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVL-RIMQQlaeegKTMVVVTHEMGFARHVSShVIFLHQGKIE 231
|
250 260
....*....|....*....|....
gi 1443040382 586 EQGPHDALVKDPDGAysqliRLQE 609
Cdd:PRK10619 232 EEGAPEQLFGNPQSP-----RLQQ 250
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
370-588 |
7.22e-25 |
|
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: 104.12 E-value: 7.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPaRPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDwIRGKIG 449
Cdd:cd03263 1 LQIRNLTKTYK-KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA-ARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQ-----------EPLLFMASIKdniiyGKKDAtlEEIKRAAELANAANFIDKLpngyDTLVGQrgtqLSGGQKQRIA 518
Cdd:cd03263 79 YCPQfdalfdeltvrEHLRFYARLK-----GLPKS--EIKEEVELLLRVLGLTDKA----NKRART----LSGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 519 IARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNV-DCITVVRKGKIVEQG 588
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALcDRIAIMSDGKLRCIG 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
370-592 |
7.32e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 104.71 E-value: 7.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPArpEQLILDgLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDG--------ISIKKLRL 441
Cdd:PRK11124 3 IQLNGINCFYGA--HQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 442 dwIRGKIGLVSQE----PLLfmaSIKDNII--------YGKKDAtleeIKRAAELANA---ANFIDKLPngydtlvgqrg 506
Cdd:PRK11124 80 --LRRNVGMVFQQynlwPHL---TVQQNLIeapcrvlgLSKDQA----LARAEKLLERlrlKPYADRFP----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 507 TQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESE----RIVQEaLNRMMVerTTLVVAHRLSTVRNVDCITV-VRK 581
Cdd:PRK11124 140 LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITaqivSIIRE-LAETGI--TQVIVTHEVEVARKTASRVVyMEN 216
|
250
....*....|.
gi 1443040382 582 GKIVEQGPHDA 592
Cdd:PRK11124 217 GHIVEQGDASC 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1070-1274 |
7.48e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 104.66 E-value: 7.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1070 FTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSwlRDQMGLVGQEPVLFND-TIRANITYG 1148
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1149 KH-----SEVTEEEITAVAKAANAHEFVSSLPQgydtvvgekgvQLSGGQKQRVAIARAILKDPKILLLDEATSALDAES 1223
Cdd:PRK10771 96 LNpglklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1224 ERVVQDALDRVMVNR--TTIVVAHRLSTikgADMIA----VLKEGKIAEKGKHEALL 1274
Cdd:PRK10771 165 RQEMLTLVSQVCQERqlTLLMVSHSLED---AARIAprslVVADGRIAWDGPTDELL 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
370-540 |
7.50e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 105.33 E-value: 7.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPA-RPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDwiRGki 448
Cdd:COG4525 4 LTVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--RG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 449 gLVSQ-EPLLFMASIKDNIIYGKKdatLEEIKRAAELANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDP 527
Cdd:COG4525 80 -VVFQkDALLPWLNVLDNVAFGLR---LRGVPKAERRARAEELLALV--GLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170
....*....|...
gi 1443040382 528 KILLLDEATSALD 540
Cdd:COG4525 154 RFLLMDEPFGALD 166
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1069-1283 |
7.71e-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: 7.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1069 DFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRS----LKVSWLRDQMGLVGQEPVLFND-TIRA 1143
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1144 NITYG------KHSEVTEEEITAVAkaanahefvsslpqGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATS 1217
Cdd:TIGR02142 95 NLRYGmkrarpSERRISFERVIELL--------------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1218 ALDAESERVVQDALDRVM--VNRTTIVVAHRLSTI-KGADMIAVLKEGKIAEKGKHEALLRIKDGAYAS 1283
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHaeFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1048-1273 |
8.70e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 104.71 E-value: 8.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1048 SIDFNNVSFKYPSrpdVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVE------IRSLKVS 1121
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1122 WLRDQMGLVGQE----PVLfndTIRANITYG--KHSEVTEEEitAVAKAA------NAHEFVSSLPQgydtvvgekgvQL 1189
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLIEApcKVLGLSKEQ--AREKAMkllarlRLTDKADRFPL-----------HL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1190 SGGQKQRVAIARAILKDPKILLLDEATSALDAE-SERVVQDALDRVMVNRTTIVVAHRLSTI-KGADMIAVLKEGKIAEK 1267
Cdd:COG4161 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVYMEKGRIIEQ 222
|
....*.
gi 1443040382 1268 GKHEAL 1273
Cdd:COG4161 223 GDASHF 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1067-1275 |
9.79e-25 |
|
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: 107.49 E-value: 9.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1067 FSDFTL----HIPSQKTIALVGESGSGKSTI---IALLERfydPDSGNISLDG-VEIRSLKVSWL---RDQMGLVGQEPV 1135
Cdd:COG4148 11 RGGFTLdvdfTLPGRGVTALFGPSGSGKTTLlraIAGLER---PDSGRIRLGGeVLQDSARGIFLpphRRRIGYVFQEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1136 LFND-TIRANITYGkhsevteeeITAVAKAANAHEFvsslpqgyDTVVGEKGV---------QLSGGQKQRVAIARAILK 1205
Cdd:COG4148 88 LFPHlSVRGNLLYG---------RKRAPRAERRISF--------DEVVELLGIghlldrrpaTLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1206 DPKILLLDEATSALDAES--------ERvVQDALDrvmvnrTTIV-VAH------RLstikgADMIAVLKEGKIAEKGKH 1270
Cdd:COG4148 151 SPRLLLMDEPLAALDLARkaeilpylER-LRDELD------IPILyVSHsldevaRL-----ADHVVLLEQGRVVASGPL 218
|
....*
gi 1443040382 1271 EALLR 1275
Cdd:COG4148 219 AEVLS 223
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
370-589 |
1.58e-24 |
|
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: 104.50 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYP------ARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR--- 440
Cdd:TIGR02769 3 LEVRDVTHTYRtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 441 LDWIRGKIGLVSQE-PLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLpnGYDTLVGQR-GTQLSGGQKQRIA 518
Cdd:TIGR02769 83 RRAFRRDVQLVFQDsPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMV--GLRSEDADKlPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 519 IARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTT--LVVAHRLSTVRNV-DCITVVRKGKIVEQGP 589
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFcQRVAVMDKGQIVEECD 234
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
371-598 |
1.89e-24 |
|
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: 103.52 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 371 ELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWI--RGkI 448
Cdd:COG0410 5 EVENLHAGYGGIH---VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarLG-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 449 GLVSQEPLLFMA-SIKDNII---YGKKD-----ATLEEI----KRAAELANaanfidklpngydtlvgQRGTQLSGGQKQ 515
Cdd:COG0410 81 GYVPEGRRIFPSlTVEENLLlgaYARRDraevrADLERVyelfPRLKERRR-----------------QRAGTLSGGEQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 516 RIAIARAILKDPKILLLDEATSALdveSERIVQE------ALNRM-----MVE---RTTLVVAHRlstvrnvdcITVVRK 581
Cdd:COG0410 144 MLAIGRALMSRPKLLLLDEPSLGL---APLIVEEifeiirRLNREgvtilLVEqnaRFALEIADR---------AYVLER 211
|
250
....*....|....*..
gi 1443040382 582 GKIVEQGPHDALVKDPD 598
Cdd:COG0410 212 GRIVLEGTAAELLADPE 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
370-585 |
2.39e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.58 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPArpeqLI-LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGisiKKLRL----DWI 444
Cdd:COG3845 6 LELRGITKRFGG----VVaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIrsprDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 445 RGKIGLVSQEPLLFMA-SIKDNIIYGKKDATL------EEIKRAAELANAANF-IDklPngyDTLVGQrgtqLSGGQKQR 516
Cdd:COG3845 79 ALGIGMVHQHFMLVPNlTVAENIVLGLEPTKGgrldrkAARARIRELSERYGLdVD--P---DAKVED----LSVGEQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 517 IAIARAILKDPKILLLDEATSAL-DVESERiVQEALNRMMVERTTLV-VAHRLSTVRNV-DCITVVRKGKIV 585
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLtPQEADE-LFEILRRLAAEGKSIIfITHKLREVMAIaDRVTVLRRGKVV 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
388-567 |
2.67e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 103.70 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYD--PQ---SGEVLIDGISIKKLRLDW--IRGKIGLVSQEPLLFMA 460
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 461 SIKDNIIYGKK----------DATLEEIKRAAELANAANfiDKLpngYDTLVGqrgtqLSGGQKQRIAIARAILKDPKIL 530
Cdd:PRK14239 101 SIYENVVYGLRlkgikdkqvlDEAVEKSLKGASIWDEVK--DRL---HDSALG-----LSGGQQQRVCIARVLATSPKII 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1443040382 531 LLDEATSALDVESERIVQEALNRMMVERTTLVVAHRL 567
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
381-540 |
2.77e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.17 E-value: 2.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 381 ARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQ---SGEVLIDGISIKKL----RldwirgKIGLVSQ 453
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALpaeqR------RIGILFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 454 EPLLF--MaSIKDNIIYG-----KKDATLEEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIARAILKD 526
Cdd:COG4136 84 DDLLFphL-SVGENLAFAlpptiGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAE 151
|
170
....*....|....
gi 1443040382 527 PKILLLDEATSALD 540
Cdd:COG4136 152 PRALLLDEPFSKLD 165
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
49-340 |
3.17e-24 |
|
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: 104.55 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 49 VVGTVGALGNGISQPLMTVLFGNVINSFGANTSGSVLRSVTKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSARIRSLY 128
Cdd:cd18574 2 VLSALAAALVNIQIPLLLGDLVNVISRSLKETNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 129 LKAVLRQDITFFDTEMtTGEAVSRMSSDtllIQgalgekggklvELLSSF--------------IGGFIIAFTRGWLLTL 194
Cdd:cd18574 82 FSSLLRQDIAFFDTHR-TGELVNRLTAD---VQ-----------EFKSSFkqcvsqglrsvtqtVGCVVSLYLISPKLTL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 195 VMLTSLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEegiiTG 274
Cdd:cd18574 147 LLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEK----LG 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 275 FGMG--------SVMCVVFGSYglafWYGGKLIIEKGYTGGKIMTILFAVLTGASSLGNATPAVAAVVEGQSAA 340
Cdd:cd18574 223 LGIGifqglsnlALNGIVLGVL----YYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAG 292
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1036-1262 |
3.92e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.74 E-value: 3.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1036 SDEGAIMENVTGSIDFNNVSFKypsRPDVQ-IFSDFTLHIPSQKTIALVGESGSGKSTI---IALLERFYdpdSGNISL- 1110
Cdd:COG4178 350 EAASRIETSEDGALALEDLTLR---TPDGRpLLEDLSLSLKPGERLLITGPSGSGKSTLlraIAGLWPYG---SGRIARp 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1111 DGveirslkvswlrDQMGLVGQEPVLFNDTIRANITY-GKHSEVTEEEITAVAKAANAHEFVSSLPQGYDTvvgekGVQL 1189
Cdd:COG4178 424 AG------------ARVLFLPQRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAERLDEEADW-----DQVL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 1190 SGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEG 1262
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
367-588 |
4.44e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 103.73 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 367 NGDIELKDVYFRYPARPEQlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGE---VLIDGISIKKLRLDW 443
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 444 IRGKIGLVSQEP--LLFMASIKDNIIYG------KKDATLEEIKRAAELANAANFIDKLPngydtlvgqrgTQLSGGQKQ 515
Cdd:PRK13640 82 IREKVGIVFQNPdnQFVGATVGDDVAFGlenravPRPEMIKIVRDVLADVGMLDYIDSEP-----------ANLSGGQKQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 516 RIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRNVDCITVVRKGKIVEQG 588
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
695-1003 |
4.46e-24 |
|
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: 104.13 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 695 VLLLGSIAASVhgvILP-LYGIIMPGVLKSFYEPPDQLRKDSRFWALMSVVLGVACLISIpAEYFLFGIAGGKLIQRVRT 773
Cdd:cd18573 3 ALLLVSSAVTM---SVPfAIGKLIDVASKESGDIEIFGLSLKTFALALLGVFVVGAAANF-GRVYLLRIAGERIVARLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 774 LSFQRIMHQEVAWFDKpsnsrcatlmyfcyfifykkiftfkpmlrghliSYSGALGTRLSVDALNVRRLVGDNLALIVQA 853
Cdd:cd18573 79 RLFKSILRQDAAFFDK---------------------------------NKTGELVSRLSSDTSVVGKSLTQNLSDGLRS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 854 VATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSIRTVASFCSEKRVVAI 933
Cdd:cd18573 126 LVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVER 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 934 YNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGKTTFSDVFKvfFALVLAAVGVS 1003
Cdd:cd18573 206 YAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTS--FLMYAVYVGSS 273
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
381-589 |
4.47e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 103.23 E-value: 4.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 381 ARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKL-RLDW--IRGKIGLVSQ---- 453
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnRAQRkaFRRDIQMVFQdsis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 454 -------------EPLLFMASIKDniiyGKKDATLEEIKRAAELAnaANFIDKLPngydtlvgqrgTQLSGGQKQRIAIA 520
Cdd:PRK10419 101 avnprktvreiirEPLRHLLSLDK----AERLARASEMLRAVDLD--DSVLDKRP-----------PQLSGGQLQRVCLA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 521 RAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTT--LVVAHRLSTVRNVdC--ITVVRKGKIVEQGP 589
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERF-CqrVMVMDNGQIVETQP 235
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1048-1273 |
5.59e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 110.21 E-value: 5.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1048 SIDFNNVSFKYPSRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTII-ALLERFYDPDSGNISLDGVEIRSLKVSWLrdq 1126
Cdd:PLN03130 614 AISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIsAMLGELPPRSDASVVIRGTVAYVPQVSWI--- 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1127 mglvgqepvlFNDTIRANITYGKHSEVTEEEiTAVAKAANAHEfVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKD 1206
Cdd:PLN03130 691 ----------FNATVRDNILFGSPFDPERYE-RAIDVTALQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1207 PKILLLDEATSALDAESERVVQDA-LDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEAL 1273
Cdd:PLN03130 759 SDVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
370-588 |
6.14e-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: 101.20 E-value: 6.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYParpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKklrlDWIRGKIG 449
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFM-ASIKDNIIYGkkdATLEEIKRAAELANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPK 528
Cdd:cd03269 74 YLPEERGLYPkMKVIDQLVYL---AQLKGLKKEEARRRIDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 529 ILLLDEATSALDVESERIVQEALNRMMVERTTLV-VAHRLSTVRNV-DCITVVRKGKIVEQG 588
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVIlSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1048-1269 |
6.16e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.29 E-value: 6.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1048 SIDFNNVSFKYPSRPDVQ--IFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLK----VS 1121
Cdd:PRK13649 2 GINLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1122 WLRDQMGLVGQ--EPVLFNDTIRANITYGKHS-EVTEEEITAVAKAANAHEFVSslpqgyDTVVGEKGVQLSGGQKQRVA 1198
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfGVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 1199 IARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIV-VAHRLSTIKG-ADMIAVLKEGKIAEKGK 1269
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
368-605 |
7.63e-24 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 109.48 E-value: 7.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 368 GDIELKDVYFRY-PARPeqLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRG 446
Cdd:PTZ00243 1307 GSLVFEGVQMRYrEGLP--LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 KIGLVSQEPLLFMASIKDNIiygkkD----ATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARA 522
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNV-----DpfleASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARA 1459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 523 ILK-DPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKDPDGAY 601
Cdd:PTZ00243 1460 LLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
....
gi 1443040382 602 SQLI 605
Cdd:PTZ00243 1540 HSMV 1543
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1048-1272 |
8.20e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 8.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1048 SIDFNNVSFKYPSRpdvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISL-----------DGVEIR 1116
Cdd:PRK11124 2 SIQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsktpSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1117 SLkvswlRDQMGLVGQE----PVLfndTIRANITYG--KHSEVTEEEITAVAKAANAH----EFVSSLPQgydtvvgekg 1186
Cdd:PRK11124 79 EL-----RRNVGMVFQQynlwPHL---TVQQNLIEApcRVLGLSKDQALARAEKLLERlrlkPYADRFPL---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1187 vQLSGGQKQRVAIARAILKDPKILLLDEATSALDAE-SERVVQDALDRVMVNRTTIVVAHRLSTI-KGADMIAVLKEGKI 1264
Cdd:PRK11124 141 -HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYMENGHI 219
|
....*...
gi 1443040382 1265 AEKGKHEA 1272
Cdd:PRK11124 220 VEQGDASC 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1047-1274 |
8.25e-24 |
|
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: 102.63 E-value: 8.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1047 GSIDFNNVSFKYPSRPDVqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDsGNISLDGVEIRSLKVSWLRDQ 1126
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1127 MGLVGQEPVLFNDTIRANIT-YGKHSEvteEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILK 1205
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKWSD---EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1206 DPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALL 1274
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
368-636 |
8.25e-24 |
|
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: 102.63 E-value: 8.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 368 GDIELKDVYFRYpARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQsGEVLIDGISIKKLRLDWIRGK 447
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 448 IGLVSQEPLLFMASIKDNI-IYGK-KDatlEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILK 525
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKwSD---EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 526 DPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKDpdgaySQLI 605
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE-----KSHF 230
|
250 260 270
....*....|....*....|....*....|.
gi 1443040382 606 RLQETHRDERHKLPDSRSkstSLSFRRSRTK 636
Cdd:cd03289 231 KQAISPSDRLKLFPRRNS---SKSKRKPRPQ 258
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
370-598 |
8.64e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.85 E-value: 8.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIK--KLRLDWIRGK 447
Cdd:PRK13639 2 LETRDLKYSYPDGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 448 IGLVSQEP--LLFMASIKDNIIYG------KKDATLEEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAI 519
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 520 ARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVA-HRLSTV-RNVDCITVVRKGKIVEQGPHDALVKDP 597
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
.
gi 1443040382 598 D 598
Cdd:PRK13639 229 E 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1053-1264 |
1.09e-23 |
|
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: 100.41 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1053 NVSFKYPSRPDvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGveiRSLKVSWLRDQMGLVGQ 1132
Cdd:cd03226 4 NISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1133 EP--VLFNDTIRANITYG-KHSEVTEEEITAVAKAANAHEFVSSLPQgydtvvgekgvQLSGGQKQRVAIARAILKDPKI 1209
Cdd:cd03226 79 DVdyQLFTDSVREELLLGlKELDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1210 LLLDEATSALDAESERVVQDALDRVM-VNRTTIVVAHRLSTIKG-ADMIAVLKEGKI 1264
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1046-1268 |
1.09e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 102.78 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1046 TGSIDFNNVSFKYPSRP--DVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEI----RSLK 1119
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1120 -VSWLRDQMGLVGQEP--VLFNDTIRANITYGK-HSEVTEEEitAVAKAANAHEFVSsLPQGYdtvVGEKGVQLSGGQKQ 1195
Cdd:PRK13645 84 eVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPvNLGENKQE--AYKKVPELLKLVQ-LPEDY---VKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 1196 RVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVN--RTTIVVAHRLSTI-KGADMIAVLKEGKIAEKG 1268
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVlRIADEVIVMHEGKVISIG 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1062-1265 |
1.63e-23 |
|
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: 98.27 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1062 PDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGveirslkvswlrdqmglvgqEPVLFNDTI 1141
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1142 RANitygkhsevteeeitavakaanahefvsslpqgydtvvgEKGV----QLSGGQKQRVAIARAILKDPKILLLDEATS 1217
Cdd:cd03216 71 DAR---------------------------------------RAGIamvyQLSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 1218 AL-DAESERVVqDALDRVMVNRTTIV-VAHRLSTIKG-ADMIAVLKEGKIA 1265
Cdd:cd03216 112 ALtPAEVERLF-KVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
370-639 |
1.63e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.99 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYP-ARPEqliLDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKL-RLDWIRGK 447
Cdd:PRK13644 2 IRLENVSYSYPdGTPA---LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 448 IGLVSQEP-LLFMA-SIKDNIIYGKKDATLE--EIKRAAELANAANFIDKLPNgydtlvgQRGTQLSGGQKQRIAIARAI 523
Cdd:PRK13644 79 VGIVFQNPeTQFVGrTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKYRH-------RSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 524 LKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLV-VAHRLSTVRNVDCITVVRKGKIVEQGPHDALVKDPDGAY- 601
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTl 231
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1443040382 602 ----SQLIRLQETHRDERHKLPDSRSKSTSlSFRRSRTKDFL 639
Cdd:PRK13644 232 gltpPSLIELAENLKMHGVVIPWENTSSPS-SFAEEICRLFL 272
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
388-582 |
2.38e-23 |
|
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: 99.71 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWI----RGKIGLVSQEPLLFMASIK 463
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 464 DNIIYGKKdATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVE- 542
Cdd:cd03290 97 ENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1443040382 543 SERIVQEALNRMMVE--RTTLVVAHRLSTVRNVDCITVVRKG 582
Cdd:cd03290 176 SDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
369-598 |
2.59e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.64 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 369 DIELKDVYFRYPAR-P-EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISI------KKLR 440
Cdd:PRK13634 2 DITFQKVEHRYQYKtPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkknKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 441 LdwIRGKIGLVSQ--EPLLFMASIKDNIIYGKKDATLEEiKRAAELANAANFIDKLPngyDTLVGQRGTQLSGGQKQRIA 518
Cdd:PRK13634 82 P--LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE-EDAKQKAREMIELVGLP---EELLARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 519 IARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRN-VDCITVVRKGKIVEQGPHDALVK 595
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
|
...
gi 1443040382 596 DPD 598
Cdd:PRK13634 236 DPD 238
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
915-1275 |
3.13e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 107.75 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 915 VGSIRTVASFCSEK----RVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQgkttfsdvfK 990
Cdd:PLN03232 486 LASMDTVKCYAWEKsfesRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGDLTPA---------R 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 991 VFFALVLAAVGVSQSSALSTNATKARDSAISIfsiidrkSRIDSS--SDEGAIMENV-----TGSIDFNNVSFKYPSRPD 1063
Cdd:PLN03232 557 AFTSLSLFAVLRSPLNMLPNLLSQVVNANVSL-------QRIEELllSEERILAQNPplqpgAPAISIKNGYFSWDSKTS 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1064 VQIFSDFTLHIPSQKTIALVGESGSGKSTII-ALLERFYDPDSGNISLDGVEIRSLKVSWLrdqmglvgqepvlFNDTIR 1142
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLIsAMLGELSHAETSSVVIRGSVAYVPQVSWI-------------FNATVR 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1143 ANITYGKHSEvTEEEITAVAKAANAHEFvsSLPQGYD-TVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDA 1221
Cdd:PLN03232 697 ENILFGSDFE-SERYWRAIDVTALQHDL--DLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1222 ESERVVQDA-LDRVMVNRTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALLR 1275
Cdd:PLN03232 774 HVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
386-588 |
3.86e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 100.63 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 386 LILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYD-----PQSGEVLIDGISIKKLRLD--WIRGKIGLVSQEPLLF 458
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 459 MASIKDNIIYGKK--------DATLEEIKRAAELANAANfiDKLPngydtlvgQRGTQLSGGQKQRIAIARAILKDPKIL 530
Cdd:PRK14243 104 PKSIYDNIAYGARingykgdmDELVERSLRQAALWDEVK--DKLK--------QSGLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 531 LLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQG 588
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGG 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1069-1271 |
3.89e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.99 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1069 DFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIrSLKVSWLRdQMGLVGQEPVLF-NDTIRANITY 1147
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQR-PINMMFQSYALFpHMTVEQNIAF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1148 G-KHSEVTEEEITA-VAKA---ANAHEFVSSLPQgydtvvgekgvQLSGGQKQRVAIARAILKDPKILLLDEATSALDAE 1222
Cdd:PRK11607 115 GlKQDKLPKAEIASrVNEMlglVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1223 -SERV---VQDALDRVMVnrTTIVVAH-RLSTIKGADMIAVLKEGKIAEKGKHE 1271
Cdd:PRK11607 184 lRDRMqleVVDILERVGV--TCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
384-597 |
4.11e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.12 E-value: 4.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 384 EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERF---YDPQ---SGEVLIDGISIKKLRLDWIRGKIGLVSQEPLL 457
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 458 F-MASIKDNIIYGKKDATLE---EIKRAAElaNAANFIDKLPNGYDTLvGQRGTQLSGGQKQRIAIARAILKDPKILLLD 533
Cdd:PRK14246 102 FpHLSIYDNIAYPLKSHGIKekrEIKKIVE--ECLRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 534 EATSALDVESERIVQEALNRMMVERTTLVVAHRLSTV-RNVDCITVVRKGKIVEQGPHDALVKDP 597
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1081-1247 |
4.57e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.85 E-value: 4.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1081 ALVGESGSGKSTIIALLERFYD--PD---SGNISLDGVEIRSLKVSW--LRDQMGLVGQEPVLFNDTIRANITYG----- 1148
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFPMSIYENVVYGlrlkg 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1149 -KHSEVTEEEITAVAKAANAHEFVSSlpQGYDTVVGekgvqLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVV 1227
Cdd:PRK14239 115 iKDKQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKI 187
|
170 180
....*....|....*....|
gi 1443040382 1228 QDALDRVMVNRTTIVVAHRL 1247
Cdd:PRK14239 188 EETLLGLKDDYTMLLVTRSM 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
370-593 |
6.46e-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: 98.60 E-value: 6.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYParpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKlRLDWIRGKIG 449
Cdd:cd03265 1 IEVENLVKKYG---DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEP-----------LLFMASikdniIYGKKDATLEEikRAAELANA---ANFIDKLPNGYdtlvgqrgtqlSGGQKQ 515
Cdd:cd03265 77 IVFQDLsvddeltgwenLYIHAR-----LYGVPGAERRE--RIDELLDFvglLEAADRLVKTY-----------SGGMRR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 516 RIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDA 592
Cdd:cd03265 139 RLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEE 218
|
.
gi 1443040382 593 L 593
Cdd:cd03265 219 L 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
388-598 |
8.78e-23 |
|
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: 99.34 E-value: 8.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWI--RG------------------- 446
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarLGiartfqnprlfpeltvlen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 -KIGLVSQEPLLFMASIKDNIIYGKKDATLEEikRAAELANAANFIDKLpngyDTLVGQrgtqLSGGQKQRIAIARAILK 525
Cdd:COG0411 100 vLVAAHARLGRGLLAALLRLPRARREEREARE--RAEELLERVGLADRA----DEPAGN----LSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 526 DPKILLLDEATSAL-DVESERIVQ--EALNRMMvERTTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKDPD 598
Cdd:COG0411 170 EPKLLLLDEPAAGLnPEETEELAEliRRLRDER-GITILLIEHDMDLVMGLaDRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
370-594 |
1.20e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.12 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQLildglSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDwiRGKIG 449
Cdd:PRK10771 2 LKLTDITWLYHHLPMRF-----DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLF-MASIKDNIIYG---------KKDATLEEIkraAELANAANFIDKLPngydtlvgqrgTQLSGGQKQRIAI 519
Cdd:PRK10771 75 MLFQENNLFsHLTVAQNIGLGlnpglklnaAQREKLHAI---ARQMGIEDLLARLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 520 ARAILKDPKILLLDEATSALDveserivqEALNRMMV--------ER--TTLVVAHRLS-TVRNVDCITVVRKGKIVEQG 588
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALD--------PALRQEMLtlvsqvcqERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDG 212
|
....*.
gi 1443040382 589 PHDALV 594
Cdd:PRK10771 213 PTDELL 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
384-588 |
1.27e-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: 97.29 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 384 EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWirGKIGLVSQEPLLFMA-SI 462
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 463 KDNI-----IYGKKDATLEEIKRAAELANAAnfidklpngydtlvGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATS 537
Cdd:cd03268 90 RENLrllarLLGIRKKRIDEVLDVVGLKDSA--------------KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 538 ALDVESERIVQEALNRMMVE-RTTLVVAHRLSTVRNV-DCITVVRKGKIVEQG 588
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1024-1271 |
1.27e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 100.68 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1024 SIIDRKSRIDSSSDEGAIMENVTGSIDFNNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDP 1103
Cdd:PRK13536 17 SPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1104 DSGNISLDGVEIRSlKVSWLRDQMGLVGQEPVLFND-TIRAN-ITYGKHSEVTEEEITAVAKAAnaHEFvSSLPQGYDTV 1181
Cdd:PRK13536 94 DAGKITVLGVPVPA-RARLARARIGVVPQFDNLDLEfTVRENlLVFGRYFGMSTREIEAVIPSL--LEF-ARLESKADAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1182 VGEkgvqLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVV-------AHRLstikgAD 1254
Cdd:PRK13536 170 VSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CD 240
|
250
....*....|....*...
gi 1443040382 1255 MIAVLKEG-KIAEKGKHE 1271
Cdd:PRK13536 241 RLCVLEAGrKIAEGRPHA 258
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1049-1264 |
1.35e-22 |
|
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: 97.58 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPDVQIfSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSwLRDQMG 1128
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA-ARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLFND-TIRANITYgkHSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGekgvQLSGGQKQRVAIARAILKDP 1207
Cdd:cd03263 79 YCPQFDALFDElTVREHLRF--YARLKGLPKSEIKEEVELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1208 KILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKG-ADMIAVLKEGKI 1264
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKL 210
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
370-567 |
1.39e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.62 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVY--FrYPARP-EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRlDWIRG 446
Cdd:COG1101 2 LELKNLSktF-NPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 K-IGLVSQEPLLFMA---SIKDN--IIYGK-KDATLeeiKRAAELANAANFIDK-------LPNGYDTLVGQrgtqLSGG 512
Cdd:COG1101 80 KyIGRVFQDPMMGTApsmTIEENlaLAYRRgKRRGL---RRGLTKKRRELFRELlatlglgLENRLDTKVGL----LSGG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 513 QKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRmMVER---TTLVVAHRL 567
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEK-IVEEnnlTTLMVTHNM 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1068-1266 |
1.67e-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: 97.89 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1068 SDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSwLRDQMGLVG--QEPVLFND-TIRAN 1144
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1145 ITYGKHS---------EVTEEEITAVAKAANAHEFVSsLPQGYDTVVGEkgvqLSGGQKQRVAIARAILKDPKILLLDEA 1215
Cdd:cd03219 96 VMVAAQArtgsglllaRARREEREARERAEELLERVG-LADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1216 TSAL-DAESERVVqDALDRVMV-NRTTIVVAHRLSTIKG-ADMIAVLKEG-KIAE 1266
Cdd:cd03219 171 AAGLnPEETEELA-ELIRELRErGITVLLVEHDMDVVMSlADRVTVLDQGrVIAE 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1048-1272 |
1.70e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.13 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1048 SIDFNNVSFKY-PSRP-DVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEI------RSLK 1119
Cdd:PRK13641 2 SIKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgnKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1120 VswLRDQMGLVGQ--EPVLFNDTIRANITYG-KHSEVTEEEitavAKAAnAHEFVSSLpqGYDTVVGEKG-VQLSGGQKQ 1195
Cdd:PRK13641 82 K--LRKKVSLVFQfpEAQLFENTVLKDVEFGpKNFGFSEDE----AKEK-ALKWLKKV--GLSEDLISKSpFELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1196 RVAIARAILKDPKILLLDEATSALDAES-ERVVQDALDRVMVNRTTIVVAHRLSTI-KGADMIAVLKEGKIAekgKHEA 1272
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLI---KHAS 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
392-601 |
2.04e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.26 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 392 SLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR----LDWIRGKIGLVSQE-PLLFMASIKDNI 466
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelREVRRKKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 467 IYGKKDATLEEIKRAAELANAANFIdklpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERI 546
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQV-----GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 547 VQEALNRMMV--ERTTLVVAHRL-STVRNVDCITVVRKGKIVEQGPHDALVKDPDGAY 601
Cdd:PRK10070 203 MQDELVKLQAkhQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1042-1259 |
2.05e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.09 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1042 MENVTGSIDFNNVSFKYPSRPDVQIFSdFTLHIPSQKTIAlvGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVS 1121
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNIS-FSLRAGEFKLIT--GPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1122 WLRDQMGLVGQEPVLFNDTIRANITYgkhsevtEEEITAvaKAANAHEFVSSLPQ-GYDTVVGEKGV-QLSGGQKQRVAI 1199
Cdd:PRK10247 78 IYRQQVSYCAQTPTLFGDTVYDNLIF-------PWQIRN--QQPDPAIFLDDLERfALPDTILTKNIaELSGGEKQRISL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1200 ARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIV--VAHRLSTIKGADMIAVL 1259
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHADKVITL 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1069-1275 |
3.48e-22 |
|
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: 102.07 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1069 DFTLHIPSQKTIALVGESGSGKST----IIALLerfydPDSGNISLDGVEIRSLKVSW---LRDQMGLVGQEPvlFND-- 1139
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDP--FGSls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1140 ---TIRANITYG---KHSEVTEEEITAVAKAANA-------------HEFvsslpqgydtvvgekgvqlSGGQKQRVAIA 1200
Cdd:COG4172 377 prmTVGQIIAEGlrvHGPGLSAAERRARVAEALEevgldpaarhrypHEF-------------------SGGQRQRIAIA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1201 RAILKDPKILLLDEATSALDaeseRVVQ----DALDRVMVNR--TTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEAL 1273
Cdd:COG4172 438 RALILEPKLLVLDEPTSALD----VSVQaqilDLLRDLQREHglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQV 513
|
..
gi 1443040382 1274 LR 1275
Cdd:COG4172 514 FD 515
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
370-588 |
3.54e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 98.28 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPA-RP-EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISI----KKLRLDW 443
Cdd:PRK13649 3 INLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 444 IRGKIGLVSQ--EPLLFMASIKDNIIYGKKD--ATLEEIKRAAELANAANFIDklpngyDTLVGQRGTQLSGGQKQRIAI 519
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 520 ARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLV-VAHRLSTVRN-VDCITVVRKGKIVEQG 588
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
699-984 |
4.15e-22 |
|
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: 98.09 E-value: 4.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 699 GSIA---ASVHGVILPLY-GIIMPGVLKSFYEPPDQLRKDSRFWALMSVVLGVACLISIPAEYFLFGIAGGKLIQRVRTL 774
Cdd:cd18780 1 GTIAllvSSGTNLALPYFfGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 775 SFQRIMHQEVAWFDKpsnsrcatlmyfcyfifykkiftfkpmlrghliSYSGALGTRLSVDALNVRRLVGDNLALIVQAV 854
Cdd:cd18780 81 LFSAIIAQEIAFFDV---------------------------------TRTGELLNRLSSDTQVLQNAVTVNLSMLLRYL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 855 ATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSIRTVASFCSEKRVVAIY 934
Cdd:cd18780 128 VQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRY 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1443040382 935 NKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGKTT 984
Cdd:cd18780 208 SEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELT 257
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1049-1274 |
4.24e-22 |
|
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: 97.08 E-value: 4.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGN-ISLDGVEIRSLKVSWLRDQM 1127
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1128 GLV---------GQEPVL------FNDTIranityGKHSEVTEEEItavakaANAHEFVSSLpqGYDTVVGEKGVQLSGG 1192
Cdd:COG1119 81 GLVspalqlrfpRDETVLdvvlsgFFDSI------GLYREPTDEQR------ERARELLELL--GLAHLADRPFGTLSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1193 QKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNR-TTIV-VAHRLSTI-KGADMIAVLKEGKIAEKGK 1269
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVlVTHHVEEIpPGITHVLLLKDGRVVAAGP 226
|
....*
gi 1443040382 1270 HEALL 1274
Cdd:COG1119 227 KEEVL 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1049-1278 |
4.31e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 98.17 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKY-PSRPDVQI-FSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEI------RSLKV 1120
Cdd:PRK13634 3 ITFQKVEHRYqYKTPFERRaLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkknKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1121 swLRDQMGLVGQ--EPVLFNDTIRANITYG-KHSEVTEEEitAVAKAANAHEFVsslpqGYDTVVGEKG-VQLSGGQKQR 1196
Cdd:PRK13634 83 --LRKKVGIVFQfpEHQLFEETVEKDICFGpMNFGVSEED--AKQKAREMIELV-----GLPEELLARSpFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1197 VAIARAILKDPKILLLDEATSALDAESERVVQDALDRVM--VNRTTIVVAHRLSTI-KGADMIAVLKEGKIAEKGKHEAL 1273
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREI 233
|
....*
gi 1443040382 1274 LRIKD 1278
Cdd:PRK13634 234 FADPD 238
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
385-600 |
6.28e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 97.47 E-value: 6.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 385 QLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDP-----QSGEVLIDGISIKKLR--LDWiRGKIGLVSQEPLL 457
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRdvLEF-RRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 458 FMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATS 537
Cdd:PRK14271 113 FPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 538 ALDVESERIVQEALNRMMVERTTLVVAHRLS-TVRNVDCITVVRKGKIVEQGPHDALVKDPDGA 600
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
370-565 |
6.52e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 96.69 E-value: 6.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGIsikklRLDWIRGKIG 449
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQ-EPLLFMASIKDNIIYGKKdatLEEIKRAAELANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPK 528
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGLQ---LAGVEKMQRLEIAHQMLKKV--GLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 1443040382 529 ILLLDEATSALDVESERIVQEALNRMMVE--RTTLVVAH 565
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITH 187
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
366-598 |
8.12e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.45 E-value: 8.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 366 MNGDIELKDVYFRYParpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQ-----SGEVLIDGISIKKLR 440
Cdd:PRK14267 1 MKFAIETVNLRVYYG---SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 441 LDWI--RGKIGLVSQEPLLF-MASIKDNIIYGKKDATL----EEIKRAAELA-NAANFIDKLPNGYDTLVGQrgtqLSGG 512
Cdd:PRK14267 78 VDPIevRREVGMVFQYPNPFpHLTIYDNVAIGVKLNGLvkskKELDERVEWAlKKAALWDEVKDRLNDYPSN----LSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 513 QKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHD 591
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGPTR 233
|
....*..
gi 1443040382 592 ALVKDPD 598
Cdd:PRK14267 234 KVFENPE 240
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
369-603 |
8.96e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 98.24 E-value: 8.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 369 DIELKDVYFRYParPEQL-ILDGLSLQVASGTTMAIVGESGSGKST----VISLVErfydPQSGEVLIDGISIKKL-RLD 442
Cdd:PRK15079 19 DIKDGKQWFWQP--PKTLkAVDGVTLRLYEGETLGVVGESGCGKSTfaraIIGLVK----ATDGEVAWLGKDLLGMkDDE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 443 W--IRGKIGLVSQEPLlfmASIKDNIIYGkkDATLE-------EIKRAAELANAANFIDK---LPNgydtLVGQRGTQLS 510
Cdd:PRK15079 93 WraVRSDIQMIFQDPL---ASLNPRMTIG--EIIAEplrtyhpKLSRQEVKDRVKAMMLKvglLPN----LINRYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 511 GGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVE-RTTLV-VAHRLSTVRNV-DCITVVRKGKIVEQ 587
Cdd:PRK15079 164 GGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIfIAHDLAVVKHIsDRVLVMYLGHAVEL 243
|
250
....*....|....*.
gi 1443040382 588 GPHDALVKDPDGAYSQ 603
Cdd:PRK15079 244 GTYDEVYHNPLHPYTK 259
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1042-1268 |
9.37e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 96.27 E-value: 9.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1042 MENVTGSIDFNNVSFKYPSRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGV------EI 1115
Cdd:PRK14246 1 MEAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1116 RSLKVSWLRDQMGLVGQEPVLF-NDTIRANITYGKHSEVTEEEITAVAKAANAHEFVSSLPQGYDTVvGEKGVQLSGGQK 1194
Cdd:PRK14246 81 FQIDAIKLRKEVGMVFQQPNPFpHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRL-NSPASQLSGGQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1195 QRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTI-KGADMIAVLKEGKIAEKG 1268
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWG 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
387-588 |
9.43e-22 |
|
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: 94.54 E-value: 9.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 387 ILDGLSLQVASGTTMAIVGESGSGKSTVISLV--ERFYDPQSGEVLIDGISIKKlrlDWIRGKIGLVSQepllfmasikD 464
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQ----------D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 465 NIIYGkkDATLEE-IKRAAELanaanfidklpngydtlvgqRGtqLSGGQKQRIAIARAILKDPKILLLDEATSALDVES 543
Cdd:cd03213 91 DILHP--TLTVREtLMFAAKL--------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1443040382 544 ERIVQEALNRMMVE-RTTLVVAHRLST--VRNVDCITVVRKGKIVEQG 588
Cdd:cd03213 147 ALQVMSLLRRLADTgRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
388-562 |
1.07e-21 |
|
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: 95.19 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLID----GISIKK--------LRldwiRGKIGLVSQ-- 453
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQaspreilaLR----RRTIGYVSQfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 454 -------------EPLLFMasikdniiyGKKDATLEEikRAAELANAANFIDKL----PNGYdtlvgqrgtqlSGGQKQR 516
Cdd:COG4778 103 rviprvsaldvvaEPLLER---------GVDREEARA--RARELLARLNLPERLwdlpPATF-----------SGGEQQR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1443040382 517 IAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLV 562
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1072-1274 |
1.46e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 95.59 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1072 LHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEI---RSLK-----VSWLRDQMGLVGQEPVLF-NDTIR 1142
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQNFNLFpHRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1143 ANITYGKH--SEVTEEEITAVAKAANAHEFVSSLPQGYDTvvgekgvQLSGGQKQRVAIARAILKDPKILLLDEATSALD 1220
Cdd:PRK11264 104 ENIIEGPVivKGEPKEEATARARELLAKVGLAGKETSYPR-------RLSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1221 AEserVVQDALDRVMV----NRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEALL 1274
Cdd:PRK11264 177 PE---LVGEVLNTIRQlaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1049-1274 |
1.52e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.32 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMG 1128
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEP--VLFNDTIRANITYGKHSE--VTEEEITAVAK---AANAHEFVSSLPqgydtvvgekgVQLSGGQKQRVAIAR 1201
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQgiPREEMIKRVDEallAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1202 AILKDPKILLLDEATSALD----AESERVVQDALDRVMVnrTTIVVAHRLSTIKGADMIAVLKEGKIAEKGKHEALL 1274
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
366-588 |
1.72e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.92 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 366 MNGDIELKDVYFRYPARPEQ---LILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLD 442
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEEStekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 443 W-IRGKIGLVSQEP--LLFMASIKDNIIYGKKDATL--EEIKRAAELA----NAANFIDKLPNgydtlvgqrgtQLSGGQ 513
Cdd:PRK13633 81 WdIRNKAGMVFQNPdnQIVATIVEEDVAFGPENLGIppEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 514 KQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRNVDCITVVRKGKIVEQG 588
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
370-591 |
1.82e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.21 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISI-KKLRLdwIRGKI 448
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARL--ARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 449 GLVSQEPLLFMA-SIKDNII-----YGKKDATLEE-IKRAAELAnaanfidKLPNGYDTLVgqrgTQLSGGQKQRIAIAR 521
Cdd:PRK13536 117 GVVPQFDNLDLEfTVRENLLvfgryFGMSTREIEAvIPSLLEFA-------RLESKADARV----SDLSGGMKRRLTLAR 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 522 AILKDPKILLLDEATSALDVESERIVQEALNRMMVE-RTTLVVAHRLSTV-RNVDCITVVRKG-KIVEQGPHD 591
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARgKTILLTTHFMEEAeRLCDRLCVLEAGrKIAEGRPHA 258
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1063-1268 |
1.93e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 94.98 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1063 DVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYD--PD---SGNISLDGVEIRSLKVSWLRDQMGLVGQEP-VL 1136
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1137 FNDTIRANITYG--------KHSEVTEEEITAVAKAanahefvsslpQGYDTV---VGEKGVQLSGGQKQRVAIARAILK 1205
Cdd:PRK14247 95 PNLSIFENVALGlklnrlvkSKKELQERVRWALEKA-----------QLWDEVkdrLDAPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1206 DPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAH------RLStikgaDMIAVLKEGKIAEKG 1268
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1051-1223 |
1.94e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1051 FNNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDgveiRSLKVSWLRdqmglv 1130
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP----KGLRIGYLP------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1131 gQEPVLFND-TIRANITYGkHSEV----------------TEEEITAVAK------AANAHEF---VSSLPQG------- 1177
Cdd:COG0488 68 -QEPPLDDDlTVLDTVLDG-DAELraleaeleeleaklaePDEDLERLAElqeefeALGGWEAearAEEILSGlgfpeed 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1443040382 1178 YDTVVGEkgvqLSGGQKQRVAIARAILKDPKILLLDEATSALDAES 1223
Cdd:COG0488 146 LDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
387-588 |
1.97e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 94.75 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 387 ILDGLSLQVASGTTMAIVGESGSGKST---VISLVERfYDPQSGEVLIDGISIKKLRLDwIRGK--IGLVSQEPL----- 456
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLMGHPK-YEVTSGSILLDGEDILELSPD-ERARagIFLAFQYPVeipgv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 457 ---LFMASIKdNIIYGKKDATLEEIKRAAELAN----AANFIDKLPNgydtlVGqrgtqLSGGQKQRIAIARAILKDPKI 529
Cdd:COG0396 93 svsNFLRTAL-NARRGEELSAREFLKLLKEKMKelglDEDFLDRYVN-----EG-----FSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 530 LLLDEATSALDVESERIVQEALNRMMVE-RTTLVVAH--RLSTVRNVDCITVVRKGKIVEQG 588
Cdd:COG0396 162 AILDETDSGLDIDALRIVAEGVNKLRSPdRGILIITHyqRILDYIKPDFVHVLVDGRIVKSG 223
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
388-617 |
2.14e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 95.29 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKST---VISLVERfydPQSGEVLIDGISIK----KLRLDWIR-------------GK 447
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTlakMLAGIIE---PTSGEILINGHKLEygdyKYRCKHIRmifqdpntslnprLN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 448 IGLVSQEPLLFMASIKDNIIYGKKDATLeeiKRAAELANAANFidkLPNgydtlvgqrgtQLSGGQKQRIAIARAILKDP 527
Cdd:COG4167 106 IGQILEEPLRLNTDLTAEEREERIFATL---RLVGLLPEHANF---YPH-----------MLSSGQKQRVALARALILQP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 528 KILLLDEATSALDVeSERIvqEALNRMMVERTTL-----VVAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKDPDGAY 601
Cdd:COG4167 169 KIIIADEALAALDM-SVRS--QIINLMLELQEKLgisyiYVSQHLGIVKHIsDKVLVMHQGEVVEYGKTAEVFANPQHEV 245
|
250
....*....|....*.
gi 1443040382 602 SQliRLQETHRDERHK 617
Cdd:COG4167 246 TK--RLIESHFGEALT 259
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
365-613 |
2.21e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.85 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 365 DMNGDIELKDVYFRYPARP--EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISI----KK 438
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 439 LR-LDWIRGKIGLVSQEP--LLFMASIKDNIIYGKKD--ATLEEI-KRAAELANaanfIDKLPNGYdtlVGQRGTQLSGG 512
Cdd:PRK13645 82 IKeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNlgENKQEAyKKVPELLK----LVQLPEDY---VKRSPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 513 QKQRIAIARAILKDPKILLLDEATSALDVESERIVQ---EALNRMMVERTTLVVAHRLSTVRNVDCITVVRKGKIVEQGP 589
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFInlfERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
250 260 270
....*....|....*....|....*....|....
gi 1443040382 590 -------HDALVK---DPDGAYSQLIRLQETHRD 613
Cdd:PRK13645 235 pfeifsnQELLTKieiDPPKLYQLMYKLKNKGID 268
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
370-588 |
2.33e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.68 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQLilDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR--LDWIRGK 447
Cdd:PRK13636 6 LKVEELNYNYSDGTHAL--KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkgLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 448 IGLVSQEP--LLFMASIKDNIIYGKKDATL--EEIKRAAELANAANFIDKLPNgydtlvgqRGTQ-LSGGQKQRIAIARA 522
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKD--------KPTHcLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 523 ILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVR-NVDCITVVRKGKIVEQG 588
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGRVILQG 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
388-604 |
2.42e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 94.99 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDG----------ISIKKLRL----DWirgkiGLVSQ 453
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlrdlyaLSEAERRRllrtEW-----GFVHQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 454 EPL--LFMA-SIKDNII----------YGKKDATLEEIKRAAELanAANFIDKLPngydtlvgqrgTQLSGGQKQRIAIA 520
Cdd:PRK11701 97 HPRdgLRMQvSAGGNIGerlmavgarhYGDIRATAGDWLERVEI--DAARIDDLP-----------TTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 521 RAILKDPKILLLDEATSALDVEseriVQEA---LNRMMVERTTL---VVAHRLSTVRNV-DCITVVRKGKIVEQGPHDAL 593
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVS----VQARlldLLRGLVRELGLavvIVTHDLAVARLLaHRLLVMKQGRVVESGLTDQV 239
|
250
....*....|.
gi 1443040382 594 VKDPDGAYSQL 604
Cdd:PRK11701 240 LDDPQHPYTQL 250
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
370-598 |
3.17e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 95.67 E-value: 3.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRY-PARPEQLI-LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISI------KKLRL 441
Cdd:PRK13641 3 IKFENVDYIYsPGTPMEKKgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgnKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 442 dwIRGKIGLVSQ--EPLLFMASIKDNIIYGKKD--ATLEEIKRAA-----ELANAANFIDKLPngydtlvgqrgTQLSGG 512
Cdd:PRK13641 83 --LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKAlkwlkKVGLSEDLISKSP-----------FELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 513 QKQRIAIARAILKDPKILLLDEATSALDVES-ERIVQEALNRMMVERTTLVVAHRLSTVRN-VDCITVVRKGKIVEQGPH 590
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASP 229
|
....*...
gi 1443040382 591 DALVKDPD 598
Cdd:PRK13641 230 KEIFSDKE 237
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
370-598 |
3.21e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.25 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIG 449
Cdd:PRK13652 4 IETRDLCYSYSGSKE--ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEP--LLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIdklpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDP 527
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 528 KILLLDEATSALDVESERIVQEALNRMMVERTTLVV--AHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKDPD 598
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1052-1264 |
3.93e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 94.36 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1052 NNVSFKYPSRpdvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNIsLDGveirSLKVSWLRDQMGLVG 1131
Cdd:PRK11247 16 NAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1132 QEPVLFN-DTIRANITY---GKHSEVTEEEITAVAKAANAHEFVSSlpqgydtvvgekgvqLSGGQKQRVAIARAILKDP 1207
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLglkGQWRDAALQALAAVGLADRANEWPAA---------------LSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1208 KILLLDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRLS-TIKGADMIAVLKEGKI 1264
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1049-1221 |
4.34e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.54 E-value: 4.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYP-SRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVswlrdQM 1127
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-----DR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1128 GLVGQEPVLFN-DTIRANITYGKhsevteeEITAVAKA---ANAHEFVSslpqgydtVVGEKGV------QLSGGQKQRV 1197
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGL-------RLRGVPKAerrARAEELLA--------LVGLADFarrriwQLSGGMRQRV 143
|
170 180
....*....|....*....|....
gi 1443040382 1198 AIARAILKDPKILLLDEATSALDA 1221
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDA 167
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
387-568 |
4.53e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 93.73 E-value: 4.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 387 ILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKL----RLDWIRGKIGLVSQ-EPLLFMAS 461
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNQKLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 462 IKDNI-----IYGKKDATLEEikRAAELANAAnfidklpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEAT 536
Cdd:PRK11629 104 ALENVampllIGKKKPAEINS--RALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190
....*....|....*....|....*....|....
gi 1443040382 537 SALDVESERIVQEALNRMMVERTT--LVVAHRLS 568
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTafLVVTHDLQ 207
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1049-1275 |
5.05e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.99 E-value: 5.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMG 1128
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVlFND--TIRANITYGK--HSE--VTEEEITAVAKAAN-------AHEFVSslpqgydtvvgekgvQLSGGQKQ 1195
Cdd:COG4604 79 ILRQENH-INSrlTVRELVAFGRfpYSKgrLTAEDREIIDEAIAyldledlADRYLD---------------ELSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1196 RVAIARAILKDPKILLLDEATSALDAESERVVQDALDRvMV---NRTTIVVAHRL---STIkgADMIAVLKEGKIAEKGK 1269
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRR-LAdelGKTVVIVLHDInfaSCY--ADHIVAMKDGRVVAQGT 219
|
....*.
gi 1443040382 1270 HEALLR 1275
Cdd:COG4604 220 PEEIIT 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1069-1271 |
5.22e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.10 E-value: 5.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1069 DFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDG-VEIRSLKVSWL---RDQMGLVGQEPVLF-NDTIRA 1143
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAEKGICLppeKRRIGYVFQDARLFpHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1144 NITYGkhsevteeeitaVAKAANAHefvsslpqgYDTVVGEKGVQ---------LSGGQKQRVAIARAILKDPKILLLDE 1214
Cdd:PRK11144 96 NLRYG------------MAKSMVAQ---------FDKIVALLGIEplldrypgsLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1215 ATSALDAESERVVQDALDRVM--VNRTTIVVAHRLSTI-KGADMIAVLKEGKIAEKGKHE 1271
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAreINIPILYVSHSLDEIlRLADRVVVLEQGKVKAFGPLE 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1042-1266 |
5.61e-21 |
|
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: 93.27 E-value: 5.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1042 MENVTGS-IDFNNVSFKYPSRP-DVQIFSDFTLHIPSQKTIALVGESGSGKST---IIALLERfydPDSGNISLDGVEIR 1116
Cdd:COG4181 1 MSSSSAPiIELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTllgLLAGLDR---PTSGTVRLAGQDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1117 SL----KVSWLRDQMGLVGQ-----------EPVLF--------NDTIRAnitygkhsevtEEEITAVAKAANAHEFvss 1173
Cdd:COG4181 78 ALdedaRARLRARHVGFVFQsfqllptltalENVMLplelagrrDARARA-----------RALLERVGLGHRLDHY--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1174 lPQgydtvvgekgvQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRvmVNR---TTIV-VAHRLST 1249
Cdd:COG4181 144 -PA-----------QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFE--LNRergTTLVlVTHDPAL 209
|
250
....*....|....*..
gi 1443040382 1250 IKGADMIAVLKEGKIAE 1266
Cdd:COG4181 210 AARCDRVLRLRAGRLVE 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1048-1268 |
6.76e-21 |
|
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: 91.84 E-value: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1048 SIDFNNVSFKYPSRP---DVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALL--ERFYDPDSGNISLDGveiRSLKVSW 1122
Cdd:cd03213 3 TLSFRNLTVTVKSSPsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1123 LRDQMGLVGQEPVLF-NDTIRANITYgkhsevteeeitavakAANAhefvsslpqgydtvvgeKGvqLSGGQKQRVAIAR 1201
Cdd:cd03213 80 FRKIIGYVPQDDILHpTLTVRETLMF----------------AAKL-----------------RG--LSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1202 AILKDPKILLLDEATSALDAESERVVQDALDR-VMVNRTTIVVAHRLST--IKGADMIAVLKEGKIAEKG 1268
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1069-1275 |
6.78e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 95.94 E-value: 6.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1069 DFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDG--VEIRSLKVswlRDqMGLVGQEPVLF-NDTIRANI 1145
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedVTHRSIQQ---RD-ICMVFQSYALFpHMSLGENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1146 TYG-KHSEVTEEEITAVAKaaNAHEFVSsLPQGYDTVVGekgvQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESE 1224
Cdd:PRK11432 100 GYGlKMLGVPKEERKQRVK--EALELVD-LAGFEDRYVD----QISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1225 RVVQDALDRVM--VNRTTIVVAHRLS-TIKGADMIAVLKEGKIAEKGKHEALLR 1275
Cdd:PRK11432 173 RSMREKIRELQqqFNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1052-1222 |
1.07e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.77 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1052 NNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPD---SGNISLDGVEIRSLKVswLRDQMG 1128
Cdd:COG4136 5 ENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA--EQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLF-NDTIRANITYGKHSEVT-EEEITAVAKA---ANAHEFVSSLPQgydtvvgekgvQLSGGQKQRVAIARAI 1203
Cdd:COG4136 80 ILFQDDLLFpHLSVGENLAFALPPTIGrAQRRARVEQAleeAGLAGFADRDPA-----------TLSGGQRARVALLRAL 148
|
170
....*....|....*....
gi 1443040382 1204 LKDPKILLLDEATSALDAE 1222
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAA 167
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1048-1275 |
1.28e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.91 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1048 SIDFNNVSFKYPSRpdvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQM 1127
Cdd:PRK13548 2 MLEARNLSVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1128 GLVGQEPVL-FNDTIRANITYGK--HSEVTEEEITAVAKA---ANAHEFVSSLPQgydtvvgekgvQLSGGQKQRVAIAR 1201
Cdd:PRK13548 79 AVLPQHSSLsFPFTVEEVVAMGRapHGLSRAEDDALVAAAlaqVDLAHLAGRDYP-----------QLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1202 AIL------KDPKILLLDEATSALD-AESERVVQDALDRVMVNRTT-IVVAHRLS-TIKGADMIAVLKEGKIAEKGKHEA 1272
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDlAHQHHVLRLARQLAHERGLAvIVVLHDLNlAARYADRIVLLHQGRLVADGTPAE 227
|
...
gi 1443040382 1273 LLR 1275
Cdd:PRK13548 228 VLT 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
372-543 |
1.63e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 372 LKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGisikklrlDWirgKIGLV 451
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK--------GL---RIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 452 SQEPLLFM-ASIKDNI----------------IYGKKDATLEEIKRAAEL-------------ANAANFIDKL---PNGY 498
Cdd:COG0488 67 PQEPPLDDdLTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAELqeefealggweaeARAEEILSGLgfpEEDL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1443040382 499 DTLVGQrgtqLSGGQKQRIAIARAILKDPKILLLDEATSALDVES 543
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
370-596 |
1.84e-20 |
|
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: 96.80 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEQLI--LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLI----DGISIKKLRLDw 443
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 444 IRGK----IGLVSQEPLLF-MASIKDNI-----------------IYGKKDATLEEIKraaelanAANFIDKLPNgydtl 501
Cdd:TIGR03269 359 GRGRakryIGILHQEYDLYpHRTVLDNLteaiglelpdelarmkaVITLKMVGFDEEK-------AEEILDKYPD----- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 502 vgqrgtQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEAL--NRMMVERTTLVVAHRLSTVRNV-DCITV 578
Cdd:TIGR03269 427 ------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDVcDRAAL 500
|
250
....*....|....*...
gi 1443040382 579 VRKGKIVEQGPHDALVKD 596
Cdd:TIGR03269 501 MRDGKIVKIGDPEEIVEE 518
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1068-1266 |
2.69e-20 |
|
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: 92.02 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1068 SDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVsWLRDQMGLV--GQEPVLFND-TIRAN 1144
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIArtFQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1145 ITYGKHS--------------EVTEEEITAVAKAANAHEFVsslpqGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKIL 1210
Cdd:COG0411 100 VLVAAHArlgrgllaallrlpRARREEREARERAEELLERV-----GLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 1211 LLDEATSAL-DAESERVVqDALDRV--MVNRTTIVVAHRLSTIKG-ADMIAVLKEG-KIAE 1266
Cdd:COG0411 175 LLDEPAAGLnPEETEELA-ELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGrVIAE 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
384-607 |
2.80e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.31 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 384 EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQsGEVLIDGISIKKL---RLDWIRGKIGLVSQEP----- 455
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLnrrQLLPVRHRIQVVFQDPnssln 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 456 -LLFMASIkdnIIYGKK--DATLEEIKRAAELANAANFIdklpnGYDTLVGQR-GTQLSGGQKQRIAIARAILKDPKILL 531
Cdd:PRK15134 377 pRLNVLQI---IEEGLRvhQPTLSAAQREQQVIAVMEEV-----GLDPETRHRyPAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 532 LDEATSALDveseRIVQE---ALNRMMVERTTLV---VAHRLSTVRNVdC--ITVVRKGKIVEQGPHDALVKDPDGAYS- 602
Cdd:PRK15134 449 LDEPTSSLD----KTVQAqilALLKSLQQKHQLAylfISHDLHVVRAL-ChqVIVLRQGEVVEQGDCERVFAAPQQEYTr 523
|
....*
gi 1443040382 603 QLIRL 607
Cdd:PRK15134 524 QLLAL 528
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
382-625 |
3.09e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 96.65 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 382 RPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVErFYDPQ----SGEVLIDGISIKKLRLDWIRGKI--------G 449
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKEMRAISAYVqqddlfipT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMASIK--DNIIYGKKDATLEEIKRAAELANAANfidklpngydTLVGQRGTQ--LSGGQKQRIAIARAILK 525
Cdd:TIGR00955 114 LTVREHLMFQAHLRmpRRVTKKEKRERVDEVLQALGLRKCAN----------TRIGVPGRVkgLSGGERKRLAFASELLT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 526 DPKILLLDEATSALDVESERIVQEALNRM-MVERTTLVVAHRLST--VRNVDCITVVRKGKIVEQGPHDALVK------- 595
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVPffsdlgh 263
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1443040382 596 ------DPDGAYSQLIRL----QETHRDERHKLPDSRSKS 625
Cdd:TIGR00955 264 pcpenyNPADFYVQVLAVipgsENESRERIEKICDSFAVS 303
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1042-1266 |
3.14e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.02 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1042 MENVTGSIDFNNVSFKYPSRpdvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDS-----GNISLDGVEI- 1115
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1116 -RSLKVSWLRDQMGLVGQEPVLFNDTIRANITYGK-----HSEVTEEEITAVA-KAANAHEFVSSlpqgydtVVGEKGVQ 1188
Cdd:PRK14258 78 eRRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVkivgwRPKLEIDDIVESAlKDADLWDEIKH-------KIHKSALD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1189 LSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALD--RVMVNRTTIVVAHRLSTI-KGADMIAVLK--EGK 1263
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVsRLSDFTAFFKgnENR 230
|
...
gi 1443040382 1264 IAE 1266
Cdd:PRK14258 231 IGQ 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
385-602 |
3.40e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.13 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 385 QLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKklRLDWIRGKIGLVSQEPLLF-MASIK 463
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFpHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 464 DNIIYGKKDATL--EEIK-RAAE---LANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIARAILKDPKILLLDEATS 537
Cdd:PRK11607 110 QNIAFGLKQDKLpkAEIAsRVNEmlgLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 538 ALDVE-SERIVQEALNrmMVER---TTLVVAH-RLSTVRNVDCITVVRKGKIVEQGPHDALVKDPDGAYS 602
Cdd:PRK11607 179 ALDKKlRDRMQLEVVD--ILERvgvTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
384-593 |
4.17e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 91.23 E-value: 4.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 384 EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLFMA-SI 462
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 463 KDNIIYGK------------KDATLeeIKRAAElanaanfidklPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKIL 530
Cdd:PRK11231 94 RELVAYGRspwlslwgrlsaEDNAR--VNQAME-----------QTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 531 LLDEATSALDVESerivQEALNRMMVE-----RTTLVVAHRLSTV-RNVDCITVVRKGKIVEQG-PHDAL 593
Cdd:PRK11231 161 LLDEPTTYLDINH----QVELMRLMRElntqgKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGtPEEVM 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
378-577 |
4.21e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.60 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 378 RYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGisikklrldwiRGKIGLVSQ---E 454
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 455 PLLFMASIKDNIIYGK-KDATLEEIKRAAELANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLD 533
Cdd:NF040873 67 PDSLPLTVRDLVAMGRwARRGLWRRLTRDDRAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1443040382 534 EATSALDVESERIVQEALNRMMVE-RTTLVVAHRLSTVRNVDCIT 577
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCV 189
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
372-584 |
4.24e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.28 E-value: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 372 LKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDwIRgkigLV 451
Cdd:PRK11247 15 LNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED-TR----LM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 452 SQEP-LLFMASIKDNIIYGKK----DATLEEIkRAAELANAANfidKLPngydtlvgqrgTQLSGGQKQRIAIARAILKD 526
Cdd:PRK11247 87 FQDArLLPWKKVIDNVGLGLKgqwrDAALQAL-AAVGLADRAN---EWP-----------AALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 527 PKILLLDEATSALDveserivqeALNRM----MVER-------TTLVVAHRLS-TVRNVDCITVVRKGKI 584
Cdd:PRK11247 152 PGLLLLDEPLGALD---------ALTRIemqdLIESlwqqhgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1052-1267 |
5.58e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.39 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1052 NNVSFKYPSRPDVQIFSdftLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSL-------KVSWLR 1124
Cdd:PRK10575 15 RNVSFRVPGRTLLHPLS---LTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWsskafarKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1125 DQMglvgqePVLFNDTIRANITYGKH-------------SEVTEEEITAVAKAANAHEFVSSLpqgydtvvgekgvqlSG 1191
Cdd:PRK10575 92 QQL------PAAEGMTVRELVAIGRYpwhgalgrfgaadREKVEEAISLVGLKPLAHRLVDSL---------------SG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 1192 GQKQRVAIARAILKDPKILLLDEATSALDAESERVVqdaldrvmvnrttIVVAHRLSTIKGADMIAVLKEGKIAEK 1267
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV-------------LALVHRLSQERGLTVIAVLHDINMAAR 213
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
121-567 |
5.69e-20 |
|
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: 96.90 E-value: 5.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 121 SARIRSLYLKAVLRQDITFFDTeMTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGG-FIIAFTRGWLLtlvmLTS 199
Cdd:TIGR01271 957 SKRLHEQMLHSVLQAPMAVLNT-MKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAiFVVSVLQPYIF----IAA 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 200 LPLIAIASAVSAQALtRVSSKRQTSYSDAGDTVEQTIgsirtVVSFNGekkaIAMYRNFIKKSYKATIEE---------- 269
Cdd:TIGR01271 1032 IPVAVIFIMLRAYFL-RTSQQLKQLESEARSPIFSHL-----ITSLKG----LWTIRAFGRQSYFETLFHkalnlhtanw 1101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 270 ----GIITGFGMGSVMCVVFGSYGLAFWYggklIIEKGYTGGKIMTILFAVLTGASSLGNATPAVAAVVEGQSAAYNLFK 345
Cdd:TIGR01271 1102 flylSTLRWFQMRIDIIFVFFFIAVTFIA----IGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFK 1177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 346 TIERKPEIDSDDNNG--------MVLEDMN--------GDIELKDVYFRYpARPEQLILDGLSLQVASGTTMAIVGESGS 409
Cdd:TIGR01271 1178 FIDLPQEEPRPSGGGgkyqlstvLVIENPHaqkcwpsgGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGS 1256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 410 GKSTVISLVERFYDPQsGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLFMASIKDNIIYGKKDATlEEIKRAAELANAAN 489
Cdd:TIGR01271 1257 GKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSD-EEIWKVAEEVGLKS 1334
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 490 FIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVAHRL 567
Cdd:TIGR01271 1335 VIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
379-603 |
5.74e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 90.91 E-value: 5.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 379 YPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDP----QSGEVLIDGISIKKLRLdwiRGK-IGLVSQ 453
Cdd:PRK10418 13 QAAQP---LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCAL---RGRkIATIMQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 454 ------EPLLFMAS--IKDNIIYGK--KDATLEEIKRAAELANAANFIDKLPngydtlvgqrgTQLSGGQKQRIAIARAI 523
Cdd:PRK10418 87 nprsafNPLHTMHThaRETCLALGKpaDDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 524 LKDPKILLLDEATSALDVESERIVQEALNRMMVERT--TLVVAHRLSTV-RNVDCITVVRKGKIVEQGPHDALVKDPDGA 600
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
...
gi 1443040382 601 YSQ 603
Cdd:PRK10418 236 VTR 238
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
366-589 |
6.23e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.95 E-value: 6.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 366 MNGDIELKDVYFRYPARPEQL-ILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWI 444
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 445 ----RGKIGLVSQE-PLLFMASIKDNIiygKKDATLEEIKRAAELANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAI 519
Cdd:PRK10535 81 aqlrREHFGFIFQRyHLLSHLTAAQNV---EVPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 520 ARAILKDPKILLLDEATSALDVESERIVQEALNRMMVE-RTTLVVAHRLSTVRNVDCITVVRKGKIVEQGP 589
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPP 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
370-589 |
9.66e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 91.32 E-value: 9.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYParpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGisiKKLRLDwIRGKIG 449
Cdd:COG4152 2 LELKGLTKRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPE-DRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLF--MaSIKDNIIY-GK-KDATLEEIKRAA-------ELANAANfiDKLpngydtlvgqrgTQLSGGQKQRIA 518
Cdd:COG4152 75 YLPEERGLYpkM-KVGEQLVYlARlKGLSKAEAKRRAdewlerlGLGDRAN--KKV------------EELSKGNQQKVQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 519 IARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVVA-HRLSTV-RNVDCITVVRKGKIVEQGP 589
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSsHQMELVeELCDRIVIINKGRKVLSGS 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1081-1264 |
1.01e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 94.31 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1081 ALVGESGSGKSTIIALLERFYDPDSGNISLDG--VEIRSLKVSWlrdQMG--LVGQEPVLFND-TIRANITYGK------ 1149
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQ---AAGiaIIHQELNLVPNlSVAENIFLGReprrgg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1150 ---HSEVTEEeitavakaanAHEFVSSL-----PqgyDTVVGEkgvqLSGGQKQRVAIARAILKDPKILLLDEATSAL-D 1220
Cdd:COG1129 111 lidWRAMRRR----------ARELLARLgldidP---DTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLtE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1443040382 1221 AESER---VVQDALDRvmvNRTTIVVAHRLSTIKG-ADMIAVLKEGKI 1264
Cdd:COG1129 174 REVERlfrIIRRLKAQ---GVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1053-1257 |
1.06e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 90.61 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1053 NVSFKYPSRPDVQifsDFTLHIPSQKTIALVGESGSGKSTIIALLER---------------FYDPDSGNISLDGVEIRS 1117
Cdd:PRK14243 15 NLNVYYGSFLAVK---NVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndlipgfrvegkvtFHGKNLYAPDVDPVEVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1118 lkvswlrdQMGLVGQEPVLFNDTIRANITYGKH--------SEVTEeeiTAVAKAANAHEFVSSLPQgydtvvgeKGVQL 1189
Cdd:PRK14243 92 --------RIGMVFQKPNPFPKSIYDNIAYGARingykgdmDELVE---RSLRQAALWDEVKDKLKQ--------SGLSL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1190 SGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRL-STIKGADMIA 1257
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMqQAARVSDMTA 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
387-597 |
1.58e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 91.68 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 387 ILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKklRLDWIRGKIGLVSQEPLLF--MaSIKD 464
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS--RLHARDRKVGFVFQHYALFrhM-TVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 465 NIIYG------KKDATLEEIKRAA----ELANAANFIDKLPngydtlvgqrgTQLSGGQKQRIAIARAILKDPKILLLDE 534
Cdd:PRK10851 94 NIAFGltvlprRERPNAAAIKAKVtqllEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 535 ATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKDP 597
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1069-1274 |
1.78e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.40 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1069 DFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRD----QMGLVGQEPVLF-NDTIRA 1143
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1144 NITYGKhsevteeEITAVAKAANAHEFVSSLPQ-GYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAE 1222
Cdd:PRK10070 126 NTAFGM-------ELAGINAEERREKALDALRQvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1223 SERVVQDALDRVMV--NRTTIVVAHRL-STIKGADMIAVLKEGKIAEKGKHEALL 1274
Cdd:PRK10070 199 IRTEMQDELVKLQAkhQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
100-332 |
1.87e-19 |
|
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: 90.48 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 100 IGTSVASFLQVSCWTMAGERQSARIRSLYLKAVLRQDITFFDtEMTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFI 179
Cdd:cd18590 47 LGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFE-KTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 180 GGFIIAFTRGWLLTLVMLTSLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFI 259
Cdd:cd18590 126 GMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEAL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 260 KKSYKATIEEGIITGFGMGSVMCVVFGSYGLAFWYGGKLIIEKGYTGGKIMT-ILF------AVLTGASSLGNATPAVAA 332
Cdd:cd18590 206 ERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSfILYqknlgsYVRTLVYIYGDMLSNVGA 285
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1049-1268 |
1.92e-19 |
|
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: 88.74 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPS-------------------RPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNIS 1109
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1110 LDGveirslKVSWLRD-----QMGLVGQEPVLFNDTIranitYGkhseVTEEEITavAKAANAHEFvSSLPQGYDTVVGE 1184
Cdd:cd03220 81 VRG------RVSSLLGlgggfNPELTGRENIYLNGRL-----LG----LSRKEID--EKIDEIIEF-SELGDFIDLPVKT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1185 kgvqLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDAL-DRVMVNRTTIVVAHRLSTIKG-ADMIAVLKEG 1262
Cdd:cd03220 143 ----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRlCDRALVLEKG 218
|
....*.
gi 1443040382 1263 KIAEKG 1268
Cdd:cd03220 219 KIRFDG 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1049-1274 |
1.95e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.21 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFkypSRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMG 1128
Cdd:PRK09536 4 IDVSDLSV---EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVL-FNDTIRANITYGKH------SEVTEEEITAVAKAANAHEFVSSLPQGYDTvvgekgvqLSGGQKQRVAIAR 1201
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQVVEMGRTphrsrfDTWTETDRAAVERAMERTGVAQFADRPVTS--------LSGGERQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1202 AILKDPKILLLDEATSALDAESE-RVVQDALDRVMVNRTTIVVAHRLS-TIKGADMIAVLKEGKIAEKGKHEALL 1274
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
370-596 |
2.59e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.83 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFrypARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIG 449
Cdd:PRK09536 4 IDVSDLSV---EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQE-PLLFMASIKDNIIYGKK----------DATLEEIKRAAELANAANFIDklpngydtlvgQRGTQLSGGQKQRIA 518
Cdd:PRK09536 81 SVPQDtSLSFEFDVRQVVEMGRTphrsrfdtwtETDRAAVERAMERTGVAQFAD-----------RPVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 519 IARAILKDPKILLLDEATSALDVeSERIVQEALNRMMVE--RTTLVVAHRLS-TVRNVDCITVVRKGKIVEQG-PHDALV 594
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDI-NHQVRTLELVRRLVDdgKTAVAAIHDLDlAARYCDELVLLADGRVRAAGpPADVLT 228
|
..
gi 1443040382 595 KD 596
Cdd:PRK09536 229 AD 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
391-589 |
3.19e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 90.70 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 391 LSLQV-----ASGTTmAIVGESGSGKSTVISLVERFYDPQSGE------VLIDgiSIKKLRLDWIRGKIGLVSQEPLLF- 458
Cdd:PRK11144 13 LCLTVnltlpAQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRivlngrVLFD--AEKGICLPPEKRRIGYVFQDARLFp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 459 MASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPngydtlvgqrgTQLSGGQKQRIAIARAILKDPKILLLDEATSA 538
Cdd:PRK11144 90 HYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 539 LDVESERIVQEALNRMMVERTT--LVVAHRLSTV-RNVDCITVVRKGKIVEQGP 589
Cdd:PRK11144 159 LDLPRKRELLPYLERLAREINIpiLYVSHSLDEIlRLADRVVVLEQGKVKAFGP 212
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
378-598 |
5.69e-19 |
|
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: 87.60 E-value: 5.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 378 RYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDwIRGKIGL--VSQEP 455
Cdd:cd03218 9 RYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH-KRARLGIgyLPQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 456 LLFMA-SIKDNIIygkkdATLEEIK--RAAELANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLL 532
Cdd:cd03218 85 SIFRKlTVEENIL-----AVLEIRGlsKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 533 DEATSALD----VESERIVQEALNRMM--------VeRTTLVVAHRlstvrnvdcITVVRKGKIVEQGPHDALVKDPD 598
Cdd:cd03218 158 DEPFAGVDpiavQDIQKIIKILKDRGIgvlitdhnV-RETLSITDR---------AYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
387-582 |
6.46e-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: 88.37 E-value: 6.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 387 ILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEvlidgisIKKlrldwiRGKIGLVSQEPLLFMASIKDNI 466
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK-------IKH------SGRISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 467 IYG--KKDATLEEIKRAAELANAanfIDKLPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESE 544
Cdd:cd03291 119 IFGvsYDEYRYKSVVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190
....*....|....*....|....*....|....*....
gi 1443040382 545 R-IVQEALNRMMVERTTLVVAHRLSTVRNVDCITVVRKG 582
Cdd:cd03291 196 KeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
370-605 |
6.49e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 88.28 E-value: 6.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRypaRPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKL---RLDWIRG 446
Cdd:PRK11831 8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsrsRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 KIGLVSQEPLLFM-ASIKDNIIYgkkdaTLEEIKRAAELANAANFIDKLpngydTLVGQRG------TQLSGGQKQRIAI 519
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAY-----PLREHTQLPAPLLHSTVMMKL-----EAVGLRGaaklmpSELSGGMARRAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 520 ARAILKDPKILLLDEATsaldVESERIVQEALNRMMVER------TTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDA 592
Cdd:PRK11831 155 ARAIALEPDLIMFDEPF----VGQDPITMGVLVKLISELnsalgvTCVVVSHDVPEVLSIaDHAYIVADKKIVAHGSAQA 230
|
250
....*....|...
gi 1443040382 593 LVKDPDGAYSQLI 605
Cdd:PRK11831 231 LQANPDPRVRQFL 243
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1052-1268 |
6.72e-19 |
|
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: 86.50 E-value: 6.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1052 NNVSFKYPSRpdvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRdqMGLVG 1131
Cdd:cd03268 4 NDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR--IGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1132 QEPVLF-NDTIRANIT-----YGKHSEVTEEEITAVAKAANAHEFVSSLpqgydtvvgekgvqlSGGQKQRVAIARAILK 1205
Cdd:cd03268 79 EAPGFYpNLTARENLRllarlLGIRKKRIDEVLDVVGLKDSAKKKVKGF---------------SLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1206 DPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTI-KGADMIAVLKEGKIAEKG 1268
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1053-1266 |
7.04e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 88.21 E-value: 7.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1053 NVSFKYPS------RPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRD- 1125
Cdd:PRK10419 8 GLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 ----QMglVGQEPV-LFN--DTIRA----------NITYGKHSEVTEEEITAVAKAAnahEFVSSLPQgydtvvgekgvQ 1188
Cdd:PRK10419 88 rrdiQM--VFQDSIsAVNprKTVREiireplrhllSLDKAERLARASEMLRAVDLDD---SVLDKRPP-----------Q 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1189 LSGGQKQRVAIARAILKDPKILLLDEATSALDaeseRVVQ----DALDRVMVNRTT--IVVAHRLSTI-KGADMIAVLKE 1261
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLD----LVLQagviRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDN 227
|
....*
gi 1443040382 1262 GKIAE 1266
Cdd:PRK10419 228 GQIVE 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1053-1275 |
7.30e-19 |
|
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: 91.67 E-value: 7.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1053 NVSFKYPSRpDVQIFSDFTLHIPSQKTIALVGESGSGKS----TIIALLERFYDPDSGNISLDGVEIRSLKVSWLR---- 1124
Cdd:COG4172 13 SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1125 DQMGLVGQEPV-----LFndTIRANI--TYGKHSEVTEEEITAVAKAA-------NAHEFVSSLPQgydtvvgekgvQLS 1190
Cdd:COG4172 92 NRIAMIFQEPMtslnpLH--TIGKQIaeVLRLHRGLSGAAARARALELlervgipDPERRLDAYPH-----------QLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1191 GGQKQRVAIARAILKDPKILLLDEATSALDAeserVVQ----DALDRvMVNRTTI----------VVAHRlstikgADMI 1256
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaqilDLLKD-LQRELGMalllithdlgVVRRF------ADRV 227
|
250
....*....|....*....
gi 1443040382 1257 AVLKEGKIAEKGKHEALLR 1275
Cdd:COG4172 228 AVMRQGEIVEQGPTAELFA 246
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
383-588 |
1.15e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 88.75 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 383 PEQL-ILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISI---------------KKL-RLDWIR 445
Cdd:PRK13631 36 ENELvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnhelitnpysKKIkNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 446 GKIGLVSQEP--LLFMASIKDNIIYGKKDATLEEIkRAAELAnaANFIDKLPNGYDTLvgQRGT-QLSGGQKQRIAIARA 522
Cdd:PRK13631 116 RRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKS-EAKKLA--KFYLNKMGLDDSYL--ERSPfGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 523 ILKDPKILLLDEATSALDVESER-IVQEALNRMMVERTTLVVAHRLSTVRNV-DCITVVRKGKIVEQG 588
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEVaDEVIVMDKGKILKTG 258
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
388-565 |
1.27e-18 |
|
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: 86.37 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIrgkigLVSQE-PLLFMASIKDNI 466
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNySLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 467 iYGKKDATLEEIKRAAELANAANFIDklpngydtLVG------QRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALD 540
Cdd:TIGR01184 76 -ALAVDRVLPDLSKSERRAIVEEHIA--------LVGlteaadKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180
....*....|....*....|....*..
gi 1443040382 541 VESERIVQEALNRMMVER--TTLVVAH 565
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEEHrvTVLMVTH 173
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
370-566 |
1.60e-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: 84.13 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPArpEQLILDGLSLQVASGTTMAIVGESGSGKSTVIslveRfydpqsgevLIDGIsikklrLDWIRGKIG 449
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLF----R---------ALAGL------WPWGSGRIG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 L--------VSQEPLLFMASIKDNIIYGKKDAtleeikraaelanaanfidklpngydtlvgqrgtqLSGGQKQRIAIAR 521
Cdd:cd03223 60 MpegedllfLPQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFAR 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1443040382 522 AILKDPKILLLDEATSALDVESERIVQEALNRMMverTTLV-VAHR 566
Cdd:cd03223 105 LLLHKPKFVFLDEATSALDEESEDRLYQLLKELG---ITVIsVGHR 147
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1051-1268 |
1.65e-18 |
|
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: 85.79 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1051 FNNVSFKYPS-RPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPD---SGNISLDGVEIRSLKVswlRDQ 1126
Cdd:cd03234 6 WWDVGLKAKNwNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQF---QKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1127 MGLVGQEPVLF-NDTIRANITYGKHSEVTEEEITAVAKAANAhefVSSLPQGYDTVVGEKGVQ-LSGGQKQRVAIARAIL 1204
Cdd:cd03234 83 VAYVRQDDILLpGLTVRETLTYTAILRLPRKSSDAIRKKRVE---DVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 1205 KDPKILLLDEATSALDAEServvqdALDRVMV-------NRTTIVVAH--RLSTIKGADMIAVLKEGKIAEKG 1268
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFT------ALNLVSTlsqlarrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1052-1234 |
1.74e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.68 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1052 NNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVeirslKVSWLRDQMGLVG 1131
Cdd:PRK11248 5 SHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1132 Q-EPVLFNDTIRANITYGKhsevteeEITAVAKAANAHEFVSSLPQgydtvVGEKGV------QLSGGQKQRVAIARAIL 1204
Cdd:PRK11248 77 QnEGLLPWRNVQDNVAFGL-------QLAGVEKMQRLEIAHQMLKK-----VGLEGAekryiwQLSGGQRQRVGIARALA 144
|
170 180 190
....*....|....*....|....*....|
gi 1443040382 1205 KDPKILLLDEATSALDAESERVVQDALDRV 1234
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKL 174
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1063-1274 |
1.80e-18 |
|
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: 85.56 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1063 DVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKvSWLRDQMGL--VGQEPVLFndt 1140
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP-PHERARAGIgyVPEGRRIF--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1141 irANITygkhsevTEEEITAVAKAANAHEFVSSLPQGYDT--VVGE----KGVQLSGGQKQRVAIARAILKDPKILLLDE 1214
Cdd:cd03224 88 --PELT-------VEENLLLGAYARRRAKRKARLERVYELfpRLKErrkqLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1215 ATSALdaeSERVVQDALDRVM-VNR---TTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEALL 1274
Cdd:cd03224 159 PSEGL---APKIVEEIFEAIReLRDegvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
370-591 |
2.23e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.55 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYParpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKlRLDWIRGKIG 449
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQ----EPLLfmaSIKDNII-----YGKKDATLEEikRAAELANAAnfidKLPNGYDTLVGQrgtqLSGGQKQRIAIA 520
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLvfgryFGLSAAAARA--LVPPLLEFA----KLENKADAKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 521 RAILKDPKILLLDEATSALDVESERIVQEALNRMMVE-RTTLVVAHRLSTV-RNVDCITVVRKG-KIVEQGPHD 591
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAeRLCDRLCVIEEGrKIAEGAPHA 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1055-1268 |
2.34e-18 |
|
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: 85.11 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1055 SFKYPSRPdVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRdQMGLVGQEP 1134
Cdd:cd03266 10 RFRDVKKT-VQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR-RLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1135 VLFND-TIRANITY--GKHSEVTEEEITAVAKAANAHEFVSSLpqgyDTVVGEkgvqLSGGQKQRVAIARAILKDPKILL 1211
Cdd:cd03266 88 GLYDRlTARENLEYfaGLYGLKGDELTARLEELADRLGMEELL----DRRVGG----FSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1212 LDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTIKG-ADMIAVLKEGKIAEKG 1268
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
370-589 |
2.38e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.29 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIG 449
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMA-SIKDNIIYG----------KKDAtlEEIKRA------AELANAanFIDklpngydtlvgqrgtQLSGG 512
Cdd:COG4604 79 ILRQENHINSRlTVRELVAFGrfpyskgrltAEDR--EIIDEAiayldlEDLADR--YLD---------------ELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 513 QKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVE--RTTLVVAHRLstvrNV-----DCITVVRKGKIV 585
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElgKTVVIVLHDI----NFascyaDHIVAMKDGRVV 215
|
....
gi 1443040382 586 EQGP 589
Cdd:COG4604 216 AQGT 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
374-588 |
2.43e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.60 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 374 DVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDG--ISIKKLRLDWIRGKIGLV 451
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 452 SQEP--LLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDklpngydtlvGQRGTQ-----LSGGQKQRIAIARAIL 524
Cdd:PRK13638 83 FQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD----------AQHFRHqpiqcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 525 KDPKILLLDEATSALDvESERIVQEALNRMMVERTTLVV--AHRLSTVRNV-DCITVVRKGKIVEQG 588
Cdd:PRK13638 153 LQARYLLLDEPTAGLD-PAGRTQMIAIIRRIVAQGNHVIisSHDIDLIYEIsDAVYVLRQGQILTHG 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1066-1274 |
2.45e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 86.69 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1066 IFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDP-----DSGNISLDGVEIRSLK-VSWLRDQMGLVGQEPVLFND 1139
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRdVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1140 TIRANITYG--KHSEVTEEEITAVAKAANAHefvSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATS 1217
Cdd:PRK14271 116 SIMDNVLAGvrAHKLVPRKEFRGVAQARLTE---VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1218 ALDAESERVVQDALDRVMVNRTTIVVAHRLS-TIKGADMIAVLKEGKIAEKGKHEALL 1274
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
370-593 |
3.06e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.06 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPAR-PEQL-ILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSG------------------EV 429
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTELkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 430 LIDGISIKKLR------LDWIRGKIGLVSQ--EPLLFMASIKDNIIYG-------KKDATleeiKRAAElanaanfidkl 494
Cdd:PRK13651 83 VLEKLVIQKTRfkkikkIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvsmgvsKEEAK----KRAAK----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 495 pngYDTLVG------QRGT-QLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVE-RTTLVVAHR 566
Cdd:PRK13651 148 ---YIELVGldesylQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHD 224
|
250 260 270
....*....|....*....|....*....|
gi 1443040382 567 LSTV--RNVDCItVVRKGKIVEQG-PHDAL 593
Cdd:PRK13651 225 LDNVleWTKRTI-FFKDGKIIKDGdTYDIL 253
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1042-1273 |
3.07e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 86.36 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1042 MENVTGSIDFNNVSFkypSRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVS 1121
Cdd:PRK11831 1 EQSVANLVDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1122 WL---RDQMGLVGQEPVLFND-TIRANITYG--KHSEVTEEEI-TAVAKAANAhefvsslpqgydtvVGEKGV------Q 1188
Cdd:PRK11831 78 RLytvRKRMSMLFQSGALFTDmNVFDNVAYPlrEHTQLPAPLLhSTVMMKLEA--------------VGLRGAaklmpsE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1189 LSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLSTIKG-ADMIAVLKEGKIA 1265
Cdd:PRK11831 144 LSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVLSiADHAYIVADKKIV 223
|
....*...
gi 1443040382 1266 EKGKHEAL 1273
Cdd:PRK11831 224 AHGSAQAL 231
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
388-565 |
3.23e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.93 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR---LDWIRGKIGLVSQEPLLFM-ASIK 463
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHHLLMdRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 464 DN-----IIYGkkdATLEEIKRAAELA-NAANFIDKLPNgydtlvgqRGTQLSGGQKQRIAIARAILKDPKILLLDEATS 537
Cdd:PRK10908 98 DNvaiplIIAG---ASGDDIRRRVSAAlDKVGLLDKAKN--------FPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190
....*....|....*....|....*....|.
gi 1443040382 538 ALDVE-SERIVQ--EALNRMMVerTTLVVAH 565
Cdd:PRK10908 167 NLDDAlSEGILRlfEEFNRVGV--TVLMATH 195
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1067-1242 |
3.25e-18 |
|
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: 85.18 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1067 FSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNI------------SLDGVEIRSLKvswlRDQMGLVGQ-- 1132
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggwvdlaQASPREILALR----RRTIGYVSQfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1133 -------------EPVLfndtiranitygkhsEVTEEEITAVAKAA------NAHEFVSSLPQGydTvvgekgvqLSGGQ 1193
Cdd:COG4778 103 rviprvsaldvvaEPLL---------------ERGVDREEARARARellarlNLPERLWDLPPA--T--------FSGGE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1443040382 1194 KQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIV 1242
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1069-1269 |
3.31e-18 |
|
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: 85.21 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1069 DFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIR-------------SLkVSWLRdqmglVGQEPV 1135
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepgpdrmvvfqnySL-LPWLT-----VRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1136 LFNDTIRANITYGKHSEVTEEEITAVAKAANAHEfvsslpqgydtvvgeKGVQLSGGQKQRVAIARAILKDPKILLLDEA 1215
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADK---------------RPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1216 TSALDAESERVVQDALDRVMVNR--TTIVVAHRL-STIKGADMIAVLKEGKIAEKGK 1269
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQ 198
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1268 |
3.95e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.21 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1052 NNVSFKYPSRPDVQI--FSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEI-------------- 1115
Cdd:PRK13631 25 KNLYCVFDEKQENELvaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnhelitnpy 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1116 -RSLK-VSWLRDQMGLVGQEP--VLFNDTIRANITYGKHS-EVTEEEITAVAKaanahEFVSSLPQGYDtVVGEKGVQLS 1190
Cdd:PRK13631 105 sKKIKnFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVAlGVKKSEAKKLAK-----FYLNKMGLDDS-YLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1191 GGQKQRVAIARAILKDPKILLLDEATSALDAESER-VVQDALDRVMVNRTTIVVAHRLSTI-KGADMIAVLKEGKIAEKG 1268
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTG 258
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1052-1268 |
4.39e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.45 E-value: 4.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1052 NNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVG 1131
Cdd:PRK11231 6 ENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1132 QEPVLFND-TIRANITYGKH------SEVTEEEITAVAKAANAHEFvsslpqgyDTVVGEKGVQLSGGQKQRVAIARAIL 1204
Cdd:PRK11231 83 QHHLTPEGiTVRELVAYGRSpwlslwGRLSAEDNARVNQAMEQTRI--------NHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1205 KDPKILLLDEATSALDAeSERVVQDALDRVMVN--RTTIVVAHRLS-TIKGADMIAVLKEGKIAEKG 1268
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDI-NHQVELMRLMRELNTqgKTVVTVLHDLNqASRYCDHLVVLANGHVMAQG 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1049-1268 |
4.85e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.91 E-value: 4.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPDVQ---IFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSW-LR 1124
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1125 DQMGLVGQEPvlfNDTIRANI-----TYGKHS-EVTEEEITA----VAKAANAHEFVSSLPQgydtvvgekgvQLSGGQK 1194
Cdd:PRK13633 85 NKAGMVFQNP---DNQIVATIveedvAFGPENlGIPPEEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1195 QRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRvmVNR----TTIVVAHRLSTIKGADMIAVLKEGKIAEKG 1268
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKE--LNKkygiTIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1049-1263 |
6.44e-18 |
|
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: 81.73 E-value: 6.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDgveiRSLKVSWLRdqmg 1128
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----STVKIGYFE---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 lvgqepvlfndtiranitygkhsevteeeitavakaanahefvsslpqgydtvvgekgvQLSGGQKQRVAIARAILKDPK 1208
Cdd:cd03221 70 -----------------------------------------------------------QLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1209 ILLLDEATSALDAESERVVQDALDRvmVNRTTIVVAH-R--LSTIkgADMIAVLKEGK 1263
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
387-593 |
6.48e-18 |
|
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: 84.11 E-value: 6.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 387 ILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDW-IRGKIGLVSQE----PLLfmaS 461
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHErARAGIAYVPQGreifPRL---T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 462 IKDNIIYGkkdatleeikrAAELANAANFIDklPNGYD------TLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEA 535
Cdd:TIGR03410 92 VEENLLTG-----------LAALPRRSRKIP--DEIYElfpvlkEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 536 TsaldvesERI-------VQEALNRMMVER--TTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDAL 593
Cdd:TIGR03410 159 T-------EGIqpsiikdIGRVIRRLRAEGgmAILLVEQYLDFARELaDRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1049-1268 |
7.02e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.51 E-value: 7.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWL--RDQ 1126
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1127 MGLVGQEP--VLFNDTIRANITYG------KHSEVtEEEITAVAKAANAHEFVSSLPQgydtvvgekgvQLSGGQKQRVA 1198
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGplnlglSKEEV-EKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1199 IARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTI-KGADMIAVLKEGKIAEKG 1268
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEG 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1065-1271 |
7.20e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.89 E-value: 7.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1065 QIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPD-----SGNISLDGVEIRSLKVSWL--RDQMGLVGQEPVLF 1137
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1138 -NDTIRANITYG--------KHSEVTEEEITAVAKAANAHEFVSSLpqgydtvvGEKGVQLSGGQKQRVAIARAILKDPK 1208
Cdd:PRK14267 98 pHLTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWDEVKDRL--------NDYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1209 ILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHR-LSTIKGADMIAVLKEGKIAEKGKHE 1271
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTR 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
370-593 |
7.89e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.82 E-value: 7.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKklrlDWIRGKI- 448
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA----DWSPAELa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 449 ---GLVSQEPLL-F---------MASIKDNIIYGKKDATLEEIKRAAELAnaanfidklpngydTLVGQRGTQLSGGQKQ 515
Cdd:PRK13548 76 rrrAVLPQHSSLsFpftveevvaMGRAPHGLSRAEDDALVAAALAQVDLA--------------HLAGRDYPQLSGGEQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 516 RIAIARAIL------KDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLS-TVRNVDCITVVRKGKIVE 586
Cdd:PRK13548 142 RVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNlAARYADRIVLLHQGRLVA 221
|
....*...
gi 1443040382 587 QG-PHDAL 593
Cdd:PRK13548 222 DGtPAEVL 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
381-588 |
8.67e-18 |
|
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: 83.86 E-value: 8.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 381 ARPEQLILDGLSLQVASGTTMAIVGESGSGKST---VISLVERFYDPQSGEVLIDGisiKKLRLDWIRGKIGLVSQ---- 453
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQddil 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 454 -------EPLLFMASIK-DNIIYGKKDATLEEIKRAAELANAanfidklpngydTLVGQRGTQLSGGQKQRIAIARAILK 525
Cdd:cd03234 93 lpgltvrETLTYTAILRlPRKSSDAIRKKRVEDVLLRDLALT------------RIGGNLVKGISGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 526 DPKILLLDEATSALDVESERIVQEALNRMMVE-RTTLVVAH--RLSTVRNVDCITVVRKGKIVEQG 588
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLARRnRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
370-540 |
8.83e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 86.44 E-value: 8.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPEqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR-LDwiRGkI 448
Cdd:PRK11650 4 LKLQAVRKSYDGKTQ--VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEpAD--RD-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 449 GLVSQEPLLF--MaSIKDNIIYGKKDATL--EEIKR----AAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIA 520
Cdd:PRK11650 79 AMVFQNYALYphM-SVRENMAYGLKIRGMpkAEIEErvaeAARILELEPLLDRKPR-----------ELSGGQRQRVAMG 146
|
170 180
....*....|....*....|
gi 1443040382 521 RAILKDPKILLLDEATSALD 540
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLD 166
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1065-1266 |
1.11e-17 |
|
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: 84.47 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1065 QIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSW---LRDQMGLVGQE-PVLFN-- 1138
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDsPSAVNpr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1139 DTIRA-------NITYGKHSEvTEEEITAVAKAANAH-EFVSSLPQgydtvvgekgvQLSGGQKQRVAIARAILKDPKIL 1210
Cdd:TIGR02769 105 MTVRQiigeplrHLTSLDESE-QKARIAELLDMVGLRsEDADKLPR-----------QLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1211 LLDEATSALDAESERVVQDALDRVMVNRTT--IVVAHRLSTI-KGADMIAVLKEGKIAE 1266
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1065-1274 |
1.14e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 84.25 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1065 QIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIR-------SLKVS------WLRDQMGLVG 1131
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVAdknqlrLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1132 QEpvlFNdtIRANITYGKHSEVTEEEITAVAKAANAHEFVSSLPQ-GYD-TVVGEKGVQLSGGQKQRVAIARAILKDPKI 1209
Cdd:PRK10619 99 QH---FN--LWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKvGIDeRAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 1210 LLLDEATSALDAEserVVQDALdRVMVN-----RTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEALL 1274
Cdd:PRK10619 174 LLFDEPTSALDPE---LVGEVL-RIMQQlaeegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
95-300 |
1.37e-17 |
|
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: 84.79 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 95 FIYLGIGTSVASFLQVSCWTMAGERQSARIR-SLYlKAVLRQDITFFDTeMTTGEAVSRMSSDTLLIQGALGEKGGKLVE 173
Cdd:cd18542 45 ILGVALLRGVFRYLQGYLAEKASQKVAYDLRnDLY-DHLQRLSFSFHDK-ARTGDLMSRCTSDVDTIRRFLAFGLVELVR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 174 LLSSFIGGFIIAFTRGWLLTLVMLTSLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIA 253
Cdd:cd18542 123 AVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1443040382 254 MYRNFIKKSYKATIEEGIITGFGMGSVMCVVFGSYGLAFWYGGKLII 300
Cdd:cd18542 203 KFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVI 249
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1046-1271 |
1.50e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.86 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1046 TGSIDFNNVSFKYPsrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSlKVSWLRD 1125
Cdd:PRK13537 5 VAPIDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 QMGLVGQEPVLFND-TIRANI-TYGKHSEVTEEEITAvaKAANAHEFvSSLPQGYDTVVGEkgvqLSGGQKQRVAIARAI 1203
Cdd:PRK13537 81 RVGVVPQFDNLDPDfTVRENLlVFGRYFGLSAAAARA--LVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 1204 LKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVV-------AHRLstikgADMIAVLKEG-KIAEKGKHE 1271
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGrKIAEGAPHA 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
370-596 |
1.81e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.41 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKL------RLDw 443
Cdd:PRK15439 12 LCARSISKQYSGVE---VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtpakahQLG- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 444 irgkIGLVSQEPLLFMA-SIKDNIIYGKKDATLEEIKRAAELANAANFIDklpngydtLVGQRGTqLSGGQKQRIAIARA 522
Cdd:PRK15439 88 ----IYLVPQEPLLFPNlSVKENILFGLPKRQASMQKMKQLLAALGCQLD--------LDSSAGS-LEVADRQIVEILRG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 523 ILKDPKILLLDEATSALD-VESERIVQEaLNRMMVERTTLV-VAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKD 596
Cdd:PRK15439 155 LMRDSRILILDEPTASLTpAETERLFSR-IRELLAQGVGIVfISHKLPEIRQLaDRISVMRDGTIALSGKTADLSTD 230
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
370-603 |
1.99e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.60 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARP--------EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKL-- 439
Cdd:PRK10261 314 LQVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLsp 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 440 -RLDWIRGKIGLVSQEPllfMASIKDNIIYGkkDATLEEI------------KRAAELANAANFIDKLPNGYDTlvgqrg 506
Cdd:PRK10261 394 gKLQALRRDIQFIFQDP---YASLDPRQTVG--DSIMEPLrvhgllpgkaaaARVAWLLERVGLLPEHAWRYPH------ 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 507 tQLSGGQKQRIAIARAILKDPKILLLDEATSALDVEserIVQEALNRMM-VER----TTLVVAHRLSTVRNVDC-ITVVR 580
Cdd:PRK10261 463 -EFSGGQRQRICIARALALNPKVIIADEAVSALDVS---IRGQIINLLLdLQRdfgiAYLFISHDMAVVERISHrVAVMY 538
|
250 260
....*....|....*....|...
gi 1443040382 581 KGKIVEQGPHDALVKDPDGAYSQ 603
Cdd:PRK10261 539 LGQIVEIGPRRAVFENPQHPYTR 561
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1049-1268 |
2.01e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.40 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKY-PSRP-DVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSL----KVSW 1122
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1123 LRDQMGLVGQEP--VLFNDTIRANITYGKHS-EVTEEEITAVAkaANAHEFVsslpqGYDTVVGEKG-VQLSGGQKQRVA 1198
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNfGIPKEKAEKIA--AEKLEMV-----GLADEFWEKSpFELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1199 IARAILKDPKILLLDEATSALDAESERVVQDALDRV-MVNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKG 1268
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1058-1259 |
2.20e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.51 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1058 YPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGveirSLKVSWLRDQMGLVGQEPVlf 1137
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1138 ndTIRANITYGKHSE-------------VTEEEITAVAKAANAHEFVSSLpqgydtvvgekgvqlSGGQKQRVAIARAIL 1204
Cdd:NF040873 73 --TVRDLVAMGRWARrglwrrltrddraAVDDALERVGLADLAGRQLGEL---------------SGGQRQRALLAQGLA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 1205 KDPKILLLDEATSALDAESERVVQDALDR-VMVNRTTIVVAHRLSTIKGADMIAVL 1259
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEeHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
387-589 |
2.23e-17 |
|
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: 81.80 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 387 ILDGLSLQVASGTTMAIVGESGSGKST---VISLVERfYDPQSGEVLIDGISIKKLRLDWI-RGKIGLVSQEPllfmasi 462
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTlakTIMGHPK-YEVTEGEILFKGEDITDLPPEERaRLGIFLAFQYP------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 463 kdniiygkkdATLEEIKraaelanAANFIDKLPNGydtlvgqrgtqLSGGQKQRIAIARAILKDPKILLLDEATSALDVE 542
Cdd:cd03217 87 ----------PEIPGVK-------NADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1443040382 543 SERIVQEALNRMMVE-RTTLVVAH--RLSTVRNVDCITVVRKGKIVEQGP 589
Cdd:cd03217 139 ALRLVAEVINKLREEgKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD 188
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
372-597 |
2.74e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.30 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 372 LKDVYFRYPARpeqLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLV 451
Cdd:PRK10575 14 LRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 452 SQE-PLLFMASIKDNIIYGK----------KDATLEEIKRAAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIA 520
Cdd:PRK10575 91 PQQlPAAEGMTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 521 RAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLS-TVRNVDCITVVRKGKIVEQGPHDALVKDP 597
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
377-588 |
3.00e-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: 82.20 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 377 FRYPARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGisikklRLDWIrgkIGL-VSQEP 455
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSL---LGLgGGFNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 456 llfMASIKDNI-----IYGKK----DATLEEIKRAAELanaANFIDKLPNGYdtlvgqrgtqlSGGQKQRIAIARAILKD 526
Cdd:cd03220 98 ---ELTGRENIylngrLLGLSrkeiDEKIDEIIEFSEL---GDFIDLPVKTY-----------SSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 527 PKILLLDEATSALDVESERIVQEALNRMMVERTTLV-VAHRLSTVRNV-DCITVVRKGKIVEQG 588
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVIlVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1070-1274 |
3.59e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 82.96 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1070 FTLHipSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPvlfNDTIRANITYGK 1149
Cdd:COG4167 34 FTLE--AGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDP---NTSLNPRLNIGQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1150 --------HSEVTEEE----ITAVAKaanaheFVSSLPQGYDTVVGEkgvqLSGGQKQRVAIARAILKDPKILLLDEATS 1217
Cdd:COG4167 109 ileeplrlNTDLTAEEreerIFATLR------LVGLLPEHANFYPHM----LSSGQKQRVALARALILQPKIIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1218 ALDAeSERvVQdaldrvMVNR----------TTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEALL 1274
Cdd:COG4167 179 ALDM-SVR-SQ------IINLmlelqeklgiSYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVF 238
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1069-1268 |
3.62e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.11 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1069 DFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFND-TIRANITY 1147
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQELVAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1148 GKH------SEVTEEEITAVAKAANAHEFVSSLPQGYDTvvgekgvqLSGGQKQRVAIARAILKDPKILLLDEATSALDA 1221
Cdd:PRK10253 105 GRYphqplfTRWRKEDEEAVTKAMQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1222 ESERVVQDALDRvmVNR----TTIVVAHRLS-TIKGADMIAVLKEGKIAEKG 1268
Cdd:PRK10253 177 SHQIDLLELLSE--LNRekgyTLAAVLHDLNqACRYASHLIALREGKIVAQG 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1080-1273 |
4.55e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 83.60 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1080 IALVGESGSGKSTIIALLERFYDPDSGNIS------------------LDGVEI-----RSLK-VSWLRDQMGLVGQ--E 1133
Cdd:PRK13651 36 IAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekekvLEKLVIqktrfKKIKkIKEIRRRVGVVFQfaE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1134 PVLFNDTIRANITYGKHS-EVTEEEitAVAKAANAHEFVSsLPQGYdtvVGEKGVQLSGGQKQRVAIARAILKDPKILLL 1212
Cdd:PRK13651 116 YQLFEQTIEKDIIFGPVSmGVSKEE--AKKRAAKYIELVG-LDESY---LQRSPFELSGGQKRRVALAGILAMEPDFLVF 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1213 DEATSALDAESERVVQDALDRVMVN-RTTIVVAHRL-STIKGADMIAVLKEGKIAEKGK-HEAL 1273
Cdd:PRK13651 190 DEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGDtYDIL 253
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1049-1274 |
6.39e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.34 E-value: 6.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSL-KVSWLRDQM 1127
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1128 GLVGQEP--VLFNDTIRANITYGKHS------EVTEEEITAVAKAAnAHEFVSSLPQgydtvvgekgvQLSGGQKQRVAI 1199
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENlclppiEIRKRVDRALAEIG-LEKYRHRSPK-----------TLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 1200 ARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIV-VAHRLSTIKGADMIAVLKEGKIAEKGKHEALL 1274
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1063-1281 |
6.58e-17 |
|
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: 80.65 E-value: 6.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1063 DVQIFSDFTLHIPSQKTIALVGESGSGKST---IIALLERfYDPDSGNISLDGVEIRSLKVSwLRDQMG--LVGQEPVlf 1137
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTlakTIMGHPK-YEVTEGEILFKGEDITDLPPE-ERARLGifLAFQYPP-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1138 ndtiranitygkhsevteeEITAVAKAanahEFVSSLPQGydtvvgekgvqLSGGQKQRVAIARAILKDPKILLLDEATS 1217
Cdd:cd03217 88 -------------------EIPGVKNA----DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1218 ALDAESERVVQDALDRVM-VNRTTIVVAHR---LSTIKgADMIAVLKEGKIAEKGKHEALLRIKDGAY 1281
Cdd:cd03217 134 GLDIDALRLVAEVINKLReEGKSVLIITHYqrlLDYIK-PDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1070-1273 |
7.16e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 83.48 E-value: 7.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1070 FTLHipSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRS---LKVSWLRDQMGLVGQEPvlfndtiranit 1146
Cdd:PRK11308 36 FTLE--RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNP------------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1147 YG------KHSEVTEE------EITAVAKAANAHEF---VSSLPQGYDTVVGekgvQLSGGQKQRVAIARAILKDPKILL 1211
Cdd:PRK11308 102 YGslnprkKVGQILEEpllintSLSAAERREKALAMmakVGLRPEHYDRYPH----MFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1212 LDEATSALDAESERVVqdaLDRVM-----VNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEAL 1273
Cdd:PRK11308 178 ADEPVSALDVSVQAQV---LNLMMdlqqeLGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
366-609 |
7.55e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.67 E-value: 7.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 366 MNGDIELKDVYFRYP-------------------ARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQS 426
Cdd:COG1134 1 MSSMIEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 427 GEVlidgisikklrldWIRGKIGlvsqePLL-----FMASI--KDNI-----IYGKK----DATLEEIKRAAELanaANF 490
Cdd:COG1134 81 GRV-------------EVNGRVS-----ALLelgagFHPELtgRENIylngrLLGLSrkeiDEKFDEIVEFAEL---GDF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 491 IDkLPngydtlVGqrgtQLSGGQKQRIAIARAILKDPKILLLDEATSALDvesERIVQEALNRM--MVE--RTTLVVAHR 566
Cdd:COG1134 140 ID-QP------VK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGD---AAFQKKCLARIreLREsgRTVIFVSHS 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1443040382 567 LSTVRNV-DCITVVRKGKIVEQGPHDALVKdpdgAYSQLIRLQE 609
Cdd:COG1134 206 MGAVRRLcDRAIWLEKGRLVMDGDPEEVIA----AYEALLAGRE 245
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
729-998 |
7.88e-17 |
|
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: 82.47 E-value: 7.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 729 DQLRKDSRFWALMSVVLGVACLISI--PAEYF---LFGIAGGKLIQRVRTLSFQRIMHQEVAWFDK-PSnsrcatlmyfc 802
Cdd:cd18552 27 DDIFVEKDLEALLLVPLAIIGLFLLrgLASYLqtyLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRnSS----------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 803 yfifykkiftfkpmlrGHLISysgalgtRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLV 882
Cdd:cd18552 96 ----------------GDLIS-------RITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 883 GAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLM 962
Cdd:cd18552 153 ALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELL 232
|
250 260 270
....*....|....*....|....*....|....*.
gi 1443040382 963 LYLTYGLCFYVGAKFVSQGKTTFSDVFKVFFALVLA 998
Cdd:cd18552 233 GAIAIALVLWYGGYQVISGELTPGEFISFITALLLL 268
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
382-594 |
9.00e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.96 E-value: 9.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 382 RPEQLIL--------DGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQ 453
Cdd:PRK10253 9 RGEQLTLgygkytvaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 454 EpllfmASIKDNIiygkkdaTLEEI----------------KRAAELANAAnfidKLPNGYDTLVGQRGTQLSGGQKQRI 517
Cdd:PRK10253 89 N-----ATTPGDI-------TVQELvargryphqplftrwrKEDEEAVTKA----MQATGITHLADQSVDTLSGGQRQRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 518 AIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLS-TVRNVDCITVVRKGKIVEQGPHDALV 594
Cdd:PRK10253 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
384-588 |
1.11e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 81.23 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 384 EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERF--YDPQSGEVLIDGISIKKLRLDwIRGKIGL----------- 450
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 451 -VSQEPLLFMASIKDNIIYGKKDAT----LEEIKRAAELAN-AANFIDKLPN-GYdtlvgqrgtqlSGGQKQRIAIARAI 523
Cdd:CHL00131 98 gVSNADFLRLAYNSKRKFQGLPELDplefLEIINEKLKLVGmDPSFLSRNVNeGF-----------SGGEKKRNEILQMA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 524 LKDPKILLLDEATSALDVESERIVQEALNRMM-VERTTLVVAH--RLSTVRNVDCITVVRKGKIVEQG 588
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTG 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
370-565 |
1.12e-16 |
|
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: 78.26 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGisikklrldwiRGKIG 449
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQepllfmasikdniiygkkdatleeikraaelanaanfidklpngydtlvgqrgtqLSGGQKQRIAIARAILKDPKI 529
Cdd:cd03221 67 YFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*...
gi 1443040382 530 LLLDEATSALDVESerivQEALNRMMVE--RTTLVVAH 565
Cdd:cd03221 92 LLLDEPTNHLDLES----IEALEEALKEypGTVILVSH 125
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
98-313 |
1.16e-16 |
|
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: 82.13 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 98 LGIGTSVASFL--QVSCWTMAgeRQSARIRSLYLKAVLRQDITFFDTEmTTGEAVSRMSSDTLLIQGALGEKGGKLVELL 175
Cdd:cd18589 45 LTIASAVSEFVcdLIYNITMS--RIHSRLQGLVFAAVLRQEIAFFDSN-QTGDIVSRVTTDTEDMSESLSENLSLLMWYL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 176 SSFIGGFIIAFTRGWLLTLVMLTSLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMY 255
Cdd:cd18589 122 ARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRY 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 256 RNFIKKSYKATIEEGII-------TGF-GMGSVMCVVFgsyglafwYGGKLIIEKGYTGGKIMTIL 313
Cdd:cd18589 202 RQRLQKTYRLNKKEAAAyavsmwtSSFsGLALKVGILY--------YGGQLVTAGTVSSGDLVTFV 259
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1049-1264 |
2.04e-16 |
|
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: 77.96 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGveirslkvswlRDQMG 1128
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLFNDTIRANITYgkhsevteeeitavakaanahefvsslPqgYDTVvgekgvqLSGGQKQRVAIARAILKDPK 1208
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY---------------------------P--WDDV-------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1209 ILLLDEATSALDAESERVVQDALDRVMVnrTTIVVAHRLSTIKGADMIAVL-KEGKI 1264
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHRPSLWKFHDRVLDLdGEGGW 166
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
381-551 |
2.38e-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: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 381 ARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRG----------KIGL 450
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENilylghlpglKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 451 VSQEPLLFMASIkdniiYGKKDATLEEIKRAAELANAAnfidklpngyDTLVGQrgtqLSGGQKQRIAIARAILKDPKIL 530
Cdd:TIGR01189 89 SALENLHFWAAI-----HGGAQRTIEDALAAVGLTGFE----------DLPAAQ----LSAGQQRRLALARLWLSRRPLW 149
|
170 180
....*....|....*....|.
gi 1443040382 531 LLDEATSALDVESERIVQEAL 551
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLL 170
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1049-1266 |
2.53e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.58 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLdGVeirSLKVSWLrDQMg 1128
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE---TVKIGYF-DQH- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 lvgQEPVLFNDTIRANITYGKhSEVTEEEITAVAKA-----ANAHEFVSSlpqgydtvvgekgvqLSGGQKQRVAIARAI 1203
Cdd:COG0488 387 ---QEELDPDKTVLDELRDGA-PGGTEQEVRGYLGRflfsgDDAFKPVGV---------------LSGGEKARLALAKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1204 LKDPKILLLDEATSALDAESERVVQDALDR----VmvnrttIVVAH-R--LSTIkgADMIAVLKEGKIAE 1266
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALDDfpgtV------LLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1046-1264 |
3.28e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.01 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1046 TGSIDFNNVSFKYPS-RPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWL- 1123
Cdd:PRK10535 2 TALLELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1124 ---RDQMGLVGQEpvlfndtiranitYGKHSEVTEE---EITAV-------AKAANAHEFVSSLpqGYDTVVGEKGVQLS 1190
Cdd:PRK10535 82 qlrREHFGFIFQR-------------YHLLSHLTAAqnvEVPAVyaglerkQRLLRAQELLQRL--GLEDRVEYQPSQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1191 GGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVN-RTTIVVAHRLSTIKGADMIAVLKEGKI 1264
Cdd:PRK10535 147 GGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1069-1269 |
3.52e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.18 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1069 DFTLHipSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSwLRDQMG--LVGQEPVLF-NDTIRANI 1145
Cdd:PRK15439 31 DFTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGiyLVPQEPLLFpNLSVKENI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1146 TYG--KHsEVTEEEITAVAKAANAHEFVSSlpqgydtvvgeKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALD-AE 1222
Cdd:PRK15439 108 LFGlpKR-QASMQKMKQLLAALGCQLDLDS-----------SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1443040382 1223 SERVVQDaLDRVMVNRTTIV-VAHRLSTIKG-ADMIAVLKEGKIAEKGK 1269
Cdd:PRK15439 176 TERLFSR-IRELLAQGVGIVfISHKLPEIRQlADRISVMRDGTIALSGK 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1064-1278 |
3.78e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.74 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1064 VQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVsWLRDQM-GLVGQEPVL---FND 1139
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAKYiGRVFQDPMMgtaPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1140 TIRANI--------TYGKHSEVTEEEItavakaANAHEFVSSLPQGY----DTVVGekgvQLSGGQKQRVAIARAILKDP 1207
Cdd:COG1101 98 TIEENLalayrrgkRRGLRRGLTKKRR------ELFRELLATLGLGLenrlDTKVG----LLSGGQRQALSLLMATLTKP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1208 KILLLDEATSALDAESERVVQDALDRVmVNR---TTIVVAHRLS-TIKGADMIAVLKEGKIAE--KGKHEALLRIKD 1278
Cdd:COG1101 168 KLLLLDEHTAALDPKTAALVLELTEKI-VEEnnlTTLMVTHNMEqALDYGNRLIMMHEGRIILdvSGEEKKKLTVED 243
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
381-551 |
3.82e-16 |
|
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: 78.30 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 381 ARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLFMA 460
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 461 SIKDNIIYGKKDATLEEIKRAAELANAANFIDkLPNGydtlvgqrgtQLSGGQKQRIAIARAILKDPKILLLDEATSALD 540
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGLNGFED-RPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170
....*....|.
gi 1443040382 541 VESERIVQEAL 551
Cdd:cd03231 158 KAGVARFAEAM 168
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
388-596 |
4.11e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.05 E-value: 4.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYdPQ---SGEVLIDGisiKKLRLDWIRGK----IGLVSQEPLLFMA 460
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEG---EELQASNIRDTeragIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 461 -SIKDNIIYGkkdatlEEIKR------AAELANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLD 533
Cdd:PRK13549 97 lSVLENIFLG------NEITPggimdyDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 534 EATSALdVESE-----RIVQEALNRMMverTTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKD 596
Cdd:PRK13549 169 EPTASL-TESEtavllDIIRDLKAHGI---ACIYISHKLNEVKAIsDTICVIRDGRHIGTRPAAGMTED 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1049-1268 |
5.21e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.85 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYpsRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMG 1128
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEP--VLFNDTIRANITYGK-----HSEVTEEEITAVAKAANAHEFVSSLPQgydtvvgekgvQLSGGQKQRVAIAR 1201
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPinlglDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1202 AILKDPKILLLDEATSALDAESERVVQDALDRVMVN--RTTIVVAHRLSTI-KGADMIAVLKEGKIAEKG 1268
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYG 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1042-1269 |
5.51e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 81.23 E-value: 5.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1042 MENVTgsidFNNVSFKYPsrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTI---IALLErfyDPDSGNISLDgvEIRSL 1118
Cdd:PRK11000 1 MASVT----LRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLlrmIAGLE---DITSGDLFIG--EKRMN 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1119 KVSWLRDQMGLVGQEPVLF-NDTIRANITYG-KHSEVTEEEITA-VAKAAN----AHefvsslpqgydtVVGEKGVQLSG 1191
Cdd:PRK11000 69 DVPPAERGVGMVFQSYALYpHLSVAENMSFGlKLAGAKKEEINQrVNQVAEvlqlAH------------LLDRKPKALSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1192 GQKQRVAIARAILKDPKILLLDEATSALDAeSERV---VQDALDRVMVNRTTIVVAH-RLSTIKGADMIAVLKEGKIAEK 1267
Cdd:PRK11000 137 GQRQRVAIGRTLVAEPSVFLLDEPLSNLDA-ALRVqmrIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQV 215
|
..
gi 1443040382 1268 GK 1269
Cdd:PRK11000 216 GK 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1072-1292 |
5.97e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.29 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1072 LHIPSQKTIALVGESGSGKSTIIALLERFYDPDS---------GN-ISLDGVEIRSLKVSwlRDQMGLVGQEPVLFND-T 1140
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRtVQREGRLARDIRKS--RANTGYIFQQFNLVNRlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1141 IRANITYG-----------------KHSEVTEEEITAVAKAANAHEFVSSLpqgydtvvgekgvqlSGGQKQRVAIARAI 1203
Cdd:PRK09984 103 VLENVLIGalgstpfwrtcfswftrEQKQRALQALTRVGMVHFAHQRVSTL---------------SGGQQQRVAIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1204 LKDPKILLLDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRLS-TIKGADMIAVLKEGKIAEKGKHEALLRIK-DG 1279
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfDH 247
|
250
....*....|...
gi 1443040382 1280 AYASLVQLRSNSE 1292
Cdd:PRK09984 248 LYRSINRVEENAK 260
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1049-1250 |
7.32e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.99 E-value: 7.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLK---VSWLRD 1125
Cdd:PRK10908 2 IRFEHVSKAYLG--GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 QMGLVGQEPVLFND-TIRAN-----ITYGKHSEVTEEEITAVAKAANAHEFVSSLPqgydtvvgekgVQLSGGQKQRVAI 1199
Cdd:PRK10908 80 QIGMIFQDHHLLMDrTVYDNvaiplIIAGASGDDIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1200 ARAILKDPKILLLDEATSALD-AESERVVQ--DALDRVMVnrTTIVVAHRLSTI 1250
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDdALSEGILRlfEEFNRVGV--TVLMATHDIGLI 200
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1049-1264 |
8.75e-16 |
|
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: 77.71 E-value: 8.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPsrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKvswlRDQMG 1128
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLFND-TIRANITY-GKHSEVTEEEItavakAANAHEFVSSLP-QGYDTVVGEkgvQLSGGQKQRVAIARAILK 1205
Cdd:cd03269 74 YLPEERGLYPKmKVIDQLVYlAQLKGLKKEEA-----RRRIDEWLERLElSEYANKRVE---ELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 1206 DPKILLLDEATSALDAESERVVQDALDRVMVNRTTIV-VAHRLSTI-KGADMIAVLKEGKI 1264
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVIlSTHQMELVeELCDRVLLLNKGRA 206
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
387-565 |
9.26e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.90 E-value: 9.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 387 ILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDW---IRGK-IGLVSQEpllFMASI 462
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKhVGFVFQS---FMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 463 KDNiiygkkdaTLEEIKRAAEL---------ANAANFIDKLPngydtlVGQR----GTQLSGGQKQRIAIARAILKDPKI 529
Cdd:PRK10584 102 TLN--------ALENVELPALLrgessrqsrNGAKALLEQLG------LGKRldhlPAQLSGGEQQRVALARAFNGRPDV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1443040382 530 LLLDEATSALDVES-ERIVQE--ALNRMMVerTTLV-VAH 565
Cdd:PRK10584 168 LFADEPTGNLDRQTgDKIADLlfSLNREHG--TTLIlVTH 205
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
388-586 |
9.29e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 81.76 E-value: 9.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKST---VISLVERF--YDpqsGEVLIDG--ISIKKLRLDWIRGkIGLVSQE----PL 456
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTlmkVLSGVYPHgsYE---GEILFDGevCRFKDIRDSEALG-IVIIHQElaliPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 457 LfmaSIKDNIIYGKKDATL------EEIKRAAELANAANfIDKLPngyDTLVGQRGTqlsgGQKQRIAIARAILKDPKIL 530
Cdd:NF040905 93 L---SIAENIFLGNERAKRgvidwnETNRRARELLAKVG-LDESP---DTLVTDIGV----GKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 531 LLDEATSAL-DVESERIvqeaLNRMMVER----TTLVVAHRLSTVRNV-DCITVVRKGKIVE 586
Cdd:NF040905 162 ILDEPTAALnEEDSAAL----LDLLLELKaqgiTSIIISHKLNEIRRVaDSITVLRDGRTIE 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
370-628 |
1.05e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.39 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRY-PARP--EQLILDgLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISI----KKLRLD 442
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfaSRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 443 WIRGKIGLVSQEP--LLFMASIKDNIIYGKKDATL---EEIKRAAE----LANAANFIDKLPngydtlvgqrgTQLSGGQ 513
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIpkeKAEKIAAEklemVGLADEFWEKSP-----------FELSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 514 KQRIAIARAILKDPKILLLDEATSALDVESeRIVQEALNRMMVE--RTTLVVAHRLSTVRN-VDCITVVRKGKIVEQGPH 590
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKA-RIEMMQLFESIHQsgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1443040382 591 DALVKDPDGAYSQLI----------RLQETHRDERHKLPDSRSKSTSL 628
Cdd:PRK13643 229 SDVFQEVDFLKAHELgvpkathfadQLQKTGAVTFEKLPITRAELVTL 276
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
388-595 |
1.28e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIK-KLRLDWIRGKIGLVSQE----PLLfmaSI 462
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQElhlvPEM---TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 463 KDNIIYGKKDATLEEIKRAAELANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDV- 541
Cdd:PRK11288 97 AENLYLGQLPHKGGIVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAr 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 542 ESERivqeaLNRMMVE-----RTTLVVAHRLSTV-RNVDCITVVRKGKIVE------QGPHDALVK 595
Cdd:PRK11288 175 EIEQ-----LFRVIRElraegRVILYVSHRMEEIfALCDAITVFKDGRYVAtfddmaQVDRDQLVQ 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
386-598 |
1.29e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.11 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 386 LILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKiGLVS--QEPLLF--MAS 461
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVRtfQHVRLFreMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 462 I-----------KDNIIYGK-KDATLEEIKRAAeLANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKI 529
Cdd:PRK11300 98 IenllvaqhqqlKTGLFSGLlKTPAFRRAESEA-LDRAATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 530 LLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKDPD 598
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGIsDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
371-585 |
1.53e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.22 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 371 ELKDVYFRYPARPEQLIL-----------DGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGisiKKL 439
Cdd:COG1129 240 ELEDLFPKRAAAPGEVVLeveglsvggvvRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 440 RL----DWIRGKIGLVS----QEPLLFMASIKDNIIYgkkdATLEE------IKRAAELANAANFIDKL---PNGYDTLV 502
Cdd:COG1129 317 RIrsprDAIRAGIAYVPedrkGEGLVLDLSIRENITL----ASLDRlsrgglLDRRRERALAEEYIKRLrikTPSPEQPV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 503 GQrgtqLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTLVV-----------AHRlstvr 571
Cdd:COG1129 393 GN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVisselpellglSDR----- 463
|
250
....*....|....
gi 1443040382 572 nvdcITVVRKGKIV 585
Cdd:COG1129 464 ----ILVMREGRIV 473
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1048-1221 |
1.53e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.89 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1048 SIDFNNVSFKYPSrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTI---IALLERFydpDSGNISLDGVEIRSLKVSwLR 1124
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLlrmVAGLERI---TSGEIWIGGRVVNELEPA-DR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1125 DqMGLVGQEPVLF-NDTIRANITYG-KHSEVTEEEITA-VAKAANAHEFVSSLPQgydtvvgeKGVQLSGGQKQRVAIAR 1201
Cdd:PRK11650 77 D-IAMVFQNYALYpHMSVRENMAYGlKIRGMPKAEIEErVAEAARILELEPLLDR--------KPRELSGGQRQRVAMGR 147
|
170 180
....*....|....*....|
gi 1443040382 1202 AILKDPKILLLDEATSALDA 1221
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDA 167
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
391-603 |
1.69e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.44 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 391 LSLQVASGTTMAIVGESGSGKS-TVISLVeRFYDPQSGEVLIDGISIKK-------------LRLDWIRG-KIGLVSQEP 455
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGLVQCDKMLLRRrsrqvielseqsaAQMRHVRGaDMAMIFQEP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 456 llfMASIKDNIIYGKKDAtlEEIK------RAAELANAANFID--KLPNGyDTLVGQRGTQLSGGQKQRIAIARAILKDP 527
Cdd:PRK10261 114 ---MTSLNPVFTVGEQIA--ESIRlhqgasREEAMVEAKRMLDqvRIPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 528 KILLLDEATSALDVESE-RIVQ--EALNRMMvERTTLVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKDPDGAYSQ 603
Cdd:PRK10261 188 AVLIADEPTTALDVTIQaQILQliKVLQKEM-SMGVIFITHDMGVVAEIaDRVLVMYQGEAVETGSVEQIFHAPQHPYTR 266
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
68-311 |
2.28e-15 |
|
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: 78.22 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 68 LFGNVINSFGANTSGSvlRSVTKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSARIRSLYLKAVLRQDITFFDtEMTTG 147
Cdd:cd18541 21 IIGRAIDALTAGTLTA--SQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQ-KNRTG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 148 EAVSRMSSDTLLIQGALGEkgGKLVELLSSFIGGFIIA--FTRGWLLTLVMLTSLPLIAIASAVSAQALTRVSSKRQTSY 225
Cdd:cd18541 98 DLMARATNDLNAVRMALGP--GILYLVDALFLGVLVLVmmFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 226 SDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFgMGSVMCVVFG-SYGLAFWYGGKLIIEKGY 304
Cdd:cd18541 176 SDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDAL-FFPLIGLLIGlSFLIVLWYGGRLVIRGTI 254
|
....*..
gi 1443040382 305 TGGKIMT 311
Cdd:cd18541 255 TLGDLVA 261
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
388-589 |
2.33e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.19 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYdPQSGEVLIDGISIKKLRLDWIRGKIGLVSQ--EPLLFMA----- 460
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQqqSPPFAMPvfqyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 461 --SIKDNIIYGKKDATLEEIKRAAELAnaanfiDKLPngydtlvgqRG-TQLSGGQKQRIAIARAILK-------DPKIL 530
Cdd:COG4138 91 alHQPAGASSEAVEQLLAQLAEALGLE------DKLS---------RPlTQLSGGEWQRVRLAAVLLQvwptinpEGQLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 531 LLDEATSALDVeserIVQEALNRMMVE-----RTTLVVAHRLS-TVRNVDCITVVRKGKIVEQGP 589
Cdd:COG4138 156 LLDEPMNSLDV----AQQAALDRLLRElcqqgITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
388-588 |
2.49e-15 |
|
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: 76.99 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRgKIGLV----SQ--------EP 455
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgqkTQlwwdlpviDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 456 LLFMASIKDnIIYGKKDATLEEIkraAELANAANFIDklpngydtlvgQRGTQLSGGQKQRIAIARAILKDPKILLLDEA 535
Cdd:cd03267 116 FYLLAAIYD-LPPARFKKRLDEL---SELLDLEELLD-----------TPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 536 TSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRNV-DCITVVRKGKIVEQG 588
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1052-1268 |
2.89e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 77.08 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1052 NNVSFKYPSRpdvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVG 1131
Cdd:COG4559 5 ENLSVRLGGR---TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1132 QEPVL-FNDTIRANIT-----YGKHSEVTEEEITAVAKAANAHEFVSSLPQgydtvvgekgvQLSGGQKQRVAIARAIL- 1204
Cdd:COG4559 82 QHSSLaFPFTVEEVVAlgrapHGSSAAQDRQIVREALALVGLAHLAGRSYQ-----------TLSGGEQQRVQLARVLAq 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1205 ------KDPKILLLDEATSALD-AESERVVQdaLDRVMVNRTTIVVA--HRLS-TIKGADMIAVLKEGKIAEKG 1268
Cdd:COG4559 151 lwepvdGGPRWLFLDEPTSALDlAHQHAVLR--LARQLARRGGGVVAvlHDLNlAAQYADRILLLHQGRLVAQG 222
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
369-588 |
2.95e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.92 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 369 DIELKDVYFRYParpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGIsikklRLDWI---- 444
Cdd:PRK11000 3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-----RMNDVppae 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 445 RGkIGLVSQEPLLF-MASIKDNIIYGKKDATLE--EIKR----AAELANAANFIDKLPNGydtlvgqrgtqLSGGQKQRI 517
Cdd:PRK11000 75 RG-VGMVFQSYALYpHLSVAENMSFGLKLAGAKkeEINQrvnqVAEVLQLAHLLDRKPKA-----------LSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 518 AIARAILKDPKILLLDEATSALD--------VESERIvQEALNRMM-------VERTTLvvahrlstvrnVDCITVVRKG 582
Cdd:PRK11000 143 AIGRTLVAEPSVFLLDEPLSNLDaalrvqmrIEISRL-HKRLGRTMiyvthdqVEAMTL-----------ADKIVVLDAG 210
|
....*.
gi 1443040382 583 KIVEQG 588
Cdd:PRK11000 211 RVAQVG 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1081-1263 |
3.07e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1081 ALVGESGSGKSTIIALLERFYDPDSGNISLDG--VEIRSLKVSwLRDQMGLVGQEPVLFND-TIRANITYGkhsevTEEE 1157
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDA-IALGIGMVHQHFMLVPNlTVAENIVLG-----LEPT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1158 ITAVAKAANAHEFVSSLPQGY------DTVVGekgvQLSGGQKQRVAIARAILKDPKILLLDEATSAL-DAESERVVqDA 1230
Cdd:COG3845 109 KGGRLDRKAARARIRELSERYgldvdpDAKVE----DLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELF-EI 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1443040382 1231 LdRVMVNR-TTIV-VAHRLSTIKG-ADMIAVLKEGK 1263
Cdd:COG3845 184 L-RRLAAEgKSIIfITHKLREVMAiADRVTVLRRGK 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
388-584 |
3.12e-15 |
|
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: 75.16 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR-LDWIRGKIGLVSQEPL---LFM-ASI 462
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPEDRKregLVLdLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 463 KDNIIygkkdatleeikraaelanaanfidkLPNgydtlvgqrgtQLSGGQKQRIAIARAILKDPKILLLDEATSALDVE 542
Cdd:cd03215 96 AENIA--------------------------LSS-----------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1443040382 543 SERIVQEALNRMMVERTTLVVahrLST-----VRNVDCITVVRKGKI 584
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
825-999 |
3.41e-15 |
|
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: 77.52 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 825 SGALGTRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAqgYAQV--KFLKGFSEESKE 902
Cdd:cd18576 92 VGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVL--VAVLfgRRIRKLSKKVQD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 903 MYEDANQVAADAVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGK 982
Cdd:cd18576 170 ELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGE 249
|
170
....*....|....*...
gi 1443040382 983 TTFSDVFK-VFFALVLAA 999
Cdd:cd18576 250 LTAGDLVAfLLYTLFIAG 267
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
370-586 |
3.72e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVlidgisikklrldwIRG--- 446
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------------KLGetv 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 KIGLVSQEPLLFmasikdniiygKKDAT-LEEIKRAAelanaanfidklPNGYDTLVGQ-------RGTQ-------LSG 511
Cdd:COG0488 379 KIGYFDQHQEEL-----------DPDKTvLDELRDGA------------PGGTEQEVRGylgrflfSGDDafkpvgvLSG 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 512 GQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMmvERTTLVVAH-R--LSTVrnVDCITVVRKGKIVE 586
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PGTVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
846-1214 |
4.16e-15 |
|
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: 79.84 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 846 NLALIVQAVATLITGFA-IAFAAdWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEmYEDANQvaadavGSIRTVASF 924
Cdd:COG4615 124 RLPELLQSVALVLGCLAyLAWLS-PPLFLLTLVLLGLGVAGYRLLVRRARRHLRRARE-AEDRLF------KHFRALLEG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 925 CSE-----KRVVAIYNK----KCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVgakFVSQGKTTFSDVFKVFFAL 995
Cdd:COG4615 196 FKElklnrRRRRAFFDEdlqpTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFL---LPALGWADPAVLSGFVLVL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 996 VLAAVGVSQ-SSALSTnATKARDSAISIFSIidrKSRIDSSSDEGAIMENVT-----GSIDFNNVSFKYPSRPDVQIFS- 1068
Cdd:COG4615 273 LFLRGPLSQlVGALPT-LSRANVALRKIEEL---ELALAAAEPAAADAAAPPapadfQTLELRGVTYRYPGEDGDEGFTl 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1069 ---DFTlhIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFNDTirani 1145
Cdd:COG4615 349 gpiDLT--IRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL----- 421
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1146 tYGKHSEVTEEEitavakaanAHEFVSSLpqGYDTVVGEKG-----VQLSGGQKQRVAIARAILKDPKILLLDE 1214
Cdd:COG4615 422 -LGLDGEADPAR---------ARELLERL--ELDHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
370-598 |
5.15e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.22 E-value: 5.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKST----VISLVErfydPQSGEVLIDGISIKKLRLdWIR 445
Cdd:COG1137 4 LEAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDITHLPM-HKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 446 GK--IGLVSQEPLLF--MaSIKDNIIygkkdATLE--EIKRAAELANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAI 519
Cdd:COG1137 76 ARlgIGYLPQEASIFrkL-TVEDNIL-----AVLElrKLSKKEREERLEELLEEF--GITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 520 ARAILKDPKILLLDEATSALD---VES-ERIVQEALNRMM--------VeRTTLVVahrlstvrnVDCITVVRKGKIVEQ 587
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDpiaVADiQKIIRHLKERGIgvlitdhnV-RETLGI---------CDRAYIISEGKVLAE 217
|
250
....*....|.
gi 1443040382 588 GPHDALVKDPD 598
Cdd:COG1137 218 GTPEEILNNPL 228
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
45-253 |
7.38e-15 |
|
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: 76.75 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 45 VLLMVVGTVGALGNGISQPLMTvlfGNVINsfGANTSGSvLRSVTKVVLNFIYLGIGTSVASFLqvscWTMAGERQS--- 121
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLT---RRAID--GPIAHGD-RSALWPLVLLLLALGVAEAVLSFL----RRYLAGRLSlgv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 122 -ARIRSLYLKAVLRQDITFFDtEMTTGEAVSRMSSDTLLIQGALGeKGGKLVELLSSFIGGFIIAFTRGWLLTLVMLTSL 200
Cdd:cd18543 71 eHDLRTDLFAHLQRLDGAFHD-RWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 201 PLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIA 253
Cdd:cd18543 149 PPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELD 201
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1063-1286 |
8.63e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.49 E-value: 8.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1063 DVQIFSDFTLHIPSQKTIALVGESGSGKST---IIALLERfYDPDSGNISLDGVEIRSLKVswlrDQ-----MGLVGQEP 1134
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLMGHPK-YEVTSGSILLDGEDILELSP----DEraragIFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1135 -----VLFNDTIRANITygkhsEVTEEEITAVAKAANAHEFVSSLpqGYDTVVGEKGVQ--LSGGQKQRVAIARAILKDP 1207
Cdd:COG0396 87 veipgVSVSNFLRTALN-----ARRGEELSAREFLKLLKEKMKEL--GLDEDFLDRYVNegFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1208 KILLLDEATSALDAESERVVQDALDRVMV-NRTTIVVAH--R-LSTIKgADMIAVLKEGKIAEKGKHEALLRIKDGAYAS 1283
Cdd:COG0396 160 KLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRiLDYIK-PDFVHVLVDGRIVKSGGKELALELEEEGYDW 238
|
...
gi 1443040382 1284 LVQ 1286
Cdd:COG0396 239 LKE 241
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
388-565 |
8.89e-15 |
|
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: 75.52 E-value: 8.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGT-----TMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIkklrldwirgkiglvsqepllfmaSI 462
Cdd:cd03237 10 LGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------------------SY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 463 KDNIIYGKKDATLEEI--KRAAELANAANFIDKL--PNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSA 538
Cdd:cd03237 66 KPQYIKADYEGTVRDLlsSITKDFYTHPYFKTEIakPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
170 180
....*....|....*....|....*....
gi 1443040382 539 LDVESERIVQEALNR--MMVERTTLVVAH 565
Cdd:cd03237 146 LDVEQRLMASKVIRRfaENNEKTAFVVEH 174
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1061-1229 |
1.06e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1061 RPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVswlRDQMGLVGQ----EPVL 1136
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACHYLGHrnamKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1137 fndTIRANIT-----YGKHSEVTEEEITAVAKAANAHefvssLPQGYdtvvgekgvqLSGGQKQRVAIARAILKDPKILL 1211
Cdd:PRK13539 89 ---TVAENLEfwaafLGGEELDIAAALEAVGLAPLAH-----LPFGY----------LSAGQKRRVALARLLVSNRPIWI 150
|
170
....*....|....*...
gi 1443040382 1212 LDEATSALDAESERVVQD 1229
Cdd:PRK13539 151 LDEPTAALDAAAVALFAE 168
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1065-1274 |
1.07e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.59 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1065 QIFSDFTLHIPSQKTIALVGESGSGKS-TIIALLERFYDPD----SGNISLDGVEIRSLKVSWLR----DQMGLVGQEP- 1134
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1135 VLFN--DTIRANItygkhSEVTEEEITAVAKAANAhEFVSSLPQgydtvVGEKGV---------QLSGGQKQRVAIARAI 1203
Cdd:PRK15134 103 VSLNplHTLEKQL-----YEVLSLHRGMRREAARG-EILNCLDR-----VGIRQAakrltdyphQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1204 LKDPKILLLDEATSALDAESERVVQDALD--RVMVNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEALL 1274
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLF 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1070-1288 |
1.20e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.59 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1070 FTLHipSQKTIALVGESGSGKSTI-IALLERFydPDSGNISLDGVEIRSL---KVSWLRDQMGLVGQEPvlfNDTI--RA 1143
Cdd:PRK15134 307 FTLR--PGETLGLVGESGSGKSTTgLALLRLI--NSQGEIWFDGQPLHNLnrrQLLPVRHRIQVVFQDP---NSSLnpRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1144 NITygkhsEVTEEEITAVAKAANAHEfvssLPQGYDTVVGEKGV----------QLSGGQKQRVAIARAILKDPKILLLD 1213
Cdd:PRK15134 380 NVL-----QIIEEGLRVHQPTLSAAQ----REQQVIAVMEEVGLdpetrhrypaEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1214 EATSALDaeseRVVQD---ALDRVMVNR---TTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEALLRIKDGAYA-SLV 1285
Cdd:PRK15134 451 EPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAPQQEYTrQLL 526
|
...
gi 1443040382 1286 QLR 1288
Cdd:PRK15134 527 ALS 529
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
388-606 |
1.21e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 76.70 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKS----TVISLVERFYDPQSGEVLIDGISIKKL----RLDWIRGKIGLVSQEPllfM 459
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRIsekeRRNLVGAEVAMIFQDP---M 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 460 ASIkdNIIYGKKDATLEEIK------------RAAELAN------AANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIAR 521
Cdd:PRK11022 100 TSL--NPCYTVGFQIMEAIKvhqggnkktrrqRAIDLLNqvgipdPASRLDVYPH-----------QLSGGMSQRVMIAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 522 AILKDPKILLLDEATSALDVESE-RIVQEALNRMMVERTTLV-VAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKDPD 598
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDVTIQaQIIELLLELQQKENMALVlITHDLALVAEAaHKIIVMYAGQVVETGKAHDIFRAPR 246
|
....*....
gi 1443040382 599 GAYSQ-LIR 606
Cdd:PRK11022 247 HPYTQaLLR 255
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
382-543 |
1.76e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.68 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 382 RPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR------LDWIrG-----KIGL 450
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRdeyhqdLLYL-GhqpgiKTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 451 VSQEPLLFMASIKDniiygkkDATLEEIKRAAELANAANFIDkLPNGydtlvgqrgtQLSGGQKQRIAIARAILKDPKIL 530
Cdd:PRK13538 90 TALENLRFYQRLHG-------PGDDEALWEALAQVGLAGFED-VPVR----------QLSAGQQRRVALARLWLTRAPLW 151
|
170
....*....|...
gi 1443040382 531 LLDEATSALDVES 543
Cdd:PRK13538 152 ILDEPFTAIDKQG 164
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1053-1274 |
1.93e-14 |
|
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: 74.12 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1053 NVSFKYPSRpdvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSwLRDQMGL--V 1130
Cdd:cd03218 5 NLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH-KRARLGIgyL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1131 GQEPVLFND-TIRANI-----TYGKHSEVTEEEITAVAkaanaHEFvsslpqGYDTVVGEKGVQLSGGQKQRVAIARAIL 1204
Cdd:cd03218 81 PQEASIFRKlTVEENIlavleIRGLSKKEREEKLEELL-----EEF------HITHLRKSKASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1205 KDPKILLLDEATSALD----AESERVVQDALDR---VMVN----RTTIVVAHRlstikgadmIAVLKEGKIAEKGKHEAL 1273
Cdd:cd03218 150 TNPKFLLLDEPFAGVDpiavQDIQKIIKILKDRgigVLITdhnvRETLSITDR---------AYIIYEGKVLAEGTPEEI 220
|
.
gi 1443040382 1274 L 1274
Cdd:cd03218 221 A 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
387-596 |
2.12e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.16 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 387 ILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLID--GISIKKLRLDWIRGkIGLVSQEPLLFMA-SIK 463
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdeDISLLPLHARARRG-IGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 464 DN---IIYGKKDATLEEIK-RAAELANAANfIDKLPNGYdtlvgqrGTQLSGGQKQRIAIARAILKDPKILLLDEATSAL 539
Cdd:PRK10895 97 DNlmaVLQIRDDLSAEQREdRANELMEEFH-IEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 540 D----VESERIVQE----ALNRMMVE---RTTLVVAHRlstvrnvdcITVVRKGKIVEQGPHDALVKD 596
Cdd:PRK10895 169 DpisvIDIKRIIEHlrdsGLGVLITDhnvRETLAVCER---------AYIVSQGHLIAHGTPTEILQD 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1064-1273 |
2.73e-14 |
|
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: 73.56 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1064 VQIFSDF------TLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEI--RSLKVswlRDQMGLVGQEPV 1135
Cdd:cd03265 7 VKKYGDFeavrgvSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrEPREV---RRRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1136 LFND-TIRANIT-----YGKHSEVTEEEITAVAKAANAHEFVSSLPQGYdtvvgekgvqlSGGQKQRVAIARAILKDPKI 1209
Cdd:cd03265 84 VDDElTGWENLYiharlYGVPGAERRERIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1210 LLLDEATSALDAESE----RVVQDALDRvmVNRTTIVVAHRLSTI-KGADMIAVLKEGKIAEKGKHEAL 1273
Cdd:cd03265 153 LFLDEPTIGLDPQTRahvwEYIEKLKEE--FGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1046-1268 |
2.85e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.96 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1046 TGSIDFNNVSFKYP-------------------SRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSG 1106
Cdd:COG1134 2 SSMIEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1107 NISLDGveirslKVSWLRD-----QMGLVGQEPVLFNDTIranitYGkhseVTEEEITAVAKA----ANAHEFVsslpqg 1177
Cdd:COG1134 82 RVEVNG------RVSALLElgagfHPELTGRENIYLNGRL-----LG----LSRKEIDEKFDEivefAELGDFI------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1178 yDTVVGekgvQLSGGQKQRVAIARAILKDPKILLLDEATSALDAE----SERVVQDALDRvmvNRTTIVVAHRLSTIKG- 1252
Cdd:COG1134 141 -DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRl 212
|
250
....*....|....*.
gi 1443040382 1253 ADMIAVLKEGKIAEKG 1268
Cdd:COG1134 213 CDRAIWLEKGRLVMDG 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
388-609 |
3.09e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVI----SLVERFYDPQSGEVLIDGISIKKLRLDW----IRGKIGLVSQE-PLLF 458
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIELLGRTVQREGRLARdirkSRANTGYIFQQfNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 459 MASIKDNIIYGKKDAT------LEEIKRAAElANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLL 532
Cdd:PRK09984 100 RLSVLENVLIGALGSTpfwrtcFSWFTREQK-QRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 533 DEATSALDVESERIVQEALNRMMVER--TTLVVAHRLS-TVRNVDCITVVRKGKIVEQGPHDALVKDP-DGAYSQLIRLQ 608
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfDHLYRSINRVE 256
|
.
gi 1443040382 609 E 609
Cdd:PRK09984 257 E 257
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1064-1266 |
3.45e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 73.27 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1064 VQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSL---KVSWLRDQ-MGLVGQEPVLFnD 1139
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhVGFVFQSFMLI-P 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1140 TIRA--NITY-----GKHSEVTEEEITAVAKAANAHEFVSSLPqgydtvvgekgVQLSGGQKQRVAIARAILKDPKILLL 1212
Cdd:PRK10584 102 TLNAleNVELpallrGESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1213 DEATSALDAESERVVQDALdrVMVNR----TTIVVAHRLSTIKGADMIAVLKEGKIAE 1266
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLL--FSLNRehgtTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
45-311 |
3.62e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 74.85 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 45 VLLMVVGTVGALgngISQPLMTVLFGNVINSFGANTSGSVLrsvtkvvLNFIYLGIGTSVAS-FLQVS-CWTMA--GERQ 120
Cdd:cd18563 5 FLLMLLGTALGL---VPPYLTKILIDDVLIQLGPGGNTSLL-------LLLVLGLAGAYVLSaLLGILrGRLLArlGERI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 121 SARIRSLYLKAVLRQDITFFDtEMTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTRGWLLTLVMLTSL 200
Cdd:cd18563 75 TADLRRDLYEHLQRLSLSFFD-KRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 201 PLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIE-EGIITGFgmGS 279
Cdd:cd18563 154 PLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRaEKLWATF--FP 231
|
250 260 270
....*....|....*....|....*....|...
gi 1443040382 280 VMCVVFGSYGLAFWY-GGKLIIEKGYTGGKIMT 311
Cdd:cd18563 232 LLTFLTSLGTLIVWYfGGRQVLSGTMTLGTLVA 264
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
383-549 |
3.72e-14 |
|
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: 76.90 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 383 PEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLI-DGIsikklrldwirgKIGLVSQEPLL---- 457
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGI------------KVGYLPQEPQLdptk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 458 --------FMASIKD-----NIIYGK-------------KDATLEEIKRAAELANAANFID------KLPNGyDTLVgqr 505
Cdd:TIGR03719 84 tvrenveeGVAEIKDaldrfNEISAKyaepdadfdklaaEQAELQEIIDAADAWDLDSQLEiamdalRCPPW-DADV--- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1443040382 506 gTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVES----ERIVQE 549
Cdd:TIGR03719 160 -TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1051-1266 |
4.20e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1051 FNNVSFKYPSrpdVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVswlRDQMG-- 1128
Cdd:PRK11288 7 FDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST---TAALAag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 --LVGQEPVLFND-TIRANITYG----KHSEVTEEEITAVAKAANAHEFVSSLPqgyDTVVGEkgvqLSGGQKQRVAIAR 1201
Cdd:PRK11288 81 vaIIYQELHLVPEmTVAENLYLGqlphKGGIVNRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1202 AILKDPKILLLDEATSALDA-ESE---RVVQDALDRvmvNRTTIVVAHRLSTI-KGADMIAVLKEGKIAE 1266
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSArEIEqlfRVIRELRAE---GRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
389-603 |
5.13e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 74.76 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 389 DGLSLQVASGTTMAIVGESGSGKS-TVISLVERFYDPQ--SGEVLIDGISIKKL---RLDWIRG-KIGLVSQEPllfMAS 461
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFNGREILNLpekELNKLRAeQISMIFQDP---MTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 462 ------IKDNII--------YGKKDATLEEIKR--AAELANAANFIDKLPNgydtlvgqrgtQLSGGQKQRIAIARAILK 525
Cdd:PRK09473 110 lnpymrVGEQLMevlmlhkgMSKAEAFEESVRMldAVKMPEARKRMKMYPH-----------EFSGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 526 DPKILLLDEATSALDVESERIVQEALNRMMVERTT--LVVAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKDPDGAYS 602
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAGIcDKVLVMYAGRTMEYGNARDVFYQPSHPYS 258
|
.
gi 1443040382 603 Q 603
Cdd:PRK09473 259 I 259
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
33-534 |
5.71e-14 |
|
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: 76.38 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 33 LFSLFRYADRLDVLLMVVGTVGALGNGIsqpLMTVlfgnvINSfGANTSGSVLRSV--TKVVLNFIYLGigTSVASFLQV 110
Cdd:COG4615 4 LRLLLRESRWLLLLALLLGLLSGLANAG---LIAL-----INQ-ALNATGAALARLllLFAGLLVLLLL--SRLASQLLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 111 scwTMAGERQSARIRSLYLKAVLRQDITFFDtEMTTGEAVSRMSSDTLLIQGAlgekggklVELLSSFIGGFIIAFT--- 187
Cdd:COG4615 73 ---TRLGQHAVARLRLRLSRRILAAPLERLE-RIGAARLLAALTEDVRTISQA--------FVRLPELLQSVALVLGcla 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 188 -RGWLLTLVMLTSLPLIAIASAVSAQALTRVsskrQTSYSDAGDTVEQTIGSIRTVVS------FNGEKKaiamyRNFIK 260
Cdd:COG4615 141 yLAWLSPPLFLLTLVLLGLGVAGYRLLVRRA----RRHLRRAREAEDRLFKHFRALLEgfkelkLNRRRR-----RAFFD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 261 KSYKATIEE--------GIITGFGMGSVMCVVFGSYGLAFWYGGKL-IIEKGYTGGKIMTILFavLTGA-SSLGNATPAV 330
Cdd:COG4615 212 EDLQPTAERyrdlriraDTIFALANNWGNLLFFALIGLILFLLPALgWADPAVLSGFVLVLLF--LRGPlSQLVGALPTL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 331 AAVvegqSAAYNLFKTIERKPEIDSDDNNGMVLEDMNGD---IELKDVYFRYPAR--PEQLILDGLSLQVASGTTMAIVG 405
Cdd:COG4615 290 SRA----NVALRKIEELELALAAAEPAAADAAAPPAPADfqtLELRGVTYRYPGEdgDEGFTLGPIDLTIRRGELVFIVG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 406 ESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIGLVSQEPLLFmasikDNiIYGKKDATLEEikRAAELA 485
Cdd:COG4615 366 GNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF-----DR-LLGLDGEADPA--RARELL 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 486 NAANFIDKLpngydTLVGQR--GTQLSGGQKQRIAIARAILKDPKILLLDE 534
Cdd:COG4615 438 ERLELDHKV-----SVEDGRfsTTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1056-1269 |
6.60e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.50 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1056 FKYPsrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLK--VSWLRDQMGLVGQE 1133
Cdd:PRK13638 9 FRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrgLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1134 P--VLFNDTIRANITYG-KHSEVTEEEITAvaKAANAHEFVSSlpQGYDtvvgEKGVQ-LSGGQKQRVAIARAILKDPKI 1209
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSlRNLGVPEAEITR--RVDEALTLVDA--QHFR----HQPIQcLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1210 LLLDEATSALDAESERVVQDALDRVMVN-RTTIVVAHRLSTI-KGADMIAVLKEGKIAEKGK 1269
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQgNHVIISSHDIDLIyEISDAVYVLRQGQILTHGA 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1081-1264 |
6.99e-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: 76.98 E-value: 6.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1081 ALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSlKVSWLRDQMGLVGQEPVLFND-TIRANITY-----GKHSEVT 1154
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHILFyaqlkGRSWEEA 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1155 EEEITAVAKAANAHEFVSslpqgydtvvgEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRV 1234
Cdd:TIGR01257 1039 QLEMEAMLEDTGLHHKRN-----------EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY 1107
|
170 180 190
....*....|....*....|....*....|..
gi 1443040382 1235 MVNRTTIVVAHRL--STIKGaDMIAVLKEGKI 1264
Cdd:TIGR01257 1108 RSGRTIIMSTHHMdeADLLG-DRIAIISQGRL 1138
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
392-591 |
8.31e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 8.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 392 SLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKK-LRldwiRGKIGLVSQEPLL---FMASIKDNII 467
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQaLQ----KNLVAYVPQSEEVdwsFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 468 YGKKdATLEEIKRAAE-----LANAANFIDKLPNGYDTLvgqrgTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVE 542
Cdd:PRK15056 103 MGRY-GHMGWLRRAKKrdrqiVTAALARVDMVEFRHRQI-----GELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1443040382 543 SERIVQEALNRMMVE-RTTLVVAHRLSTVRNVDCITVVRKGKIVEQGPHD 591
Cdd:PRK15056 177 TEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
381-549 |
9.16e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 9.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 381 ARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGisiKKLRLDWIRG-----------KIG 449
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEachylghrnamKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFMASikdniIYGKKDATLEEIKRAAELANAANfidkLPNGYdtlvgqrgtqLSGGQKQRIAIARAILKDPKI 529
Cdd:PRK13539 88 LTVAENLEFWAA-----FLGGEELDIAAALEAVGLAPLAH----LPFGY----------LSAGQKRRVALARLLVSNRPI 148
|
170 180
....*....|....*....|
gi 1443040382 530 LLLDEATSALDVESERIVQE 549
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAE 168
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1049-1268 |
9.53e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 73.34 E-value: 9.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDG--VEIRSLKVSWLRDQ 1126
Cdd:PRK13636 6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1127 MGLVGQEP--VLFNDTIRANITYGK-HSEVTEEEITAVAKAANAHEFVSSLPQgydtvvgEKGVQLSGGQKQRVAIARAI 1203
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAvNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1204 LKDPKILLLDEATSALD----AESERVVQDALDRVMVnrTTIVVAHRLSTIK-GADMIAVLKEGKIAEKG 1268
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGL--TIIIATHDIDIVPlYCDNVFVMKEGRVILQG 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1071-1273 |
1.11e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.97 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1071 TLHIPSQKTIALVGESGSGKST----IIALLErfydPDSGNISLDGVEIRSL-KVSWL--RDQMGLVGQEPvLFNDTIRA 1143
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTfaraIIGLVK----ATDGEVAWLGKDLLGMkDDEWRavRSDIQMIFQDP-LASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1144 NI---------TYgkHSEVTEEEITAVAKAANAHefVSSLPQgydtVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDE 1214
Cdd:PRK15079 116 TIgeiiaeplrTY--HPKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 1215 ATSALDAESE-RVVQ--DALDRVMvNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEAL 1273
Cdd:PRK15079 188 PVSALDVSIQaQVVNllQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1049-1275 |
1.33e-13 |
|
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: 75.22 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPS--RPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNIS-------LDGVEIRSLK 1119
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1120 VSWLRDQMGLVGQEPVLF-NDTIRANITYGKHSEVTEEeiTAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVA 1198
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYpHRTVLDNLTEAIGLELPDE--LARMKAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1199 IARAILKDPKILLLDEATSALDAESERVVQDAL--DRVMVNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEALLR 1275
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
381-597 |
1.50e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.55 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 381 ARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVI-SLVERFYDPQ-------SGEVLIDG---ISIKKLRLDWIRGKIG 449
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGaprgarvTGDVTLNGeplAAIDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFmaSIKDNIIYGK----------KDATLEEIKRAAELANAanfidklpngyDTLVGQRGTQLSGGQKQRIAI 519
Cdd:PRK13547 90 QAAQPAFAF--SAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 520 ARAILK---------DPKILLLDEATSALDVESERIVQEALNRMMVERT--TLVVAHRLS-TVRNVDCITVVRKGKIVEQ 587
Cdd:PRK13547 157 ARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNlAARHADRIAMLADGAIVAH 236
|
250
....*....|.
gi 1443040382 588 G-PHDALVKDP 597
Cdd:PRK13547 237 GaPADVLTPAH 247
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
377-588 |
1.72e-13 |
|
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: 75.82 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 377 FRYPARPEqliLDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKlRLDWIRGKIGLVSQEPL 456
Cdd:TIGR01257 938 FEPSGRPA---VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 457 LFM-ASIKDNIIYGK--KDATLEEikraAELANAANFIDklpNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLD 533
Cdd:TIGR01257 1014 LFHhLTVAEHILFYAqlKGRSWEE----AQLEMEAMLED---TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 534 EATSALDVESERIVQEALNRMMVERTTLVVAHRLSTVRNV-DCITVVRKGKIVEQG 588
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSG 1142
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1066-1248 |
1.96e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.39 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1066 IFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSW---LRDQ-MGLVGQEPVLFND-T 1140
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1141 IRAN------ITYGKHSEVTE---EEITAVAKAANAHEFVSslpqgydtvvgekgvQLSGGQKQRVAIARAILKDPKILL 1211
Cdd:PRK11629 104 ALENvampllIGKKKPAEINSralEMLAAVGLEHRANHRPS---------------ELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1443040382 1212 LDEATSALDAESERVVQDALDRVMVNRTT--IVVAHRLS 1248
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQ 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1061-1269 |
2.10e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.70 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1061 RPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLErFYDPD----SGNISLDGVEIRSLKV----SWLRDQMGLVG- 1131
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKEMraisAYVQQDDLFIPt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1132 ---QEPVLFNDTIR--ANITYGKHSEVTEEEITAVakaanahefvsSLPQGYDTVVGEKGVQ--LSGGQKQRVAIARAIL 1204
Cdd:TIGR00955 114 ltvREHLMFQAHLRmpRRVTKKEKRERVDEVLQAL-----------GLRKCANTRIGVPGRVkgLSGGERKRLAFASELL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1205 KDPKILLLDEATSALDAES-ERVVQDALDRVMVNRTTIVVAHRLST--IKGADMIAVLKEGKIAEKGK 1269
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGS 250
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
370-558 |
2.31e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 74.28 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYdPQ--------------SGEVLIDgis 435
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQgysndltlfgrrrgSGETIWD--- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 436 IKKlrldwirgKIGLVSQEplLFM-----ASIKDNIIYGKKDATleEIKRA---AELANAANFIDKLpnGYDTLVGQRGT 507
Cdd:PRK10938 334 IKK--------HIGYVSSS--LHLdyrvsTSVRNVILSGFFDSI--GIYQAvsdRQQKLAQQWLDIL--GIDKRTADAPF 399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 508 Q-LSGGQkQRIA-IARAILKDPKILLLDEATSALDveserivqeALNRMMVER 558
Cdd:PRK10938 400 HsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD---------PLNRQLVRR 442
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1063-1275 |
2.64e-13 |
|
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: 70.78 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1063 DVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWL-RDQMGLVGQEPVLFND-T 1140
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1141 IRANItygkhsevteeEITAVAKAANAhEFVSSLPQGYDT--VVGE----KGVQLSGGQKQRVAIARAILKDPKILLLDE 1214
Cdd:COG0410 95 VEENL-----------LLGAYARRDRA-EVRADLERVYELfpRLKErrrqRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1215 ATSALdaeSERVVQDALDRVM-VNR--TTIVV----AHRLSTIkgADMIAVLKEGKIAEKGKHEALLR 1275
Cdd:COG0410 163 PSLGL---APLIVEEIFEIIRrLNRegVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1049-1238 |
2.91e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.98 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWlRDQMG 1128
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEP-VLFNDTIRANITYGKHSEVTEEEITAVAKAANAHEFVsSLPQGYdtvvgekgvqLSGGQKQRVAIARAILKDP 1207
Cdd:PRK13540 78 FVGHRSgINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKA 146
|
170 180 190
....*....|....*....|....*....|.
gi 1443040382 1208 KILLLDEATSALDaesERVVQDALDRVMVNR 1238
Cdd:PRK13540 147 KLWLLDEPLVALD---ELSLLTIITKIQEHR 174
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
697-984 |
4.51e-13 |
|
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: 71.31 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 697 LLGSIAASVHGVILPLY-GIIMPGVLKSFyeppdqlrKDSRFWALMSVVLGVACLISIpAEY---FLFGIAGGKLIQRVR 772
Cdd:cd18542 5 ILALLLATALNLLIPLLiRRIIDSVIGGG--------LRELLWLLALLILGVALLRGV-FRYlqgYLAEKASQKVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 773 TLSFQRIMHQEVAWFDKpsnsrcatlmyfcyfifykkiftfkpmlrghliSYSGALGTRLSVDALNVRRLVGDNLALIVQ 852
Cdd:cd18542 76 NDLYDHLQRLSFSFHDK---------------------------------ARTGDLMSRCTSDVDTIRRFLAFGLVELVR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 853 AVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSIRTVASFCSEKRVVA 932
Cdd:cd18542 123 AVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIE 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 933 IYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGKTT 984
Cdd:cd18542 203 KFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEIT 254
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1060-1223 |
5.08e-13 |
|
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: 69.31 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1060 SRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRdQMGLVGQEPVLFND 1139
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE-NILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1140 -TIRANITY-----GKHSEVTEEEITAVAKAANAHefvssLPQGydtvvgekgvQLSGGQKQRVAIARAILKDPKILLLD 1213
Cdd:TIGR01189 88 lSALENLHFwaaihGGAQRTIEDALAAVGLTGFED-----LPAA----------QLSAGQQRRLALARLWLSRRPLWILD 152
|
170
....*....|
gi 1443040382 1214 EATSALDAES 1223
Cdd:TIGR01189 153 EPTTALDKAG 162
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
89-312 |
6.69e-13 |
|
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: 70.94 E-value: 6.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 89 TKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSARIRSLYLKAVLRQDITFFDTeMTTGEAVSRMSsDTLLIQGALGEKG 168
Cdd:cd18570 42 NIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFET-RKTGEIISRFN-DANKIREAISSTT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 169 GKL-VELLSSFIGGFIIAFTrGWLLTLVMLTSLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNG 247
Cdd:cd18570 120 ISLfLDLLMVIISGIILFFY-NWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNA 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 248 EKKAIAM----YRNFIKKSYKA---TIEEGIITGFGMGSVMCVVfgsyglaFWYGGKLIIEKGYTGGKIMTI 312
Cdd:cd18570 199 EEQFLKKiekkFSKLLKKSFKLgklSNLQSSIKGLISLIGSLLI-------LWIGSYLVIKGQLSLGQLIAF 263
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1065-1273 |
7.08e-13 |
|
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: 69.48 E-value: 7.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1065 QIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWL-RDQMGLV--GQE--PVLfnd 1139
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVpqGREifPRL--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1140 TIRANITYG------KHSEVTEE--EITAVAKAanahefvsslpqgydtVVGEKGVQLSGGQKQRVAIARAILKDPKILL 1211
Cdd:TIGR03410 91 TVEENLLTGlaalprRSRKIPDEiyELFPVLKE----------------MLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1212 LDEATSALD----AESERVVQDALDRvmVNRTTIVVAHRLS-TIKGADMIAVLKEGKIAEKGKHEAL 1273
Cdd:TIGR03410 155 LDEPTEGIQpsiiKDIGRVIRRLRAE--GGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
385-568 |
8.04e-13 |
|
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: 72.86 E-value: 8.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 385 QLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGisikklrldwiRGKIGLVSQEPLLFMASIKD 464
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 465 NIIY----------GKKDATLEEIKRAAELANaanfIDKLPNGYDTlVGQRGTQLSGGQKQRIAIARAILKDPKILLLDE 534
Cdd:TIGR00954 534 QIIYpdssedmkrrGLSDKDLEQILDNVQLTH----ILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|....
gi 1443040382 535 ATSALDVESERIVQEALNRMMVerTTLVVAHRLS 568
Cdd:TIGR00954 609 CTSAVSVDVEGYMYRLCREFGI--TLFSVSHRKS 640
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1053-1275 |
8.14e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.97 E-value: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1053 NVSFKYpSRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEI--RSLKVSWLRDQ---- 1126
Cdd:PRK10261 19 NIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrRSRQVIELSEQsaaq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1127 --------MGLVGQEPVlfnDTIRANITYGK--------HSEVTEEEitAVAKAANAHEFVSsLPQGyDTVVGEKGVQLS 1190
Cdd:PRK10261 98 mrhvrgadMAMIFQEPM---TSLNPVFTVGEqiaesirlHQGASREE--AMVEAKRMLDQVR-IPEA-QTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1191 GGQKQRVAIARAILKDPKILLLDEATSALDAESE-------RVVQDALDrvmvnRTTIVVAHRLSTIKG-ADMIAVLKEG 1262
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMS-----MGVIFITHDMGVVAEiADRVLVMYQG 245
|
250
....*....|...
gi 1443040382 1263 KIAEKGKHEALLR 1275
Cdd:PRK10261 246 EAVETGSVEQIFH 258
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1057-1214 |
8.63e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 69.67 E-value: 8.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1057 KYPSRPDVQifsDFTLHIPSQKTIALVGESGSGKST---IIALLERfydPDSGNISLDGVEIRSLKVsWLRDQMGLvG-- 1131
Cdd:COG1137 12 SYGKRTVVK---DVSLEVNQGEIVGLLGPNGAGKTTtfyMIVGLVK---PDSGRIFLDGEDITHLPM-HKRARLGI-Gyl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1132 -QEPVLFND-TIRANI-----TYGKHSEVTEEE---------ITAVAKAanahefvsslpqgydtvvgeKGVQLSGGQKQ 1195
Cdd:COG1137 84 pQEASIFRKlTVEDNIlavleLRKLSKKEREERleelleefgITHLRKS--------------------KAYSLSGGERR 143
|
170
....*....|....*....
gi 1443040382 1196 RVAIARAILKDPKILLLDE 1214
Cdd:COG1137 144 RVEIARALATNPKFILLDE 162
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
388-596 |
9.55e-13 |
|
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: 72.16 E-value: 9.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYdPQ---SGEVLIDGISIKKLRL-DWIRGKIGLVSQEPLLFMA-SI 462
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 463 KDNIIYGKkDATL--------EEIKRAAELANAANfIDKLPNGYDtlVGQRGtqlsGGQKQRIAIARAILKDPKILLLDE 534
Cdd:TIGR02633 96 AENIFLGN-EITLpggrmaynAMYLRAKNLLRELQ-LDADNVTRP--VGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 535 ATSALDVESERIVQEALNRMMVERTTLV-VAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKD 596
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKAHGVACVyISHKLNEVKAVcDTICVIRDGQHVATKDMSTMSED 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1055-1264 |
1.05e-12 |
|
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: 69.28 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1055 SFKYPSRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRdQMGLV-GQE 1133
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfGQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1134 PVLFNDtIRANITYGKHSEVTEeeITAVAKAANAHEFVSSLPQG--YDTVVGekgvQLSGGQKQRVAIARAILKDPKILL 1211
Cdd:cd03267 104 TQLWWD-LPVIDSFYLLAAIYD--LPPARFKKRLDELSELLDLEelLDTPVR----QLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 1212 LDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRLSTI-KGADMIAVLKEGKI 1264
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRL 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1052-1229 |
1.31e-12 |
|
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: 71.89 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1052 NNVSFKYPsrPDVQIFSDFTLH-IPSQKtIALVGESGSGKSTIIALLErfydpdsgnisldGVEIRSLKVSWLRD--QMG 1128
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSfFPGAK-IGVLGLNGAGKSTLLRIMA-------------GVDKDFNGEARPQPgiKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVL-FNDTIRANI----------------TYGKHSEVTEE---------EITAVAKAANAHEFVSSLPQGYDTV- 1181
Cdd:TIGR03719 72 YLPQEPQLdPTKTVRENVeegvaeikdaldrfneISAKYAEPDADfdklaaeqaELQEIIDAADAWDLDSQLEIAMDALr 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1182 --VGEKGVQ-LSGGQKQRVAIARAILKDPKILLLDEATSALDAES----ERVVQD 1229
Cdd:TIGR03719 152 cpPWDADVTkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
391-588 |
1.41e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.43 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 391 LSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDG-------ISIKKLRLDWI----------RGKIGLVSQ 453
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdYSYRSQRIRMIfqdpstslnpRQRISQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 454 EPLLFMASIKDNiiyGKKDATLEEIKRAAELANAANFIDKLpngydtlvgqrgtqLSGGQKQRIAIARAILKDPKILLLD 533
Cdd:PRK15112 112 FPLRLNTDLEPE---QREKQIIETLRQVGLLPDHASYYPHM--------------LAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 534 EATSALDVEseriVQEALNRMMVER------TTLVVAHRLSTVRNV-DCITVVRKGKIVEQG 588
Cdd:PRK15112 175 EALASLDMS----MRSQLINLMLELqekqgiSYIYVTQHLGMMKHIsDQVLVMHQGEVVERG 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
366-570 |
1.99e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 366 MNGDIELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGisikKLRLDWIR 445
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----KLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 446 GKIGLVSQEPLL---FMaSIKDNIiygKKDATLEEIKRAaelaNAANFIDklpngydtlvgQRGTQLSGGQKQRIAIARA 522
Cdd:PRK09544 74 QKLYLDTTLPLTvnrFL-RLRPGT---KKEDILPALKRV----QAGHLID-----------APMQKLSGGETQRVLLARA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1443040382 523 ILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTV 570
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSHDLHLV 184
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1067-1264 |
2.02e-12 |
|
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: 67.07 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1067 FSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRD-----------QMGLVGQEPV 1135
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRagiayvpedrkREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1136 LFNDTIranitygkhsevteeeitavakaanahefvsslpqgydtvvgekGVQLSGGQKQRVAIARAILKDPKILLLDEA 1215
Cdd:cd03215 96 AENIAL--------------------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1216 TSALD----AESERVVQDALDRvmvNRTTIVVAHRLSTIKG-ADMIAVLKEGKI 1264
Cdd:cd03215 132 TRGVDvgakAEIYRLIRELADA---GKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1080-1269 |
2.13e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 68.33 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1080 IALVGESGSGKSTIIALLERFYdPDSGNISLDGVEIRSLKV-------SWLRDQMGLVGQEPV-----LfndtiranitY 1147
Cdd:COG4138 25 IHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAaelarhrAYLSQQQSPPFAMPVfqylaL----------H 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1148 GKHSEVTEEEITAVAKAANAHEFVSSLPQGYDtvvgekgvQLSGGQKQRVAIARAILK-------DPKILLLDEATSALD 1220
Cdd:COG4138 94 QPAGASSEAVEQLLAQLAEALGLEDKLSRPLT--------QLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 1221 aeserVVQD-ALDRVMVN-----RTTIVVAHRLS-TIKGADMIAVLKEGKIAEKGK 1269
Cdd:COG4138 166 -----VAQQaALDRLLRElcqqgITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
384-566 |
2.29e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.06 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 384 EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFY--DPQSGEVLIDGISIkklrldwirgkiglvSQEpllfmAS 461
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE-----AS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 462 IKDNIiyGKKDATLE--EIKRAAELANAANFIDKlpngYDtlvgqrgtQLSGGQKQRIAIARAILKDPKILLLDEATSAL 539
Cdd:COG2401 102 LIDAI--GRKGDFKDavELLNAVGLSDAVLWLRR----FK--------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180
....*....|....*....|....*....
gi 1443040382 540 DVESERIVQEALNRMMVER-TTLVVA-HR 566
Cdd:COG2401 168 DRQTAKRVARNLQKLARRAgITLVVAtHH 196
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1056-1268 |
2.37e-12 |
|
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: 68.20 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1056 FKYPSRpdVQIFSDFTLH-----IPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIrSLKVSWLR-DQMGL 1129
Cdd:cd03237 1 YTYPTM--KKTLGEFTLEveggsISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKaDYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1130 VgqepvlfnDTIRANITYGKHSEvtEEEITAVAKaanahefvsslPQGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKI 1209
Cdd:cd03237 78 V--------RDLLSSITKDFYTH--PYFKTEIAK-----------PLQIEQILDREVPELSGGELQRVAIAACLSKDADI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1210 LLLDEATSALDAESERVVQDALDRVMVN--RTTIVVAHrlsTIKGADMIA---VLKEGKIAEKG 1268
Cdd:cd03237 137 YLLDEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEH---DIIMIDYLAdrlIVFEGEPSVNG 197
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
388-596 |
2.65e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKL--RLDWIRGkIGLVSQE-PLLFMASIKD 464
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdhKLAAQLG-IGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 465 NIIYG----KKDATLEEIKRAAELANAANFIDK--LPNGYDTLVGqrgtQLSGGQKQRIAIARAILKDPKILLLDEATSA 538
Cdd:PRK09700 100 NLYIGrhltKKVCGVNIIDWREMRVRAAMMLLRvgLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 539 LDVESERIVQEALNRMMVERTTLV-VAHRLSTVRNV-DCITVVRKGKIVEQGphdaLVKD 596
Cdd:PRK09700 176 LTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRIcDRYTVMKDGSSVCSG----MVSD 231
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1049-1265 |
2.69e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 71.43 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPdvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNIsldgveIRSLKVswlrdQMG 1128
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKV-----RMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLFNDTIRANITYGKH--SEVTEEEItavakaaNAHefvsslpQGYDTVVGEKGVQ----LSGGQKQRVAIARA 1202
Cdd:PLN03073 576 VFSQHHVDGLDLSSNPLLYMMRcfPGVPEQKL-------RAH-------LGSFGVTGNLALQpmytLSGGQKSRVAFAKI 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1203 ILKDPKILLLDEATSALDAES-ERVVQDAldrVMVNRTTIVVAHRLSTIKGA-DMIAVLKEGKIA 1265
Cdd:PLN03073 642 TFKKPHILLLDEPSNHLDLDAvEALIQGL---VLFQGGVLMVSHDEHLISGSvDELWVVSEGKVT 703
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
387-594 |
2.91e-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: 70.99 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 387 ILDGLSLQVASGTTMAIVGESGSGKSTVISLVERF--YDPQSGEVLID-----------------------GISIKKLRL 441
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvgepcpvcGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 442 D-W---------IRGKIGLVSQEPLLFMA--SIKDNIIYGKKDATL---EEIKRAAELANAANfidklpngydtlVGQRG 506
Cdd:TIGR03269 95 DfWnlsdklrrrIRKRIAIMLQRTFALYGddTVLDNVLEALEEIGYegkEAVGRAVDLIEMVQ------------LSHRI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 507 TQ----LSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVER--TTLVVAHRLSTVRNV-DCITVV 579
Cdd:TIGR03269 163 THiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDLsDKAIWL 242
|
250
....*....|....*
gi 1443040382 580 RKGKIVEQGPHDALV 594
Cdd:TIGR03269 243 ENGEIKEEGTPDEVV 257
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
48-313 |
3.03e-12 |
|
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: 68.97 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 48 MVVGTVGALGNGISQPLMTVLFGNVINSFGANTSGSV---LRSVTKVVLNFIYLGIGTSVASFLQVscWTMA--GERQSA 122
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGgvdFSGLLRILLLLLGLYLLSALFSYLQN--RLMArvSQRTVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 123 RIRS-LYLKaVLRQDITFFDTEmTTGEAVSRMSSDTLLIQGALGEKggkLVELLSSF---IGGFIIAFTRGWLLTLVMLT 198
Cdd:cd18547 79 DLRKdLFEK-LQRLPLSYFDTH-SHGDIMSRVTNDVDNISQALSQS---LTQLISSIltiVGTLIMMLYISPLLTLIVLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 199 SLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFGMG 278
Cdd:cd18547 154 TVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMP 233
|
250 260 270
....*....|....*....|....*....|....*
gi 1443040382 279 SVMCVVFGSYGLAFWYGGKLIIEKGYTGGKIMTIL 313
Cdd:cd18547 234 IMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFL 268
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
388-595 |
3.49e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.96 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVIS-----LVerfydPQSGEVLIDGISIKKLRLDWIRgKIGLV----SQepLLF 458
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKmltgiLV-----PTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQ--LWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 459 MASIKDNI-----IYGKKDATLEE-IKRAAELANAANFIDKlPngydtlVgqRgtQLSGGQKQRIAIARAILKDPKILLL 532
Cdd:COG4586 110 DLPAIDSFrllkaIYRIPDAEYKKrLDELVELLDLGELLDT-P------V--R--QLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 533 DEATSALDVESERIVQEALNRMMVER-TTLVVA-HRLSTVRNVdC--ITVVRKGKIVEQGPHDALVK 595
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIEAL-CdrVIVIDHGRIIYDGSLEELKE 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1080-1263 |
4.58e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1080 IALVGESGSGKSTIIALLERFYdPD---SGNISLDGVEirsLKVSWLRD--QMGLV--GQEPVLFND-TIRANITYGkhS 1151
Cdd:PRK13549 34 VSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEE---LQASNIRDteRAGIAiiHQELALVKElSVLENIFLG--N 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1152 EVTEEEITAVAKA-ANAHEFVSSLpqGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALdAESE-----R 1225
Cdd:PRK13549 108 EITPGGIMDYDAMyLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL-TESEtavllD 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 1443040382 1226 VVQDALDRvmvNRTTIVVAHRLSTIKG-ADMIAVLKEGK 1263
Cdd:PRK13549 185 IIRDLKAH---GIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1044-1262 |
6.36e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.81 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1044 NVTGSIDFNNVSFKYPSrpdVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSL--KVS 1121
Cdd:PRK09700 1 MATPYISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdhKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1122 WlRDQMGLVGQEPVLFND-TIRANITYGKHSE--------VTEEEITAVAKaanahefVSSLPQGYDTVVGEKGVQLSGG 1192
Cdd:PRK09700 78 A-QLGIGIIYQELSVIDElTVLENLYIGRHLTkkvcgvniIDWREMRVRAA-------MMLLRVGLKVDLDEKVANLSIS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 1193 QKQRVAIARAILKDPKILLLDEATSAL-DAESERVVQdALDRVMVNRTTIV-VAHRLSTIKG-ADMIAVLKEG 1262
Cdd:PRK09700 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLFL-IMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDG 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1062-1275 |
7.20e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.03 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1062 PDVQIFSDFTLHIPSQKTIALVGESGSGKS-TIIALLERFydP-----DSGNISLDGVEI-----RSLKVSwlrdqmgLV 1130
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGIL--PagvrqTAGRVLLDGKPVapcalRGRKIA-------TI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1131 GQEP-VLFN--DTIRAnitygkHSEvteEEITAVAKAANAHEFVSSLP----QGYDTVVGEKGVQLSGGQKQRVAIARAI 1203
Cdd:PRK10418 85 MQNPrSAFNplHTMHT------HAR---ETCLALGKPADDATLTAALEavglENAARVLKLYPFEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 1204 LKDPKILLLDEATSALDAESERVVQDALDRVMVNRT--TIVVAHRLSTI-KGADMIAVLKEGKIAEKGKHEALLR 1275
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
388-596 |
9.44e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 9.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDG--ISIKKLRLDWIRGkIGLVSQE-PLLFMASIKD 464
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkeVTFNGPKSSQEAG-IGIIHQElNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 465 NIIYGKKDAT-LEEIKRAAELANAANFIDKL--PNGYDTLVGqrgtQLSGGQKQRIAIARAILKDPKILLLDEATSAL-D 540
Cdd:PRK10762 99 NIFLGREFVNrFGRIDWKKMYAEADKLLARLnlRFSSDKLVG----ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 541 VESERIVQeALNRMMVERTTLV-VAHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKD 596
Cdd:PRK10762 175 TETESLFR-VIRELKSQGRGIVyISHRLKEIFEIcDDVTVFRDGQFIAEREVADLTED 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1052-1223 |
1.05e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.99 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1052 NNVSFKYPsrPDVQIFSDFTLH-IPSQKtIALVGESGSGKST---IIALLERFYDpdsGNISL-DGVEIrslkvswlrdq 1126
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSfFPGAK-IGVLGLNGAGKSTllrIMAGVDKEFE---GEARPaPGIKV----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1127 mGLVGQEPVLFND-TIRANITYG---------KHSEVTEE------EITAVAK----------AANAHEFVSSL------ 1174
Cdd:PRK11819 73 -GYLPQEPQLDPEkTVRENVEEGvaevkaaldRFNEIYAAyaepdaDFDALAAeqgelqeiidAADAWDLDSQLeiamda 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1175 ---PQGyDTVVGekgvQLSGGQKQRVAIARAILKDPKILLLDEATSALDAES 1223
Cdd:PRK11819 152 lrcPPW-DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1078-1273 |
1.07e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1078 KTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSL---KVSWLRDQMGLVGQEPVLFNDTiRANITYG------ 1148
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDPYASLDP-RQTVGDSimeplr 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1149 KHSEVTEEEitAVAKAANAHEFVSSLPQGYDTVVGEkgvqLSGGQKQRVAIARAILKDPKILLLDEATSALDAE-SERVV 1227
Cdd:PRK10261 430 VHGLLPGKA--AAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVSiRGQII 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1443040382 1228 QDALD--RVMvNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEAL 1273
Cdd:PRK10261 504 NLLLDlqRDF-GIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAV 551
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
383-543 |
1.12e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.99 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 383 PEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGE-VLIDGIsikklrldwirgKIGLVSQEPLL---- 457
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGI------------KVGYLPQEPQLdpek 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 458 --------FMASIKD-----NIIYGK-------------KDATLEEIKRAAELANAANFID------KLPNGyDTLVgqr 505
Cdd:PRK11819 86 tvrenveeGVAEVKAaldrfNEIYAAyaepdadfdalaaEQGELQEIIDAADAWDLDSQLEiamdalRCPPW-DAKV--- 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1443040382 506 gTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVES 543
Cdd:PRK11819 162 -TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1063-1269 |
1.14e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.06 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1063 DVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKvswlRDQMGLVGQEPVLF-NDTI 1141
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1142 RANITY-----GKHSEVTEEEITA------VAKAANahefvsslpqgydtvvgeKGVQ-LSGGQKQRVAIARAILKDPKI 1209
Cdd:COG4152 89 GEQLVYlarlkGLSKAEAKRRADEwlerlgLGDRAN------------------KKVEeLSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1210 LLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTI-KGADMIAVLKEGKIAEKGK 1269
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSsHQMELVeELCDRIVIINKGRKVLSGS 212
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1049-1247 |
1.16e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRpdvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGveirSLKVSWLRDQMG 1128
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----KLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1129 LVGQEPVLFNDTIRAnitygkHSEVTEEEITAVAKAANAHEFVSSLPQgydtvvgekgvQLSGGQKQRVAIARAILKDPK 1208
Cdd:PRK09544 78 LDTTLPLTVNRFLRL------RPGTKKEDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1443040382 1209 ILLLDEATSALDAESERVVQDALD--RVMVNRTTIVVAHRL 1247
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDqlRRELDCAVLMVSHDL 181
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
384-593 |
1.21e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.14 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 384 EQLILDGLSLQVASGTTMAIVGESGSGKSTVI-SLVERFYDPQ-SGEVLIDGISIKKLRLDwirgKIGLVSQEPLLF-MA 460
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLnALAGRIQGNNfTGTILANNRKPTKQILK----RTGFVTQDDILYpHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 461 SIKDNIIYGK-----KDATLEEIKRAAELANAANFIDKLPNgydTLVGQ---RGtqLSGGQKQRIAIARAILKDPKILLL 532
Cdd:PLN03211 156 TVRETLVFCSllrlpKSLTKQEKILVAESVISELGLTKCEN---TIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 533 DEATSALDVESE-RIVQEALNRMMVERTTLVVAHRLST--VRNVDCITVVRKGKIVEQGP-HDAL 593
Cdd:PLN03211 231 DEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKgSDAM 295
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1069-1273 |
1.46e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.17 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1069 DFTLHipSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSL---KVSwlrdQMGLVG--QEPVLFND-TIR 1142
Cdd:PRK11300 25 NLEVR--EQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghQIA----RMGVVRtfQHVRLFREmTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1143 ANITYGKHSEVT--------------EEEITAVAKAANAHEFVSSLPqgydtVVGEKGVQLSGGQKQRVAIARAILKDPK 1208
Cdd:PRK11300 99 ENLLVAQHQQLKtglfsgllktpafrRAESEALDRAATWLERVGLLE-----HANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1209 ILLLDEATSALDAESERVVQDALD--RVMVNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKGKHEAL 1273
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
759-984 |
1.84e-11 |
|
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: 66.57 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 759 LFGIAGGKLIQRVRTLSFQRIMHQEVAWFDKpsnsrcatlmyfcyfifykkiftfkpmlrghliSYSGALGTRLSVDALN 838
Cdd:cd18784 59 LFTLAMARLNIRIRNLLFRSIVSQEIGFFDT---------------------------------VKTGDITSRLTSDTTT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 839 VRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSI 918
Cdd:cd18784 106 MSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSI 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 919 RTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGiGLSFSNLMLYLT-YGLCFYVGAKFVSQGKTT 984
Cdd:cd18784 186 RTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYG-GYVWSNELTELAlTVSTLYYGGHLVITGQIS 251
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
384-566 |
2.04e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.59 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 384 EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWirgkiglvsQEPLLFMA--- 460
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY---------QKQLCFVGhrs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 461 ------SIKDNIIYG-KKDATLEEIKRAAELANAANFIDkLPNGYdtlvgqrgtqLSGGQKQRIAIARAILKDPKILLLD 533
Cdd:PRK13540 84 ginpylTLRENCLYDiHFSPGAVGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1443040382 534 EATSALDvesERIVQEALNRMMVER----TTLVVAHR 566
Cdd:PRK13540 153 EPLVALD---ELSLLTIITKIQEHRakggAVLLTSHQ 186
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
734-999 |
2.38e-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: 65.97 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 734 DSRFWALMSVVLGVAclISIPAEYFLFGIAGGKLIQRVRTLSFQRIMHQEVAWFDKPSnsrcatlmyfcyfifykkiftf 813
Cdd:cd18575 36 NRAFLLLLAVALVLA--LASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTR---------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 814 kpmlrghlisySGALGTRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFL 893
Cdd:cd18575 92 -----------TGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 894 KGFSEESKEMYEDANQVAADAVGSIRTVASFCSEKRVVAIYNKKCE-----ALRKQGIRSGIVGG-IGLSFSNLMLYLty 967
Cdd:cd18575 161 RRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEaafaaALRRIRARALLTALvIFLVFGAIVFVL-- 238
|
250 260 270
....*....|....*....|....*....|...
gi 1443040382 968 glcfYVGAKFVSQGKTTFSDVFK-VFFALVLAA 999
Cdd:cd18575 239 ----WLGAHDVLAGRMSAGELSQfVFYAVLAAG 267
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
388-565 |
3.13e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.53 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMA-----IVGESGSGKSTVISLVERFYDPQSGEVLID-GISIKKlrlDWIRGKI-GLVSQepllFMA 460
Cdd:PRK13409 350 LGDFSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElKISYKP---QYIKPDYdGTVED----LLR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 461 SIKDNIiygkkDATLEEikraAELANaanfidklPNGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALD 540
Cdd:PRK13409 423 SITDDL-----GSSYYK----SEIIK--------PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
170 180
....*....|....*....|....*..
gi 1443040382 541 VESERIVQEALNRMMVER--TTLVVAH 565
Cdd:PRK13409 486 VEQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
391-591 |
3.54e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 391 LSLQVASGTTMAIVGESGSGKSTVISLVERFYdPQSGEVLIDGisikKLRLDWIRGKIGLV------SQEPLLFMASIKD 464
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAG----QPLEAWSAAELARHraylsqQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 465 NIIYGKKDATLEEIKRA-AELANAANFIDKLPNGYdtlvgqrgTQLSGGQKQRIAIARAILK-------DPKILLLDEAT 536
Cdd:PRK03695 90 LTLHQPDKTRTEAVASAlNEVAEALGLDDKLGRSV--------NQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 537 SALDVESerivQEALNRMMVE-----RTTLVVAHRLS-TVRNVDCITVVRKGKIVEQGPHD 591
Cdd:PRK03695 162 NSLDVAQ----QAALDRLLSElcqqgIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRD 218
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
45-307 |
3.63e-11 |
|
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: 65.61 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 45 VLLMVVGTVGALGngisQP-LMTVLFGNVINSFGANTSGSVLRSVTK------VVLNFIYLGI--GTSVASFLQVSCWTM 115
Cdd:cd18564 5 LLALLLETALRLL----EPwPLKVVIDDVLGDKPLPGLLGLAPLLGPdplallLLAAAALVGIalLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 116 AGERQSARIRS-LYlKAVLRQDITFFDTeMTTGEAVSRMSSDTLLIQGALGekgGKLVELLSS---FIGGFIIAFTRGWL 191
Cdd:cd18564 81 VGQRVVLDLRRdLF-AHLQRLSLSFHDR-RRTGDLLSRLTGDVGAIQDLLV---SGVLPLLTNlltLVGMLGVMFWLDWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 192 LTLVMLTSLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEE-- 269
Cdd:cd18564 156 LALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAar 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1443040382 270 ---------GIITGFGMGSVMcvvfgsyglafWYGGKLIIEKGYTGG 307
Cdd:cd18564 236 lqallspvvDVLVAVGTALVL-----------WFGAWLVLAGRLTPG 271
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1053-1269 |
4.06e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.90 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1053 NVSFKYPSrPDVQIFSDFTLHIPSQKTIALVGESGSGKS-TIIALLERFYDPD--SGNISLDGVEIRSL---KVSWLR-D 1125
Cdd:PRK09473 19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFNGREILNLpekELNKLRaE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 QMGLVGQEPVL-FNDTIRA----------NITYGKhSEVTEEEIT---AVaKAANAHEFVSSLPQgydtvvgekgvQLSG 1191
Cdd:PRK09473 98 QISMIFQDPMTsLNPYMRVgeqlmevlmlHKGMSK-AEAFEESVRmldAV-KMPEARKRMKMYPH-----------EFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1192 GQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVM--VNRTTIVVAHRLSTIKG-ADMIAVLKEGKIAEKG 1268
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKreFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 244
|
.
gi 1443040382 1269 K 1269
Cdd:PRK09473 245 N 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
371-591 |
4.39e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.86 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 371 ELKDVYfRYPARP---EQLILDGL---------SLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDG--ISI 436
Cdd:PRK11288 241 EIGDIY-GYRPRPlgeVRLRLDGLkgpglrepiSFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDI 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 437 KKLRlDWIRGKIGLV----SQEPLLFMASIKDNIIYGKKDATLEE---IKRAAELANAANFIDKL----PNGyDTLVGQr 505
Cdd:PRK11288 320 RSPR-DAIRAGIMLCpedrKAEGIIPVHSVADNINISARRHHLRAgclINNRWEAENADRFIRSLniktPSR-EQLIMN- 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 506 gtqLSGGQKQRIAIARAILKDPKILLLDEATSALDV----ESERIVQEALNRMMverTTLVVAHRLSTVRNV-DCITVVR 580
Cdd:PRK11288 397 ---LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVgakhEIYNVIYELAAQGV---AVLFVSSDLPEVLGVaDRIVVMR 470
|
250
....*....|.
gi 1443040382 581 KGKIVEQGPHD 591
Cdd:PRK11288 471 EGRIAGELARE 481
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
384-584 |
4.91e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 67.12 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 384 EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEV-LIDGIsikklrldwirgKIGLVSQEPLLFMASi 462
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI------------KLGYFAQHQLEFLRA- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 463 kdniiygkKDATLEEIKRAAELANAANFIDKLpNGYdtlvGQRGTQL-------SGGQKQRIAIARAILKDPKILLLDEA 535
Cdd:PRK10636 391 --------DESPLQHLARLAPQELEQKLRDYL-GGF----GFQGDKVteetrrfSGGEKARLVLALIVWQRPNLLLLDEP 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1443040382 536 TSALDVESERIVQEALnrMMVERTTLVVAHRLSTVRN-VDCITVVRKGKI 584
Cdd:PRK10636 458 TNHLDLDMRQALTEAL--IDFEGALVVVSHDRHLLRStTDDLYLVHDGKV 505
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1070-1268 |
5.52e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.81 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1070 FTLHipSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPV-----------LFN 1138
Cdd:PRK15112 34 FTLR--EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqrisqILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1139 DTIRANitygkhsevTEEEITAVAKAANAH-EFVSSLPQGydtvVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATS 1217
Cdd:PRK15112 112 FPLRLN---------TDLEPEQREKQIIETlRQVGLLPDH----ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1218 ALDAEservVQDALDRVMVNR------TTIVVAHRLSTIKG-ADMIAVLKEGKIAEKG 1268
Cdd:PRK15112 179 SLDMS----MRSQLINLMLELqekqgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERG 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1067-1257 |
6.12e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 6.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1067 FSDFTLHI-PSQ----KTIALVGESGSGKSTIIALLERFYDPDSGNISLDgveirsLKVSW-----LRDQMGLVGQepVL 1136
Cdd:PRK13409 350 LGDFSLEVeGGEiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKISYkpqyiKPDYDGTVED--LL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1137 FNDTIRANITYGKHsevteeeitavakaanahEFVS--SLPQGYDTVVGEkgvqLSGGQKQRVAIARAILKDPKILLLDE 1214
Cdd:PRK13409 422 RSITDDLGSSYYKS------------------EIIKplQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDE 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1443040382 1215 ATSALDAESERVVQDALDRVMVNR--TTIVVAHRLSTIkgaDMIA 1257
Cdd:PRK13409 480 PSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI---DYIS 521
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1060-1267 |
6.24e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1060 SRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDG--VEIRSLKVSwlrdQ---MGLVGQEP 1134
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkeVTFNGPKSS----QeagIGIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1135 VLF-NDTIRANITYGKhsEVTE-------EEITAVAKAANAHefvSSLPQGYDTVVGEkgvqLSGGQKQRVAIARAILKD 1206
Cdd:PRK10762 89 NLIpQLTIAENIFLGR--EFVNrfgridwKKMYAEADKLLAR---LNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1207 PKILLLDEATSAL-DAESE---RVVQDALDRvmvNRTTIVVAHRLSTI-KGADMIAVLKEGK-IAEK 1267
Cdd:PRK10762 160 SKVIIMDEPTDALtDTETEslfRVIRELKSQ---GRGIVYISHRLKEIfEICDDVTVFRDGQfIAER 223
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1042-1274 |
7.12e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.74 E-value: 7.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1042 MENVTgsIDFNNVSFKYPSrpdVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVS 1121
Cdd:PRK11614 1 MEKVM--LSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1122 -WLRDQMGLVGQEPVLFND-TIRANITYGKHSEVTEEEITAVAKAANAhefvssLPQGYDTVVGEKGVqLSGGQKQRVAI 1199
Cdd:PRK11614 76 kIMREAVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKWVYEL------FPRLHERRIQRAGT-MSGGEQQMLAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1200 ARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLS--TIKGADMIAVLKEGKIAEKGKHEALL 1274
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
370-534 |
7.23e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.53 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPArpEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIG 449
Cdd:PRK10522 323 LELRNVTFAYQD--NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 LVSQEPLLFmasikdniiygkkDATLEEIKRAAELANAANFIDKLPNGYD-TLVGQR--GTQLSGGQKQRIAIARAILKD 526
Cdd:PRK10522 401 AVFTDFHLF-------------DQLLGPEGKPANPALVEKWLERLKMAHKlELEDGRisNLKLSKGQKKRLALLLALAEE 467
|
....*...
gi 1443040382 527 PKILLLDE 534
Cdd:PRK10522 468 RDILLLDE 475
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1076-1259 |
8.49e-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: 61.62 E-value: 8.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1076 SQKTIALVGESGSGKSTIIALLERFYDPDSGN-ISLDGVEIRSLKVSWLRDqmglvgqepvlfndtiranitygkhsevt 1154
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLL----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1155 eeeitavakaanahefvsslpqgydTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALD-- 1232
Cdd:smart00382 52 -------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180 190
....*....|....*....|....*....|..
gi 1443040382 1233 -----RVMVNRTTIVVAHRLSTIKGADMIAVL 1259
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
45-311 |
1.08e-10 |
|
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: 64.33 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 45 VLLMVVGTVGALgngiSQPLmtvLFGNVINSFGANTSGSvLRSVTKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSARI 124
Cdd:cd18544 5 LLLLLLATALEL----LGPL---LIKRAIDDYIVPGQGD-LQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 125 RSLYLKAVLRQDITFFDTeMTTGEAVSRMSSDT-----LLIQGalgekggkLVELLSSF---IGGFIIAFTRGWLLTLVM 196
Cdd:cd18544 77 RRDLFSHIQRLPLSFFDR-TPVGRLVTRVTNDTealneLFTSG--------LVTLIGDLlllIGILIAMFLLNWRLALIS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 197 LTSLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFG 276
Cdd:cd18544 148 LLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALF 227
|
250 260 270
....*....|....*....|....*....|....*
gi 1443040382 277 MGSVMCVVFGSYGLAFWYGGKLIIEKGYTGGKIMT 311
Cdd:cd18544 228 RPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYA 262
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
759-984 |
1.23e-10 |
|
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: 64.10 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 759 LFGIAGGKLIQRVRTLSFQRIMHQEVAWFDKPSnsrcatlmyfcyfifykkiftfkpmlrghlisySGALGTRLSVDALN 838
Cdd:cd18574 65 LLSVVGERVAARLRNDLFSSLLRQDIAFFDTHR---------------------------------TGELVNRLTADVQE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 839 VRR----LVGDNLALIVQAVATLITGFAIAFaadwRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADA 914
Cdd:cd18574 112 FKSsfkqCVSQGLRSVTQTVGCVVSLYLISP----KLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 915 VGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIvgGIGL--SFSNLMLYLTYGLCFYVGAKFVSQGKTT 984
Cdd:cd18574 188 LGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGL--GIGIfqGLSNLALNGIVLGVLYYGGSLVSRGELT 257
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1060-1224 |
1.28e-10 |
|
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: 62.13 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1060 SRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRDQMGLVGQEPVLFND 1139
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1140 TIRANITYGKHSEVTEEEITAVAKAA-NAHEfvsslpqgyDTVVGekgvQLSGGQKQRVAIARAILKDPKILLLDEATSA 1218
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGlNGFE---------DRPVA----QLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
....*.
gi 1443040382 1219 LDAESE 1224
Cdd:cd03231 156 LDKAGV 161
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
371-585 |
1.30e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.43 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 371 ELKDVyfRYPARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLV--ERfyDPQSGEVLIDGISIKKL-RLDWIRGK 447
Cdd:COG3845 259 EVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLsPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 448 IGLVSQEPL---LFMA-SIKDNII----YGKKDATLEEIKRAAELANAANFIDKL---PNGYDTLVGQrgtqLSGGQKQR 516
Cdd:COG3845 335 VAYIPEDRLgrgLVPDmSVAENLIlgryRRPPFSRGGFLDRKAIRAFAEELIEEFdvrTPGPDTPARS----LSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 517 IAIARAILKDPKILLLDEATSALDVESerivQEALNRMMVER-----TTLVVAHRLSTVRNV-DCITVVRKGKIV 585
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGA----IEFIHQRLLELrdagaAVLLISEDLDEILALsDRIAVMYEGRIV 481
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1063-1263 |
1.45e-10 |
|
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: 65.23 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1063 DVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDS--GNISLDGVEirsLKVSWLRDQ----MGLVGQEPVL 1136
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSP---LKASNIRDTeragIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1137 FND-TIRANITYGKHSEVTEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGvQLSGGQKQRVAIARAILKDPKILLLDEA 1215
Cdd:TIGR02633 90 VPElSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVG-DYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1216 TSALDAESERVVQDAL-DRVMVNRTTIVVAHRLSTIKG-ADMIAVLKEGK 1263
Cdd:TIGR02633 169 SSSLTEKETEILLDIIrDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
45-300 |
1.89e-10 |
|
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: 63.26 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 45 VLLMVVGTVGALGNgisqPLmtvLFGNVINSFGANTSGSVLrsvTKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSARI 124
Cdd:cd18545 6 LLLMLLSTAASLAG----PY---LIKIAIDEYIPNGDLSGL---LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 125 RS-LYLKaVLRQDITFFDtEMTTGEAVSRMSSDT-----LLIQGALGekggkLVELLSSFIGGFIIAFTRGWLLTLVMLT 198
Cdd:cd18545 76 RQdLFSH-LQKLSFSFFD-SRPVGKILSRVINDVnslsdLLSNGLIN-----LIPDLLTLVGIVIIMFSLNVRLALVTLA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 199 SLPLIAIASAV----SAQALTRVSSKRqtsySDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITG 274
Cdd:cd18545 149 VLPLLVLVVFLlrrrARKAWQRVRKKI----SNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNA 224
|
250 260
....*....|....*....|....*..
gi 1443040382 275 FGMGSV-MCVVFGSyGLAFWYGGKLII 300
Cdd:cd18545 225 LFWPLVeLISALGT-ALVYWYGGKLVL 250
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1067-1279 |
1.92e-10 |
|
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: 65.19 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1067 FSDFTLHIPSQK-----TIALVGESGSGKSTIIALLERFYDPDSGNISLDgveirsLKVSW-----LRDQMGLVgqEPVL 1136
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------LKISYkpqyiSPDYDGTV--EEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1137 FNdTIRANITygkhSEVTEEEItavakaanAHEFvsSLPQGYDTVVGEkgvqLSGGQKQRVAIARAILKDPKILLLDEAT 1216
Cdd:COG1245 423 RS-ANTDDFG----SSYYKTEI--------IKPL--GLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPS 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1217 SALDAESERVVQDALDRVMVNR--TTIVVAHRLSTIkgaDMIA---VLKEGKIAEKGKHEALLRIKDG 1279
Cdd:COG1245 484 AHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYISdrlMVFEGEPGVHGHASGPMDMREG 548
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1069-1268 |
2.23e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.64 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1069 DFTLHiPSQkTIALVGESGSGKSTIIALLERFYDPDSGNISLDG-------------VEIRSLkvswLRDQMGLVGQEPV 1135
Cdd:PRK11701 26 SFDLY-PGE-VLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlrdlyalseAERRRL----LRTEWGFVHQHPR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1136 lfnDTIR------ANIT----------YGKHSEVTEEEITAVAKAANAhefVSSLPQGYdtvvgekgvqlSGGQKQRVAI 1199
Cdd:PRK11701 100 ---DGLRmqvsagGNIGerlmavgarhYGDIRATAGDWLERVEIDAAR---IDDLPTTF-----------SGGMQQRLQI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1200 ARAILKDPKILLLDEATSALDAEservVQ----DALdRVMVNR---TTIVVAHRLSTIKG-ADMIAVLKEGKIAEKG 1268
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVS----VQarllDLL-RGLVRElglAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1049-1268 |
2.47e-10 |
|
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: 64.44 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPsrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERF--YDPDSGNI--------SLDGVEIRSL 1118
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalceKCGYVERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1119 KVSWLRDQMGLVGQEPVLF---NDTIRANITygKHSEVTEEEITAVAKAANAHEFV-SSLPQ-GYDtvvGEKGVQ----- 1188
Cdd:TIGR03269 78 VGEPCPVCGGTLEPEEVDFwnlSDKLRRRIR--KRIAIMLQRTFALYGDDTVLDNVlEALEEiGYE---GKEAVGravdl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1189 ----------------LSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRLSTI 1250
Cdd:TIGR03269 153 iemvqlshrithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVI 232
|
250
....*....|....*....
gi 1443040382 1251 -KGADMIAVLKEGKIAEKG 1268
Cdd:TIGR03269 233 eDLSDKAIWLENGEIKEEG 251
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1053-1257 |
3.68e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.83 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1053 NVSFKYPSRpdvQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKV-SWLRDQMGLVG 1131
Cdd:PRK10895 8 NLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1132 QEPVLFndtiRANITYGKHSEVTE--EEITAVAKAANAHEFVSSLPQGYdtVVGEKGVQLSGGQKQRVAIARAILKDPKI 1209
Cdd:PRK10895 85 QEASIF----RRLSVYDNLMAVLQirDDLSAEQREDRANELMEEFHIEH--LRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1210 LLLDEATSALDAES----ERVVQDALDR---VMVN----RTTIVVAHRLSTIKGADMIA 1257
Cdd:PRK10895 159 ILLDEPFAGVDPISvidiKRIIEHLRDSglgVLITdhnvRETLAVCERAYIVSQGHLIA 217
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
370-584 |
4.03e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.11 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVL--------------IDGIS 435
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 436 IkklrldwirgkiglvSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFidklpngydtlvgqrgtQLSGGQKQ 515
Cdd:PLN03073 587 L---------------SSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMY-----------------TLSGGQKS 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 516 RIAIARAILKDPKILLLDEATSALDVES-ERIVQEALnrmMVERTTLVVAHRLSTVR-NVDCITVVRKGKI 584
Cdd:PLN03073 635 RVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQGLV---LFQGGVLMVSHDEHLISgSVDELWVVSEGKV 702
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
729-984 |
6.65e-10 |
|
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: 61.59 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 729 DQLRKDSRFWALMSVVLGVaCLISIPAEYF------LFGIAGGKLIQRVRTLSFQRIMHQEVAWFDKpsnsrcatlmyfc 802
Cdd:cd18590 24 DILGGEYQHNAFTSAIGLM-CLFSLGSSLSaglrggLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEK------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 803 yfifyKKiftfkpmlrghlisySGALGTRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLV 882
Cdd:cd18590 90 -----TK---------------TGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 883 GAqgyAQVKFLKGFSEESKEMYE---DANQVAADAVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFS 959
Cdd:cd18590 150 AI---AQKVYNTYHQKLSQAVQDsiaKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVR 226
|
250 260
....*....|....*....|....*
gi 1443040382 960 NLMLYLTYGLCFYVGAKFVSQGKTT 984
Cdd:cd18590 227 RVLQLGVQVLMLYCGRQLIQSGHLT 251
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1069-1250 |
6.92e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.44 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1069 DFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIR-SLK---VSWLRDQMGLVGQEPVLFNDTIRAN 1144
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqALQknlVAYVPQSEEVDWSFPVLVEDVVMMG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1145 iTYGKHSEVTEEEITAVAKAANAHEFVSSLPQGYDTVvGEkgvqLSGGQKQRVAIARAILKDPKILLLDEATSALDAESE 1224
Cdd:PRK15056 105 -RYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQI-GE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180
....*....|....*....|....*..
gi 1443040382 1225 RVVQDALDRVMVN-RTTIVVAHRLSTI 1250
Cdd:PRK15056 179 ARIISLLRELRDEgKTMLVSTHNLGSV 205
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
387-595 |
7.39e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.96 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 387 ILDGLSLQVASGTTMAIVGESGSGKSTVISLV--ERFYDPQSGEVLIDGISIKKLRLDWIRGK-IGLVSQEPL------- 456
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGEgIFMAFQYPVeipgvsn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 457 -LFMASIKDNIiygKKDATLEEIKRAaelaNAANFID------KLPNgyDTLVGQRGTQLSGGQKQRIAIARAILKDPKI 529
Cdd:PRK09580 96 qFFLQTALNAV---RSYRGQEPLDRF----DFQDLMEekiallKMPE--DLLTRSVNVGFSGGEKKRNDILQMAVLEPEL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 530 LLLDEATSALDVESERIVQEALNRMMVE-RTTLVVAH--RLSTVRNVDCITVVRKGKIVEQGPHdALVK 595
Cdd:PRK09580 167 CILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF-TLVK 234
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
738-987 |
7.70e-10 |
|
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: 61.68 E-value: 7.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 738 WALMSVVLGVACLISIpaEYFLFGIAGGKLIQRVRTLSFQRIMHQEVAWFDKpsnsrcatlmyfcyfifykkiftfkpml 817
Cdd:cd18551 40 ALLVALFLLQAVLSAL--SSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDR---------------------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 818 rghliSYSGALGTRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFS 897
Cdd:cd18551 90 -----RRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKAS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 898 EESKEMYEDANQVAADAVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKF 977
Cdd:cd18551 165 KRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGAR 244
|
250
....*....|
gi 1443040382 978 VSQGKTTFSD 987
Cdd:cd18551 245 VASGALTVGT 254
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1066-1233 |
1.14e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.43 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1066 IFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRD------QMG----LVGQEPV 1135
Cdd:PRK13538 16 LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllylghQPGikteLTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1136 LFNDTIranitygkHSEVTEEEITAVAKAANAHEFVsslpqgyDTVVGekgvQLSGGQKQRVAIARAILKDPKILLLDEA 1215
Cdd:PRK13538 96 RFYQRL--------HGPGDDEALWEALAQVGLAGFE-------DVPVR----QLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170
....*....|....*...
gi 1443040382 1216 TSALDAESERVVQDALDR 1233
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQ 174
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1087-1265 |
1.22e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 62.34 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1087 GSGKSTIIALLERFYDPDSGNISLDG--VEIRSLKVSwLRDQMGLV----GQEPVLFNDTIRANIT------YGKHSEVT 1154
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDA-IRAGIAYVpedrKGEGLVLDLSIRENITlasldrLSRGGLLD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1155 EEEITAVAKaanahEFVSSL---PQGYDTVVGekgvQLSGGQKQRVAIARAILKDPKILLLDEATSALD--AESE--RVV 1227
Cdd:COG1129 367 RRRERALAE-----EYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAEiyRLI 437
|
170 180 190
....*....|....*....|....*....|....*....
gi 1443040382 1228 QDALDRvmvNRTTIVVAHRLSTIKG-ADMIAVLKEGKIA 1265
Cdd:COG1129 438 RELAAE---GKAVIVISSELPELLGlSDRILVMREGRIV 473
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1066-1246 |
1.51e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1066 IFSDFTLHIPSQKTIALVGESGSGKSTII-ALLERFYD-PDSGNISLDGVEIRSLKVswLRDQMGLVGQepvlFNDTIra 1143
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLrLLAGALKGtPVAGCVDVPDNQFGREAS--LIDAIGRKGD----FKDAV-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1144 nitygkhsevteeEITAVAKAANAHEFVSSlpqgYDtvvgekgvQLSGGQKQRVAIARAILKDPKILLLDEATSALDAES 1223
Cdd:COG2401 117 -------------ELLNAVGLSDAVLWLRR----FK--------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|....*..
gi 1443040382 1224 ERVV----QDALDRvmVNRTTIVVAHR 1246
Cdd:COG2401 172 AKRVarnlQKLARR--AGITLVVATHH 196
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
373-568 |
2.49e-09 |
|
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: 59.69 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 373 KDVYFRYParPEQLILDGLSLqVASGTTMAIVGESGSGKSTVISLVE--------RFYDPQSGEVLIDG-------ISIK 437
Cdd:cd03236 4 DEPVHRYG--PNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDEfrgselqNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 438 KLRLDWIRgkiglVSQEPllfmaSIKDNIIYGKKDATLEEIKRAAELANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRI 517
Cdd:cd03236 81 KLLEGDVK-----VIVKP-----QYVDLIPKAVKGKVGELLKKKDERGKLDELVDQL--ELRHVLDRNIDQLSGGELQRV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 518 AIARAILKDPKILLLDEATSALDVEsERIVQEALNRMMVE--RTTLVVAHRLS 568
Cdd:cd03236 149 AIAAALARDADFYFFDEPSSYLDIK-QRLNAARLIRELAEddNYVLVVEHDLA 200
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1066-1273 |
2.78e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1066 IFSDFTLHIPSQKTIALVGESGSGKSTII-ALLERFYDPD-SGNISLDGveiRSLKVSWLRdQMGLVGQEPVLF-NDTIR 1142
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLnALAGRIQGNNfTGTILANN---RKPTKQILK-RTGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1143 ANITYGK----HSEVTEEEITAVAKAANAHefvSSLPQGYDTVVGEKGVQ-LSGGQKQRVAIARAILKDPKILLLDEATS 1217
Cdd:PLN03211 159 ETLVFCSllrlPKSLTKQEKILVAESVISE---LGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1218 ALDAESE-RVVQDALDRVMVNRTTIVVAHRLST--IKGADMIAVLKEGKIAEKGK-HEAL 1273
Cdd:PLN03211 236 GLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKgSDAM 295
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
388-565 |
3.07e-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: 61.34 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGT-----TMAIVGESGSGKSTVISLVERFYDPQSGEVlidgisIKKLRLdwirgkiglvsqepllfmaSI 462
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLKI-------------------SY 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 463 KDNIIYGKKDATLEEIKRAA------------ELANAANfIDKLpngYDTLVgqrgTQLSGGQKQRIAIARAILKDPKIL 530
Cdd:COG1245 406 KPQYISPDYDGTVEEFLRSAntddfgssyyktEIIKPLG-LEKL---LDKNV----KDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190
....*....|....*....|....*....|....*..
gi 1443040382 531 LLDEATSALDVESERIVQEALNRMMVER--TTLVVAH 565
Cdd:COG1245 478 LLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDH 514
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
388-539 |
3.88e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.74 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKklrlDW-----IRGKIGLVSQEPLLFM-AS 461
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT----DWqtakiMREAVAIVPEGRRVFSrMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 462 IKDNIIYG----KKDATLEEIKRAAELanaanfidkLPNGYDTLVgQRGTQLSGGQKQRIAIARAILKDPKILLLDEATS 537
Cdd:PRK11614 97 VEENLAMGgffaERDQFQERIKWVYEL---------FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSL 166
|
..
gi 1443040382 538 AL 539
Cdd:PRK11614 167 GL 168
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1062-1263 |
4.13e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.57 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1062 PDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDS--GNISLDG--VEIRSLKVSwlrDQMGLV--GQE-- 1133
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevCRFKDIRDS---EALGIViiHQEla 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1134 --PVLfndTIRANITYG----KHSEVTEEEITAVAKAANAHEFVSSLPqgyDTVVGEKGVqlsgGQKQRVAIARAILKDP 1207
Cdd:NF040905 89 liPYL---SIAENIFLGneraKRGVIDWNETNRRARELLAKVGLDESP---DTLVTDIGV----GKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1208 KILLLDEATSAL-DAESERVvqdaLDRVMVNR----TTIVVAHRLSTI-KGADMIAVLKEGK 1263
Cdd:NF040905 159 KLLILDEPTAALnEEDSAAL----LDLLLELKaqgiTSIIISHKLNEIrRVADSITVLRDGR 216
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1028-1251 |
4.51e-09 |
|
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: 60.92 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1028 RKSRIDSSSDEGAIMENVTGS---------IDFNNVSFKYPSRpDVQIfSDFTLHIPSQKTIALVGESGSGKSTIIALLE 1098
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVPGRgiveyqdngIKFENIPLVTPNG-DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILG 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1099 RFYDPDSGNISLDGveirslkvswlRDQMGLVGQEPVLFNDTIRANITYGKHSE------VTEEEITAVAKAANAHEFVS 1172
Cdd:TIGR00954 500 ELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQIIYPDSSEdmkrrgLSDKDLEQILDNVQLTHILE 568
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1173 SlPQGYDTVVGEKGVqLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRvmVNRTTIVVAHRLSTIK 1251
Cdd:TIGR00954 569 R-EGGWSAVQDWMDV-LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKSLWK 643
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
695-989 |
4.96e-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: 58.94 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 695 VLLLGSIAASVhgvILP-LYGIIMPGVLKSFYEPPDQLRkdsRFWALMSVVLGVACLISIpAEYFLFGIAGGKLIQRVRT 773
Cdd:cd18544 6 LLLLLATALEL---LGPlLIKRAIDDYIVPGQGDLQGLL---LLALLYLGLLLLSFLLQY-LQTYLLQKLGQRIIYDLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 774 LSFQRIMHQEVAWFDK-PSnsrcatlmyfcyfifykkiftfkpmlrghlisysGALGTRLSVDALNVRRLVGDNLALIVQ 852
Cdd:cd18544 79 DLFSHIQRLPLSFFDRtPV----------------------------------GRLVTRVTNDTEALNELFTSGLVTLIG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 853 AVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSIRTVASFCSEKRVVA 932
Cdd:cd18544 125 DLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFE 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 933 IYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGKTTFSDVF 989
Cdd:cd18544 205 EFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLY 261
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
388-596 |
5.30e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIK-KLRLDWIRGKIGLVSQE-PLLFMASIKDN 465
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 466 II---YGKKDATLEEIKRAAElanAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALdve 542
Cdd:PRK10982 94 MWlgrYPTKGMFVDQDKMYRD---TKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL--- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 543 SERIVQEALN--RMMVERTTLVV--AHRLSTVRNV-DCITVVRKGKIVEQGPHDALVKD 596
Cdd:PRK10982 166 TEKEVNHLFTiiRKLKERGCGIVyiSHKMEEIFQLcDEITILRDGQWIATQPLAGLTMD 224
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
45-326 |
7.86e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 58.65 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 45 VLLMVVGTVGAlgnGISQPLmtvLFGNVINS--FGANtsgsvLRSVTKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSA 122
Cdd:cd18550 4 VLLLILLSALL---GLLPPL---LLREIIDDalPQGD-----LGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 123 RIRSLYLKAVLRQDITFFdTEMTTGEAVSRMSSDTLLIQGALGekgGKLVELLSSFIG---GFIIAFTRGWLLTLVMLTS 199
Cdd:cd18550 73 DLRVQLYAHLQRMSLAFF-TRTRTGEIQSRLNNDVGGAQSVVT---GTLTSVVSNVVTlvaTLVAMLALDWRLALLSLVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 200 LPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQT--IGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIItGFGM 277
Cdd:cd18550 149 LPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALA-GRWF 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 278 GSVMCVVFG-SYGLAFWYGGKLIIEKGYTGGKI--MTILFAVLTG-ASSLGNA 326
Cdd:cd18550 228 FAALGLFTAiGPALVYWVGGLLVIGGGLTIGTLvaFTALLGRLYGpLTQLLNI 280
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
397-558 |
9.21e-09 |
|
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: 55.46 E-value: 9.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 397 SGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLDWIRGKIglvsqepllfmasikdniiygkkdatle 476
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLI---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 477 eikraaelanaanfidklpngydtLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMV 556
Cdd:smart00382 53 ------------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
..
gi 1443040382 557 ER 558
Cdd:smart00382 109 LL 110
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
381-555 |
9.24e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.17 E-value: 9.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 381 ARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKklRLDWIRgKIGLVSQEPLLfma 460
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT--RGDRSR-FMAYLGHLPGL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 461 sikdniiygKKD-ATLEEI--------KRAAELANAANFIDKLPNGYDTLVgqrgTQLSGGQKQRIAIARAILKDPKILL 531
Cdd:PRK13543 94 ---------KADlSTLENLhflcglhgRRAKQMPGSALAIVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWL 160
|
170 180
....*....|....*....|....
gi 1443040382 532 LDEATSALDVESERIVqealNRMM 555
Cdd:PRK13543 161 LDEPYANLDLEGITLV----NRMI 180
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1049-1232 |
9.64e-09 |
|
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: 59.56 E-value: 9.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRPdvqIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISL-DGVeirslkvswlrdQM 1127
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV------------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1128 GLVGQepvlFNDTIRANITygkhseVTEE-----EITAVAKAA-NAHEFVSSLP-QGYDTvvgEKGV-QLSGGQKQRVAI 1199
Cdd:TIGR03719 388 AYVDQ----SRDALDPNKT------VWEEisgglDIIKLGKREiPSRAYVGRFNfKGSDQ---QKKVgQLSGGERNRVHL 454
|
170 180 190
....*....|....*....|....*....|...
gi 1443040382 1200 ARAILKDPKILLLDEATSALDAESERVVQDALD 1232
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
371-592 |
1.46e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 371 ELKDVYFRYPARpeqLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIdGISIKKLRLDWIRgkigl 450
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQHR----- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 451 vsqEPLLFMASIKDNIIYGKKDATLEEIKRAAeLANAANFIDKlPNGYDTLVgqrgTQLSGGQKQRIAIARAILKDPKIL 530
Cdd:PRK11147 392 ---AELDPEKTVMDNLAEGKQEVMVNGRPRHV-LGYLQDFLFH-PKRAMTPV----KALSGGERNRLLLARLFLKPSNLL 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 531 LLDEATSALDVESERIVQEALNRMmvERTTLVVAHRLSTVRNV--DCITVVRKGKIVE--QGPHDA 592
Cdd:PRK11147 463 ILDEPTNDLDVETLELLEELLDSY--QGTVLLVSHDRQFVDNTvtECWIFEGNGKIGRyvGGYHDA 526
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1060-1263 |
1.48e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1060 SRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEI--RSLK------VSWLRDQMGLVG 1131
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKealengISMVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1132 QEPVLfndtirANITYGKHSE----VTEEEITAVAKAANAHEFVSSLPQgydtvvgEKGVQLSGGQKQRVAIARAILKDP 1207
Cdd:PRK10982 87 QRSVM------DNMWLGRYPTkgmfVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 1208 KILLLDEATSALdaeSERVVQDALD--RVMVNR--TTIVVAHRLSTI-KGADMIAVLKEGK 1263
Cdd:PRK10982 154 KIVIMDEPTSSL---TEKEVNHLFTiiRKLKERgcGIVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
476-567 |
1.59e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 476 EEIKRAAELANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVEsERI-VQEALNRM 554
Cdd:PRK13409 182 ELLKKVDERGKLDEVVERL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR-QRLnVARLIREL 258
|
90
....*....|...
gi 1443040382 555 MVERTTLVVAHRL 567
Cdd:PRK13409 259 AEGKYVLVVEHDL 271
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
825-988 |
1.60e-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: 57.41 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 825 SGALGTRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMY 904
Cdd:cd18548 95 TSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 905 EDANQVAADAVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGKTT 984
Cdd:cd18548 175 DRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQ 254
|
....
gi 1443040382 985 FSDV 988
Cdd:cd18548 255 VGDL 258
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1049-1264 |
1.63e-08 |
|
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: 56.12 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSF-KYPSRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALL----ERFYDPdSGNISLDGVEIRSLKVSWL 1123
Cdd:cd03233 4 LSWRNISFtTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrtEGNVSV-EGDIHYNGIPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1124 RDQMgLVGQEPVLFndtirANITygkhsevTEEEITAVAKAaNAHEFVsslpqgydtvvgeKGVqlSGGQKQRVAIARAI 1203
Cdd:cd03233 83 GEII-YVSEEDVHF-----PTLT-------VRETLDFALRC-KGNEFV-------------RGI--SGGERKRVSIAEAL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1204 LKDPKILLLDEATSALDAEServvqdALDRVMVNRtTIVVAHRLSTIKGA-----------DMIAVLKEGKI 1264
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSST------ALEILKCIR-TMADVLKTTTFVSLyqasdeiydlfDKVLVLYEGRQ 198
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
354-543 |
1.76e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.35 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 354 DSDDNNGMVLEDMN--GDI-ELKDVYFRYPARPEQL-ILDGLSLQVASGTTMAIVGESGSGKSTVIS-LVERfydpQSGE 428
Cdd:TIGR00956 741 ESDDVNDEKDMEKEsgEDIfHWRNLTYEVKIKKEKRvILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAER----VTTG 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 429 VLIDGISI---KKLRLDWIRgKIGLVSQEPL-LFMASIKDNIIYG------------KKDATLEEIKRAAELANAAnfid 492
Cdd:TIGR00956 817 VITGGDRLvngRPLDSSFQR-SIGYVQQQDLhLPTSTVRESLRFSaylrqpksvsksEKMEYVEEVIKLLEMESYA---- 891
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 493 klpngyDTLVGQRGTQLSGGQKQRIAIARAILKDPKILL-LDEATSALDVES 543
Cdd:TIGR00956 892 ------DAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
345-541 |
2.04e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.26 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 345 KTIE----RKPEIDSDD-NNGMVLEDMN----------GDI--ELKDVYFRYPARPEQLILDGLSLQVASGTTMAIVGES 407
Cdd:NF040905 216 RTIEtldcRADEVTEDRiIRGMVGRDLEdrypertpkiGEVvfEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLM 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 408 GSGKSTV-ISLVERFYDPQ-SGEVLIDG--ISIKKLRlDWIRGKIGLVSQEP----LLFMASIKDNIIYgkkdATLEEIK 479
Cdd:NF040905 296 GAGRTELaMSVFGRSYGRNiSGTVFKDGkeVDVSTVS-DAIDAGLAYVTEDRkgygLNLIDDIKRNITL----ANLGKVS 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 480 RA------AELANAANFIDKL----PNgydtlVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDV 541
Cdd:NF040905 371 RRgvidenEEIKVAEEYRKKMniktPS-----VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1188-1275 |
2.11e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.44 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1188 QLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMV--NRTTIVVAHRLSTI-KGADMIAVLKEGKI 1264
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYAGQV 232
|
90
....*....|.
gi 1443040382 1265 AEKGKHEALLR 1275
Cdd:PRK11022 233 VETGKAHDIFR 243
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
134-298 |
2.13e-08 |
|
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: 57.07 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 134 RQDITFFDtEMTTGEAVSRMSSDTLLIqgalgekgGKLV-----ELLSS---FIGGFIIAFTRGWLLTLVMLTSLPLIAI 205
Cdd:cd18549 87 KLSFSFFD-NNKTGQLMSRITNDLFDI--------SELAhhgpeDLFISiitIIGSFIILLTINVPLTLIVFALLPLMII 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 206 ASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIA-------MYRNFIKKSYKATIEEGIITGF--G 276
Cdd:cd18549 158 FTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEkfdegndRFLESKKKAYKAMAYFFSGMNFftN 237
|
170 180
....*....|....*....|..
gi 1443040382 277 MGSVMCVVFGSYglaFWYGGKL 298
Cdd:cd18549 238 LLNLVVLVAGGY---FIIKGEI 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
371-584 |
2.17e-08 |
|
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: 58.30 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 371 ELKDVYFR-------YPARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQ-SGEVLIDG--ISIKKLr 440
Cdd:TIGR02633 252 EIGDVILEarnltcwDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNP- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 441 LDWIRGKIGLVSQE-------PLLfmaSIKDNIIYG--KKDATLEEIKRAAELANAANFIDKL---PNGYDTLVGQrgtq 508
Cdd:TIGR02633 331 AQAIRAGIAMVPEDrkrhgivPIL---GVGKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLkvkTASPFLPIGR---- 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 509 LSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTTL-VVAHRLSTVRNV-DCITVVRKGKI 584
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIiVVSSELAEVLGLsDRVLVIGEGKL 481
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
388-606 |
2.93e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.12 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLV------------ERFYdpqsgevlIDGISIKKL----RLDWIRGKIGLV 451
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnwrvtaDRMR--------FDDIDLLRLspreRRKLVGHNVSMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 452 SQEP---LLFMASIKDNIIYGKKDATLE---------EIKRAAELANAANFIDklpngYDTLVGQRGTQLSGGQKQRIAI 519
Cdd:PRK15093 95 FQEPqscLDPSERVGRQLMQNIPGWTYKgrwwqrfgwRKRRAIELLHRVGIKD-----HKDAMRSFPYELTEGECQKVMI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 520 ARAILKDPKILLLDEATSALDVESERIVQEALNRMMVERTT--LVVAHRLSTVRN-VDCITVVRKGKIVEQGPHDALVKD 596
Cdd:PRK15093 170 AIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTtiLLISHDLQMLSQwADKINVLYCGQTVETAPSKELVTT 249
|
250
....*....|.
gi 1443040382 597 PDGAYSQ-LIR 606
Cdd:PRK15093 250 PHHPYTQaLIR 260
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
380-541 |
3.27e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 380 PARPEQLILDGLSLQVASGTTMAIVGESGSGKS-TVISLVERFYDPQSGEVLIDG--ISIKKLRlDWIRGKIGLVSQE-- 454
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGkpVKIRNPQ-QAIAQGIAMVPEDrk 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 455 -----PLLfmaSIKDNIiygkkdaTLEEIKR---------AAELANAANFIDKL------PNgydtlvgQRGTQLSGGQK 514
Cdd:PRK13549 349 rdgivPVM---GVGKNI-------TLAALDRftggsriddAAELKTILESIQRLkvktasPE-------LAIARLSGGNQ 411
|
170 180
....*....|....*....|....*..
gi 1443040382 515 QRIAIARAILKDPKILLLDEATSALDV 541
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
370-565 |
3.43e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.59 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARPeqlILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVlidgisikklrlDWirgkig 449
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KW------ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 lvsqepllfmaSIKDNIIYGKKDatleeikRAAELANAANFID-----KLPNGYDTLVgqRGT----------------Q 508
Cdd:PRK15064 379 -----------SENANIGYYAQD-------HAYDFENDLTLFDwmsqwRQEGDDEQAV--RGTlgrllfsqddikksvkV 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 509 LSGGQKQRIAIARAILKDPKILLLDEATSALDVESerIvqEALNRM--MVERTTLVVAH 565
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES--I--ESLNMAleKYEGTLIFVSH 493
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1049-1214 |
3.98e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.67 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSrpdvQIFS----DFTLHipSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLR 1124
Cdd:PRK10522 323 LELRNVTFAYQD----NGFSvgpiNLTIK--RGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1125 DQMGLVGQEPVLFNDTIRanitygkhSEVTEEEITAVAKAANAHEFVSSLpqgydTVVGEK--GVQLSGGQKQRVAIARA 1202
Cdd:PRK10522 397 KLFSAVFTDFHLFDQLLG--------PEGKPANPALVEKWLERLKMAHKL-----ELEDGRisNLKLSKGQKKRLALLLA 463
|
170
....*....|..
gi 1443040382 1203 ILKDPKILLLDE 1214
Cdd:PRK10522 464 LAEERDILLLDE 475
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
43-317 |
4.14e-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: 56.25 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 43 LDVLLMVVGTVGALGngisQPLMTvlfGNVINSFGANTSGSVlrsVTKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSA 122
Cdd:cd18548 3 LAPLFKLLEVLLELL----LPTLM---ADIIDEGIANGDLSY---ILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 123 RIRS-LYLKaVLRQDITFFDtEMTTGEAVSRMSSDTLLIQGALGekgGKLVELLSS---FIGGFIIAFTRGWLLTLVMLT 198
Cdd:cd18548 73 DLRKdLFEK-IQSFSFAEID-KFGTSSLITRLTNDVTQVQNFVM---MLLRMLVRApimLIGAIIMAFRINPKLALILLV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 199 SLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFGMG 278
Cdd:cd18548 148 AIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNP 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1443040382 279 SVMCVVFGSYGLAFWYGGKLIIEKGYTGGKI-------MTILFAVL 317
Cdd:cd18548 228 LMMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILMSLM 273
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
825-984 |
4.17e-08 |
|
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: 56.27 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 825 SGALGTRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMY 904
Cdd:cd18541 96 TGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 905 EDANQVAADAVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGKTT 984
Cdd:cd18541 176 SDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTIT 255
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
695-984 |
5.09e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 55.98 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 695 VLLLGSIAASVHGVILP-LYGIIMPGVLKsfyeppdQLRKDSRFWALMSVVLGvacLISIPAEYFLFGIA--------GG 765
Cdd:cd18563 3 LGFLLMLLGTALGLVPPyLTKILIDDVLI-------QLGPGGNTSLLLLLVLG---LAGAYVLSALLGILrgrllarlGE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 766 KLIQRVRTLSFQRIMHQEVAWFDKPSnsrcatlmyfcyfifykkiftfkpmlrghlisySGALGTRLSVDALNVRRLVGD 845
Cdd:cd18563 73 RITADLRRDLYEHLQRLSLSFFDKRQ---------------------------------TGSLMSRVTSDTDRLQDFLSD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 846 NLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSIRTVASFC 925
Cdd:cd18563 120 GLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFG 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 926 SEKRVVAIYNKKCEALRKQGIRsgiVGGIGLSFSNLMLYLTYGLCF---YVGAKFVSQGKTT 984
Cdd:cd18563 200 QEKREIKRFDEANQELLDANIR---AEKLWATFFPLLTFLTSLGTLivwYFGGRQVLSGTMT 258
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
478-569 |
5.27e-08 |
|
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: 57.10 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 478 IKRAAELANAANFIDKLpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVeSERI-VQEALNRMMV 556
Cdd:COG1245 184 LEKVDERGKLDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI-YQRLnVARLIRELAE 260
|
90
....*....|....
gi 1443040382 557 E-RTTLVVAHRLST 569
Cdd:COG1245 261 EgKYVLVVEHDLAI 274
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1082-1275 |
6.47e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.32 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1082 LVGESGSGKSTIIA----LLerfydPDSGNISLDGVEIRSLKVSWLRDQMG-LVGQEPVLFNDTIRANITYGKHSEVTEE 1156
Cdd:PRK03695 27 LVGPNGAGKSTLLArmagLL-----PGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVFQYLTLHQPDKTRTE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1157 EITAVAkaanaHEFVSSLpqGYDTVVGEKGVQLSGGQKQRVAIARAILK-------DPKILLLDEATSALDaeserVVQD 1229
Cdd:PRK03695 102 AVASAL-----NEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD-----VAQQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 1230 -ALDRVMV-----NRTTIVVAHRLS-TIKGADMIAVLKEGKIAEKGKHEALLR 1275
Cdd:PRK03695 170 aALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1060-1222 |
7.10e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.47 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1060 SRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEI----RSLKVSWLRDQMGLVGQEPV 1135
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAtrgdRSRFMAYLGHLPGLKADLST 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1136 LFNDTIrANITYGKHSEVTEEEITAVAKAANaHEfvsslpqgyDTVVGekgvQLSGGQKQRVAIARAILKDPKILLLDEA 1215
Cdd:PRK13543 100 LENLHF-LCGLHGRRAKQMPGSALAIVGLAG-YE---------DTLVR----QLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
....*..
gi 1443040382 1216 TSALDAE 1222
Cdd:PRK13543 165 YANLDLE 171
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1047-1262 |
7.11e-08 |
|
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: 54.17 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1047 GSIDFNNVSFKYPS-RPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALL-ERFYDPD-SGNISLDGveiRSLKVSWL 1123
Cdd:cd03232 2 SVLTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILING---RPLDKNFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1124 RdQMGLVGQEPVLF-NDTIRANITYgkhsevteeeitavakaanahefvSSLPQGydtvvgekgvqLSGGQKQRVAIARA 1202
Cdd:cd03232 79 R-STGYVEQQDVHSpNLTVREALRF------------------------SALLRG-----------LSVEQRKRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 1203 ILKDPKILLLDEATSALDAESERVVQDALDRV-MVNRTTIVVAHRLS--TIKGADMIAVLKEG 1262
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1067-1257 |
7.16e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 7.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1067 FSDFTLHIPSQ-KTIALVGESGSGKSTIIALLerfydpdSGNI--SLDGVEIrslKVSWlrdqmglvgqEPVLfnDTIRA 1143
Cdd:PRK13409 88 FKLYGLPIPKEgKVTGILGPNGIGKTTAVKIL-------SGELipNLGDYEE---EPSW----------DEVL--KRFRG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1144 NITYGKHSEVTEEEITAVAKAanahEFVSSLPQGYDTVVG-------EKGV-------------------QLSGGQKQRV 1197
Cdd:PRK13409 146 TELQNYFKKLYNGEIKVVHKP----QYVDLIPKVFKGKVRellkkvdERGKldevverlglenildrdisELSGGELQRV 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 1198 AIARAILKDPKILLLDEATSALDAEsERV-VQDALDRVMVNRTTIVVAHRLSTIkgaDMIA 1257
Cdd:PRK13409 222 AIAAALLRDADFYFFDEPTSYLDIR-QRLnVARLIRELAEGKYVLVVEHDLAVL---DYLA 278
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
386-620 |
8.08e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 386 LILDGLSLQvaSGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLRLD---------WIRGKIGLVSQEPL 456
Cdd:PRK10938 19 LQLPSLTLN--AGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEqlqklvsdeWQRNNTDMLSPGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 457 LFMASIKDNIIYGKKDATleeikRAAELAnaANFidklpnGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEAT 536
Cdd:PRK10938 97 DTGRTTAEIIQDEVKDPA-----RCEQLA--QQF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 537 SALDVESERIVQEALNRMMVERTTLV-VAHRLSTVRN-VDCITVVRKGKIVEQGPHDALVKdpDGAYSQL--------IR 606
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ--QALVAQLahseqlegVQ 241
|
250
....*....|....*
gi 1443040382 607 LQET-HRDERHKLPD 620
Cdd:PRK10938 242 LPEPdEPSARHALPA 256
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1066-1275 |
8.48e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.22 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1066 IFSDFTLHIPSQKTIALVGESGSGKSTII-ALLERFYDPD-------SGNISLDG---VEIRSLKVSWLRDQMGLVGQEP 1134
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGaprgarvTGDVTLNGeplAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1135 VLFndTIRANITYGKHSEV-----TEEEITAVAKAANAHefvsslpQGYDTVVGEKGVQLSGGQKQRVAIARAILK---- 1205
Cdd:PRK13547 96 FAF--SAREIVLLGRYPHArragaLTHRDGEIAWQALAL-------AGATALVGRDVTTLSGGELARVQFARVLAQlwpp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1206 -----DPKILLLDEATSALDAESERVVQDALDRVM----VNRTTIVVAHRLSTiKGADMIAVLKEGKIAEKGKHEALLR 1275
Cdd:PRK13547 167 hdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwnLGVLAIVHDPNLAA-RHADRIAMLADGAIVAHGAPADVLT 244
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1063-1268 |
8.82e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1063 DVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERF--YDPDSGNISLDGVEIRSLKVSwLRDQMG--LVGQEPVLFN 1138
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGifLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1139 -----DTIRanITY-GKHSEVTEEEITAVakaanahEFVSSLPQGYDtVVGEKGVQL--------SGGQKQRVAIARAIL 1204
Cdd:CHL00131 98 gvsnaDFLR--LAYnSKRKFQGLPELDPL-------EFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKKRNEILQMAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1205 KDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIV-VAH--RLSTIKGADMIAVLKEGKIAEKG 1268
Cdd:CHL00131 168 LDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTG 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
370-551 |
1.05e-07 |
|
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: 56.10 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 370 IELKDVYFRYPARpeqLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIdGISIKKLRLDWIRGKIG 449
Cdd:TIGR03719 323 IEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 450 ---LVSQEpllfMASIKDNIIYGKKdatleEIKRAAELAnAANFidklpNGYD--TLVGQrgtqLSGGQKQRIAIARAIL 524
Cdd:TIGR03719 399 pnkTVWEE----ISGGLDIIKLGKR-----EIPSRAYVG-RFNF-----KGSDqqKKVGQ----LSGGERNRVHLAKTLK 459
|
170 180
....*....|....*....|....*..
gi 1443040382 525 KDPKILLLDEATSALDVESERIVQEAL 551
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEAL 486
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
329-591 |
1.71e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 329 AVAAVVEGQS----AAYNLFKTIERKPEIDSDDNNGMVLEDMNGDIelkdvyfrypaRPEQLILdglslqvasgttmaIV 404
Cdd:TIGR00956 39 GVAADSDYQPtfpnALLKILTRGFRKLKKFRDTKTFDILKPMDGLI-----------KPGELTV--------------VL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 405 GESGSGKST----VISLVERFYDPQSGEVLIDGIS---IKK-LRLDWIRgkIG--------LVSQEPLLFMASIKDNIIY 468
Cdd:TIGR00956 94 GRPGSGCSTllktIASNTDGFHIGVEGVITYDGITpeeIKKhYRGDVVY--NAetdvhfphLTVGETLDFAARCKTPQNR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 469 GKKDATLEEIKRAAELANAanfIDKLPNGYDTLVGQ---RGtqLSGGQKQRIAIARAILKDPKILLLDEATSALD----V 541
Cdd:TIGR00956 172 PDGVSREEYAKHIADVYMA---TYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDsataL 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 542 ESERIVQEALNrmMVERTTLVVAHRLS--TVRNVDCITVVRKGKIVEQGPHD 591
Cdd:TIGR00956 247 EFIRALKTSAN--ILDTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFGPAD 296
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
387-570 |
1.93e-07 |
|
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: 52.63 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 387 ILDGLSLQVASGTTMAIVGESGSGKSTVIS-LVERFYDPQ-SGEVLIDGISIKKLrldwIRGKIGLVSQEPLLFmasikd 464
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAGViTGEILINGRPLDKN----FQRSTGYVEQQDVHS------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 465 niiygkKDATLEEikraaelanAANFIDKLpngydtlvgqRGtqLSGGQKQRIAIARAILKDPKILLLDEATSALDVESE 544
Cdd:cd03232 92 ------PNLTVRE---------ALRFSALL----------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180
....*....|....*....|....*..
gi 1443040382 545 RIVQEALNRM-MVERTTLVVAHRLSTV 570
Cdd:cd03232 145 YNIVRFLKKLaDSGQAILCTIHQPSAS 171
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
818-988 |
2.09e-07 |
|
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: 54.33 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 818 RGHLISysgalgtRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGA-----QGYAQVKF 892
Cdd:cd18547 101 HGDIMS-------RVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLvtkfiAKRSQKYF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 893 LK---------GFSEESkemyedanqvaadaVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLML 963
Cdd:cd18547 174 RKqqkalgelnGYIEEM--------------ISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFIN 239
|
170 180
....*....|....*....|....*
gi 1443040382 964 YLTYGLCFYVGAKFVSQGKTTFSDV 988
Cdd:cd18547 240 NLGYVLVAVVGGLLVINGALTVGVI 264
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
825-969 |
2.16e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 54.03 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 825 SGALGTRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPL-------VGaqgyaqvKFLKGFS 897
Cdd:cd18550 95 TGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLfvlptrrVG-------RRRRKLT 167
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 898 EESKEMYEDANQVAAD--AVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVG-----GIGLSFSnLMLYLTYGL 969
Cdd:cd18550 168 REQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGrwffaALGLFTA-IGPALVYWV 245
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
43-256 |
2.18e-07 |
|
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: 54.03 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 43 LDVLLMVVGTVGALGNgisqPLmtvLFGNVINSFGANTSGSVLrsvTKVVLNFIYLGIGTSVASFLQVSCWTMAGER--Q 120
Cdd:cd18546 3 LALLLVVVDTAASLAG----PL---LVRYGIDSGVRAGDLGVL---LLAAAAYLAVVLAGWVAQRAQTRLTGRTGERllY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 121 SARIRSLylKAVLRQDITFFDTEmTTGEAVSRMSSD-----TLLIQGalgekggkLVELLSS---FIGGFIIAFTRGWLL 192
Cdd:cd18546 73 DLRLRVF--AHLQRLSLDFHERE-TSGRIMTRMTSDidalsELLQTG--------LVQLVVSlltLVGIAVVLLVLDPRL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 193 TLVMLTSLPLIAIASAVSAqaltRVSSKrqtSYSDAGDTVEQ-------TIGSIRTVVSFNGEKKAIAMYR 256
Cdd:cd18546 142 ALVALAALPPLALATRWFR----RRSSR---AYRRARERIAAvnadlqeTLAGIRVVQAFRRERRNAERFA 205
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1002-1245 |
2.45e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.90 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1002 VSQSSAlstNATKARdSAISIFSIIDrKSRID---SSSdegaimeNVTGSIDFN-------------NVSFKYPSRPdvq 1065
Cdd:PRK15064 269 VSRFSA---NASKAK-QATSRAKQID-KIKLEevkPSS-------RQNPFIRFEqdkklhrnaleveNLTKGFDNGP--- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1066 IFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGnisldgveirslKVSWlrdqmglvgqepvlfndTIRANI 1145
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG------------TVKW-----------------SENANI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1146 TY--GKHSEVTEEEITAVakaanahEFVS--SLPQGYDTVV----G---------EKGVQ-LSGGQKQRVAIARAILKDP 1207
Cdd:PRK15064 385 GYyaQDHAYDFENDLTLF-------DWMSqwRQEGDDEQAVrgtlGrllfsqddiKKSVKvLSGGEKGRMLFGKLMMQKP 457
|
250 260 270
....*....|....*....|....*....|....*...
gi 1443040382 1208 KILLLDEATSALDAESERVVQDALDrvMVNRTTIVVAH 1245
Cdd:PRK15064 458 NVLVMDEPTNHMDMESIESLNMALE--KYEGTLIFVSH 493
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
825-984 |
2.65e-07 |
|
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: 53.65 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 825 SGALGTRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAqvkflkgFSEESKEMY 904
Cdd:cd18546 95 SGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRW-------FRRRSSRAY 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 905 EDA-NQVAA------DAVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKF 977
Cdd:cd18546 168 RRArERIAAvnadlqETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWR 247
|
....*..
gi 1443040382 978 VSQGKTT 984
Cdd:cd18546 248 VAAGTLT 254
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
376-588 |
2.89e-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: 52.26 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 376 YFRYPARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVI----SLVERFYDPqSGEVLIDGISIKKLRLDWiRGKIGLV 451
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLkalaNRTEGNVSV-EGDIHYNGIPYKEFAEKY-PGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 452 SQEPLlFMASIkdniiygkkdaTLEEIKRAAELANAANFIdklpngydtlvgqRGtqLSGGQKQRIAIARAILKDPKILL 531
Cdd:cd03233 89 SEEDV-HFPTL-----------TVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 532 LDEATSALDVESerivqeALN-----RMM--VERTTLVVAhrLS-----TVRNVDCITVVRKGKIVEQG 588
Cdd:cd03233 142 WDNSTRGLDSST------ALEilkciRTMadVLKTTTFVS--LYqasdeIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
100-301 |
3.08e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 53.72 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 100 IGTSVASFLQVSCWTMAGERQSARIRSLYLKAVLRQDITFFDTEmTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFI 179
Cdd:cd18565 65 LLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDR-QTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 180 GGFIIAFTRGWLLTLVMLTSLPLIAIASAVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKkaiAMYRNFI 259
Cdd:cd18565 144 GIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAED---FERERVA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1443040382 260 KKS--YKATIEEGIITGFGMGSVMCVVFG-SYGLAFWYGGKLIIE 301
Cdd:cd18565 221 DASeeYRDANWRAIRLRAAFFPVIRLVAGaGFVATFVVGGYWVLD 265
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
509-583 |
3.45e-07 |
|
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: 51.80 E-value: 3.45e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 509 LSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNR--MMVERTTLVVAHRLSTVRNVDCITVVRKGK 583
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRlsEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
819-997 |
3.95e-07 |
|
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: 53.22 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 819 GHLISysgalgtRLSVDALNVRRLV--GDNLALIvqAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGF 896
Cdd:cd18549 99 GQLMS-------RITNDLFDISELAhhGPEDLFI--SIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 897 SEESKEMYEDANQVAADAVGSIRTVASFCSEKRVVAIYNKKCEAL---RKQGIR--SGIVGGIGLsFSNLMLYLTYGlcf 971
Cdd:cd18549 170 FRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFlesKKKAYKamAYFFSGMNF-FTNLLNLVVLV--- 245
|
170 180
....*....|....*....|....*.
gi 1443040382 972 yVGAKFVSQGKTTFSDvfkvFFALVL 997
Cdd:cd18549 246 -AGGYFIIKGEITLGD----LVAFLL 266
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1069-1275 |
4.24e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.55 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1069 DFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLKVSWLRdQMGLV-GQE-------PVLfnDT 1140
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfGQRsqlwwdlPAI--DS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1141 IRAN--ItYgkhsEVTEEEItavakAANAHEFVSSLPQG--YDTVVGekgvQLSGGQKQRVAIARAILKDPKILLLDEAT 1216
Cdd:COG4586 117 FRLLkaI-Y----RIPDAEY-----KKRLDELVELLDLGelLDTPVR----QLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1217 SALDAESERVVQDALDRvmVNR---TTIVVA-HRLSTIKG-ADMIAVLKEGKIAEKGKHEALLR 1275
Cdd:COG4586 183 IGLDVVSKEAIREFLKE--YNRergTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
388-589 |
5.52e-07 |
|
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: 52.62 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVIslVERFYdpQSGEVLIDGISIKKLRLDWIRG-----KIGLVSQEPL------ 456
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLI--NDTLY--PALARRLHLKKEQPGNHDRIEGlehidKVIVIDQSPIgrtprs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 457 --------------LFMASIKdniiyGKK--DATLE---EIKRAAELAN-----AANFIDKLPN-------------GYD 499
Cdd:cd03271 87 npatytgvfdeireLFCEVCK-----GKRynRETLEvryKGKSIADVLDmtveeALEFFENIPKiarklqtlcdvglGYI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 500 TLvGQRGTQLSGGQKQRIAIARAILK---DPKILLLDEATSALDVESERIVQEALNRmMVER--TTLVVAHRLSTVRNVD 574
Cdd:cd03271 162 KL-GQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQR-LVDKgnTVVVIEHNLDVIKCAD 239
|
250 260
....*....|....*....|.
gi 1443040382 575 CITV------VRKGKIVEQGP 589
Cdd:cd03271 240 WIIDlgpeggDGGGQVVASGT 260
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
825-997 |
6.24e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 52.54 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 825 SGALGTRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPL--VGAQGYAQvKFLKGFSEESKE 902
Cdd:cd18778 96 TGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFlaLGAWLYSK-KVRPRYRKVREA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 903 MyEDANQVAADAVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIglsFSNLMLYLT---YGLCFYVGAKFVS 979
Cdd:cd18778 175 L-GELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAI---FHPLMEFLTslgTVLVLGFGGRLVL 250
|
170
....*....|....*...
gi 1443040382 980 QGKTTFSDVFKVFFALVL 997
Cdd:cd18778 251 AGELTIGDLVAFLLYLGL 268
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
825-1006 |
6.71e-07 |
|
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: 52.47 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 825 SGALGTRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMY 904
Cdd:cd18589 92 TGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 905 EDANQVAADAVGSIRTVASFCSEKRVVAIYNKKCE---ALRKQGIRSGIVGGIGLSFSNLMLYLTyglCFYVGAKFVSQG 981
Cdd:cd18589 172 ARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQktyRLNKKEAAAYAVSMWTSSFSGLALKVG---ILYYGGQLVTAG 248
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1443040382 982 KTT-------------FSDVFKVFFAL---VLAAVGVSQSS 1006
Cdd:cd18589 249 TVSsgdlvtfvlyelqFTSAVEVLLSYypsVMKAVGSSEKI 289
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1082-1245 |
7.89e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1082 LVGESGSGKSTIIALLERFYDPDSGNISLDGVEirslKVSWLR-DQ-------------MG-----LVGQEpvlfNDTIR 1142
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDPNE----RLGKLRqDQfafeeftvldtviMGhtelwEVKQE----RDRIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1143 ANitygkhSEVTEEEITAVA--KAANAhEFvsslpQGY--DTVVGE--KGV------------QLSGGQKQRVAIARAIL 1204
Cdd:PRK15064 104 AL------PEMSEEDGMKVAdlEVKFA-EM-----DGYtaEARAGEllLGVgipeeqhyglmsEVAPGWKLRVLLAQALF 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1443040382 1205 KDPKILLLDEATSALDAESERVVQDAL-DRvmvNRTTIVVAH 1245
Cdd:PRK15064 172 SNPDILLLDEPTNNLDINTIRWLEDVLnER---NSTMIIISH 210
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
371-572 |
8.07e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.36 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 371 ELKDVYFRYPARPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDG----ISIKKlrldwirg 446
Cdd:PRK13545 23 KLKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGsaalIAISS-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 447 kiGLVSQEPLLFMASIKDNIIYGKKDATLEEIKRAAELANAANFIDKLPNGYdtlvgqrgtqlSGGQKQRIAIARAILKD 526
Cdd:PRK13545 95 --GLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHIN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1443040382 527 PKILLLDEATSALDVESERIVQEALNRMMVE-RTTLVVAHRLSTVRN 572
Cdd:PRK13545 162 PDILVIDEALSVGDQTFTKKCLDKMNEFKEQgKTIFFISHSLSQVKS 208
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
388-541 |
8.12e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDG--ISIKKLRlDWIRGKIGLVSQEP----LLFMAS 461
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGheVVTRSPQ-DGLANGIVYISEDRkrdgLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 462 IKDNII-----YGKKDATleEIKRAAELANAANFID----KLPNgYDTLVGQrgtqLSGGQKQRIAIARAILKDPKILLL 532
Cdd:PRK10762 347 VKENMSltalrYFSRAGG--SLKHADEQQAVSDFIRlfniKTPS-MEQAIGL----LSGGNQQKVAIARGLMTRPKVLIL 419
|
....*....
gi 1443040382 533 DEATSALDV 541
Cdd:PRK10762 420 DEPTRGVDV 428
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1188-1257 |
9.66e-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: 53.25 E-value: 9.66e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1188 QLSGGQKQRVAIARAILKDPKILLLDEATSALD----AESERVVQDALDRvmvNRTTIVVAHRLSTIkgaDMIA 1257
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIRELAEE---GKYVLVVEHDLAIL---DYLA 279
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
697-947 |
1.71e-06 |
|
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: 51.33 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 697 LLGSIAASVHGVILplyGIIMPGVLKSFYEPPDQLRKDSRFWALMSVVLGVAClisipAEYFLFGI---AGGKLIQRV-- 771
Cdd:cd18543 1 LILALLAALLATLA---GLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGV-----AEAVLSFLrryLAGRLSLGVeh 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 772 --RTLSFQRIMHQEVAWFDkpsnsRCATlmyfcyfifykkiftfkpmlrGHLISysgalgtRLSVDALNVRRLVGdNLAL 849
Cdd:cd18543 73 dlRTDLFAHLQRLDGAFHD-----RWQS---------------------GQLLS-------RATSDLSLVQRFLA-FGPF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 850 IVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSIRTVASFCSEKR 929
Cdd:cd18543 119 LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERR 198
|
250
....*....|....*...
gi 1443040382 930 VVAIYNKKCEALRKQGIR 947
Cdd:cd18543 199 ELDRFEAAARRLRATRLR 216
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1080-1250 |
1.74e-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: 49.49 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1080 IALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIrslkvswlrdqmglvgqepvlfndtiranitygkhsevteeeit 1159
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-------------------------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1160 avakaanahefvsslpqgydtVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVN-- 1237
Cdd:cd03222 64 ---------------------VYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgk 122
|
170
....*....|...
gi 1443040382 1238 RTTIVVAHRLSTI 1250
Cdd:cd03222 123 KTALVVEHDLAVL 135
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
806-996 |
3.07e-06 |
|
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: 50.52 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 806 FYKKIFT-----FKPMLRGHLISysgalgtRLSvDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIP 880
Cdd:cd18570 81 YFKHLLKlplsfFETRKTGEIIS-------RFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 881 LVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSN 960
Cdd:cd18570 153 LYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKG 232
|
170 180 190
....*....|....*....|....*....|....*.
gi 1443040382 961 LMLYLTYGLCFYVGAKFVSQGKTTFSDVFkVFFALV 996
Cdd:cd18570 233 LISLIGSLLILWIGSYLVIKGQLSLGQLI-AFNALL 267
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1029-1222 |
3.36e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1029 KSRIDSSSDEGAI---MENVTGSIDfnnvsfkypsrpDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDS 1105
Cdd:PRK11147 306 KMQVEEASRSGKIvfeMENVNYQID------------GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1106 GNISLdGVEirsLKVSWLrDQMglvgQEPVLFNDTIRANITYGKhsevteEEITAVAKAANA----HEFVSSlPQGYDTV 1181
Cdd:PRK11147 374 GRIHC-GTK---LEVAYF-DQH----RAELDPEKTVMDNLAEGK------QEVMVNGRPRHVlgylQDFLFH-PKRAMTP 437
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1443040382 1182 VGekgvQLSGGQKQRVAIARAILKDPKILLLDEATSALDAE 1222
Cdd:PRK11147 438 VK----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1067-1257 |
3.39e-06 |
|
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: 50.06 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1067 FSDFTLHIP-SQKTIALVGESGSGKSTIIALLE--------RFYDPDSGNISLD---GVEIRSLKVSWLRDQMGLVgQEP 1134
Cdd:cd03236 15 FKLHRLPVPrEGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVI-VKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1135 vLFNDTIRANITyGKhsevTEEEITAVAKAANAHEFVSSLpqGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDE 1214
Cdd:cd03236 94 -QYVDLIPKAVK-GK----VGELLKKKDERGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1443040382 1215 ATSALDAEsERVVQDALDRVMV--NRTTIVVAHRLSTIkgaDMIA 1257
Cdd:cd03236 166 PSSYLDIK-QRLNAARLIRELAedDNYVLVVEHDLAVL---DYLS 206
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1069-1256 |
3.93e-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: 49.92 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1069 DFTLHIPSQKTIALVGESGSGKSTII------ALLERFY--DPDSGNI-SLDGVEirslKVSWLRDqmglVGQEPV---- 1135
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLHlkKEQPGNHdRIEGLE----HIDKVIV----IDQSPIgrtp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1136 ---------LFnDTIRA----------------NITYGKHS-----EVTEEEitavakaanAHEFVSSLPQ--------- 1176
Cdd:cd03271 85 rsnpatytgVF-DEIRElfcevckgkrynretlEVRYKGKSiadvlDMTVEE---------ALEFFENIPKiarklqtlc 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1177 ----GYDTVvGEKGVQLSGGQKQRVAIARAILK---DPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLS 1248
Cdd:cd03271 155 dvglGYIKL-GQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIeHNLD 233
|
....*...
gi 1443040382 1249 TIKGADMI 1256
Cdd:cd03271 234 VIKCADWI 241
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
384-547 |
4.97e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 384 EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIKKLR---LDWIRGKIGLVSQepllfmA 460
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpyCTYIGHNLGLKLE------M 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 461 SIKDNIIYgkkdatLEEIKRAAELANAANFIDKLpngyDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALD 540
Cdd:PRK13541 86 TVFENLKF------WSEIYNSAETLYAAIHYFKL----HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
....*..
gi 1443040382 541 VESERIV 547
Cdd:PRK13541 156 KENRDLL 162
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1072-1223 |
7.55e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1072 LHIPSQKTIALVGESGSGKSTIIALLerfydpdSGNISLDGVEI---RSLKVSWL-----RDQMGLVgqepvlFnDTIRA 1143
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRIiyeQDLIVARLqqdppRNVEGTV------Y-DFVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1144 NI--------TYGKHSEVTEEE-----------ITAVAKAANAHEFVSSLPQgydtVVGEKGV-------QLSGGQKQRV 1197
Cdd:PRK11147 90 GIeeqaeylkRYHDISHLVETDpseknlnelakLQEQLDHHNLWQLENRINE----VLAQLGLdpdaalsSLSGGWLRKA 165
|
170 180
....*....|....*....|....*.
gi 1443040382 1198 AIARAILKDPKILLLDEATSALDAES 1223
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
472-588 |
8.06e-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: 50.40 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 472 DATLEEikraaelanAANFIDKLPN-------------GYDTLvGQRGTQLSGGQKQRIAIARAILKD---PKILLLDEA 535
Cdd:TIGR00630 790 DMTVEE---------AYEFFEAVPSisrklqtlcdvglGYIRL-GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEP 859
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 536 TSALDVESERIVQEALNRMMVERTTLVV-AHRLSTVRNVDCITV------VRKGKIVEQG 588
Cdd:TIGR00630 860 TTGLHFDDIKKLLEVLQRLVDKGNTVVViEHNLDVIKTADYIIDlgpeggDGGGTVVASG 919
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
404-565 |
9.74e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 404 VGESGSGKSTVISLVERFYDPQSGEVLID-GISIKKLRLDW------------IRGKIGL--VSQEpllfmasiKDNIiY 468
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQDQfafeeftvldtvIMGHTELweVKQE--------RDRI-Y 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 469 GKKDATLEEIKRAAELANAANFIDklpnGY-------DTLVG-------QRG--TQLSGGQKQRIAIARAILKDPKILLL 532
Cdd:PRK15064 104 ALPEMSEEDGMKVADLEVKFAEMD----GYtaearagELLLGvgipeeqHYGlmSEVAPGWKLRVLLAQALFSNPDILLL 179
|
170 180 190
....*....|....*....|....*....|....*
gi 1443040382 533 DEATSALDVESERIVQEALNrmmvER--TTLVVAH 565
Cdd:PRK15064 180 DEPTNNLDINTIRWLEDVLN----ERnsTMIIISH 210
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1072-1256 |
1.05e-05 |
|
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: 47.32 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1072 LHIPSQKTIALVGESGSGKSTIiaLLERFYdpdsgnisldgveirSLKVSWLRDQMGLVGQEPVLFNDTIRanitygkhs 1151
Cdd:cd03238 16 VSIPLNVLVVVTGVSGSGKSTL--VNEGLY---------------ASGKARLISFLPKFSRNKLIFIDQLQ--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1152 evteeeitavakaanaheFVSSLPQGYDTVvGEKGVQLSGGQKQRVAIARAILKDPK--ILLLDEATSALDAESERVVQD 1229
Cdd:cd03238 70 ------------------FLIDVGLGYLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE 130
|
170 180
....*....|....*....|....*...
gi 1443040382 1230 ALDR-VMVNRTTIVVAHRLSTIKGADMI 1256
Cdd:cd03238 131 VIKGlIDLGNTVILIEHNLDVLSSADWI 158
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
507-543 |
1.13e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 1.13e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1443040382 507 TQLSGGQKQRIAIARAILKDPKILLLDEATSALDVES 543
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1189-1274 |
1.57e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1189 LSGGQKQRVAIARAILKDPKILLLDEATSALD--AESErVVQdaldrvMVNR------TTIVVAHRLSTIKG-ADMIAVL 1259
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDvgAKKE-IYQ------LINQfkaeglSIILVSSEMPEVLGmSDRILVM 468
|
90 100
....*....|....*....|
gi 1443040382 1260 KEGKI-----AEKGKHEALL 1274
Cdd:PRK10762 469 HEGRIsgeftREQATQEKLM 488
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1075-1273 |
1.72e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1075 PSQKTIALvGESGSGKST----IIALLERFYDPDSGNISLDGVEIRSLKvSWLRDQMGLVGQEPVLF-----NDT----I 1141
Cdd:TIGR00956 86 PGELTVVL-GRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIK-KHYRGDVVYNAETDVHFphltvGETldfaA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1142 RANITYGKHSEVTEEE----ITAVAKAanahefVSSLPQGYDTVVGEKGVQ-LSGGQKQRVAIARAILKDPKILLLDEAT 1216
Cdd:TIGR00956 164 RCKTPQNRPDGVSREEyakhIADVYMA------TYGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQCWDNAT 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443040382 1217 SALDA----ESERVVQDALDrvMVNRTTIVVAHRLS--TIKGADMIAVLKEGKIAEKGK-HEAL 1273
Cdd:TIGR00956 238 RGLDSatalEFIRALKTSAN--ILDTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFGPaDKAK 299
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1060-1285 |
1.88e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.86 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1060 SRPDVQIFSDFTLHIPSQKTIALVGESGSGKSTIIALL--ERFYDPDSGNISLDGVEIRSLKVSwlrDQMG----LVGQE 1133
Cdd:PRK09580 10 SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE---DRAGegifMAFQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1134 PV---------LFNDTIRANITYGKhsevtEEEITAVAKAANAHEFVSSLPQGYDTVVGEKGVQLSGGQKQRVAIARAIL 1204
Cdd:PRK09580 87 PVeipgvsnqfFLQTALNAVRSYRG-----QEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1205 KDPKILLLDEATSALDAESERVVQDALDRVM-VNRTTIVVAHR---LSTIKgADMIAVLKEGKIAEKGKHEALLRIKDGA 1280
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSLRdGKRSFIIVTHYqriLDYIK-PDYVHVLYQGRIVKSGDFTLVKQLEEQG 240
|
....*
gi 1443040382 1281 YASLV 1285
Cdd:PRK09580 241 YGWLT 245
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
388-588 |
2.33e-05 |
|
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: 46.16 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 388 LDGLSLQVASGTTMAIVGESGSGKSTVISlverfydpqsgevlidgisikklrldwirgkiglvsqepllfmasikdNII 467
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN------------------------------------------------EGL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 468 YGKKDATLEEIKRAAElANAANFIDKLPN------GYDTLvGQRGTQLSGGQKQRIAIARAILKDPK--ILLLDEATSAL 539
Cdd:cd03238 43 YASGKARLISFLPKFS-RNKLIFIDQLQFlidvglGYLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 540 DVESERIVQEALNRMMVERTTL-VVAHRLSTVRNVDCITVVRK------GKIVEQG 588
Cdd:cd03238 121 HQQDINQLLEVIKGLIDLGNTViLIEHNLDVLSSADWIIDFGPgsgksgGKVVFSG 176
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1053-1264 |
2.38e-05 |
|
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: 48.67 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1053 NVSFKYPSRPDVQIFSDFTLHIPSQKTIALVGESGSGKS-TIIALLERFYDPDSGNISLDG--VEIRS---------LKV 1120
Cdd:TIGR02633 262 NLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGkpVDIRNpaqairagiAMV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1121 SWLRDQMGLVGQEPVLFNDTIRANITYGKHSEVTEE-EITAVAKAANAHEFVSSLPqgyDTVVGekgvQLSGGQKQRVAI 1199
Cdd:TIGR02633 342 PEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAaELQIIGSAIQRLKVKTASP---FLPIG----RLSGGNQQKAVL 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1200 ARAILKDPKILLLDEATSALD----AESERVVqDALDRVMVnrTTIVVAHRLSTIKG-ADMIAVLKEGKI 1264
Cdd:TIGR02633 415 AKMLLTNPRVLILDEPTRGVDvgakYEIYKLI-NQLAQEGV--AIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
391-586 |
2.61e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 391 LSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIDGISIK-KLRLDWIRGKIGLVSQ---EPLLFMA-SIKDN 465
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNGFFPNfSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 466 IIY------GKKDATLEEIKRAAELANAANFIDKLPNGYDTlVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSAL 539
Cdd:PRK09700 362 MAIsrslkdGGYKGAMGLFHEVDEQRTAENQRELLALKCHS-VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGI 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1443040382 540 DVESERIVQEALNRMMVE-RTTLVVAHRLSTVRNV-DCITVVRKGKIVE 586
Cdd:PRK09700 441 DVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1075-1274 |
3.67e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.30 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1075 PSQKTIaLVGESGSGKSTIIALLERFYDPD---SGNISLDGVEIRSL---KVSWLRDQMGL------------------- 1129
Cdd:PLN03140 190 PSRMTL-LLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFvprKTSAYISQNDVhvgvmtvketldfsarcqg 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1130 VGQEPVLFNDTIRANITYGKHSEVteeEITAVAKAANAHEFVSSLPQGY-----------DTVVGEKGVQ-LSGGQKQRV 1197
Cdd:PLN03140 269 VGTRYDLLSELARREKDAGIFPEA---EVDLFMKATAMEGVKSSLITDYtlkilgldickDTIVGDEMIRgISGGQKKRV 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1198 AIARAILKDPKILLLDEATSALDAESERVVQDALDR-VMVNRTTIVVahrlSTIKGA-------DMIAVLKEGKIAEKGK 1269
Cdd:PLN03140 346 TTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQiVHLTEATVLM----SLLQPApetfdlfDDIILLSEGQIVYQGP 421
|
....*
gi 1443040382 1270 HEALL 1274
Cdd:PLN03140 422 RDHIL 426
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1188-1274 |
4.07e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.10 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1188 QLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRV-MVNRTTI-VVAHRLSTI-KGADMIAVLKEGKI 1264
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTIlLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|
gi 1443040382 1265 AEKGKHEALL 1274
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1080-1264 |
4.21e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.71 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1080 IAlvGESGSGKSTIIALL--ERfyDPDSGNISLDGVEIRSLKVSWLRDQ-----------MGLVGQEPVLFN---DTIRa 1143
Cdd:COG3845 289 IA--GVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLgvayipedrlgRGLVPDMSVAENlilGRYR- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1144 NITYGKHSEVTEEEITAVAKAANAhEF-VSslPQGYDTVVGekgvQLSGGQKQRVAIARAILKDPKILLLDEATSALDAE 1222
Cdd:COG3845 364 RPPFSRGGFLDRKAIRAFAEELIE-EFdVR--TPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVG 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1443040382 1223 SERVVQDALDRVMVNRTTIVVahrLST-----IKGADMIAVLKEGKI 1264
Cdd:COG3845 437 AIEFIHQRLLELRDAGAAVLL---ISEdldeiLALSDRIAVMYEGRI 480
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
682-986 |
5.50e-05 |
|
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: 46.79 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 682 FGRLFNLnkpeVPVLLLGsiaASVHGVIL--PLYGIIMPGVLksfyEPPDQLrkdSRFWALMSVVLGVACLISIpAEYfL 759
Cdd:cd18565 10 LNRLFDL----APPLLIG---VAIDAVFNgeASFLPLVPASL----GPADPR---GQLWLLGGLTVAAFLLESL-FQY-L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 760 FGIAGGKLIQRV----RTLSFQRIMHQEVAWFDKPSnsrcatlmyfcyfifykkiftfkpmlrghlisySGALGTRLSVD 835
Cdd:cd18565 74 SGVLWRRFAQRVqhdlRTDTYDHVQRLDMAFFEDRQ---------------------------------TGDLMSVLNND 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 836 ALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVGAQGYaqvKFLKGFSEESKEMYEDANQVAA--- 912
Cdd:cd18565 121 VNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTY---WFQRRIEPRYRAVREAVGDLNArle 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 913 DAVGSIRTVASFCSE----KRVVAI----YNKKCEALRkqgIRSGIVGGIglsfsNLMLYLTYGLCFYVGAKFVSQGKTT 984
Cdd:cd18565 198 NNLSGIAVIKAFTAEdferERVADAseeyRDANWRAIR---LRAAFFPVI-----RLVAGAGFVATFVVGGYWVLDGPPL 269
|
..
gi 1443040382 985 FS 986
Cdd:cd18565 270 FT 271
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
349-567 |
5.60e-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: 47.70 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 349 RKPEIDSDDNngmVLED----MNG----DI-ELKDVYFRYPARPEQLIlDGLSLQVASGTTMAIVGESGSGKSTVISLVE 419
Cdd:TIGR01257 1911 KEPIFDEDDD---VAEErqriISGgnktDIlRLNELTKVYSGTSSPAV-DRLCVGVRPGECFGLLGVNGAGKTTTFKMLT 1986
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 420 RFYDPQSGEVLIDGISIKKlRLDWIRGKIGLVSQepllFMASikDNIIYGKKDATLEEIKR---AAELANAANF-IDKLp 495
Cdd:TIGR01257 1987 GDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQ----FDAI--DDLLTGREHLYLYARLRgvpAEEIEKVANWsIQSL- 2058
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 496 nGYDTLVGQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVE-RTTLVVAHRL 567
Cdd:TIGR01257 2059 -GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREgRAVVLTSHSM 2130
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1188-1264 |
5.69e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.23 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1188 QLSGGQKQRVAIARAILKDPKILLLDEATSALD----AESERVVQDALDRVMvnrTTIVVAHRLSTIKG-ADMIAVLKEG 1262
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakYEIYKLINQLVQQGV---AIIVISSELPEVLGlSDRVLVMHEG 481
|
..
gi 1443040382 1263 KI 1264
Cdd:PRK13549 482 KL 483
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
64-288 |
6.26e-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: 46.42 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 64 LMTVLFGN-VINSFGANTSGSVLRSVTKVVLN-----FIYLGIGTSVASFL---------QVSCWtmAGERQSARIRSLY 128
Cdd:cd18566 4 LPQVLLASlFINILALATPLFILQVYDRVIPNesiptLQVLVIGVVIAILLesllrllrsYILAW--IGARFDHRLSNAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 129 LKAVLRQDITFFDTEmTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGGFIIAFTrGWLLTLVMLTSLPLIAIASA 208
Cdd:cd18566 82 FEHLLSLPLSFFERE-PSGAHLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYL-GGKLVLVPLVLLGLFVLVAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 209 VSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKS----YKATIEEGIITGFGMG-----S 279
Cdd:cd18566 160 LLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAayagFKVAKINAVAQTLGQLfsqvsM 239
|
....*....
gi 1443040382 280 VMCVVFGSY 288
Cdd:cd18566 240 VAVVAFGAL 248
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
385-565 |
7.45e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 385 QLILDGlSLQVASGTTMAIVGESGSGKSTV-----------------ISLVERfydpqsgEVLIDGISIKKLRLD----- 442
Cdd:PLN03073 191 DLIVDA-SVTLAFGRHYGLVGRNGTGKTTFlrymamhaidgipkncqILHVEQ-------EVVGDDTTALQCVLNtdier 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 443 --WIRGKIGLVSQ-----EPLLFMASIKDNIIYGKKDAT---LEEIKRAAEL-------ANAANFIDKLPNGYDTLVgQR 505
Cdd:PLN03073 263 tqLLEEEAQLVAQqreleFETETGKGKGANKDGVDKDAVsqrLEEIYKRLELidaytaeARAASILAGLSFTPEMQV-KA 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 506 GTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMmvERTTLVVAH 565
Cdd:PLN03073 342 TKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW--PKTFIVVSH 399
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1049-1253 |
9.56e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 9.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRpdvQIFSDFTLHIPSQKTIaLVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSLK---VSWLRD 1125
Cdd:PRK13541 2 LSLHQLQFNIEQK---NLFDLSITFLPSAITY-IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpyCTYIGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1126 QMGLVGQEPVLFN-----------DTIRANITYGKhsevteeeitavakaanAHEFVSslpqgydtvvgEKGVQLSGGQK 1194
Cdd:PRK13541 78 NLGLKLEMTVFENlkfwseiynsaETLYAAIHYFK-----------------LHDLLD-----------EKCYSLSSGMQ 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443040382 1195 QRVAIARAILKDPKILLLDEATSALDAESERVVQDaLDRVMVNRTTIVV--AHRLSTIKGA 1253
Cdd:PRK13541 130 KIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN-LIVMKANSGGIVLlsSHLESSIKSA 189
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
45-307 |
1.30e-04 |
|
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: 45.55 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 45 VLLMVVGTVGALGNGIsQPLMTvlfGNVINSFGANTSGSVLrsvTKVVLNFIYLGIGTSVASFLQVSCWTMAGERQSARI 124
Cdd:cd18540 5 ILLIILMLLVALLDAV-FPLLT---KYAIDHFITPGTLDGL---TGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 125 RSLYLKAVLRQDITFFDTeMTTGEAVSRMSSDTlliqgalgekgGKLVELLS-----------SFIGGFIIAFTRGWLLT 193
Cdd:cd18540 78 RKKAFEHLQTLSFSYFDK-TPVGWIMARVTSDT-----------QRLGEIISwglvdlvwgitYMIGILIVMLILNWKLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 194 LVMLTSLPLIAIASA-------VSAQALTRVSSKRQTSYSDagdtveqTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKAT 266
Cdd:cd18540 146 LIVLAVVPVLAVVSIyfqkkilKAYRKVRKINSRITGAFNE-------GITGAKTTKTLVREEKNLREFKELTEEMRRAS 218
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1443040382 267 IEEGIITGFGMGSVMcvVFGSYGLAF--WYGGKLIIEKGYTGG 307
Cdd:cd18540 219 VRAARLSALFLPIVL--FLGSIATALvlWYGGILVLAGAITIG 259
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
398-568 |
1.37e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 398 GTTMAIVGESGSGKSTVISLV--ERFYDPQSGEVLIDGISIKKLRLDWIRG---KIGLVSQEpllfmASIKDNIIYGKKD 472
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKKQETFARISGyceQNDIHSPQ-----VTVRESLIYSAFL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 473 ATLEEIKRAAELanaaNFIDK------LPNGYDTLVGQRG-TQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESER 545
Cdd:PLN03140 981 RLPKEVSKEEKM----MFVDEvmelveLDNLKDAIVGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1056
|
170 180
....*....|....*....|....
gi 1443040382 546 IVQEAL-NRMMVERTTLVVAHRLS 568
Cdd:PLN03140 1057 IVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1187-1272 |
1.40e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.06 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1187 VQLSGGQKQRVAIARAILKDPKILLLDEATSALD--AESE--RVVQDALDRvmvNRTTIVVAHRLSTIKG-ADMIAVLKE 1261
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDvgAKHEiyNVIYELAAQ---GVAVLFVSSDLPEVLGvADRIVVMRE 471
|
90
....*....|..
gi 1443040382 1262 GKIA-EKGKHEA 1272
Cdd:PRK11288 472 GRIAgELAREQA 483
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1179-1248 |
1.40e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 1.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443040382 1179 DTVVGEKGVQ-LSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDAL-DRVMVNRTTIVVAHRLS 1248
Cdd:PLN03140 1009 DAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
391-541 |
1.87e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.81 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 391 LSLQVASGTTMAIVGESGSGKStviSLVERFY---DPQSGEVLIDGISIKKLRLDwIRGKIGLV-----SQEPLLFM-AS 461
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYLdAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 462 IKDNI-----------IYGKKD-ATLEEIKRAAELanaanfidKLpNGYDTLVGQrgtqLSGGQKQRIAIARAILKDPKI 529
Cdd:PRK15439 358 LAWNVcalthnrrgfwIKPAREnAVLERYRRALNI--------KF-NHAEQAART----LSGGNQQKVLIAKCLEASPQL 424
|
170
....*....|..
gi 1443040382 530 LLLDEATSALDV 541
Cdd:PRK15439 425 LIVDEPTRGVDV 436
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
382-543 |
2.54e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 382 RPEQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVErfydpqsGEVLIDGISIKkLRLDWirgKIGLVSQE-PLLFMA 460
Cdd:PRK10636 11 RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLK-------NEISADGGSYT-FPGNW---QLAWVNQEtPALPQP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 461 SIkDNIIYGKKD-ATLEEIKRAAELANAANFIDKLPNGYDTL---------------VGQRGTQL-------SGGQKQRI 517
Cdd:PRK10636 80 AL-EYVIDGDREyRQLEAQLHDANERNDGHAIATIHGKLDAIdawtirsraasllhgLGFSNEQLerpvsdfSGGWRMRL 158
|
170 180
....*....|....*....|....*.
gi 1443040382 518 AIARAILKDPKILLLDEATSALDVES 543
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLDLDA 184
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1105-1220 |
2.74e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1105 SGNISLDGVEIRSLKVSWL-----------RDQMGLVgqepvlFNDTIRANITYGKHSEVTE-------EEITAvakaan 1166
Cdd:NF040905 316 SGTVFKDGKEVDVSTVSDAidaglayvtedRKGYGLN------LIDDIKRNITLANLGKVSRrgvidenEEIKV------ 383
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1167 AHEFVSSL----PQgydtvVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALD 1220
Cdd:NF040905 384 AEEYRKKMniktPS-----VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
124-300 |
2.88e-04 |
|
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: 44.45 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 124 IRS-LYLKaVLRQDITFFDTEmTTGEAVSRMSSDT-----LLIQGalgekggkLVELLSS---FIGGFIIAFTRGWLLTL 194
Cdd:cd18778 75 LRSdLYDK-LQRLSLRYFDDR-QTGDLMSRVINDVanverLIADG--------IPQGITNvltLVGVAIILFSINPKLAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 195 VMLTSLPLIaiasAVSAQALTRVSSKR----QTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEeg 270
Cdd:cd18778 145 LTLIPIPFL----ALGAWLYSKKVRPRyrkvREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLR-- 218
|
170 180 190
....*....|....*....|....*....|..
gi 1443040382 271 IITGFGMGSVMCVVFGSYG--LAFWYGGKLII 300
Cdd:cd18778 219 AMKLWAIFHPLMEFLTSLGtvLVLGFGGRLVL 250
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
128-325 |
2.89e-04 |
|
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: 44.42 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 128 YLKAVLRQDITFFDTEmTTGEAVSRMSSDTLlIQGALGEKGGKLVELLSSFIGGFIIAFTRGWLLTLVMLTSLPLIAIAS 207
Cdd:cd18555 81 FFEHLLKLPYSFFENR-SSGDLLFRANSNVY-IRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 208 AVSAQALTRVSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIAMYRNFIKKSYKATIEEGIITGFgMGSVMCVVFGS 287
Cdd:cd18555 159 LLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNI-LNSISSSIQFI 237
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1443040382 288 YGLA-FWYGGKLIIEKGYTGGKIM---TILFAVLTGASSLGN 325
Cdd:cd18555 238 APLLiLWIGAYLVINGELTLGELIafsSLAGSFLTPIVSLIN 279
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1081-1247 |
3.13e-04 |
|
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: 45.39 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1081 ALVGESGSGKSTIIALLERFYDPDSGNISLDGVEIRSlKVSWLRDQMGLVGQepvlfNDTIRANIT-------YGKHSEV 1153
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQ-----FDAIDDLLTgrehlylYARLRGV 2042
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1154 TEEEITAVAKAAnahefVSSLpqGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDR 1233
Cdd:TIGR01257 2043 PAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170
....*....|....*
gi 1443040382 1234 VMVN-RTTIVVAHRL 1247
Cdd:TIGR01257 2116 IIREgRAVVLTSHSM 2130
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1049-1232 |
3.33e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1049 IDFNNVSFKYPSRpdvQIFSDFTLHIPSQKTIALVGESGSGKST---IIALLERfydPDSGNISL-DGVeirslkvswlr 1124
Cdd:PRK11819 325 IEAENLSKSFGDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTlfkMITGQEQ---PDSGTIKIgETV----------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1125 dQMGLVGQepvlFNDTIRANITygkhseVTEE-----EITAVAKAA-NAHEFVSSLP-QGYDTvvgEKGV-QLSGGQKQR 1196
Cdd:PRK11819 388 -KLAYVDQ----SRDALDPNKT------VWEEisgglDIIKVGNREiPSRAYVGRFNfKGGDQ---QKKVgVLSGGERNR 453
|
170 180 190
....*....|....*....|....*....|....*.
gi 1443040382 1197 VAIARAILKDPKILLLDEATSALDAESERVVQDALD 1232
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1067-1265 |
3.94e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1067 FSDFTLHIPSQKTIALVGESGSGKSTiiaLLERFY---DPDSGNISLDGVEIRSLKVSwLRDQMGLV-----GQEPVLFN 1138
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTE---LAETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1139 DT-IRANI---TY---------GKHSEVTEEEITAVA-KAANAHEFVSSLpqgydtvvgekgvqlSGGQKQRVAIARAIL 1204
Cdd:PRK15439 355 DApLAWNVcalTHnrrgfwikpARENAVLERYRRALNiKFNHAEQAARTL---------------SGGNQQKVLIAKCLE 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443040382 1205 KDPKILLLDEATSALD----AESERVVQD-ALDRVMVnrttIVVAHRLSTIKG-ADMIAVLKEGKIA 1265
Cdd:PRK15439 420 ASPQLLIVDEPTRGVDvsarNDIYQLIRSiAAQNVAV----LFISSDLEEIEQmADRVLVMHQGEIS 482
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
384-551 |
4.42e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 384 EQLILDGLSLQVASGTTMAIVGESGSGKSTVISLVERFYDPQSGEVLIdGISIKklrldwirgkIGLVSQepllFMASIK 463
Cdd:PRK11819 336 DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------LAYVDQ----SRDALD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 464 DN-------------IIYGKKdatleEIKRAAELAnAANFidklpNGYDT--LVGQrgtqLSGGQKQRIAIARAILKDPK 528
Cdd:PRK11819 401 PNktvweeisggldiIKVGNR-----EIPSRAYVG-RFNF-----KGGDQqkKVGV----LSGGERNRLHLAKTLKQGGN 465
|
170 180
....*....|....*....|...
gi 1443040382 529 ILLLDEATSALDVESERIVQEAL 551
Cdd:PRK11819 466 VLLLDEPTNDLDVETLRALEEAL 488
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
59-267 |
4.61e-04 |
|
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: 43.74 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 59 GISQPLMT-VLFGNVINSFGANTsgsvLRSVTKVVLNFIYL-GIGTSVASFLqvscWTMAGERQSARIRSLYLKAVLRQD 136
Cdd:cd18782 18 GLANPLLFqVIIDKVLVQQDLAT----LYVIGVVMLVAALLeAVLTALRTYL----FTDTANRIDLELGGTIIDHLLRLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 137 ITFFDTEmTTGEAVSRMSSDTLLIQGALGEKGGKLVELLSSFIGgFIIAFTRGWLLTLVMLTSLPLIAIASAVSAQALTR 216
Cdd:cd18782 90 LGFFDKR-PVGELSTRISELDTIRGFLTGTALTTLLDVLFSVIY-IAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1443040382 217 VSSKRQTSYSDAGDTVEQTIGSIRTVVSFNGEKKAIA----MYRNFIKKSYKATI 267
Cdd:cd18782 168 QIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWrwqnRYARSLGEGFKLTV 222
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
499-591 |
4.62e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 499 DTLVG---QRGtqLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRM--MVERTTLV--VAHRLSTVR 571
Cdd:PLN03140 326 DTIVGdemIRG--ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIvhLTEATVLMslLQPAPETFD 403
|
90 100
....*....|....*....|
gi 1443040382 572 NVDCITVVRKGKIVEQGPHD 591
Cdd:PLN03140 404 LFDDIILLSEGQIVYQGPRD 423
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1188-1245 |
6.24e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 6.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1188 QLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALdrVMVNRTTIVVAH 1245
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
503-593 |
7.97e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.19 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 503 GQRGTQLSGGQKQRIAIARAILKDPKILLLDEATSALDVESERIVQEALNRMMVE-RTTLVVAHRLSTVRNV-DCITVVR 580
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLaHELTVID 218
|
90
....*....|...
gi 1443040382 581 KGKIVEQGPHDAL 593
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1167-1273 |
8.03e-04 |
|
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: 43.85 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1167 AHEFVSSLPQ-------------GYDTVvGEKGVQLSGGQKQRVAIARAILKD---PKILLLDEATSALDAESERVVQDA 1230
Cdd:TIGR00630 796 AYEFFEAVPSisrklqtlcdvglGYIRL-GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEV 874
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1231 LDRVMVNRTTIVV-AHRLSTIKGADMIAVL------KEGKIAEKGKHEAL 1273
Cdd:TIGR00630 875 LQRLVDKGNTVVViEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1071-1292 |
8.05e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1071 TLHIPSQKTI-----ALVGESGSGKSTI-------IALLERFYDPDSGNISLDGVEIRSLKVS--WLRDQMGLVGQEPvl 1136
Cdd:PRK10938 18 TLQLPSLTLNagdswAFVGANGSGKSALaralageLPLLSGERQSQFSHITRLSFEQLQKLVSdeWQRNNTDMLSPGE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1137 fNDTIRANitygkhSEVTEEEitaVAKAANAHEFVSSLpqGYDTVVGEKGVQLSGGQKQRVAIARAILKDPKILLLDEAT 1216
Cdd:PRK10938 96 -DDTGRTT------AEIIQDE---VKDPARCEQLAQQF--GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443040382 1217 SALDAESERVVQDALDRVMVNRTTIV-VAHRLSTIKG-ADMIAVLKEGKIAEKGKHEALLRikdgayASLVQLRSNSE 1292
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ------QALVAQLAHSE 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1188-1266 |
8.76e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.62 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1188 QLSGGQKQRVAIARAILKDPKILLLDEATSALD----AESERVVQDALDRvmvNRTTIVVAHRLSTIKGA-DMIAVLKEG 1262
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvgakAEIYKVMRQLADD---GKVILMVSSELPEIITVcDRIAVFCEG 485
|
....
gi 1443040382 1263 KIAE 1266
Cdd:PRK09700 486 RLTQ 489
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1177-1265 |
1.09e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1177 GYDTVVGekgvQLSGGQKQRVAIARAILKDPKILLLDEATSALD--AESErVVQDALDRVMVNRTTIVVAHRLSTIKG-A 1253
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgAKFE-IYQLIAELAKKDKGIIIISSEMPELLGiT 458
|
90
....*....|..
gi 1443040382 1254 DMIAVLKEGKIA 1265
Cdd:PRK10982 459 DRILVMSNGLVA 470
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
841-985 |
1.17e-03 |
|
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: 42.45 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 841 RLVGDNLAL-------IVQAVATLITGFAIA---FAADWRLALIITCVIP-LVGAQGYAQVKFLKGFSEESKEMyEDANQ 909
Cdd:cd18545 102 RVINDVNSLsdllsngLINLIPDLLTLVGIViimFSLNVRLALVTLAVLPlLVLVVFLLRRRARKAWQRVRKKI-SNLNA 180
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 910 VAADAVGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRSGIVGGIGLSFSNLMLYLTYGLCFYVGAKFVSQGKTTF 985
Cdd:cd18545 181 YLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAITV 256
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
493-541 |
1.18e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 1.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1443040382 493 KLPnGYDTLVGQrgtqLSGGQKQRIAIARAILKDPKILLLDEATSALDV 541
Cdd:PRK10982 381 KTP-GHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1183-1266 |
1.25e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.80 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1183 GEKGVQLSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTIV-----------VAHRLSTIK 1251
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLlttqymeeaeqLAHELTVID 218
|
90
....*....|....*
gi 1443040382 1252 GADMIAvlkEGKIAE 1266
Cdd:NF000106 219 RGRVIA---DGKVDE 230
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
854-1000 |
1.27e-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: 42.55 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 854 VATLITGFAIAFAADWRLALIITCVIPLVGAQGYAQVKFLKGFSEESKEMYEDANQVAADAVGSIRTVASFCSEKRVvai 933
Cdd:cd18568 126 LLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPI--- 202
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443040382 934 yNKKCEALRKQGIR---SGIVGGIGLSF-SNLMLYLTYGLCFYVGAKFVSQGKTTFSDV--FKVFFALVLAAV 1000
Cdd:cd18568 203 -RWRWENKFAKALNtrfRGQKLSIVLQLiSSLINHLGTIAVLWYGAYLVISGQLTIGQLvaFNMLFGSVINPL 274
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1059-1254 |
1.63e-03 |
|
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: 40.81 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1059 PSRPDVQIfsdftLHIPSQKTIALVGESGSGKSTIIallerfydpdsgnisldgveirslkvswlrDQMGLVgqepvlfn 1138
Cdd:cd03227 8 PSYFVPND-----VTFGEGSLTIITGPNGSGKSTIL------------------------------DAIGLA-------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1139 dTIRANITYGKHSEVTEEEITAVAKAanahEFVSSLPQgydtvvgekgvqLSGGQKQRVAIA-----RAILKDPkILLLD 1213
Cdd:cd03227 45 -LGGAQSATRRRSGVKAGCIVAAVSA----ELIFTRLQ------------LSGGEKELSALAlilalASLKPRP-LYILD 106
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1443040382 1214 EATSALDAESERVVQDALDRVMVN-RTTIVVAHRLSTIKGAD 1254
Cdd:cd03227 107 EIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELAD 148
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1068-1251 |
1.88e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.57 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1068 SDFTLHIPSQKTIALVGESGSGKSTIIALLERFYDPDSGNISLDGveirslKVSWLRDQMGLVGQEPVLFNDTIRAnITY 1147
Cdd:PRK13545 41 NNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAISSGLNGQLTGIENIELKG-LMM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 1148 GKHSEVTEEEITAVAKAANAHEFVSSLPQGYdtvvgekgvqlSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVV 1227
Cdd:PRK13545 114 GLTKEKIKEIIPEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180
....*....|....*....|....*
gi 1443040382 1228 QDALDRVMVNRTTI-VVAHRLSTIK 1251
Cdd:PRK13545 183 LDKMNEFKEQGKTIfFISHSLSQVK 207
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1188-1256 |
2.14e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 2.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 1188 QLSGGQKQRVAIAR--AILK---DPkILLLDEATSALD-AESERVVQdaLDRVMVNRTT-IVVAHRLSTIKGADMI 1256
Cdd:TIGR02168 1089 LLSGGEKALTALALlfAIFKvkpAP-FCILDEVDAPLDdANVERFAN--LLKEFSKNTQfIVITHNKGTMEVADQL 1161
|
|
| PRK06851 |
PRK06851 |
hypothetical protein; Provisional |
1075-1120 |
4.06e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235878 Cd Length: 367 Bit Score: 41.10 E-value: 4.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 1075 PSQKTIALVGESGSGKSTII-----ALLERFYDPD-----SGNISLDGVEIRSLKV 1120
Cdd:PRK06851 28 GANRIFILKGGPGTGKSTLMkkigeEFLEKGYDVEflhcsSDNDSLDGVIIPELKI 83
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1067-1107 |
5.36e-03 |
|
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: 40.76 E-value: 5.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1443040382 1067 FSDFTLHIPSQKTIaLVGESGSGKSTIIALLERFYDPDSGN 1107
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSR 53
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1189-1245 |
5.83e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 5.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1443040382 1189 LSGGQKQRVAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTT--IVVAH 1245
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqlLFVSH 460
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
825-948 |
6.07e-03 |
|
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: 40.19 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443040382 825 SGALGTRLSVDALNVRRLVGDNLALIVQAVATLITGFAIAFAADWRLALIITCVIPLVgaqGYAQVKFLKGFSEESKEMY 904
Cdd:cd18564 110 TGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLL---LLAARRFSRRIKEASREQR 186
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1443040382 905 EDANQVAADA---VGSIRTVASFCSEKRVVAIYNKKCEALRKQGIRS 948
Cdd:cd18564 187 RREGALASVAqesLSAIRVVQAFGREEHEERRFARENRKSLRAGLRA 233
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
508-567 |
6.45e-03 |
|
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: 38.88 E-value: 6.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443040382 508 QLSGGQKQRIAIA-----RAILKDPkILLLDEATSALDVESERIVQEALNRMMVE-RTTLVVAHRL 567
Cdd:cd03227 77 QLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLP 141
|
|
| |
