|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
681-1263 |
2.29e-150 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 465.41 E-value: 2.29e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 681 RLLKMNRPEWKQALLGcVGAVVFGAVLPLYSYSLgslpeVYFLADDGQIRSKTRLYYFL---FLGIAVVCITANIVQHYN 757
Cdd:COG1132 11 RLLRYLRPYRGLLILA-LLLLLLSALLELLLPLL-----LGRIIDALLAGGDLSALLLLlllLLGLALLRALLSYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 758 FAVMGERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCLLVQAGATASLGFSLALAVSWR 837
Cdd:COG1132 85 LARLAQRVVADLRRDLFEHLLRLPLSFFDR--RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 838 LATVMMAMQPLIIASFYF--KKVLMAAMSKKAKKAQVQGSqlASEAVVNHRTITAFSSQRRMLRLYEAAQQGPKKDNVAH 915
Cdd:COG1132 163 LALIVLLVLPLLLLVLRLfgRRLRKLFRRVQEALAELNGR--LQESLSGIRVVKAFGREERELERFREANEELRRANLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 916 SWFSGFCLCLCQFSNTGSMAVALWYGGKLMAKGLITPTHLFQVFFMLMTMGRVIADAGSLTSDLAQGGDAVRSVLDTLDR 995
Cdd:COG1132 241 ARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 996 EPTIKDDDNdnerkKKKRKEIKGAIEFKNVHFSYPtrPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQ 1075
Cdd:COG1132 321 PPEIPDPPG-----AVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1076 RGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNIAYGAaeEHATEDEVARAAALANAHGFISAMERGYDTRVG 1155
Cdd:COG1132 394 SGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGR--PDATDEEVEEAAKAAQAHEFIEALPDGYDTVVG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1156 ERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGR 1235
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGR 551
|
570 580
....*....|....*....|....*...
gi 1002260479 1236 VAERGRHHELLAvgRAGTYYNLIKLQHG 1263
Cdd:COG1132 552 IVEQGTHEELLA--RGGLYARLYRLQFG 577
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-606 |
2.27e-145 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 452.31 E-value: 2.27e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1 MGDKEKPSFLRLVRYADAHdRCLMALGVLGSFGDGMMQPLSMLVLGDIVNSYGGAGgagsarsafSSGAVDKFALRLLYV 80
Cdd:COG1132 1 MSKSPRKLLRRLLRYLRPY-RGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG---------DLSALLLLLLLLLGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 81 AVAVGACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDAAPSSpsspqaqaqattfRVISTVSDDADAIQDFLGE 160
Cdd:COG1132 71 ALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTG-------------DLLSRLTNDVDAVEQFLAH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 161 KLPMVLANATLFFGALAVSFVFAWRLALAGLpFTLLLFVTPSVLLAGRMAAAAGEARAAYEEAGGIAQQAVSSIRTVASY 240
Cdd:COG1132 138 GLPQLVRSVVTLIGALVVLFVIDWRLALIVL-LVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 241 TAERRTVERFRGAVARSAALGVRQGLIKGAVIGSMGVI-YAVWSFLSWIGSLLVIHLHAQGGHVFVASICIVLAGMSIMM 319
Cdd:COG1132 217 GREERELERFREANEELRRANLRAARLSALFFPLMELLgNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 320 ALPNLRYFIDATAAASRMQEMIEMLPPLEGAEKkGATMERIRGEIVFKDVHFSYPsrPDTLVLNGFNLTISEGATvglvg 399
Cdd:COG1132 297 LANVLNQLQRALASAERIFELLDEPPEIPDPPG-AVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGET----- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 400 gsgsgkstvI--------------SLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENILFGDE 465
Cdd:COG1132 369 ---------ValvgpsgsgkstlvNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRP 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 466 TASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDAL 545
Cdd:COG1132 440 DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL 519
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 546 DRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLgmddgGEGGVYARMVHLQ 606
Cdd:COG1132 520 ERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELL-----ARGGLYARLYRLQ 575
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
364-606 |
2.70e-125 |
|
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: 385.74 E-value: 2.70e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIG 443
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 444 LVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRI 523
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 524 LLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLgmddgGEGGVYARMV 603
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELM-----AQKGVYAKLV 235
|
...
gi 1002260479 604 HLQ 606
Cdd:cd03249 236 KAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1020-1261 |
2.34e-122 |
|
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: 378.04 E-value: 2.34e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSGTIRDNIAYGAAEehATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDA 1179
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPD--ATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1180 RILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAvgRAGTYYNLIK 1259
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA--QKGVYAKLVK 236
|
..
gi 1002260479 1260 LQ 1261
Cdd:cd03249 237 AQ 238
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
70-1260 |
1.16e-119 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 406.34 E-value: 1.16e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 70 VDKFALRLLYVAVAVGACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDAAPSSpsspqaqaqattfRVISTVSD 149
Cdd:PTZ00265 96 VNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGS-------------KLTSDLDF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 150 DADAIQDFLGEKLPMVLANATLFFGALAVSFVFAWRLALAGLPFTLLLFVTpSVLLAGRMAAAAGEARAAYEEAGGIAQQ 229
Cdd:PTZ00265 163 YLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYIC-GVICNKKVKINKKTSLLYNNNTMSIIEE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 230 AVSSIRTVASYTAERRTVERFRGAVARSAALGVRQGLIKGAVIGSM-GVIYAVWSFLSWIGSLLVIH--LHAQGGHVFV- 305
Cdd:PTZ00265 242 ALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMInGFILASYAFGFWYGTRIIISdlSNQQPNNDFHg 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 306 ASICIVLAGMSIMM-----ALPNLRYFIDATAAASRMQEMIEMLPPLEGaEKKGATMERIRgEIVFKDVHFSYPSRPDTL 380
Cdd:PTZ00265 322 GSVISILLGVLISMfmltiILPNITEYMKSLEATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 381 VLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDD-HGIDTLNVEWLRSQIGLVSQEPVLFATSIREN 459
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNN 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 460 ILF-------------------------------------GD--------------------ETASLKQVVAAAKMANAH 482
Cdd:PTZ00265 480 IKYslyslkdlealsnyynedgndsqenknkrnscrakcaGDlndmsnttdsneliemrknyQTIKDSEVVDVSKKVLIH 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 483 EFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALD--RASVGRTTVIVAHR 560
Cdd:PTZ00265 560 DFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHR 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 561 LSTLRKADTIAVL----------------------------------------------DAGR-VVEAGTHDELLGmddg 593
Cdd:PTZ00265 640 LSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinNAGSyIIEQGTHDALMK---- 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 594 GEGGVYARMVHLQKappVAAREERHRAVDVvESEMVS--FRSVEI------MSAVSATEHRPSPAPSFCSVEH----STE 661
Cdd:PTZ00265 716 NKNGIYYTMINNQK---VSSKKSSNNDNDK-DSDMKSsaYKDSERgydpdeMNGNSKHENESASNKKSCKMSDenasENN 791
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 662 IGRKLVDHGVARSRKPSKLRLLKMNRPEW----KQALLGCVGAVVFGAVLPLYSYSLGSLPEVYFlaDDGQIRSKTRLYY 737
Cdd:PTZ00265 792 AGGKLPFLRNLFKRKPKAPNNLRIVYREIfsykKDVTIIALSILVAGGLYPVFALLYAKYVSTLF--DFANLEANSNKYS 869
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 738 FLFLGIAVVCITANIVQHYNFAVMGERLTERVRGQMLAKILSFEVGWFDEDENSSAAVCARLatqsskvrslvgDRMCLL 817
Cdd:PTZ00265 870 LYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHI------------NRDVHL 937
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 818 VQAGATASLGFSLALAVSWRLATVMMAMQPLIIAS------FYFKKV------LMAAMSKKAKKAQVQG----------- 874
Cdd:PTZ00265 938 LKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAvltgtyFIFMRVfairarLTANKDVEKKEINQPGtvfaynsddei 1017
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 875 ----SQLASEAVVNHRTITAFSSQRRMLRLYEAA----QQGPKKDNVAHSWFSGFCLCLCQFSNTgsmaVALWYGGKLMA 946
Cdd:PTZ00265 1018 fkdpSFLIQEAFYNMNTVIIYGLEDYFCNLIEKAidysNKGQKRKTLVNSMLWGFSQSAQLFINS----FAYWFGSFLIR 1093
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 947 KGLITPTHLFQVFFMLMTMGRVIADAGSLTSDLAQGGDAVRSVLDTLDREPTIkDDDNDNERKKKKRKEIKGAIEFKNVH 1026
Cdd:PTZ00265 1094 RGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNI-DVRDNGGIRIKNKNDIKGKIEIMDVN 1172
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1027 FSYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQR------------------------------ 1076
Cdd:PTZ00265 1173 FRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgdeeqnvgm 1252
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1077 ------------------------GSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNIAYGaaEEHATEDEVAR 1132
Cdd:PTZ00265 1253 knvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG--KEDATREDVKR 1330
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1133 AAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQ----DAVDRMlr 1208
Cdd:PTZ00265 1331 ACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEktivDIKDKA-- 1408
|
1370 1380 1390 1400 1410
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 1209 GRTCVVVAHRLSTVEKSDTIAVVKD-----GRVAERGRHHELLAVgRAGTYYNLIKL 1260
Cdd:PTZ00265 1409 DKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLSV-QDGVYKKYVKL 1464
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
680-1261 |
7.60e-113 |
|
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: 369.93 E-value: 7.60e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 680 LRLLKMNRPEWKQALLGCVGAVVFGAVLPLYSYSlgslpeVYflaDDGQIRSKTRLYYFLFLGIAVVCI---TANIVQHY 756
Cdd:COG2274 148 LRLLRRYRRLLLQVLLASLLINLLALATPLFTQV------VI---DRVLPNQDLSTLWVLAIGLLLALLfegLLRLLRSY 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 757 NFAVMGERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLaTQSSKVRSLVGDRMCLLVQAGATASLGFSLALAVSW 836
Cdd:COG2274 219 LLLRLGQRIDLRLSSRFFRHLLRLPLSFFES--RSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSP 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 837 RLATVMMAMQPLIIASFYF--KKVLMAAMSKKAKKAQVQGSQLasEAVVNHRTITAFSSQRRMLRLYEAAQQGPKKDNVA 914
Cdd:COG2274 296 PLALVVLLLIPLYVLLGLLfqPRLRRLSREESEASAKRQSLLV--ETLRGIETIKALGAESRFRRRWENLLAKYLNARFK 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 915 HSWFSGFCLCLCQFSNTGSMAVALWYGGKLMAKGLITPTHLFqVFFMLMtmGRVIADAGSLTSDLAQGGD---AVRSVLD 991
Cdd:COG2274 374 LRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLI-AFNILS--GRFLAPVAQLIGLLQRFQDakiALERLDD 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 992 TLDREPtikddDNDNERKKKKRKEIKGAIEFKNVHFSYPTRpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERF 1071
Cdd:COG2274 451 ILDLPP-----EREEGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1072 YDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNIAYGAaeEHATEDEVARAAALANAHGFISAMERGYD 1151
Cdd:COG2274 525 YEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD--PDATDEEIIEAARLAGLHDFIEALPMGYD 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1152 TRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVV 1231
Cdd:COG2274 603 TVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVL 682
|
570 580 590
....*....|....*....|....*....|
gi 1002260479 1232 KDGRVAERGRHHELLAvgRAGTYYNLIKLQ 1261
Cdd:COG2274 683 DKGRIVEDGTHEELLA--RKGLYAELVQQQ 710
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
74-606 |
1.23e-108 |
|
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: 358.38 E-value: 1.23e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 74 ALRLLYV-AVAVGACSFLEGLcwtrtaerqaSKMRRLYLEAVLSQEV------AFFDAAPSSPSS--PQAQAQATTFRVi 144
Cdd:COG2274 191 DLSTLWVlAIGLLLALLFEGL----------LRLLRSYLLLRLGQRIdlrlssRFFRHLLRLPLSffESRSVGDLASRF- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 145 stvsDDADAIQDFLGEKLPMVLANATLFFGALAVSFVFAWRLALAGLpFTLLLFVTPSVLLAGRMAAAAGEARAAYEEAG 224
Cdd:COG2274 260 ----RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVL-LLIPLYVLLGLLFQPRLRRLSREESEASAKRQ 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 225 GIAQQAVSSIRTVASYTAERRTVERFRGAVARSAALGVRQGLIKGAVIGSMGVIYAVWS-FLSWIGSLLVIHLHAQGGhV 303
Cdd:COG2274 335 SLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATvALLWLGAYLVIDGQLTLG-Q 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 304 FVASICIVLAGMSIMMALPNL-RYFIDATAAASRMQEMIEmLPPLEGAEKKGATMERIRGEIVFKDVHFSYPSRpDTLVL 382
Cdd:COG2274 414 LIAFNILSGRFLAPVAQLIGLlQRFQDAKIALERLDDILD-LPPEREEGRSKLSLPRLKGDIELENVSFRYPGD-SPPVL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 383 NGFNLTISEGA-------------TVglvggsgsgkstvISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEP 449
Cdd:COG2274 492 DNISLTIKPGErvaivgrsgsgksTL-------------LKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 450 VLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEA 529
Cdd:COG2274 559 FLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEA 638
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 530 TSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLgmddgGEGGVYARMVHLQ 606
Cdd:COG2274 639 TSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL-----ARKGLYAELVQQQ 710
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
698-1261 |
7.05e-108 |
|
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: 352.08 E-value: 7.05e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 698 VGAVVFGAVLPLYSYSLGSlpEVYFLADDGQIRSKTRL---YYFLFLGIAVVCITANIVQHYNFAVMGERLTERVRGQML 774
Cdd:TIGR02204 21 LAALVALLITAAATLSLPY--AVRLMIDHGFSKDSSGLlnrYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 775 AKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCLLVQAGATASLGFSLALAVSWRLATVMMAMQPLIIA--S 852
Cdd:TIGR02204 99 AHLISLSPSFFDK--NRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLpiL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 853 FYFKKVLMAAMSKKAKKAQVqgSQLASEAVVNHRTITAFSSQ----RRMLRLYEAAQQGPKKDNVAHSWFSGFCLCLCqf 928
Cdd:TIGR02204 177 LFGRRVRKLSRESQDRIADA--GSYAGETLGAIRTVQAFGHEdaerSRFGGAVEKAYEAARQRIRTRALLTAIVIVLV-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 929 snTGSMAVALWYGGKLMAKGLITPTHLFQ-VFFMLMTMGRvIADAGSLTSDLAQGGDAVRSVLDTLDREPTIKDDDNdne 1007
Cdd:TIGR02204 253 --FGAIVGVLWVGAHDVIAGKMSAGTLGQfVFYAVMVAGS-IGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAH--- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1008 rKKKKRKEIKGAIEFKNVHFSYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIR 1087
Cdd:TIGR02204 327 -PKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1088 SYSLARLRSQVALVSQEPTLFSGTIRDNIAYGaaEEHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQ 1167
Cdd:TIGR02204 406 QLDPAELRARMALVPQDPVLFAASVMENIRYG--RPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1168 RIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:TIGR02204 484 RIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA 563
|
570
....*....|....
gi 1002260479 1248 VGraGTYYNLIKLQ 1261
Cdd:TIGR02204 564 KG--GLYARLARLQ 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
673-1258 |
1.25e-105 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 350.18 E-value: 1.25e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 673 RSRKPSKLRLLKMNRPEWKQALLgcvgAVVFgavlpLYSYSLGSLPEVYF-------LADDGQIRSKTRLYYFLFLGIAV 745
Cdd:TIGR00958 143 SETADLLFRLLGLSGRDWPWLIS----AFVF-----LTLSSLGEMFIPFYtgrvidtLGGDKGPPALASAIFFMCLLSIA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 746 VCITANI-VQHYNFAVmgERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCLLVQAGATA 824
Cdd:TIGR00958 214 SSVSAGLrGGSFNYTM--ARINLRIREDLFRSLLRQDLGFFDE--NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVML 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 825 SLGFSLALAVSWRLATVMMAMQPLIIASfyfKKVLMAAMSKKAKKAQ---VQGSQLASEAVVNHRTITAFS-----SQRR 896
Cdd:TIGR00958 290 LGLLGFMLWLSPRLTMVTLINLPLVFLA---EKVFGKRYQLLSEELQeavAKANQVAEEALSGMRTVRSFAaeegeASRF 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 897 MLRLYEAAQQGPKKD--NVAHSWFSgfclclcQFSNTGSMAVALWYGGKLMAKGLITPTHLfqVFFMLMTM--GRVIADA 972
Cdd:TIGR00958 367 KEALEETLQLNKRKAlaYAGYLWTT-------SVLGMLIQVLVLYYGGQLVLTGKVSSGNL--VSFLLYQEqlGEAVRVL 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 973 GSLTSDLAQGGDAVRSVLDTLDREPTIKDDdndnerKKKKRKEIKGAIEFKNVHFSYPTRPEVAVLAGFSLEIGAGKTVA 1052
Cdd:TIGR00958 438 SYVYSGMMQAVGASEKVFEYLDRKPNIPLT------GTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVA 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1053 LVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNIAYGAaeEHATEDEVAR 1132
Cdd:TIGR00958 512 LVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGL--TDTPDEEIMA 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1133 AAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDavDRMLRGRTC 1212
Cdd:TIGR00958 590 AAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTV 667
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1002260479 1213 VVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAvgRAGTYYNLI 1258
Cdd:TIGR00958 668 LLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME--DQGCYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
66-606 |
3.21e-105 |
|
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: 344.76 E-value: 3.21e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 66 SSGAVDKFALRLLYVAVAVGACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDAAPSSpsspqaqaqattfRVIS 145
Cdd:TIGR02204 53 SSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSG-------------EVVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 146 TVSDDADAIQDFLGEKLPMVLANATLFFGALAVSFVFAWRLA---LAGLPFTLLlfvtPSVLLAGRMAAAAGEARAAYEE 222
Cdd:TIGR02204 120 RLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTslvLLAVPLVLL----PILLFGRRVRKLSRESQDRIAD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 223 AGGIAQQAVSSIRTVASYTAERRTVERFRGAVARSAALGVRQglIKGAVIGSMGVIYAVWS---FLSWIGSLLVIHLHAQ 299
Cdd:TIGR02204 196 AGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQR--IRTRALLTAIVIVLVFGaivGVLWVGAHDVIAGKMS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 300 GGHVFVASICIVLAGMSIMMALPNLRYFIDATAAASRMQEMIEMLPPLEGAEKKGATMERIRGEIVFKDVHFSYPSRPDT 379
Cdd:TIGR02204 274 AGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQ 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 380 LVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIREN 459
Cdd:TIGR02204 354 PALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMEN 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 460 ILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESER 539
Cdd:TIGR02204 434 IRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQ 513
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 540 TVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLgmddgGEGGVYARMVHLQ 606
Cdd:TIGR02204 514 LVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELI-----AKGGLYARLARLQ 575
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1020-1257 |
5.69e-103 |
|
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: 325.72 E-value: 5.69e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEvAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSGTIRDNIAYGAAEehATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDA 1179
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPG--ATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 1180 RILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAVGraGTYYNL 1257
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG--GVYAKL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
681-1261 |
1.25e-102 |
|
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: 337.46 E-value: 1.25e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 681 RLLKMNRPEWKQALLGCVGAVVFGAVLPLysysLGSLpeVYFLADDGQIRSKTRLYYFLFL---GIAVVCITANIVQHYN 757
Cdd:TIGR02203 4 RLWSYVRPYKAGLVLAGVAMILVAATEST----LAAL--LKPLLDDGFGGRDRSVLWWVPLvviGLAVLRGICSFVSTYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 758 FAVMGERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCLLVQAGATASLGFSLALAVSWR 837
Cdd:TIGR02203 78 LSWVSNKVVRDIRVRMFEKLLGLPVSFFDR--QPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 838 LATVMMAMQPLI--IASFYFKKVLMAAMSKKAKKAQVqgSQLASEAVVNHRTITAFSSQRRMLRLYEAAQQG----PKKD 911
Cdd:TIGR02203 156 LTLIVVVMLPVLsiLMRRVSKRLRRISKEIQNSMGQV--TTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRnrrlAMKM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 912 NVAHSWFSGFClclcQFSNTGSMAVALWYGGKLMAKGLITPTHlFQVFFMlmTMGRVIADAGSLT---SDLAQGGDAVRS 988
Cdd:TIGR02203 234 TSAGSISSPIT----QLIASLALAVVLFIALFQAQAGSLTAGD-FTAFIT--AMIALIRPLKSLTnvnAPMQRGLAAAES 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 989 VLDTLDREPTIKDddndnerKKKKRKEIKGAIEFKNVHFSYPTRpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLI 1068
Cdd:TIGR02203 307 LFTLLDSPPEKDT-------GTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1069 ERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNIAYGAAEEhATEDEVARAAALANAHGFISAMER 1148
Cdd:TIGR02203 379 PRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQ-ADRAEIERALAAAYAQDFVDKLPL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1149 GYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTI 1228
Cdd:TIGR02203 458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
|
570 580 590
....*....|....*....|....*....|...
gi 1002260479 1229 AVVKDGRVAERGRHHELLAvgRAGTYYNLIKLQ 1261
Cdd:TIGR02203 538 VVMDDGRIVERGTHNELLA--RNGLYAQLHNMQ 568
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1020-1261 |
1.18e-98 |
|
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: 314.17 E-value: 1.18e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPtrPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSGTIRDNIAYGaaEEHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDA 1179
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYG--RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1180 RILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAvgRAGTYYNLIK 1259
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA--KGGLYAEMWK 234
|
..
gi 1002260479 1260 LQ 1261
Cdd:cd03253 235 AQ 236
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
683-999 |
1.68e-97 |
|
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: 314.39 E-value: 1.68e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 683 LKMNRPEWKQALLGCVGAVVFGAVLPLYSYSLGSLPEVYFLADDGQIRSKTRLYYFLFLGIAVVCITANIVQHYNFAVMG 762
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 763 ERLTERVRGQMLAKILSFEVGWFDEDENSSAAVCARLATQSSKVRSLVGDRMCLLVQAGATASLGFSLALAVSWRLATVM 842
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 843 MAMQPLIIASFYFKKVLMAAMSKKAKKAQVQGSQLASEAVVNHRTITAFSSQRRMLRLYEAAQQGPKKDNVAHSWFSGFC 922
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 923 LCLCQFSNTGSMAVALWYGGKLMAKGLITPTHLFQVFFMLMTMGRVIADAGSLTSDLAQGGDAVRSVLDTLDREPTI 999
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
73-603 |
9.21e-97 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 325.91 E-value: 9.21e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 73 FALRLLYVAVAVGAcsFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDAAPsspsspqaqaqatTFRVISTVSDDAD 152
Cdd:TIGR00958 205 FFMCLLSIASSVSA--GLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENK-------------TGELTSRLSSDTQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 153 AIQDFLGEKLPMVLANATLFFGALAVSFVFAWRLALAGLPFTLLLFVTPSVLlAGRMAAAAGEARAAYEEAGGIAQQAVS 232
Cdd:TIGR00958 270 TMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVF-GKRYQLLSEELQEAVAKANQVAEEALS 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 233 SIRTVASYTAERRTVERFRGAVARSAALGVRQGLIKGAVIGS-----MGVIYAVWsflsWIGSLLVIHLHAQGGHVfvas 307
Cdd:TIGR00958 349 GMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTtsvlgMLIQVLVL----YYGGQLVLTGKVSSGNL---- 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 308 ICIVLAGMSIMMALPNLRYF----IDATAAASRMQEMIEMLP--PLEGaekkGATMERIRGEIVFKDVHFSYPSRPDTLV 381
Cdd:TIGR00958 421 VSFLLYQEQLGEAVRVLSYVysgmMQAVGASEKVFEYLDRKPniPLTG----TLAPLNLEGLIEFQDVSFSYPNRPDVPV 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 382 LNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENIL 461
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIA 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 462 FGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTV 541
Cdd:TIGR00958 577 YGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 542 QDalDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELlgMDDggeGGVYARMV 603
Cdd:TIGR00958 657 QE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQL--MED---QGCYKHLV 711
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
931-1261 |
1.29e-96 |
|
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: 322.15 E-value: 1.29e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 931 TGSMAVALWYGGKLMAKGLITP-------THLFQVFFMLMTMGRVIAD-AGSLTsDLAQggdavrsVLDTLDREPTIKDD 1002
Cdd:COG5265 274 ALGLTAMMLMAAQGVVAGTMTVgdfvlvnAYLIQLYIPLNFLGFVYREiRQALA-DMER-------MFDLLDQPPEVADA 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1003 DNdnerkKKKRKEIKGAIEFKNVHFSY-PTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLV 1081
Cdd:COG5265 346 PD-----APPLVVGGGEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1082 DGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNIAYGAAEehATEDEVARAAALANAHGFISAMERGYDTRVGERGAQL 1161
Cdd:COG5265 418 DGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPD--ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKL 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1162 SGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGR 1241
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGT 575
|
330 340
....*....|....*....|
gi 1002260479 1242 HHELLAvgRAGTYYNLIKLQ 1261
Cdd:COG5265 576 HAELLA--QGGLYAQMWARQ 593
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1018-1247 |
2.08e-93 |
|
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: 299.53 E-value: 2.08e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFSYptRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQ 1097
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLFSGTIRDNIAYGaaEEHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLK 1177
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG--RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1178 DARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
958-1263 |
1.10e-91 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 307.72 E-value: 1.10e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 958 VFFMLMTMGRVIADAGSLTSDLAQGGDAVRSVLDTLDREPTiKDDdndnerKKKKRKEIKGAIEFKNVHFSYPTRPEVAv 1037
Cdd:PRK11176 287 VFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQE-KDE------GKRVIERAKGDIEFRNVTFTYPGKEVPA- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1038 LAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNIA 1117
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1118 YgAAEEHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASER 1197
Cdd:PRK11176 439 Y-ARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESER 517
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1198 LVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAvgRAGTYYNLIKLQHG 1263
Cdd:PRK11176 518 AIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLA--QNGVYAQLHKMQFG 581
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
364-602 |
2.77e-90 |
|
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: 291.06 E-value: 2.77e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPDtLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIG 443
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 444 LVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRI 523
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 524 LLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLgmddgGEGGVYARM 602
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL-----AQGGVYAKL 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
931-1247 |
1.43e-88 |
|
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: 298.60 E-value: 1.43e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 931 TGSMAVALWYGGKLMAKGLITpthLFQVFFMLMtmgrvIA--------DAGSLTSDLAQGGDAVRSVLDTLDREPTIKDD 1002
Cdd:COG4988 253 SLSIALVAVYIGFRLLGGSLT---LFAALFVLL-----LApefflplrDLGSFYHARANGIAAAEKIFALLDAPEPAAPA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1003 DNDnerkkKKRKEIKGAIEFKNVHFSYPTRPEVavLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVD 1082
Cdd:COG4988 325 GTA-----PLPAAGPPSIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1083 GEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNIAYGAAEehATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLS 1162
Cdd:COG4988 398 GVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPD--ASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLS 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1163 GGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRH 1242
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTH 555
|
....*
gi 1002260479 1243 HELLA 1247
Cdd:COG4988 556 EELLA 560
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
816-1260 |
2.05e-85 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 289.74 E-value: 2.05e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 816 LLVQAGATASLGFslalaVSWRLATVMMAMqpLIIASFYFKKVLMAAMSKKAKKAQVQGSQLAS---EAVVNHRTITAFS 892
Cdd:COG4987 140 LLVILAAVAFLAF-----FSPALALVLALG--LLLAGLLLPLLAARLGRRAGRRLAAARAALRArltDLLQGAAELAAYG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 893 SQRRMLRLYEAAQQGPKKDNVAHSWFSGFCLCLCQFSNTGSMAVALWYGGKLMAKGLITPTHLFQVFFMLMTMGRVIADA 972
Cdd:COG4987 213 ALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 973 GSLTSDLAQGGDAVRSVLDTLDREPTIKDDDNDnerkkkKRKEIKGAIEFKNVHFSYPTRPEvAVLAGFSLEIGAGKTVA 1052
Cdd:COG4987 293 PAAAQHLGRVRAAARRLNELLDAPPAVTEPAEP------APAPGGPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1053 LVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNIAYGAAEehATEDEVAR 1132
Cdd:COG4987 366 IVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD--ATDEELWA 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1133 AAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTC 1212
Cdd:COG4987 444 ALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV 523
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1002260479 1213 VVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAvgRAGTYYNLIKL 1260
Cdd:COG4987 524 LLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA--QNGRYRQLYQR 569
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
362-588 |
2.79e-85 |
|
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: 277.18 E-value: 2.79e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 362 GEIVFKDVHFSYpsRPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQ 441
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 442 IGLVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDP 521
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 522 RILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
337-618 |
6.14e-85 |
|
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: 289.80 E-value: 6.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 337 MQEMIEML--PPlEGAEKKGATMERIR-GEIVFKDVHFSY-PSRPdtlVLNGFNLTISEGATVGLVGGSGSGKSTVISLL 412
Cdd:COG5265 329 MERMFDLLdqPP-EVADAPDAPPLVVGgGEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 413 QRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGY 492
Cdd:COG5265 405 FRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGY 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 493 ETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAV 572
Cdd:COG5265 485 DTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILV 564
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1002260479 573 LDAGRVVEAGTHDELLGMddggeGGVYARMVHLQKAPPVAAREERH 618
Cdd:COG5265 565 LEAGRIVERGTHAELLAQ-----GGLYAQMWARQQEEEEAEEALAA 605
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
364-606 |
2.18e-83 |
|
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: 272.18 E-value: 2.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSY-PSRPdtlVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQI 442
Cdd:cd03253 1 IEFENVTFAYdPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 443 GLVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPR 522
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 523 ILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLgmddgGEGGVYARM 602
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-----AKGGLYAEM 232
|
....
gi 1002260479 603 VHLQ 606
Cdd:cd03253 233 WKAQ 236
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1018-1236 |
3.32e-82 |
|
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: 268.57 E-value: 3.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFSYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQ 1097
Cdd:cd03248 10 GIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLFSGTIRDNIAYGAAEehATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLK 1177
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1178 DARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRV 1236
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-606 |
2.35e-80 |
|
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: 275.83 E-value: 2.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 8 SFLRLVRYADAHdRCLMALGVLGSFGDGMMQPLSMLVLGDIVNSyggaggagsarsAFSSGAVDK-FALRLLYVAVAV-- 84
Cdd:TIGR02203 1 TFRRLWSYVRPY-KAGLVLAGVAMILVAATESTLAALLKPLLDD------------GFGGRDRSVlWWVPLVVIGLAVlr 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 85 GACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDAAPSSpsspqaqaqattfRVISTVSDDADAIQDFLGEKLPM 164
Cdd:TIGR02203 68 GICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTG-------------TLLSRITFDSEQVASAATDAFIV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 165 VLANATLFFGALAVSFVFAWRLALAglpftLLLFVTPSVLLAGRMAAAAGEARAAYEEAGG----IAQQAVSSIRTVASY 240
Cdd:TIGR02203 135 LVRETLTVIGLFIVLLYYSWQLTLI-----VVVMLPVLSILMRRVSKRLRRISKEIQNSMGqvttVAEETLQGYRVVKLF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 241 TAERRTVERF------------RGAVARSAALGVRQGLIKGAvigsMGVIYAVWSFLSWIGSLLVihlhaqGGhvFVASI 308
Cdd:TIGR02203 210 GGQAYETRRFdavsnrnrrlamKMTSAGSISSPITQLIASLA----LAVVLFIALFQAQAGSLTA------GD--FTAFI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 309 CIVLAGMSIMMALPNLryfidataaASRMQEMI-------EMLPPLEGAEKKGATMERIRGEIVFKDVHFSYPSRpDTLV 381
Cdd:TIGR02203 278 TAMIALIRPLKSLTNV---------NAPMQRGLaaaeslfTLLDSPPEKDTGTRAIERARGDVEFRNVTFRYPGR-DRPA 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 382 LNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENIL 461
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIA 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 462 FGD-ETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERT 540
Cdd:TIGR02203 428 YGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERL 507
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 541 VQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLGMDdggegGVYARMVHLQ 606
Cdd:TIGR02203 508 VQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARN-----GLYAQLHNMQ 568
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1020-1235 |
3.79e-80 |
|
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: 260.39 E-value: 3.79e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEvAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSGTIRDNIaygaaeehatedevaraaalanahgfisamergydtrvgergaqLSGGQRQRIALARAVLKDA 1179
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1180 RILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGR 1235
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1018-1261 |
1.31e-77 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 268.37 E-value: 1.31e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFSYPTRPEVavLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQ 1097
Cdd:PRK13657 333 GAVEFDDVSFSYDNSRQG--VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLFSGTIRDNIAYGaaEEHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLK 1177
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIRVG--RPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1178 DARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAVGraGTYYNL 1257
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARG--GRFAAL 566
|
....
gi 1002260479 1258 IKLQ 1261
Cdd:PRK13657 567 LRAQ 570
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
364-606 |
1.63e-77 |
|
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: 255.87 E-value: 1.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYpsRPDT-LVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQI 442
Cdd:cd03252 1 ITFEHVRFRY--KPDGpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 443 GLVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPR 522
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 523 ILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLgmddgGEGGVYARM 602
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL-----AENGLYAYL 233
|
....
gi 1002260479 603 VHLQ 606
Cdd:cd03252 234 YQLQ 237
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
329-588 |
6.24e-76 |
|
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: 262.77 E-value: 6.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 329 DATAAASRMQEMIEMLPPLEGAEKKGATMERIrGEIVFKDVHFSYPSRpdTLVLNGFNLTISEGA-------------TV 395
Cdd:COG4988 303 NGIAAAEKIFALLDAPEPAAPAGTAPLPAAGP-PSIELEDVSFSYPGG--RPALDGLSLTIPPGErvalvgpsgagksTL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 396 glvggsgsgkstvISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENILFGDETASLKQVVAA 475
Cdd:COG4988 380 -------------LNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAA 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 476 AKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTV 555
Cdd:COG4988 447 LEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVI 526
|
250 260 270
....*....|....*....|....*....|...
gi 1002260479 556 IVAHRLSTLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:COG4988 527 LITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
933-1263 |
1.65e-74 |
|
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: 262.37 E-value: 1.65e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 933 SMAVALWYGGKLMAKGLITPTHLFqVFFMLMtmGRV---IADAGSLTSDLAQGGDAVRSVLDTLD--REPTikdddndnE 1007
Cdd:TIGR01846 375 TFAILLWFGAHLVIGGALSPGQLV-AFNMLA--GRVtqpVLRLAQLWQDFQQTGIALERLGDILNspTEPR--------S 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1008 RKKKKRKEIKGAIEFKNVHFSY-PTRPEVavLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDI 1086
Cdd:TIGR01846 444 AGLAALPELRGAITFENIRFRYaPDSPEV--LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDL 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1087 RSYSLARLRSQVALVSQEPTLFSGTIRDNIAYGaaEEHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQR 1166
Cdd:TIGR01846 522 AIADPAWLRRQMGVVLQENVLFSRSIRDNIALC--NPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQR 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1167 QRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELL 1246
Cdd:TIGR01846 600 QRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELL 679
|
330
....*....|....*..
gi 1002260479 1247 AVGraGTYYNLIKLQHG 1263
Cdd:TIGR01846 680 ALQ--GLYARLWQQQSG 694
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
360-578 |
6.39e-74 |
|
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: 245.07 E-value: 6.39e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 360 IRGEIVFKDVHFSYPSRPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLR 439
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 440 SQIGLVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVR 519
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 520 DPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRV 578
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
24-337 |
6.73e-74 |
|
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: 247.77 E-value: 6.73e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 24 MALGVLGSFGDGMMQPLSMLVLGDIVNSYGGAGGAGSARSAFSSgAVDKFALRLLYVAVAVGACSFLEGLCWTRTAERQA 103
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPDEFLD-DVNKYALYFVYLGIGSFVLSYIQTACWTITGERQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 104 SKMRRLYLEAVLSQEVAFFDAAPSSpsspqaqaqattfRVISTVSDDADAIQDFLGEKLPMVLANATLFFGALAVSFVFA 183
Cdd:cd18577 80 RRIRKRYLKALLRQDIAWFDKNGAG-------------ELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 184 WRLALAGLPFTLLLFVTpSVLLAGRMAAAAGEARAAYEEAGGIAQQAVSSIRTVASYTAERRTVERFRGAVARSAALGVR 263
Cdd:cd18577 147 WKLTLVLLATLPLIAIV-GGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIK 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 264 QGLIKGAVIG-SMGVIYAVWSFLSWIGSLLVIHLHAQGGHVFVASICIVLAGMSIMMALPNLRYFIDATAAASRM 337
Cdd:cd18577 226 KGLVSGLGLGlLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1020-1261 |
8.40e-74 |
|
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: 245.09 E-value: 8.40e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSY-PTRPEVavLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQV 1098
Cdd:cd03252 1 ITFEHVRFRYkPDGPVI--LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQEPTLFSGTIRDNIAygAAEEHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKD 1178
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIA--LADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1179 ARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAvgRAGTYYNLI 1258
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA--ENGLYAYLY 234
|
...
gi 1002260479 1259 KLQ 1261
Cdd:cd03252 235 QLQ 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
333-606 |
1.26e-73 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 256.81 E-value: 1.26e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 333 AASRMQEMIEML---PPLEgaEKKGAT-MERIRGEIVFKDVHFSYPSRPDTLvlNGFNLTISEGATVGLVGGSGSGKSTV 408
Cdd:PRK13657 302 AAPKLEEFFEVEdavPDVR--DPPGAIdLGRVKGAVEFDDVSFSYDNSRQGV--EDVSFEAKPGQTVAIVGPTGAGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 409 ISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKL 488
Cdd:PRK13657 378 INLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 489 PHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKAD 568
Cdd:PRK13657 458 PDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNAD 537
|
250 260 270
....*....|....*....|....*....|....*...
gi 1002260479 569 TIAVLDAGRVVEAGTHDELLgmddgGEGGVYARMVHLQ 606
Cdd:PRK13657 538 RILVFDNGRVVESGSFDELV-----ARGGRFAALLRAQ 570
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
74-605 |
1.37e-72 |
|
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: 253.54 E-value: 1.37e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 74 ALRLLYVAVAVGACSFleglcwTRTAERqaskmrrlYLEAVLSQEVAF----------FDAApsspsSPQAQAQATTFR- 142
Cdd:COG4987 51 ILNLFVPIVGVRAFAI------GRTVFR--------YLERLVSHDATLrlladlrvrlYRRL-----EPLAPAGLARLRs 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 143 --VISTVSDDADAIQDF-LGEKLPMVLAnATLFFGALAVSFVFAWRLALAGLPFTLLLFVTPSVLLAGRMAAAAGEARAA 219
Cdd:COG4987 112 gdLLNRLVADVDALDNLyLRVLLPLLVA-LLVILAAVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 220 YEEAGGIAQQAVSSIRTVASYTAERRTVERFRGAVARSAALGVRQGLIKGAvigSMGVIYAVWSFLSWIGSLLVIHLHAQ 299
Cdd:COG4987 191 RAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSAL---AQALLQLAAGLAVVAVLWLAAPLVAA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 300 GGH--VFVASIC-IVLAGMSIMMALPN-LRYFIDATAAASRMQEMIEMLPPLEgaEKKGATMERIRGEIVFKDVHFSYPS 375
Cdd:COG4987 268 GALsgPLLALLVlAALALFEALAPLPAaAQHLGRVRAAARRLNELLDAPPAVT--EPAEPAPAPGGPSLELEDVSFRYPG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 376 RPDTlVLNGFNLTISEGA-------------TVglvggsgsgkstvISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQI 442
Cdd:COG4987 346 AGRP-VLDGLSLTLPPGErvaivgpsgsgksTL-------------LALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 443 GLVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPR 522
Cdd:COG4987 412 AVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAP 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 523 ILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLgmddgGEGGVYARM 602
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELL-----AQNGRYRQL 566
|
...
gi 1002260479 603 VHL 605
Cdd:COG4987 567 YQR 569
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
358-606 |
2.14e-71 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 250.32 E-value: 2.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 358 ERIRGEIVFKDVHFSYPSRpDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEW 437
Cdd:PRK11176 336 ERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLAS 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 438 LRSQIGLVSQEPVLFATSIRENILFG-DETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARA 516
Cdd:PRK11176 415 LRNQVALVSQNVHLFNDTIANNIAYArTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 517 LVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLGMDdggeg 596
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN----- 569
|
250
....*....|
gi 1002260479 597 GVYARMVHLQ 606
Cdd:PRK11176 570 GVYAQLHKMQ 579
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
229-606 |
5.93e-71 |
|
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: 251.97 E-value: 5.93e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 229 QAVSSIRTVASYTAERRTVERFRGAVARSAALGvrQGLIKGAVIGSMG---VIYAVWSFLSWIGSLLVIhlhaqGGHVFV 305
Cdd:TIGR01846 322 ESVTGIETIKATATEPQFQNRWDRQLAAYVAAS--FRVTNLGNIAGQAielIQKLTFAILLWFGAHLVI-----GGALSP 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 306 ASICI--VLAGMsimMALPNLRY------FIDATAAASRMQEMIEmlPPLEGAEKKGATMERIRGEIVFKDVHFSYpsRP 377
Cdd:TIGR01846 395 GQLVAfnMLAGR---VTQPVLRLaqlwqdFQQTGIALERLGDILN--SPTEPRSAGLAALPELRGAITFENIRFRY--AP 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 378 DT-LVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSI 456
Cdd:TIGR01846 468 DSpEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSI 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 457 RENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAE 536
Cdd:TIGR01846 548 RDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYE 627
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 537 SERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLgmddgGEGGVYARMVHLQ 606
Cdd:TIGR01846 628 SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELL-----ALQGLYARLWQQQ 692
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1018-1236 |
1.16e-66 |
|
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: 224.39 E-value: 1.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFSYPTRpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQ 1097
Cdd:cd03245 1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLFSGTIRDNIAYGAAeeHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLK 1177
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAP--LADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1178 DARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRV 1236
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
364-577 |
1.02e-64 |
|
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: 216.48 E-value: 1.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPDTlVLNGFNLTISEGA-------------TVglvggsgsgkstvISLLQRFYSPDSGEISMDDHGI 430
Cdd:cd03228 1 IEFKNVSFSYPGRPKP-VLKDVSLTIKPGEkvaivgpsgsgksTL-------------LKLLLRLYDPTSGEILIDGVDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 431 DTLNVEWLRSQIGLVSQEPVLFATSIRENILfgdetaslkqvvaaakmanahefivklphgyethvgqfgtqlSGGQKQR 510
Cdd:cd03228 67 RDLDLESLRKNIAYVPQDPFLFSGTIRENIL------------------------------------------SGGQRQR 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 511 IAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGR 577
Cdd:cd03228 105 IAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1018-1240 |
6.05e-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: 216.59 E-value: 6.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFSYptRPE-VAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRS 1096
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEPTLFSGTIRDNIAygaAEEHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVL 1176
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD---PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 1177 KDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERG 1240
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
975-1259 |
1.64e-62 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 227.52 E-value: 1.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 975 LTSDLAQGGDAVRSVLDTLDREPTIKDDDNDnerkkkKRKEIKGAIEFKNVHFSYpTRPEVAVLAGFSLEIGAGKTVALV 1054
Cdd:TIGR03796 439 LEGDLNRLDDVLRNPVDPLLEEPEGSAATSE------PPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALV 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1055 GPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNIAYgaAEEHATEDEVARAA 1134
Cdd:TIGR03796 512 GGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTL--WDPTIPDADLVRAC 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1135 ALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRmlRGRTCVV 1214
Cdd:TIGR03796 590 KDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCII 667
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1002260479 1215 VAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAVGraGTYYNLIK 1259
Cdd:TIGR03796 668 VAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVG--GAYARLIR 710
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
144-604 |
2.00e-61 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 224.44 E-value: 2.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 144 ISTVSDDADAIQDFLGEKL-PMVLANATLFFGALaVSFVFAWRLALAGLPFTLLLFVTpSVLLAGRMAAAAGEARAAYEE 222
Cdd:TIGR03796 253 IASRVQLNDQVAEFLSGQLaTTALDAVMLVFYAL-LMLLYDPVLTLIGIAFAAINVLA-LQLVSRRRVDANRRLQQDAGK 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 223 AGGIAQQAVSSIRTVASYTAERRTVERFRGAVARsaALGVRQGLikGAVIGSMGVIYAVWSFLS-----WIGSLLVIhlh 297
Cdd:TIGR03796 331 LTGVAISGLQSIETLKASGLESDFFSRWAGYQAK--LLNAQQEL--GVLTQILGVLPTLLTSLNsalilVVGGLRVM--- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 298 aqGGHVfvaSICIVLAGMSIMMA----LPNLRYFI----DATAAASRMQEMIE--MLPPLEGAEKKGATME---RIRGEI 364
Cdd:TIGR03796 404 --EGQL---TIGMLVAFQSLMSSflepVNNLVGFGgtlqELEGDLNRLDDVLRnpVDPLLEEPEGSAATSEpprRLSGYV 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 365 VFKDVHFSYpSRPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGL 444
Cdd:TIGR03796 479 ELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAM 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 445 VSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRIL 524
Cdd:TIGR03796 558 VDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSIL 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 525 LLDEATSALDAESERTVQDALDRAsvGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLgmddgGEGGVYARMVH 604
Cdd:TIGR03796 638 ILDEATSALDPETEKIIDDNLRRR--GCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELW-----AVGGAYARLIR 710
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
1018-1259 |
1.37e-60 |
|
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: 218.99 E-value: 1.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFSYPTRPEVavLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQ 1097
Cdd:TIGR01192 333 GAVEFRHITFEFANSSQG--VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKS 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLFSGTIRDNIAYGaaEEHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLK 1177
Cdd:TIGR01192 411 IATVFQDAGLFNRSIRENIRLG--REGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1178 DARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELlaVGRAGTYYNL 1257
Cdd:TIGR01192 489 NAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQEL--IQKDGRFYKL 566
|
..
gi 1002260479 1258 IK 1259
Cdd:TIGR01192 567 LR 568
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
985-1258 |
5.86e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 217.00 E-value: 5.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 985 AVRSVLDTLDREPTIKDDDNDNERKKKkrkeikGAIEFKNVHFSYPTRPEvAVLAGFSLEIGAGKTVALVGPSGSGKSTV 1064
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAADQ------VSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1065 IGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNIAYgaAEEHATEDEVARAAALANAHGFIS 1144
Cdd:PRK11160 383 LQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL--AAPNASDEALIEVLQQVGLEKLLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1145 AmERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEK 1224
Cdd:PRK11160 461 D-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQ 539
|
250 260 270
....*....|....*....|....*....|....
gi 1002260479 1225 SDTIAVVKDGRVAERGRHHELLAvgRAGTYYNLI 1258
Cdd:PRK11160 540 FDRICVMDNGQIIEQGTHQELLA--QQGRYYQLK 571
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
936-1231 |
6.89e-60 |
|
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: 215.61 E-value: 6.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 936 VALWYGGKLMAKGLitptHLFQVFFMLMTMGRV---IADAGSLTSDLAQGGDAVRSVLDTLDREPTIKDDDNDnerkkkK 1012
Cdd:TIGR02857 245 VAVYIGFRLLAGDL----DLATGLFVLLLAPEFylpLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAP------V 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1013 RKEIKGAIEFKNVHFSYPTRPevAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLA 1092
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1093 RLRSQVALVSQEPTLFSGTIRDNIAYGAAEehATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALA 1172
Cdd:TIGR02857 393 SWRDQIAWVPQHPFLFAGTIAENIRLARPD--ASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALA 470
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1173 RAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVV 1231
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
362-582 |
1.08e-56 |
|
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: 195.50 E-value: 1.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 362 GEIVFKDVHFSYPSRPdTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQ 441
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 442 IGLVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDP 521
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 522 RILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAG 582
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
260-1259 |
2.16e-56 |
|
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: 215.19 E-value: 2.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 260 LGVRQGLIKgaVIGSMGVIYAVWSFlSWIGSLLVIHL---------------HAQGGHVFVASICIVLAGMSIM-MALPN 323
Cdd:TIGR00957 523 EGIRQEELK--VLKKSAYLHAVGTF-TWVCTPFLVALitfavyvtvdennilDAEKAFVSLALFNILRFPLNILpMVISS 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 324 LryfIDATAAASRMQEMI--EMLPPlEGAEKKgaTMERIRG-EIVFKDVHFSYpSRPDTLVLNGFNLTISEGATVGLVGG 400
Cdd:TIGR00957 600 I---VQASVSLKRLRIFLshEELEP-DSIERR--TIKPGEGnSITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQ 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 401 SGSGKSTVISLLQRFYSPDSGEISMddhgidtlnvewlRSQIGLVSQEPVLFATSIRENILFGD--ETASLKQVVAAAKM 478
Cdd:TIGR00957 673 VGCGKSSLLSALLAEMDKVEGHVHM-------------KGSVAYVPQQAWIQNDSLRENILFGKalNEKYYQQVLEACAL 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 479 ANAHEFivkLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDAL---DRASVGRTTV 555
Cdd:TIGR00957 740 LPDLEI---LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRI 816
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 556 IVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLGMDdggegGVYARMVHlQKAPpvaAREERHRAVDVVESemvsfrsve 635
Cdd:TIGR00957 817 LVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRD-----GAFAEFLR-TYAP---DEQQGHLEDSWTAL--------- 878
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 636 imsaVSATEHRPSPAPSFCSVEHSteIGRKLVDH---------GVARSRKPS-KLRLLKMNRPEWK-----QALLGCVGA 700
Cdd:TIGR00957 879 ----VSGEGKEAKLIENGMLVTDV--VGKQLQRQlsasssdsgDQSRHHGSSaELQKAEAKEETWKlmeadKAQTGQVEL 952
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 701 VV-------------FGAVLPLYSYSLGSLPEVYFL--------ADDGQIRSKTRLYYFLFLGIavvcITANIVQHYNFA 759
Cdd:TIGR00957 953 SVywdymkaiglfitFLSIFLFVCNHVSALASNYWLslwtddpmVNGTQNNTSLRLSVYGALGI----LQGFAVFGYSMA 1028
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 760 V-MGERLTERVRGQ-MLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCLLVQAGATAsLGFSLALAVSWR 837
Cdd:TIGR00957 1029 VsIGGIQASRVLHQdLLHNKLRSPMSFFER--TPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNV-IGALIVILLATP 1105
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 838 LATVMMAmqPLIIASFYFKKVLMAAMSKKAKKAQVQGSQLAS---EAVVNHRTITAFSSQRRMLRL----YEAAQQGPKK 910
Cdd:TIGR00957 1106 IAAVIIP--PLGLLYFFVQRFYVASSRQLKRLESVSRSPVYShfnETLLGVSVIRAFEEQERFIHQsdlkVDENQKAYYP 1183
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 911 DNVAHSWFS------GFCLCLcqFSntgsmAVALWYGGKLMAKGLI--TPTHLFQVFFMLMTMGRviadagsLTSDLAQG 982
Cdd:TIGR00957 1184 SIVANRWLAvrlecvGNCIVL--FA-----ALFAVISRHSLSAGLVglSVSYSLQVTFYLNWLVR-------MSSEMETN 1249
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 983 GDAVRSVLDTLDRE---PTIKDDdndneRKKKKRKEIKGAIEFKNVHFSYptRPEV-AVLAGFSLEIGAGKTVALVGPSG 1058
Cdd:TIGR00957 1250 IVAVERLKEYSETEkeaPWQIQE-----TAPPSGWPPRGRVEFRNYCLRY--REDLdLVLRHINVTIHGGEKVGIVGRTG 1322
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1059 SGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNI-AYGAAeehaTEDEVARAAALA 1137
Cdd:TIGR00957 1323 AGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQY----SDEEVWWALELA 1398
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1138 NAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAH 1217
Cdd:TIGR00957 1399 HLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAH 1478
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|..
gi 1002260479 1218 RLSTVEKSDTIAVVKDGRVAERGRHHELLAvgRAGTYYNLIK 1259
Cdd:TIGR00957 1479 RLNTIMDYTRVIVLDKGEVAEFGAPSNLLQ--QRGIFYSMAK 1518
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
133-1247 |
6.60e-55 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 210.60 E-value: 6.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 133 QAQAQATTFRVISTVSDDADAIQDfLGEKL------PM-VLANATLFFGALAVSFVFAwrlalaglPFTLLLFVTPSVLL 205
Cdd:PLN03232 390 EARKNFASGKVTNMITTDANALQQ-IAEQLhglwsaPFrIIVSMVLLYQQLGVASLFG--------SLILFLLIPLQTLI 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 206 AGRMAAAAGEARAAYEEAGGIAQQAVSSIRTVASYTAERRTVERFRG------AVARSAALgvrQGLIKGAVIGSMGVIY 279
Cdd:PLN03232 461 VRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGirneelSWFRKAQL---LSAFNSFILNSIPVVV 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 280 AVWSFlswiGSLLVIhlhaqGGHVFVASICIVLAGMSIMMA----LPNL-RYFIDATAAASRMQEMI---EML----PPL 347
Cdd:PLN03232 538 TLVSF----GVFVLL-----GGDLTPARAFTSLSLFAVLRSplnmLPNLlSQVVNANVSLQRIEELLlseERIlaqnPPL 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 348 EgaekKGATmerirgEIVFKDVHFSYPSRPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQrfyspdsGEIS-MD 426
Cdd:PLN03232 609 Q----PGAP------AISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML-------GELShAE 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 427 DHGIDtlnvewLRSQIGLVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVkLPHGYETHVGQFGTQLSGG 506
Cdd:PLN03232 672 TSSVV------IRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDL-LPGRDLTEIGERGVNISGG 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 507 QKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASV-GRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHD 585
Cdd:PLN03232 745 QKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELkGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFA 824
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 586 ELLGmddggEGGVYARMvhLQKAPPVAAREERHRavdvvESEMVSFRSVEIMSAVSATehrpspapSFCSVEHSTEiGRK 665
Cdd:PLN03232 825 ELSK-----SGSLFKKL--MENAGKMDATQEVNT-----NDENILKLGPTVTIDVSER--------NLGSTKQGKR-GRS 883
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 666 LVDHGVARSRKPSKLRLLKmnrpEWKQALLGC-VGAVVFGAVLPLYSYSLGSLPEVYFLADDGQIRSKTRLYY---FLFL 741
Cdd:PLN03232 884 VLVKQEERETGIISWNVLM----RYNKAVGGLwVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYSPGFYivvYALL 959
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 742 GIAVVCIT-ANivqhyNFAVMGERL--TERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCLLV 818
Cdd:PLN03232 960 GFGQVAVTfTN-----SFWLISSSLhaAKRLHDAMLNSILRAPMLFFHT--NPTGRVINRFSKDIGDIDRNVANLMNMFM 1032
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 819 QAGATASLGFSLALAVSwrlATVMMAMQPLII----ASFYFKKVLMAAMSKKAKKAQVQGSQLAsEAVVNHRTITAFSSQ 894
Cdd:PLN03232 1033 NQLWQLLSTFALIGTVS---TISLWAIMPLLIlfyaAYLYYQSTSREVRRLDSVTRSPIYAQFG-EALNGLSSIRAYKAY 1108
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 895 RRMLRLyeaaqQGPKKDNvahswfsGFCLCLCQFSNTGSMAVALWYGGKLMakglITPTHLFQVF---------FMLMTM 965
Cdd:PLN03232 1109 DRMAKI-----NGKSMDN-------NIRFTLANTSSNRWLTIRLETLGGVM----IWLTATFAVLrngnaenqaGFASTM 1172
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 966 GRVIADAGSLTSDLA----QGGDAVRSvLDTLDREPTIKD-----DDNDNERKKKKRKEIKGAIEFKNVHFSYptRPEVA 1036
Cdd:PLN03232 1173 GLLLSYTLNITTLLSgvlrQASKAENS-LNSVERVGNYIDlpseaTAIIENNRPVSGWPSRGSIKFEDVHLRY--RPGLP 1249
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1037 -VLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDN 1115
Cdd:PLN03232 1250 pVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFN 1329
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1116 IayGAAEEHATEDeVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAAS 1195
Cdd:PLN03232 1330 I--DPFSEHNDAD-LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 1196 ERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:PLN03232 1407 DSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1033-1257 |
8.27e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 202.00 E-value: 8.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1033 PEVAVLAG-FSLEIGAGKTVALVGPSGSGKSTVIGLIERF--YdaqRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFS 1109
Cdd:PRK11174 360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1110 GTIRDNIAYGAAeeHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATS 1189
Cdd:PRK11174 437 GTLRDNVLLGNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 1190 ALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAVGraGTYYNL 1257
Cdd:PRK11174 515 SLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG--GLFATL 580
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
111-588 |
6.58e-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: 198.82 E-value: 6.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 111 LEAVLSQEV--AFFDAAPSSPSSPQAQAQattfrvistvsDDADAIQDFLGEKLPMVLANA--TLFFgaLAVSFVFAWRL 186
Cdd:COG4618 91 LDRRLGPRVfdAAFRAALRGGGGAAAQAL-----------RDLDTLRQFLTGPGLFALFDLpwAPIF--LAVLFLFHPLL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 187 ALAGLPFTLLLFVTpSVLLAGRMAAAAGEARAAYEEAGGIAQQAVSSIRTVASYTAERRTVERFRGAVARSAALGVR--- 263
Cdd:COG4618 158 GLLALVGALVLVAL-ALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARasd 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 264 -----QGLIKGAVIGSMGVIYAVwsflswiGSLLVIHLHAQGGHVFVASIcivLAG---MSIMMALPNLRYFIDATAAAS 335
Cdd:COG4618 237 raggfSALSKFLRLLLQSAVLGL-------GAYLVIQGEITPGAMIAASI---LMGralAPIEQAIGGWKQFVSARQAYR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 336 RMQEMIEMLPPlegaEKKGATMERIRGEIVFKDVHFSYPSRpDTLVLNGFNLTISEGATVGlvggsgsgkstvI------ 409
Cdd:COG4618 307 RLNELLAAVPA----EPERMPLPRPKGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLG------------Vigpsgs 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 410 --SLLQR----FYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENI-LFGDETASlkQVVAAAKMANAH 482
Cdd:COG4618 370 gkSTLARllvgVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFGDADPE--KVVAAAKLAGVH 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 483 EFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRA-SVGRTTVIVAHRL 561
Cdd:COG4618 448 EMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRP 527
|
490 500
....*....|....*....|....*..
gi 1002260479 562 STLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:COG4618 528 SLLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
71-607 |
1.70e-51 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 199.48 E-value: 1.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 71 DKFALRLLYVAVAVGACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDAAPSSPSSPQAQaqattfrvistVSDD 150
Cdd:PTZ00265 866 NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAH-----------INRD 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 151 ADAIQDFLGEKLPMVLANATLFFGALAVSFVFAWRLAlAGLPFTLLLFVtpSVLLAGRMAAAAGEARAAYEEAGGIA--- 227
Cdd:PTZ00265 935 VHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVA-AVLTGTYFIFM--RVFAIRARLTANKDVEKKEINQPGTVfay 1011
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 228 --------------QQAVSSIRTVASYTAERRTVERFRGAVARSAALGVRQGLIKGAVIG-SMGVIYAVWSFLSWIGSLL 292
Cdd:PTZ00265 1012 nsddeifkdpsfliQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGfSQSAQLFINSFAYWFGSFL 1091
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 293 VihlhaQGGHV----FVASICIVLAGMSIMMALPNLRY-FIDATAAASRMQEMIEMLPPLEGAEKKGATMER---IRGEI 364
Cdd:PTZ00265 1092 I-----RRGTIlvddFMKSLFTFLFTGSYAGKLMSLKGdSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKI 1166
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 365 VFKDVHFSYPSRPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYS--------------------------- 417
Cdd:PTZ00265 1167 EIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgde 1246
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 ---------------------------PDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENILFGDETASLK 470
Cdd:PTZ00265 1247 eqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATRE 1326
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 471 QVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAES----ERTVQDALD 546
Cdd:PTZ00265 1327 DVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSekliEKTIVDIKD 1406
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 547 RASvgRTTVIVAHRLSTLRKADTIAVLD----AGRVVEA-GTHDELLGMDDggegGVYARMVHLQK 607
Cdd:PTZ00265 1407 KAD--KTIITIAHRIASIKRSDKIVVFNnpdrTGSFVQAhGTHEELLSVQD----GVYKKYVKLAK 1466
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1018-1247 |
7.05e-51 |
|
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: 189.57 E-value: 7.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFSYPTRpEVAVLAGFSLEIGAGKTVALVGPSGSGKST----VIGLIErfydAQRGSVLVDGEDIRSYSLAR 1093
Cdd:COG4618 329 GRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTlarlLVGVWP----PTAGSVRLDGADLSQWDREE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1094 LRSQVALVSQEPTLFSGTIRDNIA-YGAAeehaTEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALA 1172
Cdd:COG4618 404 LGRHIGYLPQDVELFDGTIAENIArFGDA----DPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1173 RAVLKDARILLLDEATSALDAASERLVQDAVDRM-LRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1020-1240 |
8.19e-51 |
|
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: 177.12 E-value: 8.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSlARLRSQVA 1099
Cdd:cd03247 1 LSINNVSFSYPEQEQQ-VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSGTIRDNIaygaaeehatedevaraaalanahgfisamergydtrvgerGAQLSGGQRQRIALARAVLKDA 1179
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 1180 RILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERG 1240
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
331-607 |
1.06e-50 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 189.54 E-value: 1.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 331 TAAASRMQEMIEMLPPLEGAEKkgaTMERIRGEIVFKDVHFSYPSRpDTLVLNGFNLTISEGATVGLVGGSGSGKSTVIS 410
Cdd:PRK10789 284 SAAYSRIRAMLAEAPVVKDGSE---PVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLS 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 411 LLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPH 490
Cdd:PRK10789 360 LIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 491 GYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTI 570
Cdd:PRK10789 440 GYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEI 519
|
250 260 270
....*....|....*....|....*....|....*..
gi 1002260479 571 AVLDAGRVVEAGTHDELLgmddgGEGGVYARMVHLQK 607
Cdd:PRK10789 520 LVMQHGHIAQRGNHDQLA-----QQSGWYRDMYRYQQ 551
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
6-606 |
2.04e-50 |
|
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: 190.94 E-value: 2.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 6 KPSFLRLVRYA-DAHDRCLMALGVLGSFGD--GMMQPLSMlvlGDIVNSYGGAGgagsarsafSSGAVDKFALRLLYVAV 82
Cdd:TIGR03797 120 ALGLRDLLRFAlRGARRDLLAILAMGLLGTllGMLVPIAT---GILIGTAIPDA---------DRSLLVQIALALLAAAV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 83 AVGACSFLEGLCWTRTAER-----QASKMRRLyleavLSQEVAFFDAAPSSPSSPQAQAQATTFRVISTVsddadaiqdf 157
Cdd:TIGR03797 188 GAAAFQLAQSLAVLRLETRmdaslQAAVWDRL-----LRLPVSFFRQYSTGDLASRAMGISQIRRILSGS---------- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 158 lgeklpMVLANATLFFGA--LAVSFVFAWRLALAGLPFTLLLFVTPSVLlAGRMAAAAGEARAAYEEAGGIAQQ---AVS 232
Cdd:TIGR03797 253 ------TLTTLLSGIFALlnLGLMFYYSWKLALVAVALALVAIAVTLVL-GLLQVRKERRLLELSGKISGLTVQlinGIS 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 233 SIRTVAsytAERRTVERFRGAVARSAALGVRQGLIKGA---------VIGSMGVIYAVWSFLSWIGsllvihlhaQGGHV 303
Cdd:TIGR03797 326 KLRVAG---AENRAFARWAKLFSRQRKLELSAQRIENLltvfnavlpVLTSAALFAAAISLLGGAG---------LSLGS 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 304 FVASICIVLAGMSIMMALPNLryFIDATAAA---SRMQEMIEMLPPLEGAEKKGAtmeRIRGEIVFKDVHFSYpsRPDT- 379
Cdd:TIGR03797 394 FLAFNTAFGSFSGAVTQLSNT--LISILAVIplwERAKPILEALPEVDEAKTDPG---KLSGAIEVDRVTFRY--RPDGp 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 380 LVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIREN 459
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFEN 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 460 ILfGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESER 539
Cdd:TIGR03797 547 IA-GGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQA 625
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 540 TVQDALDRASVGRttVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLgmddgGEGGVYARMVHLQ 606
Cdd:TIGR03797 626 IVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELM-----AREGLFAQLARRQ 685
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1018-1261 |
2.40e-50 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 188.77 E-value: 2.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFSYptRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQ 1097
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLFSGTIRDNIAYGaaeEHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLK 1177
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1178 DARILLLDEATSALDAASERLVQDAVdRMLRGRTC-VVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAvgRAGTYYN 1256
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQAL-AAVREHTTlVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLA--AQGRYWQ 570
|
....*
gi 1002260479 1257 LIKLQ 1261
Cdd:PRK10790 571 MYQLQ 575
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
438-1247 |
6.71e-50 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 194.57 E-value: 6.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 438 LRSQIGLVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVkLPHGYETHVGQFGTQLSGGQKQRIAIARAL 517
Cdd:PLN03130 677 IRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAV 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 518 VRDPRILLLDEATSALDAESERTVQDA-LDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELlgMDDGgeg 596
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL--SNNG--- 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 597 gvyarmVHLQKAPPVAAREErhravDVVESEMVSfrSVEIMSAVSATEHRPSPAPSFCSVEHSTEIGRKLVDHGVARSRK 676
Cdd:PLN03130 831 ------PLFQKLMENAGKME-----EYVEENGEE--EDDQTSSKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEERETG 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 677 PSKLRLLKmnrpEWKQALLGC-VGAVVFGAVLPLYSYSLGSLPEVYFLADDGQIRSKTRLYYFL---FLGIAVVCITanI 752
Cdd:PLN03130 898 VVSWKVLE----RYKNALGGAwVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTPKTHGPLFYNLiyaLLSFGQVLVT--L 971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 753 VQHYNFAVMGERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKV-RSLVGDRMCLLVQAGATASLGFSLA 831
Cdd:PLN03130 972 LNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHT--NPLGRIINRFAKDLGDIdRNVAVFVNMFLGQIFQLLSTFVLIG 1049
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 832 LAVSWRLATVMmamqPLII----ASFYFKKVLMAAMSKKAKKAQVQGSQLaSEAVVNHRTITAFSSQRRMlrlyeAAQQG 907
Cdd:PLN03130 1050 IVSTISLWAIM----PLLVlfygAYLYYQSTAREVKRLDSITRSPVYAQF-GEALNGLSTIRAYKAYDRM-----AEING 1119
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 908 PKKDNVAHswfsgfcLCLCQFSNTGSMAVALWYGGKLMakglITPTHLFQVF---------FMLMTMGRVIADAGSLTS- 977
Cdd:PLN03130 1120 RSMDNNIR-------FTLVNMSSNRWLAIRLETLGGLM----IWLTASFAVMqngraenqaAFASTMGLLLSYALNITSl 1188
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 978 --------DLAQGG-DAVRSVLDTLDRE---PTIKDDDNDnerkkKKRKEIKGAIEFKNVHFSYptRPEVA-VLAGFSLE 1044
Cdd:PLN03130 1189 ltavlrlaSLAENSlNAVERVGTYIDLPseaPLVIENNRP-----PPGWPSSGSIKFEDVVLRY--RPELPpVLHGLSFE 1261
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1045 IGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNIayGAAEEH 1124
Cdd:PLN03130 1262 ISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL--DPFNEH 1339
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1125 ATEDevaraaalanahgFISAMER------------GYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALD 1192
Cdd:PLN03130 1340 NDAD-------------LWESLERahlkdvirrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 1193 AASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:PLN03130 1407 VRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1020-1217 |
5.31e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.08 E-value: 5.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSGTIRDNIA--YGAAEEHATEDEVaraaalanahgfISAMER-GYDTRVGERGA-QLSGGQRQRIALARAV 1175
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPfpFQLRERKFDRERA------------LELLERlGLPPDILDKPVeRLSGGERQRLALIRAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1002260479 1176 LKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAH 1217
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSH 189
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1018-1258 |
6.20e-49 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 186.87 E-value: 6.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFSYPTRPEVavLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQ 1097
Cdd:TIGR01193 472 GDIVINDVSYSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLFSGTIRDNIAYGAaEEHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLK 1177
Cdd:TIGR01193 550 INYLPQEPYIFSGSILENLLLGA-KENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1178 DARILLLDEATSALDAASERLVqdaVDRM--LRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAvgRAGTYY 1255
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKI---VNNLlnLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLD--RNGFYA 703
|
...
gi 1002260479 1256 NLI 1258
Cdd:TIGR01193 704 SLI 706
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
19-345 |
1.22e-48 |
|
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: 176.10 E-value: 1.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 19 HDRCLMALGVLGSFGDGMMQPLSMLVLGDIVNSYGGAGGAGSARSafssgaVDKFALRLLYVAVAVGACSFLEGLCWTRT 98
Cdd:cd18578 6 PEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSE------ANFWALMFLVLAIVAGIAYFLQGYLFGIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 99 AERQASKMRRLYLEAVLSQEVAFFDAAPSSPSSpqaqaqattfrVISTVSDDADAIQDFLGEKLPMVLANATLFFGALAV 178
Cdd:cd18578 80 GERLTRRLRKLAFRAILRQDIAWFDDPENSTGA-----------LTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 179 SFVFAWRLALAGLPFTLLLFVTpSVLLAGRMAAAAGEARAAYEEAGGIAQQAVSSIRTVASYTAERRTVERFRGAVARSA 258
Cdd:cd18578 149 AFVYGWKLALVGLATVPLLLLA-GYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 259 ALGVRQGLIKGAVIG-SMGVIYAVWSFLSWIGSLLVIHLHAQGGHVFVASICIVLAGMSIMMALPNLRYFIDATAAASRM 337
Cdd:cd18578 228 KKGLRRALISGLGFGlSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARI 307
|
....*...
gi 1002260479 338 QEMIEMLP 345
Cdd:cd18578 308 FRLLDRKP 315
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1026-1261 |
1.53e-48 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 182.99 E-value: 1.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1026 HFSYPTRpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEP 1105
Cdd:PRK10789 320 QFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1106 TLFSGTIRDNIAYGAAEehATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLD 1185
Cdd:PRK10789 399 FLFSDTVANNIALGRPD--ATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1186 EATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAvgRAGTYYNLIKLQ 1261
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ--QSGWYRDMYRYQ 550
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
688-1256 |
2.09e-48 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 189.47 E-value: 2.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 688 PEWKQALLGC--VGAVVFGAVLPLYSYSLGSLPEVYFLADDgqirskTRLYYFLFLGIAVVCITANIVQHYNFAVMGERL 765
Cdd:PTZ00265 55 PASHRKLLGVsfVCATISGGTLPFFVSVFGVIMKNMNLGEN------VNDIIFSLVLIGIFQFILSFISSFCMDVVTTKI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 766 TERVRGQMLAKILsFEVGWFdEDENSSAAVCARLATQSSKVRSLVGDRMcLLVQAGATASLGFSL-ALAVSWRLATVMMA 844
Cdd:PTZ00265 129 LKTLKLEFLKSVF-YQDGQF-HDNNPGSKLTSDLDFYLEQVNAGIGTKF-ITIFTYASAFLGLYIwSLFKNARLTLCITC 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 845 MQPLIIASFYF--KKVLMAAMSKKAKKAQVQgsQLASEAVVNHRTITAFSSQRRMLRLYEAAQQGPKKDNVAHSWFSGFC 922
Cdd:PTZ00265 206 VFPLIYICGVIcnKKVKINKKTSLLYNNNTM--SIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 923 LCLCQFSNTGSMAVALWYGGKLMAKGLIT--PTHLFQVFFMLMTMGRVIADAGSLT------SDLAQGGDAVRSVLDTLD 994
Cdd:PTZ00265 284 IGMINGFILASYAFGFWYGTRIIISDLSNqqPNNDFHGGSVISILLGVLISMFMLTiilpniTEYMKSLEATNSLYEIIN 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 995 REPTIKDDDNDNERKKKKrkeikgAIEFKNVHFSYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDA 1074
Cdd:PTZ00265 364 RKPLVENNDDGKKLKDIK------KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDP 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1075 QRGSVLV-DGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNIAYG--------AAEEHATED----------------- 1128
Cdd:PTZ00265 438 TEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdleALSNYYNEDgndsqenknkrnscrak 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1129 ------------------------------EVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKD 1178
Cdd:PTZ00265 518 cagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRN 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1179 ARILLLDEATSALDAASERLVQDAVDRmLRG---RTCVVVAHRLSTVEKSDTIAVVKDgrvAERGRHHELLAVGRAGTYY 1255
Cdd:PTZ00265 598 PKILILDEATSSLDNKSEYLVQKTINN-LKGnenRITIIIAHRLSTIRYANTIFVLSN---RERGSTVDVDIIGEDPTKD 673
|
.
gi 1002260479 1256 N 1256
Cdd:PTZ00265 674 N 674
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1020-1236 |
4.35e-48 |
|
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: 169.32 E-value: 4.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSGTIRDNIaygaaeehatedevaraaalanahgfisamergydtrvgergaqLSGGQRQRIALARAVLKDA 1179
Cdd:cd03246 80 YLPQDDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 1180 RILLLDEATSALDAASERLVQDAVDRM-LRGRTCVVVAHRLSTVEKSDTIAVVKDGRV 1236
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1018-1241 |
4.75e-48 |
|
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: 170.29 E-value: 4.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFSY-PTRPEVavLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRS 1096
Cdd:cd03369 5 GEIEVENLSVRYaPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEPTLFSGTIRDNIAygaAEEHATEDEVARAAalanahgfisamergydtRVGERGAQLSGGQRQRIALARAVL 1176
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLD---PFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 1177 KDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGR 1241
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
329-573 |
1.37e-47 |
|
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: 179.02 E-value: 1.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 329 DATAAASRMQEMIEMlPPLEGAEKKGATMERIRgEIVFKDVHFSYPSRPDtlVLNGFNLTISEGATVGLVGGSGSGKSTV 408
Cdd:TIGR02857 289 DGVAAAEALFAVLDA-APRPLAGKAPVTAAPAS-SLEFSGVSVAYPGRRP--ALRPVSFTVPPGERVALVGPSGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 409 ISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKL 488
Cdd:TIGR02857 365 LNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAAL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 489 PHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKAD 568
Cdd:TIGR02857 445 PQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALAD 524
|
....*
gi 1002260479 569 TIAVL 573
Cdd:TIGR02857 525 RIVVL 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1018-1261 |
2.04e-47 |
|
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: 181.69 E-value: 2.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFSYptRPE-VAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRS 1096
Cdd:TIGR03797 450 GAIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRR 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEPTLFSGTIRDNIAYGAAeehATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVL 1176
Cdd:TIGR03797 528 QLGVVLQNGRLMSGSIFENIAGGAP---LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALV 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1177 KDARILLLDEATSALDAASERLVQDAVDRMlrGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAVGraGTYYN 1256
Cdd:TIGR03797 605 RKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMARE--GLFAQ 680
|
....*
gi 1002260479 1257 LIKLQ 1261
Cdd:TIGR03797 681 LARRQ 685
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
362-583 |
2.41e-47 |
|
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: 168.83 E-value: 2.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 362 GEIVFKDVHFSYpsRPDT-LVLNGFNLTISEG-------------ATVglvggsgsgkstvISLLQRFYSPDSGEISMDD 427
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLpPVLKNISFSIKPGekvgivgrtgsgkSSL-------------LLALFRLVELSSGSILIDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 428 HGIDTLNVEWLRSQIGLVSQEPVLFATSIRENILFGDEtASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQ 507
Cdd:cd03244 66 VDISKIGLHDLRSRISIIPQDPVLFSGTIRSNLDPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 508 KQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGT 583
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
89-608 |
4.64e-47 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 179.14 E-value: 4.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 89 FLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDAAPSSpsspqaqaqattfRVISTVSDDADAIQDFLGEKLPMVLAN 168
Cdd:PRK10790 83 YAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVG-------------QLISRVTNDTEVIRDLYVTVVATVLRS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 169 ATLFFGALAVSFVFAWRLALAGL---PFTLLL------FVTPSVLLAGRMAAAAGEARAAYEEAGGIAQQAVSSIR---- 235
Cdd:PRK10790 150 AALIGAMLVAMFSLDWRMALVAImifPAVLVVmviyqrYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARfger 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 236 ----TVASYTAERRTVeRFRGAVAR------SA----ALGVRQGLIKGAVIGsMGVIYAvwsFLSWIGSL--LVIHLHAQ 299
Cdd:PRK10790 230 mgeaSRSHYMARMQTL-RLDGFLLRpllslfSAlilcGLLMLFGFSASGTIE-VGVLYA---FISYLGRLnePLIELTTQ 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 300 GGHVFVAsiciVLAGMSI--MMALPNLRYFIDATAAASrmqemiemlpplegaekkgatmerirGEIVFKDVHFSYpsRP 377
Cdd:PRK10790 305 QSMLQQA----VVAGERVfeLMDGPRQQYGNDDRPLQS--------------------------GRIDIDNVSFAY--RD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 378 DTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIR 457
Cdd:PRK10790 353 DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 458 ENILFGDETaSLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAES 537
Cdd:PRK10790 433 ANVTLGRDI-SEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT 511
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 538 ERTVQDALdRASVGRTT-VIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLgmddgGEGGVYARMVHLQKA 608
Cdd:PRK10790 512 EQAIQQAL-AAVREHTTlVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL-----AAQGRYWQMYQLQLA 577
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
77-588 |
3.22e-46 |
|
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: 175.61 E-value: 3.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 77 LLYVAVAVGACSFLEGLCWTRTAERQASKMRrlyLEAVLSQEVafFDAAPSSPSSPQAQAQATTFRvistvsdDADAIQD 156
Cdd:TIGR01842 46 LMLTVLALGLYLFLGLLDALRSFVLVRIGEK---LDGALNQPI--FAASFSATLRRGSGDGLQALR-------DLDQLRQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 157 FLGEKLPMVLANATLFFGALAVSFVFAWRLALAGLPFTLLLFVTpSVL---LAGRMAAAAGEARAAYEEAGGIAQQAVSS 233
Cdd:TIGR01842 114 FLTGPGLFAFFDAPWMPIYLLVCFLLHPWIGILALGGAVVLVGL-ALLnnrATKKPLKEATEASIRANNLADSALRNAEV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 234 IRTVASYTAERRTVERFR-GAVARSAALGVRQGLIKGaviGSMGVIYAVWSFLSWIGSLLVIHLHAQGGHVFVASICIVL 312
Cdd:TIGR01842 193 IEAMGMMGNLTKRWGRFHsKYLSAQSAASDRAGMLSN---LSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 313 AGMSIMMALPNLRYFIDATAAASRMQEMIEMLPPLEGAEKkgatMERIRGEIVFKDVHFSYPSrPDTLVLNGFNLTISEG 392
Cdd:TIGR01842 270 ALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMP----LPEPEGHLSVENVTIVPPG-GKKPTLRGISFSLQAG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 393 ATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENILFGDETASLKQV 472
Cdd:TIGR01842 345 EALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 473 VAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASV-G 551
Cdd:TIGR01842 425 IEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArG 504
|
490 500 510
....*....|....*....|....*....|....*..
gi 1002260479 552 RTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:TIGR01842 505 ITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
332-593 |
4.51e-46 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 175.78 E-value: 4.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 332 AAASRMQEMIEMLPPLEGAEKKGAtmERIRGEIVFKDVHFSYPSRPDTlVLNGFNLTISEGATVGLVGGSGSGKSTVISL 411
Cdd:PRK11160 309 ASARRINEITEQKPEVTFPTTSTA--AADQVSLTLNNVSFTYPDQPQP-VLKGLSLQIKAGEKVALLGRTGCGKSTLLQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 412 LQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENILFGDETAS-------LKQVvaaakmanAHEF 484
Cdd:PRK11160 386 LTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASdealievLQQV--------GLEK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 485 IVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTL 564
Cdd:PRK11160 458 LLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGL 537
|
250 260
....*....|....*....|....*....
gi 1002260479 565 RKADTIAVLDAGRVVEAGTHDELLGMDDG 593
Cdd:PRK11160 538 EQFDRICVMDNGQIIEQGTHQELLAQQGR 566
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1020-1235 |
5.70e-45 |
|
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: 161.48 E-value: 5.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVA--VLAGFSLEIGAGKTVALVGPSGSGKSTVIGLI--ErfYDAQRGSVLVDGedirsyslarlr 1095
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPG------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1096 sQVALVSQEPTLFSGTIRDNIAYGAAEEHATEDEVaraaalanahgfISA---------MERGYDTRVGERGAQLSGGQR 1166
Cdd:cd03250 67 -SIAYVSQEPWIQNGTIRENILFGKPFDEERYEKV------------IKAcalepdleiLPDGDLTEIGEKGINLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 1167 QRIALARAVLKDARILLLDEATSALDAA-SERLVQDAV-DRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGR 1235
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
433-602 |
6.86e-45 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 172.34 E-value: 6.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 433 LNVEWLRSQIGLVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIA 512
Cdd:PRK11174 416 LDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLA 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 513 IARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELlgmdd 592
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAEL----- 570
|
170
....*....|
gi 1002260479 593 GGEGGVYARM 602
Cdd:PRK11174 571 SQAGGLFATL 580
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
264-604 |
9.24e-45 |
|
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: 174.16 E-value: 9.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 264 QGLIKGAVIGSMGViyavwsFLSWIGSLLVIHLHAQGGHV--FVASICIVLAGMSIMMAL-PNLRyfiDATAAASRMQEM 340
Cdd:TIGR01193 381 QQAIKAVTKLILNV------VILWTGAYLVMRGKLTLGQLitFNALLSYFLTPLENIINLqPKLQ---AARVANNRLNEV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 341 ieMLPPLEGAEKKGAT-MERIRGEIVFKDVHFSYP-SRPdtlVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSP 418
Cdd:TIGR01193 452 --YLVDSEFINKKKRTeLNNLNGDIVINDVSYSYGyGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQA 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 419 DSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENILFG-DETASLKQVVAAAKMANAHEFIVKLPHGYETHVG 497
Cdd:TIGR01193 527 RSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELS 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 498 QFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASvGRTTVIVAHRLSTLRKADTIAVLDAGR 577
Cdd:TIGR01193 607 EEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ-DKTIIFVAHRLSVAKQSDKIIVLDHGK 685
|
330 340
....*....|....*....|....*..
gi 1002260479 578 VVEAGTHDELLgmddgGEGGVYARMVH 604
Cdd:TIGR01193 686 IIEQGSHDELL-----DRNGFYASLIH 707
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1020-1219 |
2.63e-44 |
|
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: 169.46 E-value: 2.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVavLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:TIGR02868 335 LELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSGTIRDNIAYGAAEehATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDA 1179
Cdd:TIGR02868 413 VCAQDAHLFDTTVRENLRLARPD--ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1002260479 1180 RILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRL 1219
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1020-1247 |
2.70e-44 |
|
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: 168.93 E-value: 2.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRP--EVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYS---LARL 1094
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1095 RSQVALVSQEPT--LFSG-TIRDNIA-----YGAAEEHATEDEVAraaalanahgfiSAMER-GYDTRVGER-GAQLSGG 1164
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIAeplrlHGLLSRAERRERVA------------ELLERvGLPPDLADRyPHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1165 QRQRIALARAVLKDARILLLDEATSALDAAserlVQDAVDRMLR------GRTCVVVAHRLSTVEK-SDTIAVVKDGRVA 1237
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVS----VQAQILNLLRdlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
250
....*....|
gi 1002260479 1238 ERGRHHELLA 1247
Cdd:COG1123 485 EDGPTEEVFA 494
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1020-1245 |
4.28e-44 |
|
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: 159.65 E-value: 4.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRpevAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQR-----GSVLVDGEDIRSYSLAR- 1093
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1094 -LRSQVALVSQEPTLFSGTIRDNIAYGA-----AEEHATEDEVAraaalanahgfiSAMER-GYDTRVGER--GAQLSGG 1164
Cdd:cd03260 78 eLRRRVGMVFQKPNPFPGSIYDNVAYGLrlhgiKLKEELDERVE------------EALRKaALWDEVKDRlhALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1165 QRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHH 1243
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTE 225
|
..
gi 1002260479 1244 EL 1245
Cdd:cd03260 226 QI 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1020-1247 |
1.21e-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: 158.65 E-value: 1.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPtrPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPT--LFSGTIRDNIAYGAAEEHATEDEVARAAAlanahgfiSAMErgydtRVG-----ERG-AQLSGGQRQRIAL 1171
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVE--------EALE-----LVGlehlaDRPpHELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 1172 ARAVLKDARILLLDEATSALDAASERLVQDAVDRM-LRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELLA 1247
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFS 223
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
437-1245 |
3.19e-43 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 172.66 E-value: 3.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 437 WLRSQIGLVSQEPVLFATSIRENILFGDE--TASLKQVVAAAKMANAhefIVKLPHGYETHVGQFGTQLSGGQKQRIAIA 514
Cdd:PTZ00243 718 WAERSIAYVPQQAWIMNATVRGNILFFDEedAARLADAVRVSQLEAD---LAQLGGGLETEIGEKGVNLSGGQKARVSLA 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 515 RALVRDPRILLLDEATSALDAE-SERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLgmddg 593
Cdd:PTZ00243 795 RAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM----- 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 594 gEGGVYARMVhlqkappVAAREERHRAVDVVESEMVSfrsVEIMSAVSATEHRPSPAPsfcsvehsteigRKLVDHGVAR 673
Cdd:PTZ00243 870 -RTSLYATLA-------AELKENKDSKEGDADAEVAE---VDAAPGGAVDHEPPVAKQ------------EGNAEGGDGA 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 674 SRKPSKLRLlkMNRPE-------WK--QALLG-CVGAVVFGAVLPLYSYS-LGSLPEVYFLA--DDGQIRSKTRLYYFLF 740
Cdd:PTZ00243 927 ALDAAAGRL--MTREEkasgsvpWStyVAYLRfCGGLHAAGFVLATFAVTeLVTVSSGVWLSmwSTRSFKLSAATYLYVY 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 741 LGIAVVCITANIVQHY-NFAVM--GERLTERVrgqMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCLL 817
Cdd:PTZ00243 1005 LGIVLLGTFSVPLRFFlSYEAMrrGSRNMHRD---LLRSVSRGTMSFFDT--TPLGRILNRFSRDIDILDNTLPMSYLYL 1079
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 818 VQagatasLGFSLALAVswrlaTVMMAMQPLIIASF------YFKkvLMAAMSKKAKKAQVQGS-------QLASEAVVN 884
Cdd:PTZ00243 1080 LQ------CLFSICSSI-----LVTSASQPFVLVALvpcgylYYR--LMQFYNSANREIRRIKSvakspvfTLLEEALQG 1146
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 885 HRTITAFSSQRRM----LRLYEAAQQGPKKDNVAHSWFS---GFCLCLCQFS-----NTGSMAVALWYGGKLMAKGLITP 952
Cdd:PTZ00243 1147 SATITAYGKAHLVmqeaLRRLDVVYSCSYLENVANRWLGvrvEFLSNIVVTVialigVIGTMLRATSQEIGLVSLSLTMA 1226
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 953 THLFQVFFMLMTM-GRVIADAGSL------TSDLAQGG-DAVRSVLDTLDREPTIKDD-------DNDNERKKKKRKEIK 1017
Cdd:PTZ00243 1227 MQTTATLNWLVRQvATVEADMNSVerllyyTDEVPHEDmPELDEEVDALERRTGMAADvtgtvviEPASPTSAAPHPVQA 1306
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFSYptRPEVA-VLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRS 1096
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEPTLFSGTIRDNIaygAAEEHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVL 1176
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNV---DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALL 1461
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1177 K-DARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHEL 1245
Cdd:PTZ00243 1462 KkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1019-1241 |
6.27e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 156.36 E-value: 6.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPT-RPEVAVLAGFSLEIGAGKTVALVGPSGSGKST---VIGLIERfydAQRGSVLVDGEDIRSYS---L 1091
Cdd:COG1136 4 LLELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSereL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1092 ARLRSQ-VALVSQEPTLFSG-TIRDNIA---------YGAAEEHATEdevaraaalanahgfisAMER-GYDTRVGERGA 1159
Cdd:COG1136 81 ARLRRRhIGFVFQFFNLLPElTALENVAlplllagvsRKERRERARE-----------------LLERvGLGDRLDHRPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1160 QLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTVEKSDTIAVVKDGRVA 1237
Cdd:COG1136 144 QLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
....
gi 1002260479 1238 ERGR 1241
Cdd:COG1136 224 SDER 227
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1018-1247 |
1.10e-42 |
|
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: 164.83 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFSyPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQ 1097
Cdd:TIGR01842 315 GHLSVENVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLFSGTIRDNIAygAAEEHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLK 1177
Cdd:TIGR01842 394 IGYLPQDVELFPGTVAENIA--RFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYG 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 1178 DARILLLDEATSALDAASERLVQDAVDRM-LRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1020-1247 |
5.07e-42 |
|
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: 154.25 E-value: 5.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPtrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLaRLRSQVA 1099
Cdd:COG4555 2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIAYgAAEEHATEDEVARAAALANAHGFIsaMERGYDTRVGErgaqLSGGQRQRIALARAVLKD 1178
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRY-FAELYGLFDEELKKRIEELIELLG--LEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 1179 ARILLLDEATSALDAASERLVQDAVDRML-RGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELLA 1247
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
694-982 |
1.10e-41 |
|
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: 155.32 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 694 LLGCVGAVVFGAVLPLYSYSLGSL-----PEVYFLADDGQIRSKTRLYYFLFLGIAVVCITANIVQHYNFAVMGERLTER 768
Cdd:cd18577 2 IIGLLAAIAAGAALPLMTIVFGDLfdaftDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 769 VRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCLLVQAGATASLGFSLALAVSWRLATVMMAMQPL 848
Cdd:cd18577 82 IRKRYLKALLRQDIAWFDK--NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 849 IIASFYFKKVLMAAMSKKAKKAQVQGSQLASEAVVNHRTITAFSSQRRMLRLYEAAQQGPKKDNVAHSWFSGFCLCLCQF 928
Cdd:cd18577 160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 929 SNTGSMAVALWYGGKLMAKGLITPTHLFQVFFMLMTMGRVIADAGSLTSDLAQG 982
Cdd:cd18577 240 IIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKA 293
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
77-561 |
3.61e-41 |
|
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: 160.22 E-value: 3.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 77 LLYVAVAVGACSFLeGLcwTRTAERqaskmrrlYLEAVLSQEVAFFDAAPS--------SPSSPQAQAQATTFRVISTVS 148
Cdd:TIGR02868 49 VLYLSVAAVAVRAF-GI--GRAVFR--------YLERLVGHDAALRSLGALrvrvyerlARQALAGRRRLRRGDLLGRLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 149 DDADAIQDFLGEKL-PMVLAnATLFFGALAVSFVFAWRLALAGLPFTLL-LFVTPSVLLAGRMAAAAGEARAAYeeagGI 226
Cdd:TIGR02868 118 ADVDALQDLYVRVIvPAGVA-LVVGAAAVAAIAVLSVPAALILAAGLLLaGFVAPLVSLRAARAAEQALARLRG----EL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 227 AQQAVSSIRTVASYTAERRTVERFRGAVARSAAL-------GVRQGLIKGAVIGSMGViyAVWSFLsWIGSLLVIHlHAQ 299
Cdd:TIGR02868 193 AAQLTDALDGAAELVASGALPAALAQVEEADRELtraerraAAATALGAALTLLAAGL--AVLGAL-WAGGPAVAD-GRL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 300 GGHVFVASICIVLAGMSIMMALPN-LRYFIDATAAASRMQEMIEmlPPLEGAEKKGATMERIRGE---IVFKDVHFSYPs 375
Cdd:TIGR02868 269 APVTLAVLVLLPLAAFEAFAALPAaAQQLTRVRAAAERIVEVLD--AAGPVAEGSAPAAGAVGLGkptLELRDLSAGYP- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 376 rPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATS 455
Cdd:TIGR02868 346 -GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTT 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 456 IRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDA 535
Cdd:TIGR02868 425 VRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
490 500
....*....|....*....|....*.
gi 1002260479 536 ESERTVQDALDRASVGRTTVIVAHRL 561
Cdd:TIGR02868 505 ETADELLEDLLAALSGRTVVLITHHL 530
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1019-1246 |
1.15e-40 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 150.96 E-value: 1.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQV 1098
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQEPTL-FSGTIRDNIAYG------------AAEEHATEDevaraaalanahgfisAMERgydTRVG---ERG-AQL 1161
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGryphlglfgrpsAEDREAVEE----------------ALER---TGLEhlaDRPvDEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1162 SGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRM--LRGRTCVVVAH------RLstvekSDTIAVVKD 1233
Cdd:COG1120 139 SGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHdlnlaaRY-----ADRLVLLKD 213
|
250
....*....|...
gi 1002260479 1234 GRVAERGRHHELL 1246
Cdd:COG1120 214 GRIVAQGPPEEVL 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1020-1239 |
1.25e-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: 149.54 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTR-PEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRsyslaRLRSQV 1098
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQEPTLFS-GTIRDNIAYG---------AAEEHATEdevaraaalanahgfisAMErgydtRVGERGA------QLS 1162
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqgvpkaEARERAEE-----------------LLE-----LVGLSGFenayphQLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1163 GGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLS-TVEKSDTIAVV--KDGRVA 1237
Cdd:cd03293 134 GGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLsaRPGRIV 213
|
..
gi 1002260479 1238 ER 1239
Cdd:cd03293 214 AE 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1020-1235 |
2.39e-40 |
|
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: 147.33 E-value: 2.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPtrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLAR--LRSQ 1097
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLFSG-TIRDNIAYGaaeehatedevaraaalanahgfisamergydtrvgergaqLSGGQRQRIALARAVL 1176
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG-----------------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 1177 KDARILLLDEATSALDAAS----ERLVQDAVDRMlrGRTCVVVAHRLSTVEK-SDTIAVVKDGR 1235
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITrrevRALLKSLQAQL--GITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1021-1235 |
3.14e-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: 148.00 E-value: 3.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1021 EFKNVHFSYPTRPEvAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVAL 1100
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1101 VSQEPT--LFSGTIRDNIAYGAAEEHATEDEVARAAALANAHGFISAMErgyDTRVgergAQLSGGQRQRIALARAVLKD 1178
Cdd:cd03225 80 VFQNPDdqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLR---DRSP----FTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1179 ARILLLDEATSALDAASERLVQDAVDRMLR-GRTCVVVAHRLSTV-EKSDTIAVVKDGR 1235
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1020-1247 |
3.61e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 148.67 E-value: 3.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSlARLRSQVA 1099
Cdd:COG1131 1 IEVRGLTKRYGDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNI-----AYGAAEEHATE--DEVARAAalanahgfisAMERGYDTRVGergaQLSGGQRQRIAL 1171
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEAREriDELLELF----------GLTDAADRKVG----TLSGGMKQRLGL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 1172 ARAVLKDARILLLDEATSALDAASERLVQDAVDRML-RGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELLA 1247
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1020-1236 |
1.36e-39 |
|
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: 146.48 E-value: 1.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPE-VAVLAGFSLEIGAGKTVALVGPSGSGKST---VIGLIERfydAQRGSVLVDGEDIRSYSLARL- 1094
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1095 ---RSQVALVSQEPTLFSG-TIRDNIAYGA--AEEHATEDEVAraaalanahgFISAMER-GYDTRVGERGAQLSGGQRQ 1167
Cdd:cd03255 78 afrRRHIGFVFQSFNLLPDlTALENVELPLllAGVPKKERRER----------AEELLERvGLGDRLNHYPSELSGGQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 1168 RIALARAVLKDARILLLDEATSALDAASERLVQDAVDRM--LRGRTCVVVAHRLSTVEKSDTIAVVKDGRV 1236
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1038-1189 |
1.67e-39 |
|
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: 143.56 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1038 LAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSG-TIRDNI 1116
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 1117 AYGAAEEHATEDEVARAaalanahgFISAMER-----GYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATS 1189
Cdd:pfam00005 81 RLGLLLKGLSKREKDAR--------AEEALEKlglgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1020-1240 |
3.49e-39 |
|
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: 145.73 E-value: 3.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRP-EVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARL---R 1095
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1096 SQVALVSQE------PTLfsgTIRDNIA-----YGAAEEHATEDEVARAAalanahgfisAMERGYDTRVGER-GAQLSG 1163
Cdd:cd03257 82 KEIQMVFQDpmsslnPRM---TIGEQIAeplriHGKLSKKEARKEAVLLL----------LVGVGLPEEVLNRyPHELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1164 GQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRM--LRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERG 1240
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1019-1247 |
5.16e-39 |
|
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: 153.14 E-value: 5.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRpEVAVLAGFSLEIGAGKTVALVGPSGSGKST----VIGLIERFYDAqRGSVLVDGEDIRSYSLARL 1094
Cdd:COG1123 4 LLEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTlalaLMGLLPHGGRI-SGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1095 RSQVALVSQEPT--LFSGTIRDNIAYGAAEEHATEDEVARAAalanahgfISAMER-GYDTRVGERGAQLSGGQRQRIAL 1171
Cdd:COG1123 82 GRRIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARV--------LELLEAvGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1172 ARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTV-EKSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1021-1235 |
9.26e-39 |
|
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: 142.00 E-value: 9.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1021 EFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVAL 1100
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1101 VSQeptlfsgtirdniaygaaeehatedevaraaalanahgfisamergydtrvgergaqLSGGQRQRIALARAVLKDAR 1180
Cdd:cd00267 78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 1181 ILLLDEATSALDAASERLVQDAVDRML-RGRTCVVVAHRLSTVEK-SDTIAVVKDGR 1235
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1020-1247 |
3.94e-38 |
|
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: 143.03 E-value: 3.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYS---LARLRS 1096
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEPTLFSG-TIRDNIAYGAAEEHATEDEVARAAALANAHgfisamergydtRVGERG------AQLSGGQRQRI 1169
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREHTRLSEEEIREIVLEKLE------------AVGLRGaedlypAELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1170 ALARAVLKDARILLLDEATSALDAASerlvQDAVDRMLR------GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRH 1242
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIA----SGVIDDLIRslkkelGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTP 221
|
....*
gi 1002260479 1243 HELLA 1247
Cdd:cd03261 222 EELRA 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1019-1247 |
4.06e-38 |
|
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: 143.20 E-value: 4.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKST----VIGLIErfydAQRGSVLVDGEDIRSYS---L 1091
Cdd:COG1127 5 MIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVllklIIGLLR----PDSGEILVDGQDITGLSekeL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1092 ARLRSQVALVSQEPTLFSG-TIRDNIAYGaAEEHA--TEDEVARAaalanahgfisAMERgyDTRVGERGA------QLS 1162
Cdd:COG1127 78 YELRRRIGMLFQGGALFDSlTVFENVAFP-LREHTdlSEAEIREL-----------VLEK--LELVGLPGAadkmpsELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1163 GGQRQRIALARAVLKDARILLLDEATSALD----AASERLVQDAVDRMlrGRTCVVVAHRLSTVEK-SDTIAVVKDGRVA 1237
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDpitsAVIDELIRELRDEL--GLTSVVVTHDLDSAFAiADRVAVLADGKII 221
|
250
....*....|
gi 1002260479 1238 ERGRHHELLA 1247
Cdd:COG1127 222 AEGTPEELLA 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1020-1240 |
4.32e-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: 141.89 E-value: 4.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPtrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRsqVA 1099
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN--IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIAYGAAEEHATEDEVARAAALANAHGFISAMErgydtrvGERGAQLSGGQRQRIALARAVLKD 1178
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLL-------NRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 1179 ARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLS-TVEKSDTIAVVKDGRVAERG 1240
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1019-1247 |
6.27e-38 |
|
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: 142.63 E-value: 6.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRPE-VAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQ 1097
Cdd:COG1124 1 MLEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLfS----GTIRDNIAYGAAEEHATEDEVaraaalanahGFISAMER-GYDTRVGER-GAQLSGGQRQRIAL 1171
Cdd:COG1124 81 VQMVFQDPYA-SlhprHTVDRILAEPLRIHGLPDREE----------RIAELLEQvGLPPSFLDRyPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1172 ARAVLKDARILLLDEATSALDAaserLVQDAVDRML------RGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHE 1244
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDV----SVQAEILNLLkdlreeRGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
...
gi 1002260479 1245 LLA 1247
Cdd:COG1124 226 LLA 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1019-1247 |
1.39e-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: 142.15 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRP-EVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRsyslaRLRSQ 1097
Cdd:COG1116 7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-----GPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLFs-gTIRDNIAYGAAEEHATEDEVARAaalanahgfisAMErgYDTRVGERGA------QLSGGQRQRIA 1170
Cdd:COG1116 82 RGVVFQEPALLpwlTVLDNVALGLELRGVPKAERRER-----------ARE--LLELVGLAGFedayphQLSGGMRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1171 LARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAH------RLstvekSDTIAVVKD--GRVAE-- 1238
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVEei 223
|
250
....*....|....
gi 1002260479 1239 -----RGRHHELLA 1247
Cdd:COG1116 224 dvdlpRPRDRELRT 237
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1020-1247 |
2.90e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 140.28 E-value: 2.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevavlAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARlRSqVA 1099
Cdd:COG3840 2 LRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RP-VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIAYG-------AAEEHATEDEvaraaalanahgfisAMER----GYDTRvgeRGAQLSGGQRQ 1167
Cdd:COG3840 75 MLFQENNLFPHlTVAQNIGLGlrpglklTAEQRAQVEQ---------------ALERvglaGLLDR---LPGQLSGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1168 RIALARAVLKDARILLLDEATSALDAA--SE--RLVQDAVDRmlRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRH 1242
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPAlrQEmlDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPT 214
|
....*
gi 1002260479 1243 HELLA 1247
Cdd:COG3840 215 AALLD 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1020-1236 |
7.73e-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: 136.76 E-value: 7.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSlARLRSQVA 1099
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIaygaaeehatedevaraaalanahgfisamergydtrvgergaQLSGGQRQRIALARAVLKD 1178
Cdd:cd03230 77 YLPEEPSLYENlTVRENL-------------------------------------------KLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1179 ARILLLDEATSALDAASERLVQDAVDRML-RGRTCVVVAHRLSTVEK-SDTIAVVKDGRV 1236
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1019-1245 |
1.69e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 141.77 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPtrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIrsyslARL---R 1095
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLppeK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1096 SQVALVSQEPTLFSG-TIRDNIAYG-------AAEEHATEDEvaraaalanahgfisAMER----GYDTRvgeRGAQLSG 1163
Cdd:COG3842 77 RNVGMVFQDYALFPHlTVAENVAFGlrmrgvpKAEIRARVAE---------------LLELvgleGLADR---YPHQLSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1164 GQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLS---TVekSDTIAVVKDGRVAE 1238
Cdd:COG3842 139 GQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQ 216
|
....*..
gi 1002260479 1239 RGRHHEL 1245
Cdd:COG3842 217 VGTPEEI 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1020-1240 |
5.18e-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: 137.05 E-value: 5.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDI--RSYSLARLRSQ 1097
Cdd:COG1126 2 IEIENLHKSFGDLE---VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLFSG-TIRDNIAYG----------AAEEHAtedevaraaalanahgfisameRGYDTRVG--ERG----AQ 1160
Cdd:COG1126 79 VGMVFQQFNLFPHlTVLENVTLApikvkkmskaEAEERA----------------------MELLERVGlaDKAdaypAQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1161 LSGGQRQRIALARAVLKDARILLLDEATSALDAaseRLVQDAVDRML----RGRTCVVVAHRLSTVEK-SDTIAVVKDGR 1235
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDP---ELVGEVLDVMRdlakEGMTMVVVTHEMGFAREvADRVVFMDGGR 213
|
....*
gi 1002260479 1236 VAERG 1240
Cdd:COG1126 214 IVEEG 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
364-582 |
7.87e-36 |
|
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: 134.36 E-value: 7.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRpDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEwLRSQIG 443
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 444 LVSQEPVLFATSIRENIlfgdetaslkqvvaaakmanahefivklphgyethvgqfGTQLSGGQKQRIAIARALVRDPRI 523
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 524 LLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAG 582
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
364-592 |
2.98e-35 |
|
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: 134.38 E-value: 2.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPsrPDTLVLNGFNLTISEGA-------------TvglvggsgsgkstvisLLQRF---YSPDSGEISMDD 427
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEfvaiigpngsgksT----------------LLRLLnglLKPTSGEVLVDG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 428 HGIDTLNVEWLRSQIGLVSQEPV--LFATSIRENILFG------DETASLKQVVAAAKMANAHEFIVKLPHgyethvgqf 499
Cdd:COG1122 63 KDITKKNLRELRRKVGLVFQNPDdqLFAPTVEEDVAFGpenlglPREEIRERVEEALELVGLEHLADRPPH--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 500 gtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLSTLRK-ADTIAVLDAGR 577
Cdd:COG1122 134 --ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGR 211
|
250
....*....|....*
gi 1002260479 578 VVEAGTHDELLGMDD 592
Cdd:COG1122 212 IVADGTPREVFSDYE 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1021-1240 |
3.80e-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: 132.17 E-value: 3.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1021 EFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVAL 1100
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1101 VSQEPTLFsgtirdNIAYGAaeehatedevaraaalanahgfisamERGYDTrvgergaqLSGGQRQRIALARAVLKDAR 1180
Cdd:cd03214 78 VPQALELL------GLAHLA--------------------------DRPFNE--------LSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 1181 ILLLDEATSALDAASERLVQDAVDRM--LRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERG 1240
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
418-587 |
4.48e-35 |
|
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: 133.85 E-value: 4.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTL--NVEWLRSQIGLVSQEPVLFATSIRENILFG------DETASLKQVVAAA-KMANAHEfivkl 488
Cdd:cd03260 57 PDEGEVLLDGKDIYDLdvDVLELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEAlRKAALWD----- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 489 phgyETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLS-TLRKA 567
Cdd:cd03260 132 ----EVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVA 207
|
170 180
....*....|....*....|
gi 1002260479 568 DTIAVLDAGRVVEAGTHDEL 587
Cdd:cd03260 208 DRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1020-1247 |
8.39e-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: 133.58 E-value: 8.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIA-------YGAAEEHATEDEVaraaalanahgfISAMERGYDTRVGERGAQLSGGQRQRIAL 1171
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIAlvpkllkWPKEKIRERADEL------------LALVGLDPAEFADRYPHELSGGQQQRVGV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1172 ARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELLA 1247
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1019-1238 |
4.26e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.75 E-value: 4.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRsyslaRLRSQV 1098
Cdd:COG1121 6 AIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-----RARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQEPTL---FSGTIRDNIAYGA-----------AEEHATEDEvaraaalanahgfisAMER----GY-DTRVGErga 1159
Cdd:COG1121 78 GYVPQRAEVdwdFPITVRDVVLMGRygrrglfrrpsRADREAVDE---------------ALERvgleDLaDRPIGE--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1160 qLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR-GRTCVVVAHRLSTVEK-SDTIAVVKDGRVA 1237
Cdd:COG1121 140 -LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREyFDRVLLLNRGLVA 218
|
.
gi 1002260479 1238 E 1238
Cdd:COG1121 219 H 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1020-1246 |
4.48e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 134.50 E-value: 4.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLI---ERfydAQRGSVLVDGEDIRSYSLARLRs 1096
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIaglET---PDSGRIVLNGRDLFTNLPPRER- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEPTLFSG-TIRDNIAYGAAEEHATEDEVARAAalanaHGFISAME-RGYDTRvgeRGAQLSGGQRQRIALARA 1174
Cdd:COG1118 76 RVGFVFQHYALFPHmTVAENIAFGLRVRPPSKAEIRARV-----EELLELVQlEGLADR---YPSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1175 VLKDARILLLDEATSALDAAserlVQDAVDRMLR------GRTCVVVAH-RLSTVEKSDTIAVVKDGRVAERGRHHELL 1246
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAK----VRKELRRWLRrlhdelGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1020-1247 |
4.69e-34 |
|
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: 131.16 E-value: 4.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRP-EVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLI---ERfYDAqrGSVLVDGEDIRSYS---LA 1092
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInglER-PTS--GSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1093 RLRSQVALVSQEPTLFSG-TIRDNIAYgaAEEHATEDEVARAAALANAHGFIsamerGYDTRVGERGAQLSGGQRQRIAL 1171
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVAL--PLEIAGVPKAEIEERVLELLELV-----GLEDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1172 ARAVLKDARILLLDEATSALDAASER----LVQDAVDRmlRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELL 1246
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQsilaLLRDINRE--LGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
.
gi 1002260479 1247 A 1247
Cdd:cd03258 230 A 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1020-1247 |
7.08e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 133.66 E-value: 7.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRP-EVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLI---ERfydAQRGSVLVDGEDIRSYS---LA 1092
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInllER---PTSGSVLVDGVDLTALSereLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1093 RLRSQVALVSQEPTLFSG-TIRDNIAYgaAEEHAtedevaraaalanahGfISAMERgyDTRVGE---------RG---- 1158
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTVAENVAL--PLEIA---------------G-VPKAEI--RKRVAEllelvglsdKAdayp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1159 AQLSGGQRQRIALARAVLKDARILLLDEATSALDAASER----LVQDAVDRMlrGRTCVVVAHRLSTVEK-SDTIAVVKD 1233
Cdd:COG1135 139 SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRsildLLKDINREL--GLTIVLITHEMDVVRRiCDRVAVLEN 216
|
250
....*....|....
gi 1002260479 1234 GRVAERGRHHELLA 1247
Cdd:COG1135 217 GRIVEQGPVLDVFA 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
364-578 |
7.51e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.55 E-value: 7.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPdtlVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIG 443
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 444 LVSQEPVLFATSIRENILFGDETASLKqvvaaAKMANAHEFI--VKLPHGY-ETHVgqfgTQLSGGQKQRIAIARALVRD 520
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQLRERK-----FDRERALELLerLGLPPDIlDKPV----ERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 521 PRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAH-RLSTLRKADTIAVLDAGRV 578
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1020-1236 |
1.35e-33 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 129.19 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDI--RSYSLARLRSQ 1097
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLFSG-TIRDNIAYG----------AAEEHATEdevaraaalanahgfisAMER-GYDTRVGERGAQLSGGQ 1165
Cdd:cd03262 78 VGMVFQQFNLFPHlTVLENITLApikvkgmskaEAEERALE-----------------LLEKvGLADKADAYPAQLSGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1166 RQRIALARAVLKDARILLLDEATSALDAaseRLVQDAVDRMLR----GRTCVVVAHRLSTVEK-SDTIAVVKDGRV 1236
Cdd:cd03262 141 QQRVAIARALAMNPKVMLFDEPTSALDP---ELVGEVLDVMKDlaeeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1020-1237 |
1.64e-33 |
|
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: 129.61 E-value: 1.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYS---LARLRS 1096
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEPTLFSG-TIRDNIAYGAAEEHATEDEVARAAALANAHGFISAMER-GYDTRVGERGAQLSGGQRQRIALARA 1174
Cdd:cd03256 79 QIGMIFQQFNLIERlSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERvGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1175 VLKDARILLLDEATSALDAASERLVQDAVDR--MLRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVA 1237
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1019-1240 |
2.97e-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: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIER---FYDAQR--GSVLVDGEDI--RSYSL 1091
Cdd:COG1117 11 KIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGARveGEILLDGEDIydPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1092 ARLRSQVALVSQEPTLFSGTIRDNIAYGA--------AE-EHATE---------DEVaraaalanahgfisamergYDtR 1153
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgikskSElDEIVEeslrkaalwDEV-------------------KD-R 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1154 VGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAAS----ERLVQDavdrmLRGR-TCVVVAH------RLstv 1222
Cdd:COG1117 148 LKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStakiEELILE-----LKKDyTIVIVTHnmqqaaRV--- 219
|
250
....*....|....*...
gi 1002260479 1223 ekSDTIAVVKDGRVAERG 1240
Cdd:COG1117 220 --SDYTAFFYLGELVEFG 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
364-588 |
1.75e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 126.72 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPsrpDTLVLNGFNLTISEGA-------------TVglvggsgsgkstvISLLQRFYSPDSGEISMDDHGI 430
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEifgllgpngagktTT-------------IRMLLGLLRPTSGEVRVLGEDV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 431 DTLNVEWlRSQIGLVSQEPVLFAT-SIRENILFgdeTASLKQVVAAAKMANAHEFI--VKLPHGYETHVGQfgtqLSGGQ 507
Cdd:COG1131 65 ARDPAEV-RRRIGYVPQEPALYPDlTVRENLRF---FARLYGLPRKEARERIDELLelFGLTDAADRKVGT----LSGGM 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 508 KQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLSTL-RKADTIAVLDAGRVVEAGTHD 585
Cdd:COG1131 137 KQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPD 216
|
...
gi 1002260479 586 ELL 588
Cdd:COG1131 217 ELK 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
409-589 |
2.26e-32 |
|
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: 126.16 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 409 ISLLQRfysPDSGEISMDDHGIDTLN---VEWLRSQIGLVSQEPVLFAT-SIRENILFGDETASLKQVVAAAKMANAHEF 484
Cdd:cd03258 51 INGLER---PTSGSVLVDGTDLTLLSgkeLRKARRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLEL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 485 IvklphGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLS 562
Cdd:cd03258 128 V-----GLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEME 202
|
170 180
....*....|....*....|....*...
gi 1002260479 563 TLRK-ADTIAVLDAGRVVEAGTHDELLG 589
Cdd:cd03258 203 VVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1037-1247 |
2.69e-32 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 126.95 E-value: 2.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1037 VLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNI 1116
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1117 AygaAEEHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASE 1196
Cdd:cd03288 116 D---PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 1197 RLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:cd03288 193 NILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLA 243
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
24-294 |
3.60e-31 |
|
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: 123.91 E-value: 3.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 24 MALGVLGSFGDGMMQPLSMLVLGDIVNSYGGAGGagsarsaFSSGAVDKFALRLLYVAVAVGACSFLEGLCWTRTAERQA 103
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGD-------PETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 104 SKMRRLYLEAVLSQEVAFFDAAPSSpsspqaqaqattfRVISTVSDDADAIQDFLGEKLPMVLANATLFFGALAVSFVFA 183
Cdd:pfam00664 74 RRLRRKLFKKILRQPMSFFDTNSVG-------------ELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 184 WRLALAGLPFTLLLFVTpSVLLAGRMAAAAGEARAAYEEAGGIAQQAVSSIRTVASYTAERRTVERFRGAVARSAALGVR 263
Cdd:pfam00664 141 WKLTLVLLAVLPLYILV-SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIK 219
|
250 260 270
....*....|....*....|....*....|..
gi 1002260479 264 QGLIKGAVIGSMGVI-YAVWSFLSWIGSLLVI 294
Cdd:pfam00664 220 KAVANGLSFGITQFIgYLSYALALWFGAYLVI 251
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
440-577 |
4.15e-31 |
|
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: 121.42 E-value: 4.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 440 SQIGLVSQEPVLFATSIRENILFG---DEtASLKQVVAAAKManaHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARA 516
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENILFGkpfDE-ERYEKVIKACAL---EPDLEILPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 517 LVRDPRILLLDEATSALDAESERTV-QDAL-DRASVGRTTVIVAHRLSTLRKADTIAVLDAGR 577
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIfENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1020-1247 |
6.76e-31 |
|
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: 124.78 E-value: 6.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRP-EVAVLAGFSLEIGAGKTVALVGPSGSGKST----VIGLIERFYDAqRGSVLVDGEDIRSYSLARL 1094
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTlaraILGLLPPPGIT-SGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1095 RS----QVALVSQEPT-----LFsgTIRDNIAygaaeehatedEVARAaalanaHGFIS---AMERGYD--TRVGERGA- 1159
Cdd:COG0444 81 RKirgrEIQMIFQDPMtslnpVM--TVGDQIA-----------EPLRI------HGGLSkaeARERAIEllERVGLPDPe 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1160 --------QLSGGQRQRIALARAVLKDARILLLDEATSALDAaserLVQDAVDRMLR------GRTCVVVAHRLSTVEK- 1224
Cdd:COG0444 142 rrldryphELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQILNLLKdlqrelGLAILFITHDLGVVAEi 217
|
250 260
....*....|....*....|...
gi 1002260479 1225 SDTIAVVKDGRVAERGRHHELLA 1247
Cdd:COG0444 218 ADRVAVMYAGRIVEEGPVEELFE 240
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
362-583 |
2.17e-30 |
|
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: 119.82 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 362 GEIVFKDVHFSY-PSRPDtlVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRS 440
Cdd:cd03369 5 GEIEVENLSVRYaPDLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 441 QIGLVSQEPVLFATSIRENILFGDETaSLKQVVAAAKmanahefivklphgyethVGQFGTQLSGGQKQRIAIARALVRD 520
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLDPFDEY-SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 521 PRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGT 583
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
418-582 |
2.51e-30 |
|
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: 119.55 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTLNVEwlRSQIGLVSQEPVLFAT-SIRENILFG------DETASLKQVVAAAKMANAHEFIVKLPH 490
Cdd:cd03259 52 PDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 491 gyethvgqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLS-TLRKA 567
Cdd:cd03259 130 -----------ELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALA 198
|
170
....*....|....*
gi 1002260479 568 DTIAVLDAGRVVEAG 582
Cdd:cd03259 199 DRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
364-580 |
2.77e-30 |
|
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: 119.88 E-value: 2.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPDTL-VLNGFNLTISEG-------------ATVglvggsgsgkstvISLLQRFYSPDSGEISMDDHG 429
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtALEDISLSVEEGefvalvgpsgcgkSTL-------------LRIIAGLERPTSGEVLVDGEP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 430 IDTLNvewlrSQIGLVSQEPVLFA-TSIRENILFGDEtasLKQVVAAAKMANAHEFI--VKLPhGYETHvgqFGTQLSGG 506
Cdd:cd03293 68 VTGPG-----PDRGYVFQQDALLPwLTVLDNVALGLE---LQGVPKAEARERAEELLelVGLS-GFENA---YPHQLSGG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 507 QKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLS-TLRKADTIAVLDA--GRVVE 580
Cdd:cd03293 136 MRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1018-1236 |
3.57e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 123.26 E-value: 3.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFSYPtrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIrsyslARLRSQ 1097
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-----TDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 ---VALVSQEPTLF-SGTIRDNIAYGAAEEHATEDEVaraaalanahgfisamergyDTRVGE-------------RGAQ 1160
Cdd:COG3839 74 drnIAMVFQSYALYpHMTVYENIAFPLKLRKVPKAEI--------------------DRRVREaaellgledlldrKPKQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1161 LSGGQRQRIALARAVLKDARILLLDEATSALDAA------SE--RLVQDavdrmlRGRTCVVVAHRLstVEK---SDTIA 1229
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKlrvemrAEikRLHRR------LGTTTIYVTHDQ--VEAmtlADRIA 205
|
....*..
gi 1002260479 1230 VVKDGRV 1236
Cdd:COG3839 206 VMNDGRI 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
364-588 |
4.18e-30 |
|
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: 120.10 E-value: 4.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPDtlVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIG 443
Cdd:cd03295 1 IEFENVTKRYGGGKK--AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 444 LVSQEPVLFA-TSIRENILFgdeTASLKQVVAAAKMANAHEFI--VKLPHgyETHVGQFGTQLSGGQKQRIAIARALVRD 520
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIAL---VPKLLKWPKEKIRERADELLalVGLDP--AEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 521 PRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRL-STLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRlqQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
364-577 |
4.78e-30 |
|
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: 117.67 E-value: 4.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPsrpDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLN--VEWLRSQ 441
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 442 IGLVSQEPVLFAT-SIRENILFGdetaslkqvvaaakmanahefivklphgyethvgqfgtqLSGGQKQRIAIARALVRD 520
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 521 PRILLLDEATSALDAESERTVQDALD--RASVGRTTVIVAHRLSTLRK-ADTIAVLDAGR 577
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
364-587 |
6.05e-30 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 122.51 E-value: 6.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPsrpDTLVLNGFNLTISEGATvglvggsgsgkstvISLL----------QR----FYSPDSGEISMDDHG 429
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEF--------------VALLgpsgcgkttlLRmiagFETPDSGRILLDGRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 430 IDTLNVEwlRSQIGLVSQEPVLFA-TSIRENILFGdetasLKQ--VVAAAKMANAHEFI--VKLPHgyetHVGQFGTQLS 504
Cdd:COG3842 69 VTGLPPE--KRNVGMVFQDYALFPhLTVAENVAFG-----LRMrgVPKAEIRARVAELLelVGLEG----LADRYPHQLS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 505 GGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLS---TLrkADTIAVLDAGRVV 579
Cdd:COG3842 138 GGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIE 215
|
....*...
gi 1002260479 580 EAGTHDEL 587
Cdd:COG3842 216 QVGTPEEI 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
418-578 |
6.63e-30 |
|
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: 116.93 E-value: 6.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENILfgdetaslkqvvaaakmanahefivklphgyethvg 497
Cdd:cd03246 54 PTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSGSIAENIL------------------------------------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 498 qfgtqlSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASV-GRTTVIVAHRLSTLRKADTIAVLDAG 576
Cdd:cd03246 98 ------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDG 171
|
..
gi 1002260479 577 RV 578
Cdd:cd03246 172 RV 173
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
364-589 |
6.73e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 119.33 E-value: 6.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPsrpDTLVLNGFNLTISEGATvglvggsgsgkstvISL--------------LQRFYSPDSGEISMDDH- 428
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEV--------------VVIigpsgsgkstllrcINLLEEPDSGTITVDGEd 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 429 -GIDTLNVEWLRSQIGLVSQEPVLFA-TSIRENILFGDETAsLKQVVAAAKmANAHEFI--VKLPHgyetHVGQFGTQLS 504
Cdd:COG1126 65 lTDSKKDINKLRRKVGMVFQQFNLFPhLTVLENVTLAPIKV-KKMSKAEAE-ERAMELLerVGLAD----KADAYPAQLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 505 GGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDAL-DRASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAG 582
Cdd:COG1126 139 GGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMrDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEG 218
|
....*..
gi 1002260479 583 THDELLG 589
Cdd:COG1126 219 PPEEFFE 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
366-582 |
8.03e-30 |
|
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: 118.76 E-value: 8.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 366 FKDVHFSYPSRPDTL-VLNGFNLTISEGATvglvggsgsgkstvISL--------------LQRFYSPDSGEISMDDHGI 430
Cdd:cd03257 4 VKNLSVSFPTGGGSVkALDDVSFSIKKGET--------------LGLvgesgsgkstlaraILGLLKPTSGSIIFDGKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 431 DTLNVEWL---RSQIGLVSQEPVL-------FATSIRE--NILFGDETASLKQVVAAAKMA---NAHEFIVKLPHgyeth 495
Cdd:cd03257 70 LKLSRRLRkirRKEIQMVFQDPMSslnprmtIGEQIAEplRIHGKLSKKEARKEAVLLLLVgvgLPEEVLNRYPH----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 496 vgqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALD--RASVGRTTVIVAHRLSTLRK-ADTIAV 572
Cdd:cd03257 145 ------ELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAKiADRVAV 218
|
250
....*....|
gi 1002260479 573 LDAGRVVEAG 582
Cdd:cd03257 219 MYAGKIVEEG 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
365-577 |
1.05e-29 |
|
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: 117.95 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 365 VFKDVHFSYPSRpDTLVLNGFNLTISEGA-------------TVglvggsgsgkstvISLLQRFYSPDSGEISMDDHGID 431
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEfvlivgpngsgksTL-------------LRLLNGLLGPTSGEVLVDGKDLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 432 TLNVEWLRSQIGLVSQEP--VLFATSIRENILFG------DETASLKQVVAAAKMANAHEFIVKLPHgyethvgqfgtQL 503
Cdd:cd03225 67 KLSLKELRRKVGLVFQNPddQFFGPTVEEEVAFGlenlglPEEEIEERVEEALELVGLEGLRDRSPF-----------TL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 504 SGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLSTLRK-ADTIAVLDAGR 577
Cdd:cd03225 136 SGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
382-531 |
1.37e-29 |
|
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: 115.44 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 382 LNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLF-ATSIRENI 460
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 461 LFGDETASLKQVVAAAKMANAHEFiVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATS 531
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
364-588 |
1.82e-29 |
|
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: 118.04 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPdtlVLNGFNLTISEGA-------------TVglvggsgsgkstvISLLQRFYSPDSGEISMDDHGI 430
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEitgllgpngagktTL-------------LRMLAGLLKPDSGSILIDGEDV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 431 DTLNVEWlRSQIGLVSQEPVLFAT-SIRENILFgdeTASLKQVVAAAKMANAHEFI--VKLPHGYETHVGQFgtqlSGGQ 507
Cdd:COG4555 66 RKEPREA-RRQIGVLPDERGLYDRlTVRENIRY---FAELYGLFDEELKKRIEELIelLGLEEFLDRRVGEL----STGM 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 508 KQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHD 585
Cdd:COG4555 138 KKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLD 217
|
...
gi 1002260479 586 ELL 588
Cdd:COG4555 218 ELR 220
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
694-965 |
2.79e-29 |
|
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: 118.51 E-value: 2.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 694 LLGCVGAVVFGAVLPLYSYSLGSLPEVYF-LADDGQIRSKTRLYYFLFLGIAVVCitANIVQHYNFAVMGERLTERVRGQ 772
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLpDGDPETQALNVYSLALLLLGLAQFI--LSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 773 MLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCLLVQAGATASLGFSLALAVSWRLATVMMAMQPLII-- 850
Cdd:pfam00664 80 LFKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIlv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 851 ASFYFKKVLMAAMSKKAKKAQVqgSQLASEAVVNHRTITAFSSQRRMLRLYEAAQQGPKKDNVAHSWFSGFCLCLCQFSN 930
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKA--SSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIG 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 1002260479 931 TGSMAVALWYGGKLMAKGLITPTHL--FQVFFMLMTM 965
Cdd:pfam00664 236 YLSYALALWFGAYLVISGELSVGDLvaFLSLFAQLFG 272
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1041-1247 |
4.42e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 116.61 E-value: 4.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1041 FSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARlrSQVALVSQEPTLFSG-TIRDNIAYG 1119
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENNLFSHlTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1120 -------AAEEHATEDEVARAAalanahGFISAMERgydtrvgeRGAQLSGGQRQRIALARAVLKDARILLLDEATSALD 1192
Cdd:PRK10771 96 lnpglklNAAQREKLHAIARQM------GIEDLLAR--------LPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 1193 AA--SE--RLVQDAVDRmlRGRTCVVVAHRLstvEKSDTIA----VVKDGRVAERGRHHELLA 1247
Cdd:PRK10771 162 PAlrQEmlTLVSQVCQE--RQLTLLMVSHSL---EDAARIAprslVVADGRIAWDGPTDELLS 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
364-580 |
4.76e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 116.30 E-value: 4.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPS-RPDTLVLNGFNLTISEGATVGlvggsgsgkstvI---------------SLLQRfysPDSGEISMDD 427
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVA------------IvgpsgsgkstllnilGGLDR---PTSGEVLIDG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 428 HGIDTLN----VEWLRSQIGLVSQEPVLFAT-SIRENILFGdetASLKQVVAAAKMANAHEFIVKLphGYETHVGQFGTQ 502
Cdd:COG1136 70 QDISSLSerelARLRRRHIGFVFQFFNLLPElTALENVALP---LLLAGVSRKERRERARELLERV--GLGDRLDHRPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 503 LSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVE 580
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1020-1230 |
6.90e-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: 6.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSySLARLRSQVA 1099
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIAYGAA--EEHATEDEVAraaalanahgfiSAMER-GYDTRVGERGAQLSGGQRQRIALARAV 1175
Cdd:COG4133 79 YLGHADGLKPElTVRENLRFWAAlyGLRADREAID------------EALEAvGLAGLADLPVRQLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1176 LKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVA-HRLSTVEKSDTIAV 1230
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1020-1246 |
7.88e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 116.35 E-value: 7.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNV--HFSyptrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSL-ARL-R 1095
Cdd:PRK09493 2 IEFKNVskHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVdERLiR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1096 SQVALVSQEPTLFSG-TIRDNIAYG----------AAEEHATE--DEVaraaalanahgfisamerGYDTRVGERGAQLS 1162
Cdd:PRK09493 77 QEAGMVFQQFYLFPHlTALENVMFGplrvrgaskeEAEKQAREllAKV------------------GLAERAHHYPSELS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1163 GGQRQRIALARAVLKDARILLLDEATSALDAASE----RLVQDAVDrmlRGRTCVVVAHRLSTVEKSDTIAVVKD-GRVA 1237
Cdd:PRK09493 139 GGQQQRVAIARALAVKPKLMLFDEPTSALDPELRhevlKVMQDLAE---EGMTMVIVTHEIGFAEKVASRLIFIDkGRIA 215
|
....*....
gi 1002260479 1238 ERGRHHELL 1246
Cdd:PRK09493 216 EDGDPQVLI 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
331-588 |
7.99e-29 |
|
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: 122.70 E-value: 7.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 331 TAAASRMQEMIEMLPPLEGAEKKGATMERIRGEIV-FKDVHFSYPSRP--DTLVLNGFNLTISEGATvglvggsgsgkst 407
Cdd:COG1123 227 PEEILAAPQALAAVPRLGAARGRAAPAAAAAEPLLeVRNLSKRYPVRGkgGVRAVDDVSLTLRRGET------------- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 408 vISL--------------LQRFYSPDSGEISMDDHGIDTLNVE---WLRSQIGLVSQEPV--LFAT-SIRENILFGdeTA 467
Cdd:COG1123 294 -LGLvgesgsgkstlarlLLGLLRPTSGSILFDGKDLTKLSRRslrELRRRVQMVFQDPYssLNPRmTVGDIIAEP--LR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 468 SLKQVVAAAKMANAHEFI--VKLPhgyETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDAL 545
Cdd:COG1123 371 LHGLLSRAERRERVAELLerVGLP---PDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLL 447
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1002260479 546 D--RASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDELL 588
Cdd:COG1123 448 RdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVF 493
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1020-1240 |
8.35e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 120.05 E-value: 8.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSlARLRsQVA 1099
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AENR-HVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIAYGAAEEHATEDEVaraaalanahgfisamergyDTRVGE-------------RGAQLSGGQ 1165
Cdd:PRK09452 90 TVFQSYALFPHmTVFENVAFGLRMQKTPAAEI--------------------TPRVMEalrmvqleefaqrKPHQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1166 RQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAH----RLSTvekSDTIAVVKDGRVAER 1239
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQD 226
|
.
gi 1002260479 1240 G 1240
Cdd:PRK09452 227 G 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1042-1247 |
1.08e-28 |
|
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: 116.59 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1042 SLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARL----RSQVALVSQEPTLFSG-TIRDNI 1116
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1117 AYG-------AAEEHATEDEVaraAALANAHGFISAMERgydtrvgergaQLSGGQRQRIALARAVLKDARILLLDEATS 1189
Cdd:cd03294 124 AFGlevqgvpRAEREERAAEA---LELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 1190 ALDAASERLVQDAVDRMLR--GRTCVVVAHRLS-TVEKSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1020-1238 |
1.44e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 114.76 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVavLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYS---LARLRS 1096
Cdd:COG2884 2 IRFENVSKRYPGGREA--LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEPTLFSG-TIRDNIAY-----GaAEEHATEDEVAraaalanahgfiSAMER-GYDTRVGERGAQLSGGQRQRI 1169
Cdd:COG2884 80 RIGVVFQDFRLLPDrTVYENVALplrvtG-KSRKEIRRRVR------------EVLDLvGLSDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 1170 ALARAVLKDARILLLDEATSALD-AASERLVQ--DAVDRMlrGRTCVVVAHRLSTVEKSD--TIaVVKDGRVAE 1238
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDpETSWEIMEllEEINRR--GTTVLIATHDLELVDRMPkrVL-ELEDGRLVR 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
361-604 |
1.66e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 124.70 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 361 RGEIVFKDVHFSY-PSRPDtlVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLR 439
Cdd:PLN03232 1232 RGSIKFEDVHLRYrPGLPP--VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 440 SQIGLVSQEPVLFATSIRENI-LFGDET-ASLKQVVAAAKMANAhefIVKLPHGYETHVGQFGTQLSGGQKQRIAIARAL 517
Cdd:PLN03232 1310 RVLSIIPQSPVLFSGTVRFNIdPFSEHNdADLWEALERAHIKDV---IDRNPFGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 518 VRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLGMDdggeGG 597
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRD----TS 1462
|
....*..
gi 1002260479 598 VYARMVH 604
Cdd:PLN03232 1463 AFFRMVH 1469
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
357-580 |
2.01e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 115.57 E-value: 2.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 357 MERIRGEIVFKDVHFSYPSRP-DTLVLNGFNLTISEGATvglvggsgsgkstvISLLQR--------------FYSPDSG 421
Cdd:COG1116 1 MSAAAPALELRGVSKRFPTGGgGVTALDDVSLTVAAGEF--------------VALVGPsgcgkstllrliagLEKPTSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 422 EISMDDHgidtlNVEWLRSQIGLVSQEPVLFA-TSIRENILFGdetASLKQVVAAAKMANAHEFI--VKLpHGYETHvgq 498
Cdd:COG1116 67 EVLVDGK-----PVTGPGPDRGVVFQEPALLPwLTVLDNVALG---LELRGVPKAERRERARELLelVGL-AGFEDA--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 499 FGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAH------RLstlrkADTI 570
Cdd:COG1116 135 YPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRV 209
|
250
....*....|..
gi 1002260479 571 AVLDA--GRVVE 580
Cdd:COG1116 210 VVLSArpGRIVE 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
364-592 |
2.18e-28 |
|
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: 115.99 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRpDTLVLNGFNLTISEG-------------ATvglvggsgsgkstvIS-LLQRFYSPDSGEISMDdhG 429
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGefvaiighngsgkST--------------LAkLLNGLLLPTSGKVTVD--G 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 430 IDTLNVE--W-LRSQIGLVSQEP--VLFATSIRENILFGDE-----TASLKQVVA-AAKMANAHEFIVKLPHgyethvgq 498
Cdd:TIGR04520 64 LDTLDEEnlWeIRKKVGMVFQNPdnQFVGATVEDDVAFGLEnlgvpREEMRKRVDeALKLVGMEDFRDREPH-------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 499 fgtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALD--RASVGRTTVIVAHRLSTLRKADTIAVLDAG 576
Cdd:TIGR04520 136 ---LLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRklNKEEGITVISITHDMEEAVLADRVIVMNKG 212
|
250
....*....|....*.
gi 1002260479 577 RVVEAGTHDELLGMDD 592
Cdd:TIGR04520 213 KIVAEGTPREIFSQVE 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
362-603 |
2.23e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 124.47 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 362 GEIVFKDVHFSYpsRPD-TLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRS 440
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 441 QIGLVSQEPVLFATSIRENI-LFGD----------ETASLKQVvaaakmanahefIVKLPHGYETHVGQFGTQLSGGQKQ 509
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLdPFNEhndadlweslERAHLKDV------------IRRNSLGLDAEVSEAGENFSVGQRQ 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 510 RIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLg 589
Cdd:PLN03130 1382 LLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLL- 1460
|
250
....*....|....
gi 1002260479 590 mddGGEGGVYARMV 603
Cdd:PLN03130 1461 ---SNEGSAFSKMV 1471
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1021-1232 |
3.12e-28 |
|
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: 113.78 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1021 EFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKST----VIGLIERFydaqRGSVLVDGEDIRsyslaRLRS 1096
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTllkaILGLLKPT----SGSIRVFGKPLE-----KERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEPTL---FSGTIRDNIAYGAaeehatedevaraAALANAHGFIS---------AMERgydtrVG------ERG 1158
Cdd:cd03235 69 RIGYVPQRRSIdrdFPISVRDVVLMGL-------------YGHKGLFRRLSkadkakvdeALER-----VGlseladRQI 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1159 AQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRM-LRGRTCVVVAHRLSTVEKS-DTIAVVK 1232
Cdd:cd03235 131 GELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYfDRVLLLN 206
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1020-1240 |
3.13e-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: 113.74 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevavlAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARlrSQVA 1099
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIAYGAAEE-HATEDEVARAAALANAHGFISAMERgydtrvgeRGAQLSGGQRQRIALARAVLK 1177
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGLSPGlKLTAEDRQAIEVALARVGLAGLEKR--------LPGELSGGERQRVALARVLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1178 DARILLLDEATSALDAASERLVQDAVD--RMLRGRTCVVVAHRLSTVEKSDTIAV-VKDGRVAERG 1240
Cdd:cd03298 146 DKPVLLLDEPFAALDPALRAEMLDLVLdlHAETKMTVLMVTHQPEDAKRLAQRVVfLDNGRIAAQG 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
364-592 |
3.20e-28 |
|
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: 114.14 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPdtlVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWL---RS 440
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 441 QIGLVSQEPVLF-ATSIRENILF-----GDETASLKQVVAAAK--MANAHEFIVKLPHgyethvgqfgtQLSGGQKQRIA 512
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVAFplrehTRLSEEEIREIVLEKleAVGLRGAEDLYPA-----------ELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 513 IARALVRDPRILLLDEATSALD-------AESERTVQDALdrasvGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTH 584
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKEL-----GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTP 221
|
....*...
gi 1002260479 585 DELLGMDD 592
Cdd:cd03261 222 EELRASDD 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
364-634 |
3.77e-28 |
|
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: 120.39 E-value: 3.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPDTlVLNGFNLTISEGATVGLVGGSGS---GKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRS 440
Cdd:COG1123 5 LEVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSgksTLALALMGLLPHGGRISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 441 QIGLVSQEP--VLFATSIRENILFGDETASLKQVVAAAKMANAHEFIvklphGYETHVGQFGTQLSGGQKQRIAIARALV 518
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAV-----GLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 519 RDPRILLLDEATSALDAESERTVQDALD--RASVGRTTVIVAHRLST-LRKADTIAVLDAGRVVEAGTHDELLgmddgge 595
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEIL------- 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 1002260479 596 ggvyARMVHLQKAPPVAAREERHRAVDVVESEMVSFRSV 634
Cdd:COG1123 232 ----AAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNL 266
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1019-1240 |
4.86e-28 |
|
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: 113.97 E-value: 4.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSlARLRsQV 1098
Cdd:cd03296 2 SIEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP-VQER-NV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQEPTLFSG-TIRDNIAYGAAEEHAT----EDEVARAAALANAHGFISAMERGYDtrvgergAQLSGGQRQRIALAR 1173
Cdd:cd03296 77 GFVFQHYALFRHmTVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLADRYP-------AQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 1174 AVLKDARILLLDEATSALDAAserlVQDAVDRMLR------GRTCVVVAHRLS-TVEKSDTIAVVKDGRVAERG 1240
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAK----VRKELRRWLRrlhdelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVG 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
409-588 |
7.05e-28 |
|
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: 114.28 E-value: 7.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 409 ISLLQRFYSPDSGEISMDDHGIDTLNVEWL----RSQIGLVSQEPVLFA-TSIRENILFGDETASLKQVVAAAKMANAHE 483
Cdd:cd03294 67 LRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPhRTVLENVAFGLEVQGVPRAEREERAAEALE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 484 fIVKLpHGYETHvgqFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRL 561
Cdd:cd03294 147 -LVGL-EGWEHK---YPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlqAELQKTIVFITHDL 221
|
170 180
....*....|....*....|....*...
gi 1002260479 562 S-TLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:cd03294 222 DeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1019-1240 |
7.52e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.45 E-value: 7.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRPEVavLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQV 1098
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQEP--TLFSGTIRDNIAYGAAEEHATEDEVARAAALANahgfisAMERGYDTRvgERGA-QLSGGQRQRIALARAV 1175
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEAL------KAVRMWDFR--DKPPyHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 1176 LKDARILLLDEATSALDAASERLVQDAVDRM-LRGRTCVVVAHRLS-TVEKSDTIAVVKDGRVAERG 1240
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEG 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
364-583 |
7.75e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 115.95 E-value: 7.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPDTLV-LNGFNLTISEGA-----------------TvglvggsgsgkstvISLLQRfysPDSGEISM 425
Cdd:COG1135 2 IELENLSKTFPTKGGPVTaLDDVSLTIEKGEifgiigysgagkstlirC--------------INLLER---PTSGSVLV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 426 DDHGIDTLNVEWL---RSQIGLVSQEPVLFAT-SIRENILFGDETASLKQVVAAAKMANAHEFIvklphGYETHVGQFGT 501
Cdd:COG1135 65 DGVDLTALSERELraaRRKIGMIFQHFNLLSSrTVAENVALPLEIAGVPKAEIRKRVAELLELV-----GLSDKADAYPS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRV 578
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDinRELGLTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
....*
gi 1002260479 579 VEAGT 583
Cdd:COG1135 220 VEQGP 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1020-1247 |
1.47e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 112.14 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPtrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSL-ARLRSQV 1098
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQEPTLFSG-TIRDNI---AYGAAEEHATEDevaraaalanahgfisaMERGYD------TRVGERGAQLSGGQRQR 1168
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLllgAYARRRAKRKAR-----------------LERVYElfprlkERRKQLAGTLSGGEQQM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1169 IALARAVLKDARILLLDEATSALDAASERLVQDAVDRM-LRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELL 1246
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELrDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
.
gi 1002260479 1247 A 1247
Cdd:cd03224 221 A 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
418-588 |
1.68e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 115.24 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTlNVEWLRSQIGLVSQEPVLFA-TSIRENILFGdetASLKQVVAAAKMANAHEFI--VKLPHgyet 494
Cdd:COG1118 54 PDSGRIVLNGRDLFT-NLPPRERRVGFVFQHYALFPhMTVAENIAFG---LRVRPPSKAEIRARVEELLelVQLEG---- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 495 HVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDA----ESERTVQDALDRasVGRTTVIVAH-RLSTLRKADT 569
Cdd:COG1118 126 LADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDE--LGGTTVFVTHdQEEALELADR 203
|
170
....*....|....*....
gi 1002260479 570 IAVLDAGRVVEAGTHDELL 588
Cdd:COG1118 204 VVVMNQGRIEQVGTPDEVY 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
378-587 |
2.17e-27 |
|
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: 111.95 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 378 DTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDdhGIDTLNVEWLRSQIGLVSQEPVLFA-TSI 456
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD--GKDITNLPPHKRPVNTVFQNYALFPhLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 457 RENILFGDETASLKQVVAAAKMANAHEfIVKLphgyETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAE 536
Cdd:cd03300 90 FENIAFGLRLKKLPKAEIKERVAEALD-LVQL----EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 537 SERTVQDALDR--ASVGRTTVIVAHRLS-TLRKADTIAVLDAGRVVEAGTHDEL 587
Cdd:cd03300 165 LRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1020-1247 |
2.20e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 114.90 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPT-RPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYS---LARLR 1095
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1096 SQVALVSQEPTLFSG-TIRDNIAYGAAEEHATEDEVaraaalanahgfisamergyDTRVGER----G---------AQL 1161
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALPLELAGTPKAEI--------------------KARVTELlelvGlsdkadrypAQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1162 SGGQRQRIALARAVLKDARILLLDEATSALDAASER----LVQDaVDRMLrGRTCVVVAHRLSTVeKS--DTIAVVKDGR 1235
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPATTRsileLLKD-INREL-GLTIVLITHEMDVV-KRicDRVAVIDAGR 218
|
250
....*....|..
gi 1002260479 1236 VAERGRHHELLA 1247
Cdd:PRK11153 219 LVEQGTVSEVFS 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1038-1240 |
2.22e-27 |
|
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: 111.23 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1038 LAGFSLEIG---AGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDG----EDIRSYSLARLRSQVALVSQEPTLFSG 1110
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfDSRKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1111 -TIRDNIAYGAAEEHATEDEVARAAALANAHgfISAMERGYDtrvgergAQLSGGQRQRIALARAVLKDARILLLDEATS 1189
Cdd:cd03297 90 lNVRENLAFGLKRKRNREDRISVDELLDLLG--LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 1190 ALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERG 1240
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1019-1241 |
2.41e-27 |
|
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: 111.76 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRP-EVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLI---ERfydAQRGSVLVDGEDIRSYS---L 1091
Cdd:COG4181 8 IIELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLaglDR---PTSGTVRLAGQDLFALDedaR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1092 ARLRSQ-VALVSQE----PTLfsgTIRDNIA-------YGAAEEHATEdevaraaalanahgfisAMER-GYDTRVGERG 1158
Cdd:COG4181 85 ARLRARhVGFVFQSfqllPTL---TALENVMlplelagRRDARARARA-----------------LLERvGLGHRLDHYP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1159 AQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTVEKSDTIAVVKDGRV 1236
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRerGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
....*
gi 1002260479 1237 AERGR 1241
Cdd:COG4181 225 VEDTA 229
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1020-1240 |
2.51e-27 |
|
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: 112.91 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPtRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYS-LARLRSQV 1098
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQEPT--LFSGTIRDNIAYG------AAEEhatedevaraaalanahgfisaMERGYD---TRVG-----ERG-AQL 1161
Cdd:TIGR04520 80 GMVFQNPDnqFVGATVEDDVAFGlenlgvPREE----------------------MRKRVDealKLVGmedfrDREpHLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1162 SGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVdRMLR---GRTCVVVAHRLSTVEKSDTIAVVKDGRVAE 1238
Cdd:TIGR04520 138 SGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETI-RKLNkeeGITVISITHDMEEAVLADRVIVMNKGKIVA 216
|
..
gi 1002260479 1239 RG 1240
Cdd:TIGR04520 217 EG 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1020-1236 |
6.37e-27 |
|
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: 109.80 E-value: 6.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPtrPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDI---RSYSLARLRS 1096
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEPTLFSG-TIRDNIAYGAaeehatedEVARAAALANAHGFISAMER-GYDTRVGERGAQLSGGQRQRIALARA 1174
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFAL--------EVTGVPPREIRKRVPAALELvGLSHKHRALPAELSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 1175 VLKDARILLLDEATSALDAASERLVQDAVDRM-LRGRTCVVVAHRLSTVEK-SDTIAVVKDGRV 1236
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTtRHRVIALERGKL 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1037-1246 |
7.08e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 110.87 E-value: 7.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1037 VLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSG-TIRDN 1115
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1116 IAYG-----------AAEEHATEDevaraaalanahgfiSAMER-GYDTRVGERGAQLSGGQRQRIALARAVLKDARILL 1183
Cdd:PRK11231 97 VAYGrspwlslwgrlSAEDNARVN---------------QAMEQtRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1184 LDEATSALDAASerlvQDAVDRMLR-----GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELL 1246
Cdd:PRK11231 162 LDEPTTYLDINH----QVELMRLMRelntqGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
420-587 |
8.31e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 110.90 E-value: 8.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 420 SGEISMDDHGI--DTLNVEWLRSQIGLVSQEPVLFATSIRENILFG------------DETA--SLKQV-----VAAakm 478
Cdd:COG1117 70 EGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgikskselDEIVeeSLRKAalwdeVKD--- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 479 anahefivKLphgyethvGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVA 558
Cdd:COG1117 147 --------RL--------KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVT 210
|
170 180 190
....*....|....*....|....*....|
gi 1002260479 559 HRLS-TLRKADTIAVLDAGRVVEAGTHDEL 587
Cdd:COG1117 211 HNMQqAARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1020-1246 |
8.53e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 110.56 E-value: 8.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIAYG---------AAEEHATEDEVaraaalanahgfISAME------RGYDtrvgergaQLSG 1163
Cdd:COG4604 79 ILRQENHINSRlTVRELVAFGrfpyskgrlTAEDREIIDEA------------IAYLDledladRYLD--------ELSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1164 GQRQRIALARAVLKDARILLLDEATSALD--AASE--RLVQDAVDRMlrGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAE 1238
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDmkHSVQmmKLLRRLADEL--GKTVVIVLHDINFASCyADHIVAMKDGRVVA 216
|
....*...
gi 1002260479 1239 RGRHHELL 1246
Cdd:COG4604 217 QGTPEEII 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
364-588 |
9.10e-27 |
|
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: 110.52 E-value: 9.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPdtlVLNGFNLTISEGA-------------TVglvggsgsgkstvISLLQRFYSPDSGEISMDDHGI 430
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEvtallgpngsgksTL-------------LRALAGLLKPSSGEVLLDGRDL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 431 DTLNVEWLRSQIGLVSQEPVL-FATSIRENIL---------FGDETASLKQVVAAAkMAnahefivklphgyETHVGQFG 500
Cdd:COG1120 66 ASLSRRELARRIAYVPQEPPApFGLTVRELVAlgryphlglFGRPSAEDREAVEEA-LE-------------RTGLEHLA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 501 ----TQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLS-TLRKADTIAVL 573
Cdd:COG1120 132 drpvDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLL 211
|
250
....*....|....*
gi 1002260479 574 DAGRVVEAGTHDELL 588
Cdd:COG1120 212 KDGRIVAQGPPEEVL 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
364-578 |
1.16e-26 |
|
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: 109.12 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPDTL-VLNGFNLTISEGA-------------TVGLVggsgsgkstvISLLQRfysPDSGEISMDDHG 429
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqALKGVSLSIEKGEfvaivgpsgsgksTLLNI----------LGGLDR---PTSGEVRVDGTD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 430 IDTLNVEWL----RSQIGLVSQEPVLFAT-SIRENILFGdetASLKQVVAAAKMANAHEFI--VKLPHgyetHVGQFGTQ 502
Cdd:cd03255 68 ISKLSEKELaafrRRHIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLerVGLGD----RLNHYPSE 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 503 LSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLSTLRKADTIAVLDAGRV 578
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1020-1237 |
1.21e-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: 107.51 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTrpeVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLAR-LRSQV 1098
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQeptlfsgtirdniaygaaeehatedevaraaalanahgfisamergydtrvgergaqLSGGQRQRIALARAVLKD 1178
Cdd:cd03216 78 AMVYQ---------------------------------------------------------LSVGERQMVEIARALARN 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 1179 ARILLLDEATSALDAA-SERLVqdAVDRMLR--GRTCVVVAHRLSTV-EKSDTIAVVKDGRVA 1237
Cdd:cd03216 101 ARLLILDEPTAALTPAeVERLF--KVIRRLRaqGVAVIFISHRLDEVfEIADRVTVLRDGRVV 161
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1019-1249 |
1.26e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 118.69 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIglierfydaqrgSVLVDGEDIRSYSLARLRSQV 1098
Cdd:PLN03130 614 AISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLI------------SAMLGELPPRSDASVVIRGTV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQEPTLFSGTIRDNIAYGAAEEHATEDEVARaaalanahgfISAMERGYD-------TRVGERGAQLSGGQRQRIAL 1171
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSPFDPERYERAID----------VTALQHDLDllpggdlTEIGERGVNISGGQKQRVSM 751
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1172 ARAVLKDARILLLDEATSALDAASERLVQDA-VDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAVG 1249
Cdd:PLN03130 752 ARAVYSNSDVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNG 830
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1019-1246 |
1.28e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.85 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQV 1098
Cdd:PRK13632 7 MIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQEP-TLFSG-TIRDNIAYGAAEEHATEDEvaraaalanahgfISAMERGYDTRVG-----ERGAQ-LSGGQRQRIA 1170
Cdd:PRK13632 86 GIIFQNPdNQFIGaTVEDDIAFGLENKKVPPKK-------------MKDIIDDLAKKVGmedylDKEPQnLSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 1171 LARAVLKDARILLLDEATSALDAASERLVQDAVD--RMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELL 1246
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1020-1247 |
1.35e-26 |
|
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: 115.94 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTR--------PEVAVLAGFSLEIGAGKTVALVGPSGSGKST----VIGLIErfydaQRGSVLVDGEDIR 1087
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIP-----SEGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1088 SYS---LARLRSQVALVSQEPtlFSG-----TIRDNIAYG------AAEEHATEDEVaraaalanahgfISAMER-GYDT 1152
Cdd:COG4172 351 GLSrraLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhgpGLSAAERRARV------------AEALEEvGLDP 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1153 RVGER-GAQLSGGQRQRIALARAVLKDARILLLDEATSALDaaseRLVQDAVDRMLR------GRTCVVVAHRLSTVEK- 1224
Cdd:COG4172 417 AARHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQILDLLRdlqrehGLAYLFISHDLAVVRAl 492
|
250 260
....*....|....*....|...
gi 1002260479 1225 SDTIAVVKDGRVAERGRHHELLA 1247
Cdd:COG4172 493 AHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1019-1251 |
1.66e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.12 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTrpeVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGE--DIRSYSLARlRS 1096
Cdd:COG1129 4 LLEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvRFRSPRDAQ-AA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEPTLFSG-TIRDNIAYGaaeehatedevaraaALANAHGFIS--AMER---------GYDTRVGERGAQLSGG 1164
Cdd:COG1129 80 GIAIIHQELNLVPNlSVAENIFLG---------------REPRRGGLIDwrAMRRrarellarlGLDIDPDTPVGDLSVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1165 QRQRIALARAVLKDARILLLDEATSALDAA-SERLVqdAVDRMLR--GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERG 1240
Cdd:COG1129 145 QQQLVEIARALSRDARVLILDEPTASLTEReVERLF--RIIRRLKaqGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTG 222
|
250
....*....|....*...
gi 1002260479 1241 RHHEL-------LAVGRA 1251
Cdd:COG1129 223 PVAELtedelvrLMVGRE 240
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1019-1249 |
1.71e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 118.15 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVI-GLIERFYDAQRGSVLVdgedirsyslarlRSQ 1097
Cdd:PLN03232 614 AISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLIsAMLGELSHAETSSVVI-------------RGS 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLFSGTIRDNIAYGAAEEhaTEDEVARAAALANAHGFisAMERGYD-TRVGERGAQLSGGQRQRIALARAVL 1176
Cdd:PLN03232 681 VAYVPQVSWIFNATVRENILFGSDFE--SERYWRAIDVTALQHDL--DLLPGRDlTEIGERGVNISGGQKQRVSMARAVY 756
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 1177 KDARILLLDEATSALDAASERLVQDA-VDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAVG 1249
Cdd:PLN03232 757 SNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSG 830
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
1041-1240 |
2.93e-26 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 108.02 E-value: 2.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1041 FSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIrsYSLARLRSQVALVSQEPTLFSG-TIRDNIAYG 1119
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH--TGLAPYQRPVSMLFQENNLFAHlTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1120 --------AAEEHATEDevaraaalanahgfiSAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSAL 1191
Cdd:TIGR01277 95 lhpglklnAEQQEKVVD---------------AAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 1192 DAA--SERLVQDAVDRMLRGRTCVVVAHRLSTVEKS-DTIAVVKDGRVAERG 1240
Cdd:TIGR01277 160 DPLlrEEMLALVKQLCSERQRTLLMVTHHLSDARAIaSQIAVVSQGKIKVVS 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1020-1245 |
4.43e-26 |
|
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: 108.09 E-value: 4.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTrpeVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIrsYSLARLRSQVA 1099
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIAYGAAEEHATEDEVARAAALANAhgfISAMErGYDTRvgeRGAQLSGGQRQRIALARAVLKD 1178
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGLRLKKLPKAEIKERVAEALD---LVQLE-GYANR---KPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1179 ARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLS-TVEKSDTIAVVKDGRVAERGRHHEL 1245
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1020-1208 |
4.49e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 107.88 E-value: 4.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSGTIRDNIAYGAAEEHATEDEvaraaalanaHGFISAMERGY--DTRVGERGAQLSGGQRQRIALARAVLK 1177
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPWQIRNQQPDP----------AIFLDDLERFAlpDTILTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190
....*....|....*....|....*....|.
gi 1002260479 1178 DARILLLDEATSALDAASERLVQDAVDRMLR 1208
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVR 185
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1020-1240 |
4.72e-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: 107.34 E-value: 4.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPtrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIrSYSLARLRSqVA 1099
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRD-IA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIAYGAAEEHATEDEVARAAALAnahgfisAMERGYDTRVGERGAQLSGGQRQRIALARAVLKD 1178
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGLKLRKVPKDEIDERVREV-------AELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 1179 ARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHrlSTVEK---SDTIAVVKDGRVAERG 1240
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTH--DQVEAmtmADRIAVMNDGQIQQIG 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1031-1245 |
5.43e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 110.59 E-value: 5.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1031 TRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYS---LARLRSQVALVSQEPtl 1107
Cdd:COG4608 27 TVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1108 FSG-----TIRDNIA-----YGAAEEHATEDEVAraaalanahgfiSAMER-GYDTRVGERGA-QLSGGQRQRIALARAV 1175
Cdd:COG4608 105 YASlnprmTVGDIIAeplriHGLASKAERRERVA------------ELLELvGLRPEHADRYPhEFSGGQRQRIGIARAL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 1176 LKDARILLLDEATSALDAAserlVQDAVDRMLR------GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHEL 1245
Cdd:COG4608 173 ALNPKLIVCDEPVSALDVS----IQAQVLNLLEdlqdelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1020-1236 |
5.58e-26 |
|
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: 107.21 E-value: 5.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVAVlAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRsYSLARLRSQVA 1099
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIAYGA---AEEHATEDEVaraaalanahgfISAMERGY------DTRVGergaQLSGGQRQRI 1169
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFYArlkGLPKSEIKEE------------VELLLRVLgltdkaNKRAR----TLSGGMKRKL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 1170 ALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEK-SDTIAVVKDGRV 1236
Cdd:cd03263 143 SLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKL 210
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
24-335 |
8.54e-26 |
|
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: 109.67 E-value: 8.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 24 MALGVLGSFGDGMMQPLSMLVLGDIVNSYGGAGGAGSARSAFSSGA-----------VDKFALRLLYVAVAVGACSFLEG 92
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSGLNSsagpfekleeeMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 93 LCWTRTAERQASKMRRLYLEAVLSQEVAFFDaapsspsspqaqaQATTFRVISTVSDDADAIQDFLGEKLPMVLANATLF 172
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD-------------VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 173 FGALAVSFVFAWRLALaglpftLLLFVTP-----SVLLAGRMAAAAGEARAAYEEAGGIAQQAVSSIRTVASYTAERRTV 247
Cdd:cd18558 148 GTGFIIGFIRGWKLTL------VILAISPvlglsAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 248 ERFRGAVARSAALGVRQGLIKGAVIG-SMGVIYAVWSFLSWIGSLLVIHLHAQGGHVFVASICIVLAGMSIMMALPNLRY 326
Cdd:cd18558 222 TRYAQNLEIAKRNGIKKAITFNISMGaAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEA 301
|
....*....
gi 1002260479 327 FIDATAAAS 335
Cdd:cd18558 302 FANARGAAY 310
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1053-1245 |
9.06e-26 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 109.89 E-value: 9.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1053 LVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIrSYSLARLRSqVALVSQEPTLFSG-TIRDNIAYGAAEEHATEDEVA 1131
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-TNVPPHLRH-INMVFQSYALFPHmTVEENVAFGLKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1132 RaaalanahgfiSAMERGYDTRVGERGA----QLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRML 1207
Cdd:TIGR01187 79 P-----------RVLEALRLVQLEEFADrkphQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1002260479 1208 R--GRTCVVVAHRLS-TVEKSDTIAVVKDGRVAERGRHHEL 1245
Cdd:TIGR01187 148 EqlGITFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1020-1240 |
9.24e-26 |
|
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: 106.51 E-value: 9.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRpevAVLAGFSLEIGAGKTvALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLArLRSQVA 1099
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIAYGAA-------EEHATEDEVaraaalanahgfisaMER-GYDTRVGERGAQLSGGQRQRIA 1170
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYIAWlkgipskEVKARVDEV---------------LELvNLGDRAKKKIGSLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 1171 LARAVLKDARILLLDEATSALDAAsERLvqdAVDRMLR----GRTCVVVAHRLSTVEKS-DTIAVVKDGRVAERG 1240
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPE-ERI---RFRNLLSelgeDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1037-1246 |
1.28e-25 |
|
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: 106.65 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1037 VLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSysLARLRSQVALVSQEPTLFSG-TIRDN 1115
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN--LPPEKRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1116 IAYGAAEEHATEDEVARAAALanahgfISAMeRGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAAS 1195
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLE------IAEM-LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 1196 -ERLVQD-AVDRMLRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELL 1246
Cdd:cd03299 165 kEKLREElKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1020-1234 |
1.69e-25 |
|
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: 105.88 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPtrPEVAVLAGFSLEIGAGKTVALVGPSGSGKST----VIGLIERFYDAQRGSVLVDGEDIRSYSLARLR 1095
Cdd:cd03290 1 VQVTNGYFSWG--SGLATLSNINIRIPTGQLTMIVGQVGCGKSSlllaILGEMQTLEGKVHWSNKNESEPSFEATRSRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1096 SQVALVSQEPTLFSGTIRDNIAYGAAEEHATEDEVARAAALANAhgfISAMERGYDTRVGERGAQLSGGQRQRIALARAV 1175
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPD---IDLLPFGDQTEIGERGINLSGGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 1176 LKDARILLLDEATSALDA-ASERLVQDAVDRMLRG--RTCVVVAHRLSTVEKSDTIAVVKDG 1234
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIhLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1031-1250 |
1.78e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 110.70 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1031 TRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTL-FS 1109
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1110 GTIRDNIAYGAA---EEHATEDEVARAAALanahgfiSAMERGYDTRVGERG-AQLSGGQRQRIALARAVLKDARILLLD 1185
Cdd:PRK09536 92 FDVRQVVEMGRTphrSRFDTWTETDRAAVE-------RAMERTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1186 EATSALDAASE----RLVQDAVDrmlRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELLAVGR 1250
Cdd:PRK09536 165 EPTASLDINHQvrtlELVRRLVD---DGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTADT 231
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
726-981 |
1.92e-25 |
|
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: 107.65 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 726 DGQIRSKTRLYYFLFLGIAVVCITANIVQHYNFAVMGERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSK 805
Cdd:cd18557 28 KGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDK--HKTGELTSRLSSDTSV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 806 VRSLVGDRMCLLVQAGATASLGFSLALAVSWRLATVMMA-MQPLIIASFYFKKvLMAAMSKKAKKAQVQGSQLASEAVVN 884
Cdd:cd18557 106 LQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLvIPLLLIASKIYGR-YIRKLSKEVQDALAKAGQVAEESLSN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 885 HRTITAFSSQRRMLRLYEAAQQGPKKDNVAHSWFSGFCLCLCQFSNTGSMAVALWYGGKLMAKGLITPTHLFQvfFMLMT 964
Cdd:cd18557 185 IRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTS--FILYT 262
|
250
....*....|....*...
gi 1002260479 965 MgrVIADA-GSLTSDLAQ 981
Cdd:cd18557 263 I--MVASSvGGLSSLLAD 278
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
364-578 |
2.38e-25 |
|
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: 104.02 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPdtlVLNGFNLTISEGA-------------TVglvggsgsgkstvISLLQRFYSPDSGEISMDDHGI 430
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEiygllgpngagktTL-------------IKIILGLLKPDSGEIKVLGKDI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 431 DTlNVEWLRSQIGLVSQEPVLFAT-SIRENIlfgdetaslkqvvaaakmanahefivklphgyethvgqfgtQLSGGQKQ 509
Cdd:cd03230 65 KK-EPEEVKRRIGYLPEEPSLYENlTVRENL-----------------------------------------KLSGGMKQ 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 510 RIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVA-HRLSTL-RKADTIAVLDAGRV 578
Cdd:cd03230 103 RLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAeRLCDRVAILNNGRI 173
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
364-592 |
2.39e-25 |
|
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: 106.22 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPdtlVLNGFNLTISEGATVGLVGGSGsgkstviS-----------LLQrfysPDSGEISMDDHGIDT 432
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSG-------SgksvllkliigLLR----PDSGEILVDGQDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 433 LNVE---WLRSQIGLVSQEPVLFaTS--IRENILF-----GDETASLKQVVAAAKMANAH--EFIVKLPHgyethvgqfg 500
Cdd:COG1127 72 LSEKelyELRRRIGMLFQGGALF-DSltVFENVAFplrehTDLSEAEIRELVLEKLELVGlpGAADKMPS---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 501 tQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESE-------RTVQDALdrasvGRTTVIVAHRLSTLRK-ADTIAV 572
Cdd:COG1127 141 -ELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSavideliRELRDEL-----GLTSVVVTHDLDSAFAiADRVAV 214
|
250 260
....*....|....*....|
gi 1002260479 573 LDAGRVVEAGTHDELLGMDD 592
Cdd:COG1127 215 LADGKIIAEGTPEELLASDD 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
364-588 |
2.95e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.00 E-value: 2.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRpDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIG 443
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 444 LVSQEP--VLFATSIRENILFGDETASLKQ------VVAAAKMANAHEFIVKLPHgyethvgqfgtQLSGGQKQRIAIAR 515
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENKKVPPkkmkdiIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 516 ALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVI-VAHRLSTLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDlRKTRKKTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1023-1217 |
4.27e-25 |
|
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: 104.26 E-value: 4.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1023 KNVHFSYPTRPEVavLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIrsySLARLRSQVALVS 1102
Cdd:cd03226 3 ENISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1103 QEPT--LFSGTIRDNIAYGAAEEHATEDEVARAAALANAHGFisaMERgydtrvgeRGAQLSGGQRQRIALARAVLKDAR 1180
Cdd:cd03226 78 QDVDyqLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYAL---KER--------HPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002260479 1181 ILLLDEATSALDAASERLVQDAVDRM-LRGRTCVVVAH 1217
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELaAQGKAVIVITH 184
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
366-577 |
4.32e-25 |
|
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: 102.71 E-value: 4.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 366 FKDVHFSYPSRPdtlVLNGFNLTISEGA-------------TVglvggsgsgkstvISLLQRFYSPDSGEISMDDHGIDT 432
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEivalvgpngsgksTL-------------LRAIAGLLKPTSGEILIDGKDIAK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 433 LNVEWLRSQIGLVSQepvlfatsirenilfgdetaslkqvvaaakmanahefivklphgyethvgqfgtqLSGGQKQRIA 512
Cdd:cd00267 66 LPLEELRRRIGYVPQ-------------------------------------------------------LSGGQRQRVA 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 513 IARALVRDPRILLLDEATSALDAESERTVQDALDRASV-GRTTVIVAHRLSTLRKA-DTIAVLDAGR 577
Cdd:cd00267 91 LARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1020-1249 |
5.68e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 106.35 E-value: 5.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEP-TLFSG-TIRDNIAYGAAEEHATEDEVARAAALANAhgfISAMErGYDTRvgeRGAQLSGGQRQRIALARAVLK 1177
Cdd:PRK13650 85 MVFQNPdNQFVGaTVEDDVAFGLENKGIPHEEMKERVNEALE---LVGMQ-DFKER---EPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1178 DARILLLDEATSALDAASE----RLVQDAVDRMlrGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLAVG 1249
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRleliKTIKGIRDDY--QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRG 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1019-1232 |
7.35e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 105.50 E-value: 7.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRpevAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQ-----RGSVLVDGEDI--RSYSL 1091
Cdd:PRK14258 7 AIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1092 ARLRSQVALVSQEPTLFSGTIRDNIAYGAaeehatedEVARAAALANAHGFISAMERGYD------TRVGERGAQLSGGQ 1165
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGV--------KIVGWRPKLEIDDIVESALKDADlwdeikHKIHKSALDLSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 1166 RQRIALARAVLKDARILLLDEATSALDAAS----ERLVQDAvdRMLRGRTCVVVAHRLSTVEK-SDTIAVVK 1232
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQSL--RLRSELTMVIVSHNLHQVSRlSDFTAFFK 225
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
694-974 |
8.21e-25 |
|
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: 106.59 E-value: 8.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 694 LLGCVGAVVFGAVLPLYSYSLGSLPEVYFLADDGQI-----------------RSKTRLYYFLFLGIAVVCITANIVQHY 756
Cdd:cd18558 2 VVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNItgnssglnssagpfeklEEEMTLYAYYYLIIGAIVLITAYIQGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 757 NFAVMGERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCLLVQAGATASLGFSLALAVSW 836
Cdd:cd18558 82 FWGLAAGRQTKKIRYKFFHAIMRQEIGWFDV--NDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 837 RLATVMMAMQPLI-IASFYFKKVLMAAMSKKAKKAQVQGSqLASEAVVNHRTITAFSSQRRMLRLYEAAQQGPKKDNVAH 915
Cdd:cd18558 160 KLTLVILAISPVLgLSAVVWAKILSGFTDKEKKAYAKAGA-VAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 916 SWFSGFCLCLCQFSNTGSMAVALWYGGKLMAKGLITPTHLFQVFFMLMTMGRVIADAGS 974
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVP 297
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
364-578 |
1.08e-24 |
|
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: 103.38 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPdtlVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGI--DTLNVEWLRSQ 441
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 442 IGLVSQEPVLFA-TSIRENILFGDETAsLKQVVAAAKmANAHEFIVKLphGYETHVGQFGTQLSGGQKQRIAIARALVRD 520
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPIKV-KGMSKAEAE-ERALELLEKV--GLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 521 PRILLLDEATSALDAESERTVQDAL-DRASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRV 578
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMkDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
421-607 |
1.18e-24 |
|
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: 104.61 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 421 GEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENiLFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFG 500
Cdd:cd03288 76 GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN-LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 501 TQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVE 580
Cdd:cd03288 155 ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVE 234
|
170 180
....*....|....*....|....*..
gi 1002260479 581 AGTHDELLGMDDggegGVYARMVHLQK 607
Cdd:cd03288 235 CDTPENLLAQED----GVFASLVRTDK 257
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
362-587 |
1.23e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 107.08 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 362 GEIVFKDVHFSYPSRPdtlVLNGFNLTISEGATvglvggsgsgkstvISL----------LQR----FYSPDSGEISMDD 427
Cdd:COG3839 2 ASLELENVSKSYGGVE---ALKDIDLDIEDGEF--------------LVLlgpsgcgkstLLRmiagLEDPTSGEILIGG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 428 HGIDTLNVEwlRSQIGLVSQEPVLF-ATSIRENILFG--------DETAslKQVVAAAKMANAHEFIVKLPhgyethvgq 498
Cdd:COG3839 65 RDVTDLPPK--DRNIAMVFQSYALYpHMTVYENIAFPlklrkvpkAEID--RRVREAAELLGLEDLLDRKP--------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 499 fgTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLS---TLrkADTIAVL 573
Cdd:COG3839 132 --KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRlhRRLGTTTIYVTHDQVeamTL--ADRIAVM 207
|
250
....*....|....
gi 1002260479 574 DAGRVVEAGTHDEL 587
Cdd:COG3839 208 NDGRIQQVGTPEEL 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1019-1240 |
1.49e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.47 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYS---LARLR 1095
Cdd:PRK13548 2 MLEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpaeLARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1096 sqvALVSQEPTL-FSGTIRDNIAYGAAEEHATEDEVARAAAlanahgfiSAMER----GYDTRvgeRGAQLSGGQRQRIA 1170
Cdd:PRK13548 79 ---AVLPQHSSLsFPFTVEEVVAMGRAPHGLSRAEDDALVA--------AALAQvdlaHLAGR---DYPQLSGGEQQRVQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1171 LARaVL-------KDARILLLDEATSALDAASE----RLVQDAVDRmlRGRTCVVVAHRLS-TVEKSDTIAVVKDGRVAE 1238
Cdd:PRK13548 145 LAR-VLaqlwepdGPPRWLLLDEPTSALDLAHQhhvlRLARQLAHE--RGLAVIVVLHDLNlAARYADRIVLLHQGRLVA 221
|
..
gi 1002260479 1239 RG 1240
Cdd:PRK13548 222 DG 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1036-1246 |
2.09e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.97 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1036 AVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERF---YDAQ---RGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFS 1109
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1110 G-TIRDNIAYgAAEEHATEDEVARAAALANAHGFISAMERGYDtRVGERGAQLSGGQRQRIALARAVLKDARILLLDEAT 1188
Cdd:PRK14246 104 HlSIYDNIAY-PLKSHGIKEKREIKKIVEECLRKVGLWKEVYD-RLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1189 SALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELL 1246
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1020-1251 |
3.18e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 103.94 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVAvLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:PRK13635 6 IRVEHISFRYPDAATYA-LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEP-TLFSG-TIRDNIAYGAAEEHATEDEVaraaalanahgfisaMERGYD--TRVG------ERGAQLSGGQRQRI 1169
Cdd:PRK13635 85 MVFQNPdNQFVGaTVQDDVAFGLENIGVPREEM---------------VERVDQalRQVGmedflnREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1170 ALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
....
gi 1002260479 1248 VGRA 1251
Cdd:PRK13635 230 SGHM 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1035-1236 |
3.92e-24 |
|
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: 102.52 E-value: 3.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1035 VAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDI---RSYSLARLRsqVALVSQEPTLFSG- 1110
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglPPHEIARLG--IGRTFQIPRLFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1111 TIRDNIAYGAAEEHAtedevARAAALANAHGFISAMER--------GYDTRVGERGAQLSGGQRQRIALARAVLKDARIL 1182
Cdd:cd03219 91 TVLENVMVAAQARTG-----SGLLLARARREEREARERaeellervGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1183 LLDEATSALdaaSERLVQDAVDRML----RGRTCVVVAHRLSTVEK-SDTIAVVKDGRV 1236
Cdd:cd03219 166 LLDEPAAGL---NPEETEELAELIRelreRGITVLLVEHDMDVVMSlADRVTVLDQGRV 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1018-1218 |
4.61e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.36 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFsypTRPEVAVL-AGFSLEIGAGKTVALVGPSGSGKSTVI----GLierfYDAQRGSVLV-DGEDirsysl 1091
Cdd:COG4178 361 GALALEDLTL---RTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLraiaGL----WPYGSGRIARpAGAR------ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1092 arlrsqVALVSQEPTLFSGTIRDNIAYGAAEEHATEDEVaraaalanahgfISAMER----GYDTRVGER---GAQLSGG 1164
Cdd:COG4178 428 ------VLFLPQRPYLPLGTLREALLYPATAEAFSDAEL------------REALEAvglgHLAERLDEEadwDQVLSLG 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 1165 QRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHR 1218
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
364-587 |
4.74e-24 |
|
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: 102.26 E-value: 4.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSrpDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWL---RS 440
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 441 QIGLVSQEPVLFA-TSIRENILFG--DETA---SLKQVVAAAKMANAHEFIVKLphGYETHVGQFGTQLSGGQKQRIAIA 514
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGrlGRRStwrSLFGLFPKEEKQRALAALERV--GLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 515 RALVRDPRILLLDEATSALDAESERTVQDALDRA--SVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDEL 587
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1020-1247 |
5.38e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 103.25 E-value: 5.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEP--TLFSGTIRDNIAYGAAEEHATEDEVaraaALANAHGFISAMERGYDTRvgeRGAQLSGGQRQRIALARAVLK 1177
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEM----IKRVDEALLAVNMLDFKTR---EPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 1178 DARILLLDEATSALDAASE----RLVQDAVDRMlrGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRqeimRVIHEIKEKY--QLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1038-1247 |
7.81e-24 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 104.80 E-value: 7.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1038 LAGFSLEI-----GAGKTvALVGPSGSGKSTVIGLI---ERfydAQRGSVLVDGEDI----RSYSLARLRSQVALVSQEP 1105
Cdd:COG4148 11 RGGFTLDVdftlpGRGVT-ALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEVLqdsaRGIFLPPHRRRIGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1106 TLFSG-TIRDNIAYG-----AAEEHATEDEVARAAAlanahgfISA-MERgydtrvgeRGAQLSGGQRQRIALARAVLKD 1178
Cdd:COG4148 87 RLFPHlSVRGNLLYGrkrapRAERRISFDEVVELLG-------IGHlLDR--------RPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 1179 ARILLLDEATSALDAASERLVQDAVDRmLRGRT---CVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELLA 1247
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLER-LRDELdipILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
415-588 |
1.00e-23 |
|
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: 101.26 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 415 FYSPDSGEISMDDHGIDTLNVEwlRSQIGLVSQEPVLFA-TSIRENILFG------DETASLKQVVAAAKMANAHEFIVK 487
Cdd:cd03299 48 FIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPhMTVYKNIAYGlkkrkvDKKEIERKVLEIAEMLGIDHLLNR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 488 LPhgyethvgqfgTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRA-SVGRTTVI-VAHRLSTLR 565
Cdd:cd03299 126 KP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIrKEFGVTVLhVTHDFEEAW 194
|
170 180
....*....|....*....|....
gi 1002260479 566 K-ADTIAVLDAGRVVEAGTHDELL 588
Cdd:cd03299 195 AlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1035-1236 |
1.36e-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: 101.65 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1035 VAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDI---RSYSLARL---RS-QValvsqePTL 1107
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglPPHRIARLgiaRTfQN------PRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1108 FSG-TIRDNIAYGA-------------------AEEHATEDEVAraaalanahgfiSAMER-GYDTRVGERGAQLSGGQR 1166
Cdd:COG0411 91 FPElTVLENVLVAAharlgrgllaallrlprarREEREARERAE------------ELLERvGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 1167 QRIALARAVLKDARILLLDEATSALDAA-SERLVqDAVDRM--LRGRTCVVVAHRLSTVEK-SDTIAVVKDGRV 1236
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEeTEELA-ELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1021-1247 |
1.75e-23 |
|
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: 100.44 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1021 EFKNVHFSYPtrpEVAVLAGFSLEIGAGKTVALVGPSGSGKST----VIGLIerfyDAQRGSVLVDGEDI---RSYSLAR 1093
Cdd:COG0410 5 EVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTllkaISGLL----PPRSGSIRFDGEDItglPPHRIAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1094 LRsqVALVSQEPTLFSG-TIRDNI---AYGAAEEHATEDevaraaalanahgfisAMERGYDT--RVGER----GAQLSG 1163
Cdd:COG0410 78 LG--IGYVPEGRRIFPSlTVEENLllgAYARRDRAEVRA----------------DLERVYELfpRLKERrrqrAGTLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1164 GQRQRIALARAVLKDARILLLDEATSALdaaSERLVQDAVD--RMLR--GRTCVVV---AHRLSTVekSDTIAVVKDGRV 1236
Cdd:COG0410 140 GEQQMLAIGRALMSRPKLLLLDEPSLGL---APLIVEEIFEiiRRLNreGVTILLVeqnARFALEI--ADRAYVLERGRI 214
|
250
....*....|.
gi 1002260479 1237 AERGRHHELLA 1247
Cdd:COG0410 215 VLEGTAAELLA 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1020-1246 |
2.14e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 100.96 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:COG4559 2 LEAENLSVRLGGRT---LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTL-FSGTIRDNIAYGAA---EEHATEDEVARAaalanahgfisAMER-GYDTRVGERGAQLSGGQRQRIALARA 1174
Cdd:COG4559 79 VLPQHSSLaFPFTVEEVVALGRAphgSSAAQDRQIVRE-----------ALALvGLAHLAGRSYQTLSGGEQQRVQLARV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1175 -------VLKDARILLLDEATSALDAASerlvQDAVDRMLR-----GRTCVVVAHRLS-TVEKSDTIAVVKDGRVAERGR 1241
Cdd:COG4559 148 laqlwepVDGGPRWLFLDEPTSALDLAH----QHAVLRLARqlarrGGGVVAVLHDLNlAAQYADRILLLHQGRLVAQGT 223
|
....*
gi 1002260479 1242 HHELL 1246
Cdd:COG4559 224 PEEVL 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1029-1240 |
2.37e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 107.94 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1029 YPTRPEVaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDgedirsyslarlRSqVALVSQEPTLF 1108
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RS-IAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1109 SGTIRDNIAYGAAEEHATEDEVARAAALANAHGFISAmerGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEAT 1188
Cdd:PTZ00243 734 NATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGG---GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 1189 SALDA-ASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERG 1240
Cdd:PTZ00243 811 SALDAhVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
364-579 |
2.88e-23 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 100.52 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSrpDTLVLNGFNLTISEGA-------------TVglvggsgsgkstvISLLQRFYSPDSGEISMDDHGI 430
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEfvaligpsgagksTL-------------LRCLNGLVEPTSGEILVDGQDV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 431 DTLNVEWL---RSQIGLVSQEPVLFA-TSIRENILFG--DET---ASLKQVVAAAKMANAHEFI--VKLPHgyetHVGQF 499
Cdd:COG3638 68 TALRGRALrrlRRRIGMIFQQFNLVPrLSVLTNVLAGrlGRTstwRSLLGLFPPEDRERALEALerVGLAD----KAYQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 500 GTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASV--GRTTVIVAHRLSTLRK-ADTIAVLDAG 576
Cdd:COG3638 144 ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDG 223
|
...
gi 1002260479 577 RVV 579
Cdd:COG3638 224 RVV 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1020-1240 |
3.03e-23 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 99.36 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSY-PTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIrSYSLARLRSQV 1098
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQEPTLFSG-TIRDNIAYGA-------AEEHATEDEVARAAAlanahgfisaMERGYDTRVGErgaqLSGGQRQRIA 1170
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAglyglkgDELTARLEELADRLG----------MEELLDRRVGG----FSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 1171 LARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVA-HRLSTVEK-SDTIAVVKDGRVAERG 1240
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
367-582 |
3.70e-23 |
|
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: 97.89 E-value: 3.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 367 KDVHFSYPSRPdtlVLNGFNLTISEGA-------------TVglvggsgsgkstvISLLQRFYSPDSGEISMDDHGIDTL 433
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEivgilgpngagksTL-------------LKTLAGLLKPSSGEILLDGKDLASL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 434 NVEWLRSQIGLVSQepvlfatsirenilfgdetaSLKQVVAAAKmanAHEFIvklphgyethvgqfgTQLSGGQKQRIAI 513
Cdd:cd03214 67 SPKELARKIAYVPQ--------------------ALELLGLAHL---ADRPF---------------NELSGGERQRVLL 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 514 ARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLS-TLRKADTIAVLDAGRVVEAG 582
Cdd:cd03214 109 ARALAQEPPILLLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1020-1240 |
4.58e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.89 E-value: 4.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSY-PTRP-EVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDI--RSYSLARLR 1095
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1096 SQVALVSQEP--TLFSGTIRDNIAYGAAEEHATEDEVARAAalanahgfISAMER---GYDTRVGERGAQLSGGQRQRIA 1170
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEEEIENRV--------KRAMNIvglDYEDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 1171 LARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERG 1240
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQG 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
364-588 |
7.27e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 99.01 E-value: 7.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPdtlVLNGFNLTISEGA------------TvglvggsgsgkstviSLLQ---RFYSPDSGEISMDDH 428
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEfvaivgpngagkS---------------TLLKailGLLPPTSGTVRLFGK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 429 gidtlNVEWLRSQIGLVSQEPVL---FATSIRENI---------LFGDETASLKQVVAAA-KMANAHEFIVKlphgyeth 495
Cdd:COG1121 69 -----PPRRARRRIGYVPQRAEVdwdFPITVRDVVlmgrygrrgLFRRPSRADREAVDEAlERVGLEDLADR-------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 496 vgQFGtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLSTLRK-ADTIAVL 573
Cdd:COG1121 136 --PIG-ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLL 212
|
250
....*....|....*
gi 1002260479 574 DaGRVVEAGTHDELL 588
Cdd:COG1121 213 N-RGLVAHGPPEEVL 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
364-588 |
1.01e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 98.63 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDV--HFSypsrpDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDdhGIDTL----NVEW 437
Cdd:PRK09493 2 IEFKNVskHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVD--GLKVNdpkvDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 438 LRSQIGLVSQEPVLFA--TSIrENILFGDetaslKQVVAAAKMA---NAHEFIVKLphGYETHVGQFGTQLSGGQKQRIA 512
Cdd:PRK09493 75 IRQEAGMVFQQFYLFPhlTAL-ENVMFGP-----LRVRGASKEEaekQARELLAKV--GLAERAHHYPSELSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 513 IARALVRDPRILLLDEATSALDAESERTVQDAL-DRASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDELL 588
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMqDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
364-582 |
1.13e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.42 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSrpDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIG 443
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 444 LVSQEP--VLFATSIRENILFGDETASLKQ------VVAAAKMANAHEFIVKLPHgyethvgqfgtQLSGGQKQRIAIAR 515
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNMGLDKdeverrVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 516 ALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVA-HRLS-TLRKADTIAVLDAGRVVEAG 582
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEG 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1019-1193 |
1.16e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 99.17 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYP-TRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARlrsq 1097
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 vALVSQEPTLFSG-TIRDNIAYG-------AAEEHATEDEVARaaalanahgfisamergydtRVGERGA------QLSG 1163
Cdd:COG4525 79 -GVVFQKDALLPWlNVLDNVAFGlrlrgvpKAERRARAEELLA--------------------LVGLADFarrriwQLSG 137
|
170 180 190
....*....|....*....|....*....|
gi 1002260479 1164 GQRQRIALARAVLKDARILLLDEATSALDA 1193
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1038-1247 |
1.94e-22 |
|
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: 100.57 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1038 LAGFSLEI-----GAGKTvALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYS----LARLRSQVALVSQEPTLF 1108
Cdd:TIGR02142 9 LGDFSLDAdftlpGQGVT-AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgifLPPEKRRIGYVFQEARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1109 SG-TIRDNIAYG-----AAEEHATEDEVARAAalanahgfisamerGYDTRVGERGAQLSGGQRQRIALARAVLKDARIL 1182
Cdd:TIGR02142 88 PHlSVRGNLRYGmkrarPSERRISFERVIELL--------------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 1183 LLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELLA 1247
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1019-1246 |
2.35e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 99.91 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYslARL-RSQ 1097
Cdd:PRK13536 41 AIDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR--ARLaRAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTL-FSGTIRDN-IAYGAA-EEHATEDEVARAAALAnahgfISAMERGYDTRVgergAQLSGGQRQRIALARA 1174
Cdd:PRK13536 116 IGVVPQFDNLdLEFTVRENlLVFGRYfGMSTREIEAVIPSLLE-----FARLESKADARV----SDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 1175 VLKDARILLLDEATSALDAASERLVQDAVDRML-RGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELL 1246
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALI 260
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1020-1247 |
2.99e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 98.23 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVavLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIR--SYSLARLRSQ 1097
Cdd:PRK13639 2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEP--TLFSGTIRDNIAYGAAEEHATEDEVARAAALANAHgfiSAMErGYDTRVGErgaQLSGGQRQRIALARAV 1175
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKA---VGME-GFENKPPH---HLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 1176 LKDARILLLDEATSALD--AASE--RLVQDAVDrmlRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELLA 1247
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDpmGASQimKLLYDLNK---EGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
378-583 |
4.22e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.02 E-value: 4.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 378 DTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEwlRSQIGLVSQEPVLFA-TSI 456
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFPhMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 457 RENILFG--------DETAslKQVVAAAKMANAHEFIVKLPHgyethvgqfgtQLSGGQKQRIAIARALVRDPRILLLDE 528
Cdd:PRK09452 104 FENVAFGlrmqktpaAEIT--PRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 529 ATSALDAESERTVQD---ALDRaSVGRTTVIVAH-RLSTLRKADTIAVLDAGRVVEAGT 583
Cdd:PRK09452 171 SLSALDYKLRKQMQNelkALQR-KLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
409-588 |
5.79e-22 |
|
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: 96.41 E-value: 5.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 409 ISLLQRfysPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVL-------FATSIRENILFGDETASLKQVVAAAKMAN- 480
Cdd:COG1124 51 LAGLER---PWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQVGl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 481 AHEFIVKLPHgyethvgqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALD--RASVGRTTVIVA 558
Cdd:COG1124 128 PPSFLDRYPH-----------QLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKdlREERGLTYLFVS 196
|
170 180 190
....*....|....*....|....*....|.
gi 1002260479 559 HRLSTLRK-ADTIAVLDAGRVVEAGTHDELL 588
Cdd:COG1124 197 HDLAVVAHlCDRVAVMQNGRIVEELTVADLL 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
364-566 |
5.97e-22 |
|
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: 95.55 E-value: 5.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPsrPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLN---VEWLRS 440
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 441 QIGLVSQEPVLFAT-SIRENILFGDETASLKQVVAAAKMANAHEfIVKLPHGYEThvgqFGTQLSGGQKQRIAIARALVR 519
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEVTGVPPREIRKRVPAALE-LVGLSHKHRA----LPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 520 DPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVA-----------HRLSTLRK 566
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAthakelvdttrHRVIALER 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1038-1245 |
9.50e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.00 E-value: 9.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1038 LAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYD-----AQRGSVLVDGEDIRS--YSLARLRSQVALVSQEPTLFSG 1110
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSprTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1111 TIRDNIAYG----AAEEHATEDEVARAAALANAHgFISAMERGYDTRVGergaqLSGGQRQRIALARAVLKDARILLLDE 1186
Cdd:PRK14239 101 SIYENVVYGlrlkGIKDKQVLDEAVEKSLKGASI-WDEVKDRLHDSALG-----LSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1187 ATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHEL 1245
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1020-1246 |
1.51e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 95.36 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPtrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVI----GLIERFYDAQ-RGSVLVDGEDIRSYSLARL 1094
Cdd:PRK14247 4 IEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfnRLIELYPEARvSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1095 RSQVALVSQEPTLFSG-TIRDNIAYGAAEEHATEDEVARAAALANahgfisAMERG-----YDTRVGERGAQLSGGQRQR 1168
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNlSIFENVALGLKLNRLVKSKKELQERVRW------ALEKAqlwdeVKDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1169 IALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELL 1246
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVF 233
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
417-587 |
1.66e-21 |
|
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: 95.10 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 417 SPDSGEISMDDHGIDTLNVEwlRSQIGLVSQEPVLFA-TSIRENILFGDETASLKQVVAAAKM-ANAHEFI--VKLpHGY 492
Cdd:cd03296 53 RPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRhMTVFDNVAFGLRVKPRSERPPEAEIrAKVHELLklVQL-DWL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 493 EThvgQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRA--SVGRTTVIVAHRLS-TLRKADT 569
Cdd:cd03296 130 AD---RYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLhdELHVTTVFVTHDQEeALEVADR 206
|
170
....*....|....*...
gi 1002260479 570 IAVLDAGRVVEAGTHDEL 587
Cdd:cd03296 207 VVVMNKGRIEQVGTPDEV 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
418-588 |
1.66e-21 |
|
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: 97.86 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDH-------GIDtLNVEwlRSQIGLVSQEPVLFAT-SIRENILFGdetasLKQVVAAAKMANAHEfIVKLp 489
Cdd:COG4148 51 PDSGRIRLGGEvlqdsarGIF-LPPH--RRRIGYVFQEARLFPHlSVRGNLLYG-----RKRAPRAERRISFDE-VVEL- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 490 HGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLS-TLRK 566
Cdd:COG4148 121 LGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERlrDELDIPILYVSHSLDeVARL 200
|
170 180
....*....|....*....|..
gi 1002260479 567 ADTIAVLDAGRVVEAGTHDELL 588
Cdd:COG4148 201 ADHVVLLEQGRVVASGPLAEVL 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
381-588 |
1.89e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 95.20 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 381 VLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDT---LN-----VEWLRSQIGLVSQEPVLF 452
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarsLSqqkglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 453 A-TSIRENILFGdeTASLKQVVAAAKMANAHEFIVKLphGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATS 531
Cdd:PRK11264 98 PhRTVLENIIEG--PVIVKGEPKEEATARARELLAKV--GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 532 ALDAESERTVQDALDR-ASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDELL 588
Cdd:PRK11264 174 ALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1019-1240 |
2.34e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.64 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRPEvAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFY---DAQRGSVLVDGEDIRSYSLARLR 1095
Cdd:PRK13640 5 IVEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1096 SQVALVSQEP-TLFSG-TIRDNIAYGAAEEHATEDEVARAAALANAhgfisamERGYDTRVGERGAQLSGGQRQRIALAR 1173
Cdd:PRK13640 84 EKVGIVFQNPdNQFVGaTVGDDVAFGLENRAVPRPEMIKIVRDVLA-------DVGMLDYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1174 AVLKDARILLLDEATSALDAASERLVQDAVDRML--RGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERG 1240
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
364-582 |
4.36e-21 |
|
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: 93.09 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPdtlVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDdhGIDTLNVEWLRSQIG 443
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG--GRDVTDLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 444 LVSQEPVLFA-TSIRENILFGDETASLKQVVAAAKMANAHEFIvklphGYETHVGQFGTQLSGGQKQRIAIARALVRDPR 522
Cdd:cd03301 76 MVFQNYALYPhMTVYDNIAFGLKLRKVPKDEIDERVREVAELL-----QIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 523 ILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAH-RLSTLRKADTIAVLDAGRVVEAG 582
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
694-982 |
4.37e-21 |
|
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: 95.31 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 694 LLGCVGAVVFGAVLPLYSYSLGslpevyFLADDGQIRSKTRLYY---FLFLGIAVVCITANIVQHYNFAVMGERLTERVR 770
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTK------LLIDDVIPAGDLSLLLwiaLLLLLLALLRALLSYLRRYLAARLGQRVVFDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 771 GQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCLLVQAGATASLGFSLALAVSWRLATVMMAMQPLII 850
Cdd:cd07346 76 RDLFRHLQRLSLSFFDR--NRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 851 ASFYF--KKVLMAAMSKKAKKAQVqgSQLASEAVVNHRTITAFSSQRRMLRLYEAAQQGPKKDNVAHSWFSGFCLCLCQF 928
Cdd:cd07346 154 LILRYfrRRIRKASREVRESLAEL--SAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 929 SNTGSMAVALWYGGKLMAKGLITPTHLFQVFFMLMTMGRVIADAGSLTSDLAQG 982
Cdd:cd07346 232 LTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQA 285
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
364-582 |
4.61e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 93.19 E-value: 4.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPsrPDTLVLNGFNLTISEGA-------------TVglvggsgsgkstvISLLQRFYSPDSGEISMDDHGI 430
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEfvfltgpsgagksTL-------------LKLLYGEERPTSGQVLVNGQDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 431 DTLN---VEWLRSQIGLVSQE-PVLFATSIRENILF-----GDETASLKQVVAAA----KMAN-AHefivKLPHgyethv 496
Cdd:COG2884 67 SRLKrreIPYLRRRIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRRVREVldlvGLSDkAK----ALPH------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 497 gqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVA-HRLSTLRKAD--TIaVL 573
Cdd:COG2884 137 -----ELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkrVL-EL 210
|
....*....
gi 1002260479 574 DAGRVVEAG 582
Cdd:COG2884 211 EDGRLVRDE 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
418-587 |
5.44e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 94.70 E-value: 5.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTLNVEWLRSQIGLVSQEP--VLFATSIRENILFGDE------TASLKQVVAAAKMANAHEFIVKLP 489
Cdd:PRK13635 59 PEAGTITVGGMVLSEETVWDVRRQVGMVFQNPdnQFVGATVQDDVAFGLEnigvprEEMVERVDQALRQVGMEDFLNREP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 490 HgyethvgqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSALD----AESERTVQDALDRasvGRTTVI-VAHRLSTL 564
Cdd:PRK13635 139 H-----------RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQ---KGITVLsITHDLDEA 204
|
170 180
....*....|....*....|...
gi 1002260479 565 RKADTIAVLDAGRVVEAGTHDEL 587
Cdd:PRK13635 205 AQADRVIVMNKGEILEEGTPEEI 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1020-1240 |
5.80e-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: 92.23 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHF---SYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLI--ERFYDAQRGSVLVDGEDIrsySLARL 1094
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1095 RSQVALVSQE----PTLfsgTIRDNIAYgaaeehatedevaraaalanahgfiSAMERGydtrvgergaqLSGGQRQRIA 1170
Cdd:cd03213 81 RKIIGYVPQDdilhPTL---TVRETLMF-------------------------AAKLRG-----------LSGGERKRVS 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 1171 LARAVLKDARILLLDEATSALDAASERLVQDAVDRM-LRGRTCVVVAHRLST--VEKSDTIAVVKDGRVAERG 1240
Cdd:cd03213 122 IALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1028-1226 |
6.85e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.91 E-value: 6.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1028 SYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGedirsyslarlRSQVALVSQ---E 1104
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1105 PTLFSGTIRDNIAYGA-----------AEEHATEDEvaraaalanahgfisAMER-GYDTRVGERGAQLSGGQRQRIALA 1172
Cdd:NF040873 67 PDSLPLTVRDLVAMGRwarrglwrrltRDDRAAVDD---------------ALERvGLADLAGRQLGELSGGQRQRALLA 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 1173 RAVLKDARILLLDEATSALDAASERLVQDAVDRML-RGRTCVVVAHRLSTVEKSD 1226
Cdd:NF040873 132 QGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRAD 186
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1019-1236 |
7.05e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.51 E-value: 7.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSY-PTRP-EVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIR----SYSLA 1092
Cdd:PRK13641 2 SIKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1093 RLRSQVALVSQ--EPTLFSGTIRDNIAYGAAEEHATEDEVARAAalanahgfISAMER-GYDTRVGERGA-QLSGGQRQR 1168
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKA--------LKWLKKvGLSEDLISKSPfELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1169 IALARAVLKDARILLLDEATSALDAAS-ERLVQDAVDRMLRGRTCVVVAHRLSTV-EKSDTIAVVKDGRV 1236
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKL 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1020-1241 |
7.51e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.06 E-value: 7.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVAvlaGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSysLARLRSQVA 1099
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIAYGAAEEHATEDEVARAAALANahGFISAMERGydtrvGERGAQLSGGQRQRIALARAVLKD 1178
Cdd:PRK11607 95 MMFQSYALFPHmTVEQNIAFGLKQDKLPKAEIASRVNEML--GLVHMQEFA-----KRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 1179 ARILLLDEATSALDAA-SERLVQDAVDRMLR-GRTCVVVAHrlsTVEKSDTIAvvkdGRVA--ERGR 1241
Cdd:PRK11607 168 PKLLLLDEPMGALDKKlRDRMQLEVVDILERvGVTCVMVTH---DQEEAMTMA----GRIAimNRGK 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
419-588 |
7.51e-21 |
|
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: 95.12 E-value: 7.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 419 DSGEISMDDHGIDTLNVEWLRS----QIGLVSQEPvlfATS----------IRENILF---GDETASLKQVVAAAKM--- 478
Cdd:COG0444 61 TSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDP---MTSlnpvmtvgdqIAEPLRIhggLSKAEARERAIELLERvgl 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 479 ANAHEFIVKLPHgyethvgqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAeserTVQ-DALD-----RASVGR 552
Cdd:COG0444 138 PDPERRLDRYPH-----------ELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGL 202
|
170 180 190
....*....|....*....|....*....|....*..
gi 1002260479 553 TTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDELL 588
Cdd:COG0444 203 AILFITHDLGVVAEiADRVAVMYAGRIVEEGPVEELF 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
364-585 |
9.48e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 92.77 E-value: 9.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSrpdTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDH------GIDTLNVEW 437
Cdd:PRK11124 3 IQLNGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfskTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 438 LRSQIGLVSQEPVLFA-TSIRENILfgdeTASLKqVVAAAK---MANAHEFIVKLPhgYETHVGQFGTQLSGGQKQRIAI 513
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPhLTVQQNLI----EAPCR-VLGLSKdqaLARAEKLLERLR--LKPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 514 ARALVRDPRILLLDEATSALDAE-SERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAV-LDAGRVVEAGTHD 585
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVyMENGHIVEQGDAS 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1019-1241 |
9.91e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 93.66 E-value: 9.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYP--TRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYS----LA 1092
Cdd:PRK13649 2 GINLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1093 RLRSQVALVSQ--EPTLFSGTIRDNIAYGAAEEHATEDEVARAaalanahgfisAMER----GYDTRVGERGA-QLSGGQ 1165
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEAL-----------AREKlalvGISESLFEKNPfELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 1166 RQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRM-LRGRTCVVVAHRLSTV-EKSDTIAVVKDGRVAERGR 1241
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1042-1246 |
1.09e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.26 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1042 SLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRS----QVALVSQEPTLFSG-TIRDNI 1116
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1117 AYGAAEEHATEDEVARAAALANAHGFISAMERGYDTrvgergaQLSGGQRQRIALARAVLKDARILLLDEATSALDAASE 1196
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 1197 RLVQDAVDRML--RGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELL 1246
Cdd:PRK10070 201 TEMQDELVKLQakHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1022-1217 |
1.24e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1022 FKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGeDIRsyslarlrsqVALV 1101
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1102 SQEPTLFSG-TIRDNIAYGAAE-----------EHATEDEVARAAALANAHGFISAM-------------------ERGY 1150
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAElraleaeleelEAKLAEPDEDLERLAELQEEFEALggweaearaeeilsglgfpEEDL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1151 DTRVGErgaqLSGGQRQRIALARAVLKDARILLLDEATSALDAAS-ERLVQdavdrMLRGR--TCVVVAH 1217
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiEWLEE-----FLKNYpgTVLVVSH 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1034-1247 |
1.32e-20 |
|
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: 97.45 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1034 EVAVLAGFSLEIGAGKTVALVGPSGSGKS----TVIGLIERFYDAQRGSVLVDGEDIRSYSLARLR----SQVALVSQEP 1105
Cdd:COG4172 22 TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1106 T-----LFsgTIRDNIAYG----------AAEEHATE--DEVAraaalanahgfISAMERgydtRVGERGAQLSGGQRQR 1168
Cdd:COG4172 102 MtslnpLH--TIGKQIAEVlrlhrglsgaAARARALEllERVG-----------IPDPER----RLDAYPHQLSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1169 IALARAVLKDARILLLDEATSALDAASER----LVQDAVDRMlrGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHH 1243
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVQAqildLLKDLQREL--GMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTA 242
|
....
gi 1002260479 1244 ELLA 1247
Cdd:COG4172 243 ELFA 246
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1020-1219 |
1.33e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.84 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVH--FSYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQ 1097
Cdd:COG1101 2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEP---TLFSGTIRDN--IAYGAAEehatedevaraaalanAHGFISAMERGY-------------------DTR 1153
Cdd:COG1101 82 IGRVFQDPmmgTAPSMTIEENlaLAYRRGK----------------RRGLRRGLTKKRrelfrellatlglglenrlDTK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 1154 VGergaQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGR--TCVVVAHRL 1219
Cdd:COG1101 146 VG----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNM 209
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1020-1245 |
1.35e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.79 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTrpeVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARlrSQVA 1099
Cdd:PRK11432 7 VVLKNITKRFGS---NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIAYG------AAEEHATEdeVARAAALANAHGFisaMERGYDtrvgergaQLSGGQRQRIALA 1172
Cdd:PRK11432 82 MVFQSYALFPHmSLGENVGYGlkmlgvPKEERKQR--VKEALELVDLAGF---EDRYVD--------QISGGQQQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 1173 RAVLKDARILLLDEATSALDAASERLVQDAVdRMLRGR---TCVVVAHRLS-TVEKSDTIAVVKDGRVAERGRHHEL 1245
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKI-RELQQQfniTSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
65-294 |
1.49e-20 |
|
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: 93.39 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 65 FSSGAVDKFALRLLYVAVAVGACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDaapsspsspqaqaQATTFRVI 144
Cdd:cd18557 30 GDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFD-------------KHKTGELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 145 STVSDDADAIQDFLGEKLPMVLANATLFFGALAVSFVFAWRLALAGLPFTLLLFVTpSVLLAGRMAAAAGEARAAYEEAG 224
Cdd:cd18557 97 SRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIA-SKIYGRYIRKLSKEVQDALAKAG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 225 GIAQQAVSSIRTVASYTAERRTVERFRGAVARSAALGVRQGLIKGAVIGSMGVIYAVWSFLS-WIGSLLVI 294
Cdd:cd18557 176 QVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVlWYGGYLVL 246
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
417-582 |
1.49e-20 |
|
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: 91.59 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 417 SPDSGEISMDDhgidtlnVEWLRSQ-----------IGLVSQEPVLFA-TSIRENILFGdetasLKQVVAAAKMANAHEF 484
Cdd:cd03297 48 KPDGGTIVLNG-------TVLFDSRkkinlppqqrkIGLVFQQYALFPhLNVRENLAFG-----LKRKRNREDRISVDEL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 485 IVKLphGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLS 562
Cdd:cd03297 116 LDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQikKNLNIPVIFVTHDLS 193
|
170 180
....*....|....*....|.
gi 1002260479 563 TL-RKADTIAVLDAGRVVEAG 582
Cdd:cd03297 194 EAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1020-1236 |
2.53e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 90.80 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTrpeVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRsyslARLRSQVA 1099
Cdd:cd03269 1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIAYGAAEEHATEDEVARAAAlanahgfiSAMER-GYDTRVGERGAQLSGGQRQRIALARAVLK 1177
Cdd:cd03269 74 YLPEERGLYPKmKVIDQLVYLAQLKGLKKEEARRRID--------EWLERlELSEYANKRVEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 1178 DARILLLDEATSALDAASERLVQDAVDRMLR-GRTCVVVAHRLSTVEK-SDTIAVVKDGRV 1236
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELARaGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1023-1246 |
3.38e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.77 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1023 KNVHFSYPTRpevAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVS 1102
Cdd:PRK10575 15 RNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1103 QE-PTLFSGTIRDNIA------------YGAAEEHATEDEVARAAALANAHGFISAmergydtrvgergaqLSGGQRQRI 1169
Cdd:PRK10575 92 QQlPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEAISLVGLKPLAHRLVDS---------------LSGGERQRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1170 ALARAVLKDARILLLDEATSALDAASERLVQDAVDRM--LRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELL 1246
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsqERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1019-1246 |
3.66e-20 |
|
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: 91.30 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERF-YDAQRGSVLVDGEDIRSYSLARLRSQ 1097
Cdd:COG1119 3 LLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLF---SGTIRDNIAYGA-----------AEEHATEDEVaraaalanahgfisaMER-GYDTRVGERGAQLS 1162
Cdd:COG1119 80 IGLVSPALQLRfprDETVLDVVLSGFfdsiglyreptDEQRERAREL---------------LELlGLAHLADRPFGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1163 GGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR-GRTCVV-VAHRLSTVEKSDTIAVV-KDGRVAER 1239
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVlVTHHVEEIPPGITHVLLlKDGRVVAA 224
|
....*..
gi 1002260479 1240 GRHHELL 1246
Cdd:COG1119 225 GPKEEVL 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1018-1247 |
3.69e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 92.38 E-value: 3.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFSYPTRP--EVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDI-----RSYS 1090
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1091 LARLRSQVALVSQEP--TLFSGTIRDNIAYGAAEEHATEDEVARAAALANAhgfISAMERGYDTRvgeRGAQLSGGQRQR 1168
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLK---LVQLPEDYVKR---SPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1169 IALARAVLKDARILLLDEATSALDAASErlvQDAVDRMLR-----GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRH 1242
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGE---EDFINLFERlnkeyKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSP 235
|
....*
gi 1002260479 1243 HELLA 1247
Cdd:PRK13645 236 FEIFS 240
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
502-583 |
5.05e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 92.94 E-value: 5.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRV 578
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDinRELGLTIVLITHEMDVVKRiCDRVAVIDAGRL 219
|
....*
gi 1002260479 579 VEAGT 583
Cdd:PRK11153 220 VEQGT 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
363-585 |
5.21e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.84 E-value: 5.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 363 EIVFKDVHFSYPSRPdtlVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDH------GIDTLNVE 436
Cdd:COG4161 2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 437 WLRSQIGLVSQE----PVLfatSIRENiLFGDETASLKQVVAAAKmANAHEFIVKLphGYETHVGQFGTQLSGGQKQRIA 512
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMEN-LIEAPCKVLGLSKEQAR-EKAMKLLARL--RLTDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 513 IARALVRDPRILLLDEATSALDAE-SERTVQDALDRASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHD 585
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1020-1236 |
6.75e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.56 E-value: 6.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPE-VAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDI---RSYSLARLR 1095
Cdd:PRK10535 5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatlDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1096 SQ-VALVSQEPTLFSG-TIRDNI----AYGAAEEHATEDEVaraaalanahgfISAMER-GYDTRVGERGAQLSGGQRQR 1168
Cdd:PRK10535 85 REhFGFIFQRYHLLSHlTAAQNVevpaVYAGLERKQRLLRA------------QELLQRlGLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1169 IALARAVLKDARILLLDEATSALDAASERLVQdAVDRMLR--GRTCVVVAHRLSTVEKSDTIAVVKDGRV 1236
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVM-AILHQLRdrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1034-1235 |
8.96e-20 |
|
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: 89.80 E-value: 8.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1034 EVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGE----DIRSYS----LARLRSQVALVSQ-- 1103
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASpreiLALRRRTIGYVSQfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1104 -------------EPTLFSGTIRDniaygAAEEHATEdevaraaalanahgfisAMERgydTRVGERGAQL-----SGGQ 1165
Cdd:COG4778 103 rviprvsaldvvaEPLLERGVDRE-----EARARARE-----------------LLAR---LNLPERLWDLppatfSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 1166 RQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVV-VAHRLSTVEK-SDTIAVVKDGR 1235
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPFS 229
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1038-1240 |
9.06e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 90.61 E-value: 9.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1038 LAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYD-----AQRGSVLVDGEDIRSYSL--ARLRSQVALVSQEPTLFSG 1110
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVdpVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1111 TIRDNIAYGAAEE--HATEDEVARAAALAnahgfiSAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEAT 1188
Cdd:PRK14243 106 SIYDNIAYGARINgyKGDMDELVERSLRQ------AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 1189 SALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERG 1240
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGG 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1027-1251 |
9.22e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.84 E-value: 9.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1027 FSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGE--DIRSYSLARLRSQVALVSQE 1104
Cdd:PRK13638 9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1105 P--TLFSGTIRDNIAYGAAEEHATEDEVAraaalanahgfisameRGYDTRVGERGAQ---------LSGGQRQRIALAR 1173
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNLGVPEAEIT----------------RRVDEALTLVDAQhfrhqpiqcLSHGQKKRVAIAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1174 AVLKDARILLLDEATSALDAASERLVQDAVDRML-RGRTCVVVAHRLSTV-EKSDTIAVVKDGRVAERGRHHELLAVGRA 1251
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
366-582 |
1.08e-19 |
|
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: 89.13 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 366 FKDVHFSYPSRPdtlVLNGFNLTISEGA-------------TVglvggsgsgkstvISLLQRFYSPDSGEISmddhgIDT 432
Cdd:cd03235 2 VEDLTVSYGGHP---VLEDVSFEVKPGEflaivgpngagksTL-------------LKAILGLLKPTSGSIR-----VFG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 433 LNVEWLRSQIGLVSQEPVL---FATSIRENIL---------FGDETASLKQVVAAA-KMANAHEFIVKlphgyethvgQF 499
Cdd:cd03235 61 KPLEKERKRIGYVPQRRSIdrdFPISVRDVVLmglyghkglFRRLSKADKAKVDEAlERVGLSELADR----------QI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 500 GtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLSTLRK-ADTIAVLDaGR 577
Cdd:cd03235 131 G-ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLN-RT 208
|
....*
gi 1002260479 578 VVEAG 582
Cdd:cd03235 209 VVASG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
367-579 |
1.10e-19 |
|
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: 88.85 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 367 KDVHFSYpsRPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDdhGIDTLNVEWLRSqIGLVS 446
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN--GKPIKAKERRKS-IGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 447 QEP--VLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYEthvgqfgtqLSGGQKQRIAIARALVRDPRIL 524
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLS---------LSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 525 LLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVV 579
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1020-1245 |
1.12e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.58 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTrPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEP-TLFSGTI-RDNIAYGAAEEHATEDEVARAAALAnahgfISAMERgYDTRVGERGAqLSGGQRQRIALARAVLK 1177
Cdd:PRK13648 87 IVFQNPdNQFVGSIvKYDVAFGLENHAVPYDEMHRRVSEA-----LKQVDM-LERADYEPNA-LSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1178 DARILLLDEATSALDAASERLVQDAVDRMLRGR--TCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHEL 1245
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1037-1240 |
1.32e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.07 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1037 VLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIrSYSLARLRsQVALVSQEPTLFSG-TIRDN 1115
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDR-KVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1116 IAYGAA--------EEHATEDEVAraaalanahgfiSAMERGYDTRVGER-GAQLSGGQRQRIALARAVLKDARILLLDE 1186
Cdd:PRK10851 95 IAFGLTvlprrerpNAAAIKAKVT------------QLLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 1187 ATSALDAAserlVQDAVDRMLRGR------TCVVVAH-RLSTVEKSDTIAVVKDGRVAERG 1240
Cdd:PRK10851 163 PFGALDAQ----VRKELRRWLRQLheelkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1034-1246 |
1.44e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.51 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1034 EVAV---LAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQrGSVLVDGEDIRSYSLARLRSQVA-LVSQEPTLFS 1109
Cdd:COG4138 5 DVAVagrLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDWSAAELARHRAyLSQQQSPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1110 GTIRDNIA-YGAAEEHATEDEvaraaalanahgfiSAMER-----GYDTRVGERGAQLSGGQRQRIALARAVLK------ 1177
Cdd:COG4138 84 MPVFQYLAlHQPAGASSEAVE--------------QLLAQlaealGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptin 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1178 -DARILLLDEATSALDAASerlvQDAVDRMLR-----GRTCVVVAHRLS-TVEKSDTIAVVKDGRVAERGRHHELL 1246
Cdd:COG4138 150 pEGQLLLLDEPMNSLDVAQ----QAALDRLLRelcqqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1035-1247 |
1.63e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 91.18 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1035 VAVLAGFSLEIGAGKTVALVGPSGSGKSTV---IGLIERfydAQRGSVLVDGEDIRSYS---LARLRSQVALVSQEPtlF 1108
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIET---PTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP--Y 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1109 S--------GTIRD-----NIAYGAAEEHATedevaraaalanahgfISAMERgydtRVGERGAQ-------LSGGQRQR 1168
Cdd:PRK11308 103 GslnprkkvGQILEeplliNTSLSAAERREK----------------ALAMMA----KVGLRPEHydryphmFSGGQRQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1169 IALARAVLKDARILLLDEATSALD----AASERLVQDAVDRMlrGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHH 1243
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPVSALDvsvqAQVLNLMMDLQQEL--GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKE 240
|
....
gi 1002260479 1244 ELLA 1247
Cdd:PRK11308 241 QIFN 244
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1036-1238 |
1.73e-19 |
|
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: 89.86 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1036 AVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSY---SLARLRSQVALVSQE-PTLFSG- 1110
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDsPSAVNPr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1111 -TIRDNIayGAAEEHATE-DEVARAAAlanahgfISAMERGYDTR---VGERGAQLSGGQRQRIALARAVLKDARILLLD 1185
Cdd:TIGR02769 105 mTVRQII--GEPLRHLTSlDESEQKAR-------IAELLDMVGLRsedADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1186 EATSALDaaseRLVQDAVDRMLR------GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAE 1238
Cdd:TIGR02769 176 EAVSNLD----MVLQAVILELLRklqqafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1018-1236 |
2.06e-19 |
|
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: 89.91 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1018 GAIEFKNVHFSYpTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQrGSVLVDGEDIRSYSLARLRSQ 1097
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLFSGTIRDNI-AYGaaeeHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVL 1176
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYG----KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1177 KDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRV 1236
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
418-589 |
2.11e-19 |
|
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: 91.33 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDD-------HGIDtLNVEwlRSQIGLVSQEPVLFA-TSIRENILFGdetasLKQVVAAAKMANAHEFIVKLp 489
Cdd:TIGR02142 49 PDEGEIVLNGrtlfdsrKGIF-LPPE--KRRIGYVFQEARLFPhLSVRGNLRYG-----MKRARPSERRISFERVIELL- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 490 hGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLS-TLRK 566
Cdd:TIGR02142 120 -GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERlhAEFGIPILYVSHSLQeVLRL 198
|
170 180
....*....|....*....|...
gi 1002260479 567 ADTIAVLDAGRVVEAGTHDELLG 589
Cdd:TIGR02142 199 ADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
409-588 |
2.28e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 88.66 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 409 ISLLQRFYSPDSGEISMDDHGIDTLNVEwlRSQIGLVSQEPVLFA-TSIRENILFGdETASLK-------QVVAAAKMAN 480
Cdd:COG3840 42 LNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVSMLFQENNLFPhLTVAQNIGLG-LRPGLKltaeqraQVEQALERVG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 481 AHEFIVKLPhgyethvgqfgTQLSGGQKQRIAIARALVRDPRILLLDEATSALD----AESERTVQDALDRAsvGRTTVI 556
Cdd:COG3840 119 LAGLLDRLP-----------GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLM 185
|
170 180 190
....*....|....*....|....*....|...
gi 1002260479 557 VAHRLS-TLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:COG3840 186 VTHDPEdAARIADRVLLVADGRIAADGPTAALL 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1023-1236 |
2.45e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.97 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1023 KNVHFSYPTRpevAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDgedirSYSLARLRSQVALVS 1102
Cdd:PRK11247 16 NAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1103 QEPTLFS-GTIRDNIAYG-------AAEEhatedevaraaalanahgfisAMER-GYDTRVGERGAQLSGGQRQRIALAR 1173
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLGlkgqwrdAALQ---------------------ALAAvGLADRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1174 AVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLS-TVEKSDTIAVVKDGRV 1236
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
364-587 |
2.96e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.04 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSrpDT-LVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQI 442
Cdd:PRK13648 8 IVFKNVSFQYQS--DAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 443 GLVSQEPV-LFATSI-RENILFGDETASL---------KQVVAAAKMANAHEfivklphgYETHvgqfgtQLSGGQKQRI 511
Cdd:PRK13648 86 GIVFQNPDnQFVGSIvKYDVAFGLENHAVpydemhrrvSEALKQVDMLERAD--------YEPN------ALSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 512 AIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVA--HRLSTLRKADTIAVLDAGRVVEAGTHDEL 587
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1037-1247 |
3.88e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.00 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1037 VLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDA-----QRGSVLVDGEDIRSY-SLARLRSQVALVSQEPTLFSG 1110
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1111 TIRDNIAYGA-AEEHATEDEVARAAALANAH-GFISAMErgydTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEAT 1188
Cdd:PRK14271 116 SIMDNVLAGVrAHKLVPRKEFRGVAQARLTEvGLWDAVK----DRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1189 SALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELLA 1247
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1019-1240 |
4.06e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 88.36 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRpevAVLAGFSLEIGAGKTVALVGPSGSGKSTVIG----LIERFYDAQ-RGSVLVDGEDIRSYSL-- 1091
Cdd:PRK14267 4 AIETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNEEARvEGEVRLFGRNIYSPDVdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1092 ARLRSQVALVSQEPTLFSG-TIRDNIAYGA-----AEEHATEDEVARAAALAnahgfiSAMERGYDTRVGERGAQLSGGQ 1165
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPHlTIYDNVAIGVklnglVKSKKELDERVEWALKK------AALWDEVKDRLNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1166 RQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERG 1240
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
420-588 |
4.83e-19 |
|
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: 87.49 E-value: 4.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 420 SGEISMDDHGIDTLNV-EWLRSQIGLVSQEPVLFAT-SIRENILFGDETasLKQVVAAAKMANAHEFIVKLphgyETHVG 497
Cdd:cd03224 54 SGSIRFDGRDITGLPPhERARAGIGYVPEGRRIFPElTVEENLLLGAYA--RRRAKRKARLERVYELFPRL----KERRK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 498 QFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLS-TLRKADTIAVLDA 575
Cdd:cd03224 128 QLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARfALEIADRAYVLER 207
|
170
....*....|...
gi 1002260479 576 GRVVEAGTHDELL 588
Cdd:cd03224 208 GRVVLEGTAAELL 220
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1033-1235 |
5.56e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 91.91 E-value: 5.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1033 PEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFY--DAQRGSVLVDGEDIRSYSLARL-RSQVALVSQEPTLFS 1109
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphGTYEGEIIFEGEELQASNIRDTeRAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1110 G-TIRDNIAYGAAEEHatedevaraaalanaHGFI--SAM---------ERGYDTRVGERGAQLSGGQRQRIALARAVLK 1177
Cdd:PRK13549 96 ElSVLENIFLGNEITP---------------GGIMdyDAMylraqkllaQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1178 DARILLLDEATSALDAASERLVQDAV-DRMLRGRTCVVVAHRLSTVEK-SDTIAVVKDGR 1235
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIrDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1037-1247 |
6.12e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 87.88 E-value: 6.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1037 VLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDI---RSYS-----LARLRSQVALVSQEPTLF 1108
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1109 SG-TIRDNIAYGAAEEHATEDEvaraaalanahgfiSAMERGYD--TRVGERGAQ------LSGGQRQRIALARAVLKDA 1179
Cdd:PRK11264 98 PHrTVLENIIEGPVIVKGEPKE--------------EATARAREllAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 1180 RILLLDEATSALDAaseRLVQDaVDRMLRG-----RTCVVVAHRLSTV-EKSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:PRK11264 164 EVILFDEPTSALDP---ELVGE-VLNTIRQlaqekRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1020-1247 |
8.56e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.12 E-value: 8.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYS-LARLRSQV 1098
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQEP-TLFSG-TIRDNIAYGAAEEHATEDEVARAAALANAhgfisamERGYDTRVGERGAQLSGGQRQRIALARAVL 1176
Cdd:PRK13644 80 GIVFQNPeTQFVGrTVEEDLAFGPENLCLPPIEIRKRVDRALA-------EIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 1177 KDARILLLDEATSALDAASERLVQDAVDRMLR-GRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
367-581 |
9.97e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 86.69 E-value: 9.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 367 KDVHFSYPSRPdtlVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVS 446
Cdd:PRK10247 11 QNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 447 QEPVLFATSIRENILFGDETASlKQVVAAAKMANAHEFivKLPhgyETHVGQFGTQLSGGQKQRIAIARALVRDPRILLL 526
Cdd:PRK10247 88 QTPTLFGDTVYDNLIFPWQIRN-QQPDPAIFLDDLERF--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 527 DEATSALDAESERTVQDALDR-ASVGRTTVI-VAHRLSTLRKADTIAVLD--AGRVVEA 581
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVITLQphAGEMQEA 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1020-1240 |
1.02e-18 |
|
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: 85.66 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSyptRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERF--YDAQRGSVLVDGEDIRSYSLA-RLRS 1096
Cdd:cd03217 1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEeRARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEPTLFSG-TIRDniaygaaeehatedevaraaalanahgFISAMERGydtrvgergaqLSGGQRQRIALARAV 1175
Cdd:cd03217 78 GIFLAFQYPPEIPGvKNAD---------------------------FLRYVNEG-----------FSGGEKKRNEILQLL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 1176 LKDARILLLDEATSALDAASERLVQDAVDRMLR-GRTCVVVAH--RLSTVEKSDTIAVVKDGRVAERG 1240
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1024-1245 |
1.02e-18 |
|
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: 87.99 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1024 NVHFSYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIErfydaqrgsvlvdGEDIRSYSLARLRSQVALVSQ 1103
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLIL-------------GELEPSEGKIKHSGRISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1104 EPTLFSGTIRDNIAYGAAEEHATEDEVARAAALANAhgfISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILL 1183
Cdd:cd03291 106 FSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 1184 LDEATSALDAASERLVQDA-VDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHEL 1245
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1024-1247 |
1.10e-18 |
|
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: 86.44 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1024 NVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSL-ARLRSQVALVS 1102
Cdd:cd03218 5 NLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1103 QEPTLFSG-TIRDNIaYGAAEEHATEDEVARAAALANAHGF-ISAMERgydtrvgERGAQLSGGQRQRIALARAVLKDAR 1180
Cdd:cd03218 82 QEASIFRKlTVEENI-LAVLEIRGLSKKEREEKLEELLEEFhITHLRK-------SKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1181 ILLLDEATSALDAASERLVQDAVDRM-LRGRTCVVVAHRLS-TVEKSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILkDRGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
408-586 |
1.16e-18 |
|
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: 86.72 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 408 VISLLQRFYSPDSGEISMDDHGIDTLNVEwLRSQIGLVS--QEPVLFAT-SIRENILFG-----DETASLKQVVAAAKMA 479
Cdd:cd03219 42 LFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPElTVLENVMVAaqartGSGLLLARARREEREA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 480 N--AHEFI--VKLPHGYETHVGqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSAL-DAESERTVQDALDRASVGRTT 554
Cdd:cd03219 121 RerAEELLerVGLADLADRPAG----ELSYGQQRRLEIARALATDPKLLLLDEPAAGLnPEETEELAELIRELRERGITV 196
|
170 180 190
....*....|....*....|....*....|...
gi 1002260479 555 VIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDE 586
Cdd:cd03219 197 LLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
418-592 |
1.34e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.55 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTLNVEWLRSQIGLVSQEP--VLFATSIRENILFG------DETASLKQVVAAAKMANAHEFIVKLP 489
Cdd:PRK13652 56 PTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 490 HgyethvgqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASV--GRTTVIVAHRLSTLRK- 566
Cdd:PRK13652 136 H-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEm 204
|
170 180
....*....|....*....|....*.
gi 1002260479 567 ADTIAVLDAGRVVEAGTHDELLGMDD 592
Cdd:PRK13652 205 ADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1020-1240 |
1.35e-18 |
|
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: 85.73 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLArlRSQVA 1099
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG-TIRDNIAYGAAE---EHATEDEVARAAalanahgfisamerGYDTRVGERGAQLSGGQRQRIALARAV 1175
Cdd:cd03268 76 ALIEAPGFYPNlTARENLRLLARLlgiRKKRIDEVLDVV--------------GLKDSAKKKVKGFSLGMKQRLGIALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 1176 LKDARILLLDEATSALDAASERLVQDAVdRMLR--GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERG 1240
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRELI-LSLRdqGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
24-295 |
1.37e-18 |
|
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: 87.61 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 24 MALGVLGSFGDGMMQPLSMLVLGDIVNSYGGAGGAgsarsafssGAVDKFALRLLYVAVAVGACSFLEGLCWTRTAERQA 103
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDL---------SLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 104 SKMRRLYLEAVLSQEVAFFDAAPSSpsspqaqaqattfRVISTVSDDADAIQDFLGEKLPMVLANATLFFGALAVSFVFA 183
Cdd:cd07346 72 FDLRRDLFRHLQRLSLSFFDRNRTG-------------DLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 184 WRLALAGLPFTLLLFVTpSVLLAGRMAAAAGEARAAYEEAGGIAQQAVSSIRTVASYTAERRTVERFRGAVARSAALGVR 263
Cdd:cd07346 139 WKLTLVALLLLPLYVLI-LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLR 217
|
250 260 270
....*....|....*....|....*....|...
gi 1002260479 264 QGLIKGAVIGSMGVIYAV-WSFLSWIGSLLVIH 295
Cdd:cd07346 218 AARLSALFSPLIGLLTALgTALVLLYGGYLVLQ 250
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1031-1194 |
1.54e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 85.61 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1031 TRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQ---RGSVLVDGEDIRSysLARLRSQVALVSQEPTL 1107
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTA--LPAEQRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1108 FSG-TIRDNIAYGAAEE---HATEDEVARAAALANAHGFisamergydtrvGERG-AQLSGGQRQRIALARAVLKDARIL 1182
Cdd:COG4136 88 FPHlSVGENLAFALPPTigrAQRRARVEQALEEAGLAGF------------ADRDpATLSGGQRARVALLRALLAEPRAL 155
|
170
....*....|..
gi 1002260479 1183 LLDEATSALDAA 1194
Cdd:COG4136 156 LLDEPFSKLDAA 167
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
502-579 |
1.85e-18 |
|
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: 84.02 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVV 579
Cdd:cd03216 82 QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRlRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1034-1247 |
2.38e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.18 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1034 EVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIR-------------SYSLARLRSQVAL 1100
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1101 VSQEPTLFSG-TIRDNI------AYGAAEEHATEDEVARAAALanahgfisamerGYDTRV-GERGAQLSGGQRQRIALA 1172
Cdd:PRK10619 97 VFQHFNLWSHmTVLENVmeapiqVLGLSKQEARERAVKYLAKV------------GIDERAqGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1173 RAVLKDARILLLDEATSALDAaseRLVQDAVDRMLR----GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELLA 1247
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDP---ELVGEVLRIMQQlaeeGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
386-588 |
2.84e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.55 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 386 NLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDdhGIDTLNV------EWLRSQIGLVSQEPVLFA-TSIRE 458
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID--GVDIAKIsdaelrEVRRKKIAMVFQSFALMPhMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 459 NILFGDETASlkqVVAAAKMANAHEFIVKLphGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESE 538
Cdd:PRK10070 126 NTAFGMELAG---INAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 539 RTVQDALDR--ASVGRTTVIVAHRL-STLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:PRK10070 201 TEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1020-1247 |
3.55e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.44 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVavLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIrSYS---LARLRS 1096
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSrkgLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEP--TLFSGTIRDNIAYGAAEEHATEDEVARAAAlanahgfiSAMERGYDTRVGERGAQ-LSGGQRQRIALAR 1173
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVD--------NALKRTGIEHLKDKPTHcLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 1174 AVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTVE-KSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1037-1245 |
3.76e-18 |
|
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: 91.13 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1037 VLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIErfydaqrgsvlvdGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNI 1116
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM-------------GELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1117 AYGAAEEHATEDEVARAAALANAhgfISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASE 1196
Cdd:TIGR01271 508 IFGLSYDEYRYTSVIKACQLEED---IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1197 R-LVQDAVDRMLRGRTCVVVAHRLSTVEKSDTIAVVKDGRVAERGRHHEL 1245
Cdd:TIGR01271 585 KeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
441-1246 |
3.82e-18 |
|
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: 91.13 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 441 QIGLVSQEPVLFATSIRENILFG---DETaSLKQVVAAAKManaHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARAL 517
Cdd:TIGR01271 488 RISFSPQTSWIMPGTIKDNIIFGlsyDEY-RYTSVIKACQL---EEDIALFPEKDKTVLGEGGITLSGGQRARISLARAV 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 518 VRDPRILLLDEATSALDAESERTV-QDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLG------- 589
Cdd:TIGR01271 564 YKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAkrpdfss 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 590 ----------------------------MDDGGEGGVYARMVHLQ-KAPPVAAREERH-----------RAVDVVESEMV 629
Cdd:TIGR01271 644 lllgleafdnfsaerrnsiltetlrrvsIDGDSTVFSGPETIKQSfKQPPPEFAEKRKqsiilnpiasaRKFSFVQMGPQ 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 630 SFRSVEIMSAVSA-TEHRPSPAPSFCSVEHS-----------TEIGRK------LVDHGV----------ARSRKPSKL- 680
Cdd:TIGR01271 724 KAQATTIEDAVREpSERKFSLVPEDEQGEESlprgnqyhhglQHQAQRrqsvlqLMTHSNrgenrreqlqTSFRKKSSIt 803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 681 --------------RLLK---------MNRPEWKQ------------------------------ALLGCV---GAVVFG 704
Cdd:TIGR01271 804 qqnelaseldiysrRLSKdsvyeiseeINEEDLKEcfaderenvfetttwntylryittnrnlvfVLIFCLvifLAEVAA 883
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 705 AVLPLysYSLGSLPeVYFLADDGQ-------------IRSKTRLYY--FLFLGIAVVCITANIVQHYNFAVMGERLTERV 769
Cdd:TIGR01271 884 SLLGL--WLITDNP-SAPNYVDQQhanasspdvqkpvIITPTSAYYifYIYVGTADSVLALGFFRGLPLVHTLLTVSKRL 960
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 770 RGQMLAKILSFEVGWFdedeNSSAAvcARLATQSSKVRSLVGDRMCL----LVQagataslgfsLALAVSWRLATVMMaM 845
Cdd:TIGR01271 961 HEQMLHSVLQAPMAVL----NTMKA--GRILNRFTKDMAIIDDMLPLtlfdFIQ----------LTLIVLGAIFVVSV-L 1023
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 846 QPLIIASFYFKKVLMAAMSKKAKKAQVQGSQLASEA---VVNHR--------TITAFSSQRRMLRLYEAAQQgpkkdnvA 914
Cdd:TIGR01271 1024 QPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEArspIFSHLitslkglwTIRAFGRQSYFETLFHKALN-------L 1096
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 915 HS--WFSgFCLCLCQFSNTGSMAVALWYGGKLMAKGLITPTHLFQV-----FFMLMTMGRVIADAGSLTSD-LAQGGDAV 986
Cdd:TIGR01271 1097 HTanWFL-YLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVgiiltLAMNILSTLQWAVNSSIDVDgLMRSVSRV 1175
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 987 RSVLDTLDREPTIKDDDNDNERKKKKRKE---------IKGAIEFKNVHFSYpTRPEVAVLAGFSLEIGAGKTVALVGPS 1057
Cdd:TIGR01271 1176 FKFIDLPQEEPRPSGGGGKYQLSTVLVIEnphaqkcwpSGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRT 1254
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1058 GSGKSTVIGLIERFYDAQrGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGTIRDNIaygAAEEHATEDEVARAAALA 1137
Cdd:TIGR01271 1255 GSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEV 1330
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1138 NAHGFISAMERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVAH 1217
Cdd:TIGR01271 1331 GLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEH 1410
|
970 980
....*....|....*....|....*....
gi 1002260479 1218 RLSTVEKSDTIAVVKDGRVAERGRHHELL 1246
Cdd:TIGR01271 1411 RVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
386-587 |
5.80e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 87.58 E-value: 5.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 386 NLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDdhGIDTLNVEWLRSQIGLVSQEPVLFA-TSIRENILFGD 464
Cdd:PRK11607 39 SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD--GVDLSHVPPYQRPINMMFQSYALFPhMTVEQNIAFGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 465 ETASLKQVVAAAKMA------NAHEFIVKLPHgyethvgqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESE 538
Cdd:PRK11607 117 KQDKLPKAEIASRVNemlglvHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 539 RTVQ----DALDRasVGRTTVIVAH-RLSTLRKADTIAVLDAGRVVEAGTHDEL 587
Cdd:PRK11607 186 DRMQlevvDILER--VGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1020-1261 |
6.03e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 85.60 E-value: 6.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYP--TRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYS----LAR 1093
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1094 LRSQVALVSQ--EPTLFSGTIRDNIAYGAAEEHATEDEVARaaalanaHGFISAMERGYDTRVGERGA-QLSGGQRQRIA 1170
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKN-------YAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1171 LARAVLKDARILLLDEATSALDAASERLVQDAVDRML--RGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELLA 1247
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
250
....*....|....*....
gi 1002260479 1248 VGRAGTYYNL-----IKLQ 1261
Cdd:PRK13646 236 DKKKLADWHIglpeiVQLQ 254
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
418-587 |
6.48e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.52 E-value: 6.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDdhGIDTLNVE--W-LRSQIGLVSQEP--VLFATSIRENILFGDETASL------KQVVAAAKMANAHEFIV 486
Cdd:PRK13633 62 PSEGKVYVD--GLDTSDEEnlWdIRNKAGMVFQNPdnQIVATIVEEDVAFGPENLGIppeeirERVDESLKKVGMYEYRR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 487 KLPHgyethvgqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRAS--VGRTTVIVAHRLSTL 564
Cdd:PRK13633 140 HAPH-----------LLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNkkYGITIILITHYMEEA 208
|
170 180
....*....|....*....|...
gi 1002260479 565 RKADTIAVLDAGRVVEAGTHDEL 587
Cdd:PRK13633 209 VEADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
364-582 |
7.07e-18 |
|
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: 83.70 E-value: 7.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPDTlvlngFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMddHGIDTLNVEWLRSQIG 443
Cdd:cd03298 1 VRLDKIRFSYGEQPMH-----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLI--NGVDVTAAPPADRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 444 LVSQEPVLFA-TSIRENILFGDE-----TASLKQVV--AAAKMANAhEFIVKLPHgyethvgqfgtQLSGGQKQRIAIAR 515
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSpglklTAEDRQAIevALARVGLA-GLEKRLPG-----------ELSGGERQRVALAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 516 ALVRDPRILLLDEATSALDAESERTVQDALD--RASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAG 582
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDPALRAEMLDLVLdlHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
364-582 |
7.40e-18 |
|
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: 83.40 E-value: 7.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRpdtLVLNGFNLTISEG------------ATVglvggsgsgkstvISLLQRFYSPDSGEISMDdhGID 431
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGmygllgpngagkTTL-------------MRILATLTPPSSGTIRID--GQD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 432 TL-NVEWLRSQIGLVSQEPVLFAT-SIREnilFGDETASLKQVVAAAKMANAHEFIVKLphGYETHVGQFGTQLSGGQKQ 509
Cdd:cd03264 63 VLkQPQKLRRRIGYLPQEFGVYPNfTVRE---FLDYIAWLKGIPSKEVKARVDEVLELV--NLGDRAKKKIGSLSGGMRR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 510 RIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAG 582
Cdd:cd03264 138 RVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
439-576 |
7.55e-18 |
|
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: 83.92 E-value: 7.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 439 RSQIGLVSQEPVLFATSIRENILFGD--ETASLKQVVAAAKManaHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARA 516
Cdd:cd03290 78 RYSVAYAAQKPWLLNATVEENITFGSpfNKQRYKAVTDACSL---QPDIDLLPFGDQTEIGERGINLSGGQRQRICVARA 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 517 LVRDPRILLLDEATSALDAE-SERTVQDALDR--ASVGRTTVIVAHRLSTLRKADTIAVLDAG 576
Cdd:cd03290 155 LYQNTNIVFLDDPFSALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
416-587 |
7.97e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.15 E-value: 7.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 416 YSPDSGEISMDDHGIDTLNV-EWLRSQIGLVSQEPVLFAT-SIRENILFGDETASLKqVVAAAKM-ANAHEFIVKLphGY 492
Cdd:COG1129 54 YQPDSGEILLDGEPVRFRSPrDAQAAGIAIIHQELNLVPNlSVAENIFLGREPRRGG-LIDWRAMrRRARELLARL--GL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 493 ETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSAL-DAESER---TVQDALDRasvGRTTVIVAHRLSTLRK-A 567
Cdd:COG1129 131 DIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLtEREVERlfrIIRRLKAQ---GVAIIYISHRLDEVFEiA 207
|
170 180
....*....|....*....|....*
gi 1002260479 568 DTIAVLDAGRVVEAG-----THDEL 587
Cdd:COG1129 208 DRVTVLRDGRLVGTGpvaelTEDEL 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
409-587 |
8.46e-18 |
|
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: 83.71 E-value: 8.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 409 ISLLQRFYSPDSGEISMDDHGIDTlNVEWLRSQIGLVSQEPVLFAT-SIRENILFgdeTASLKQVVAAAKMANAHEFI-- 485
Cdd:cd03263 45 LKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDElTVREHLRF---YARLKGLPKSEIKEEVELLLrv 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 486 VKLPHGYETHVGQfgtqLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAH------ 559
Cdd:cd03263 121 LGLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHsmdeae 196
|
170 180
....*....|....*....|....*...
gi 1002260479 560 RLstlrkADTIAVLDAGRVVEAGTHDEL 587
Cdd:cd03263 197 AL-----CDRIAIMSDGKLRCIGSPQEL 219
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1021-1240 |
9.07e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 84.35 E-value: 9.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1021 EFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKST---VIGLIERfYDAQRGSVLVDGEDIRSYSL-ARLRS 1096
Cdd:COG0396 2 EIKNLHVSVEGKE---ILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLMGHPK-YEVTSGSILLDGEDILELSPdERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEPTLFSG-TIRD--NIAYGAAEEHAtedevaraaalanahgfISAME-----RGYDTRVG------ERG--AQ 1160
Cdd:COG0396 78 GIFLAFQYPVEIPGvSVSNflRTALNARRGEE-----------------LSAREflkllKEKMKELGldedflDRYvnEG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1161 LSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR-GRTCVVVAH--RLSTVEKSDTIAVVKDGRVA 1237
Cdd:COG0396 141 FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIV 220
|
...
gi 1002260479 1238 ERG 1240
Cdd:COG0396 221 KSG 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
413-582 |
9.31e-18 |
|
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: 82.98 E-value: 9.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 413 QRFYSPDSGEISMDDHGIDTlnvEWLRSQIGLVSQEPVLFAT-SIRENILFgdeTASLKQvvaaakmanahefivklphg 491
Cdd:cd03213 58 RRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILHPTlTVRETLMF---AAKLRG-------------------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 492 yethvgqfgtqLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLSTL--RKAD 568
Cdd:cd03213 112 -----------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSEifELFD 180
|
170
....*....|....
gi 1002260479 569 TIAVLDAGRVVEAG 582
Cdd:cd03213 181 KLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
363-587 |
9.44e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.07 E-value: 9.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 363 EIVFKDVHFSY-PSRP-DTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGI----DTLNVE 436
Cdd:PRK13634 2 DITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 437 WLRSQIGLVSQ--EPVLFATSIRENILFGDETASLKQVVAAAKmanAHEFI--VKLPHGYETHvGQFgtQLSGGQKQRIA 512
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQK---AREMIelVGLPEELLAR-SPF--ELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 513 IARALVRDPRILLLDEATSALDAESERTVQD---ALDRASvGRTTVIVAHRLS-TLRKADTIAVLDAGRVVEAGTHDEL 587
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHKEK-GLTTVLVTHSMEdAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
367-587 |
9.47e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 84.74 E-value: 9.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 367 KDVHFSYPSrpDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWL--RSQIGL 444
Cdd:PRK13639 5 RDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 445 VSQEP--VLFATSIRENILFG--------DETAslKQVVAAAKMANAHEFIVKLPHgyethvgqfgtQLSGGQKQRIAIA 514
Cdd:PRK13639 83 VFQNPddQLFAPTVEEDVAFGplnlglskEEVE--KRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 515 RALVRDPRILLLDEATSALDAESERTVQDAL-DRASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDEL 587
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
417-575 |
1.08e-17 |
|
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: 82.91 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 417 SPDSGEISMDDHGIDTLNVEWlRSQIGLVSQEPVLFAT-SIRENILFgdeTASLKQVVAAAKMANAHEFIVKLPHgyetH 495
Cdd:COG4133 53 PPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKPElTVRENLRF---WAALYGLRADREAIDEALEAVGLAG----L 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 496 VGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVA-HRLSTLRKADTIAVLD 574
Cdd:COG4133 125 ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDLGD 204
|
.
gi 1002260479 575 A 575
Cdd:COG4133 205 F 205
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
420-582 |
1.27e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.06 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 420 SGEISMDDHGI-----DTLNvewLRSQIGLVSQEPVLFATSIRENILFG------DETASLKQVVAAAKMANAHEFIVKl 488
Cdd:PRK14239 64 TGSIVYNGHNIysprtDTVD---LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEAVEKSLKGASIWDEVK- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 489 PHGYETHVGqfgtqLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTL-RKA 567
Cdd:PRK14239 140 DRLHDSALG-----LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRIS 214
|
170
....*....|....*
gi 1002260479 568 DTIAVLDAGRVVEAG 582
Cdd:PRK14239 215 DRTGFFLDGDLIEYN 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
434-583 |
1.32e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.29 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 434 NVEWLRSQIGLVSQEP--VLFATSIRENILFGDETASLKQVVAAAKmanAHEFIVKLPHGYE-THVGQFGtqLSGGQKQR 510
Cdd:PRK13631 110 NFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKL---AKFYLNKMGLDDSyLERSPFG--LSGGQKRR 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 511 IAIARALVRDPRILLLDEATSALDAESER-TVQDALDRASVGRTTVIVAHRL-STLRKADTIAVLDAGRVVEAGT 583
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGT 259
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1019-1247 |
1.89e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.86 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPtrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSlARLRSQV 1098
Cdd:PRK13537 7 PIDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQEPTL---FsgTIRDNIA----YGAAEEHATEDEVARAAAlanahgfISAMERGYDTRVGErgaqLSGGQRQRIAL 1171
Cdd:PRK13537 83 GVVPQFDNLdpdF--TVRENLLvfgrYFGLSAAAARALVPPLLE-------FAKLENKADAKVGE----LSGGMKRRLTL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 1172 ARAVLKDARILLLDEATSALDAASERLVQDAVDRML-RGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELLA 1247
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1019-1193 |
1.97e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.60 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARlrsqv 1098
Cdd:PRK11248 1 MLQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQEPTLFS-GTIRDNIAYG---AAEEHATEDEVARAAALanahgfisamergydtRVGERGA------QLSGGQRQR 1168
Cdd:PRK11248 73 GVVFQNEGLLPwRNVQDNVAFGlqlAGVEKMQRLEIAHQMLK----------------KVGLEGAekryiwQLSGGQRQR 136
|
170 180
....*....|....*....|....*
gi 1002260479 1169 IALARAVLKDARILLLDEATSALDA 1193
Cdd:PRK11248 137 VGIARALAANPQLLLLDEPFGALDA 161
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1020-1224 |
2.10e-17 |
|
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: 81.05 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVhfSYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGedirsyslarlRSQVA 1099
Cdd:cd03223 1 IELENL--SLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSGTIRDNIAYgaaeehaTEDEVaraaalanahgfisamergydtrvgergaqLSGGQRQRIALARAVLKDA 1179
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-------PWDDV------------------------------LSGGEQQRLAFARLLLHKP 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002260479 1180 RILLLDEATSALDAASErlvqDAVDRMLRGR--TCVVVAHRlSTVEK 1224
Cdd:cd03223 111 KFVFLDEATSALDEESE----DRLYQLLKELgiTVISVGHR-PSLWK 152
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1021-1247 |
2.48e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.89 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1021 EFKNVHFSYPTrpeVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRsYSLAR--LRSQV 1098
Cdd:PRK11288 6 SFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR-FASTTaaLAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQE----PTLfsgTIRDNIAYGAAEEhatedevaraaalanAHGFIS-------AMER----GYDTRVGERGAQLSG 1163
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGQLPH---------------KGGIVNrrllnyeAREQlehlGVDIDPDTPLKYLSI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1164 GQRQRIALARAVLKDARILLLDEATSALDA-ASERLVqdAVDRMLR--GRTCVVVAHRLSTV-EKSDTIAVVKDGRVAer 1239
Cdd:PRK11288 144 GQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLF--RVIRELRaeGRVILYVSHRMEEIfALCDAITVFKDGRYV-- 219
|
....*...
gi 1002260479 1240 gRHHELLA 1247
Cdd:PRK11288 220 -ATFDDMA 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
364-592 |
2.62e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.63 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIG 443
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 444 LVSQEP--VLFATSIRENILFGDETASL------KQVVAAAKMANAHEFIVKLPhgyethvgqfgTQLSGGQKQRIAIAR 515
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIpheemkERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 516 ALVRDPRILLLDEATSALDAESE----RTVQDAldRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDEL---- 587
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRleliKTIKGI--RDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELfsrg 231
|
250
....*....|
gi 1002260479 588 -----LGMDD 592
Cdd:PRK13650 232 ndllqLGLDI 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
418-588 |
3.02e-17 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 86.66 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTLNVEW---LRSQIGLVSQEPvlFAT-----SIRENILFG--------DETASLKQVVAA------ 475
Cdd:COG4172 337 PSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhgpglSAAERRARVAEAleevgl 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 476 -AKMAN--AHEFivklphgyethvgqfgtqlSGGQKQRIAIARALVRDPRILLLDEATSALDaeseRTVQ----DALDR- 547
Cdd:COG4172 415 dPAARHryPHEF-------------------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaqilDLLRDl 471
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1002260479 548 -ASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDELL 588
Cdd:COG4172 472 qREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVF 514
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1019-1240 |
3.37e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 82.37 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGE------DIRSYSLA 1092
Cdd:COG4161 2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1093 RLRSQVALVSQE----PTLfsgTIRDNI------AYGAAEEHATEdevaraaalanahgfiSAMERGYDTRVGERG---- 1158
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLieapckVLGLSKEQARE----------------KAMKLLARLRLTDKAdrfp 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1159 AQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR-GRTCVVVAHRLSTVEKSDT-IAVVKDGRV 1236
Cdd:COG4161 140 LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASqVVYMEKGRI 219
|
....
gi 1002260479 1237 AERG 1240
Cdd:COG4161 220 IEQG 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
418-586 |
3.94e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 83.17 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGI--DTLNVEWLRSQIGLVSQEP--VLFATSIRENILFGDETASL------KQVVAAAKManahefiVK 487
Cdd:PRK13637 59 PTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIEKDIAFGPINLGLseeeieNRVKRAMNI-------VG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 488 LPhgYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAeseRTVQDALDRAS-----VGRTTVIVAHRLS 562
Cdd:PRK13637 132 LD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP---KGRDEILNKIKelhkeYNMTIILVSHSME 206
|
170 180
....*....|....*....|....*
gi 1002260479 563 TLRK-ADTIAVLDAGRVVEAGTHDE 586
Cdd:PRK13637 207 DVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1021-1245 |
3.98e-17 |
|
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: 81.80 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1021 EFKNVHFSYPtrpEVAVLAGFSLEIGAGKTVALVGPSGSGKST----VIGLIerfyDAQRGSVLVDGEDI-RSYSLARLR 1095
Cdd:TIGR03410 2 EVSNLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTllktLMGLL----PVKSGSIRLDGEDItKLPPHERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1096 SQVALVSQEPTLFSG-TIRDNIAYGAA----EEHATEDEVARAaalanahgF--ISAMergydtrVGERGAQLSGGQRQR 1168
Cdd:TIGR03410 75 AGIAYVPQGREIFPRlTVEENLLTGLAalprRSRKIPDEIYEL--------FpvLKEM-------LGRRGGDLSGGQQQQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1169 IALARAVLKDARILLLDEATSALDAASERLVQDAVDRM--LRGRTCVVVAHRLS-TVEKSDTIAVVKDGRVAERGRHHEL 1245
Cdd:TIGR03410 140 LAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1020-1245 |
4.20e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.89 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARL---RS 1096
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEPTLFSG-TIRDNIAYGAAEEHATEDEVARAAALANAHGfisamergydtrVGERGA------QLSGGQRQRI 1169
Cdd:PRK11831 85 RMSMLFQSGALFTDmNVFDNVAYPLREHTQLPAPLLHSTVMMKLEA------------VGLRGAaklmpsELSGGMARRA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1170 ALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTV-EKSDTIAVVKDGRVAERGRHHEL 1245
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVlSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
712-951 |
4.32e-17 |
|
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: 83.33 E-value: 4.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 712 YSLGSLPEVYFLADDGQIRSKTRLYYFLF--LGIAVVCITANIVQHYNFAVMGERLTERVRGQMLAKILSFEVGWFDEde 789
Cdd:cd18573 17 FAIGKLIDVASKESGDIEIFGLSLKTFALalLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDK-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 790 NSSAAVCARLATQSSKVRSLVGDRMCLLVQAGATASLGFSLALAVSWRLATVMMAMQPLI--IASFYFKKVlmaamskKA 867
Cdd:cd18573 95 NKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIavGAVFYGRYV-------RK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 868 KKAQVQGS-----QLASEAVVNHRTITAFSSQRRMLRLY----EAAQQGPKKDNVAHSWFSGFclclCQFSNTGSMAVAL 938
Cdd:cd18573 168 LSKQVQDAladatKVAEERLSNIRTVRAFAAERKEVERYakkvDEVFDLAKKEALASGLFFGS----TGFSGNLSLLSVL 243
|
250
....*....|...
gi 1002260479 939 WYGGKLMAKGLIT 951
Cdd:cd18573 244 YYGGSLVASGELT 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1035-1235 |
4.50e-17 |
|
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: 86.03 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1035 VAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFY--DAQRGSVLVDGEDIRSYSLARL-RSQVALVSQEPTLFSG- 1110
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPEl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1111 TIRDNIAYGAAEEH----ATEDEVARAAALANAHGFISAMErgyDTR-VGERGaqlsGGQRQRIALARAVLKDARILLLD 1185
Cdd:TIGR02633 94 SVAENIFLGNEITLpggrMAYNAMYLRAKNLLRELQLDADN---VTRpVGDYG----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 1186 EATSALDAASERLVQDAV-DRMLRGRTCVVVAHRLSTVEK-SDTIAVVKDGR 1235
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIrDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
411-587 |
4.65e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 84.01 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 411 LLQRFYSPDSGEISMDDHGIDTLNVE---WLRSQIGLVSQEPvlFA---------TSIRENIL-FGDETAslkqvvaAAK 477
Cdd:COG4608 63 LLLRLEEPTSGEILFDGQDITGLSGRelrPLRRRMQMVFQDP--YAslnprmtvgDIIAEPLRiHGLASK-------AER 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 478 MANAHEFI--VKLPhgyETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAeserTVQdaldrASV----- 550
Cdd:COG4608 134 RERVAELLelVGLR---PEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDV----SIQ-----AQVlnlle 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1002260479 551 ------GRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDEL 587
Cdd:COG4608 202 dlqdelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1020-1247 |
4.99e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 83.60 E-value: 4.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSY----PTrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVI-----------GLIERFYDAQR-------- 1076
Cdd:PRK13651 3 IKVKNIVKIFnkklPT--ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIehlnalllpdtGTIEWIFKDEKnkkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1077 GSVLVDGEDIRSYS-----LARLRSQVALVSQ--EPTLFSGTIRDNIAYGAAEEHATEDEvaraaalanahgfisAMERG 1149
Cdd:PRK13651 81 EKVLEKLVIQKTRFkkikkIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEE---------------AKKRA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1150 --YDTRVG------ERGA-QLSGGQRQRIALARAVLKDARILLLDEATSALDAAserlvqdAVDRML--------RGRTC 1212
Cdd:PRK13651 146 akYIELVGldesylQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQ-------GVKEILeifdnlnkQGKTI 218
|
250 260 270
....*....|....*....|....*....|....*.
gi 1002260479 1213 VVVAHRLSTV-EKSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:PRK13651 219 ILVTHDLDNVlEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1040-1245 |
5.41e-17 |
|
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: 81.26 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1040 GFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSlARLRSQVALVSQEPTLFSG-TIRDNIA- 1117
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIVFQDLSVDDElTGWENLYi 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1118 ----YGAAEEHATE--DEVARaaalanahgFISAMERGyDTRVGergaQLSGGQRQRIALARAVLKDARILLLDEATSAL 1191
Cdd:cd03265 97 harlYGVPGAERREriDELLD---------FVGLLEAA-DRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 1192 DAASERLVQDAVDRMLR--GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHEL 1245
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
362-587 |
9.41e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 86.37 E-value: 9.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 362 GEIVFKDVHFSY----PsrpdtLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEW 437
Cdd:PTZ00243 1307 GSLVFEGVQMRYreglP-----LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 438 LRSQIGLVSQEPVLFATSIRENILFGDEtASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARAL 517
Cdd:PTZ00243 1382 LRRQFSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARAL 1460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 518 V-RDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDEL 587
Cdd:PTZ00243 1461 LkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1019-1243 |
1.16e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 80.83 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRpevAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDG------EDIRSYSLA 1092
Cdd:PRK11124 2 SIQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1093 RLRSQVALVSQEPTLFSG-TIRDNI------AYGAAEEHATEDevaraaalanahgfisAMERGYDTRVGERGA----QL 1161
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHlTVQQNLieapcrVLGLSKDQALAR----------------AEKLLERLRLKPYADrfplHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1162 SGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVdRMLR--GRTCVVVAHRLSTVEKSDTIAV-VKDGRVAE 1238
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSII-RELAetGITQVIVTHEVEVARKTASRVVyMENGHIVE 221
|
....*
gi 1002260479 1239 RGRHH 1243
Cdd:PRK11124 222 QGDAS 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1020-1240 |
1.29e-16 |
|
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: 80.27 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPT-------------------RPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVL 1080
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1081 VDGedirsyslaRLRSQVAL-VSQEPTLfsgTIRDNIAYGA-------AEEHATEDEVaraaalanaHGFiSAMERGYDT 1152
Cdd:cd03220 81 VRG---------RVSSLLGLgGGFNPEL---TGRENIYLNGrllglsrKEIDEKIDEI---------IEF-SELGDFIDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1153 RVGErgaqLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRML-RGRTCVVVAHRLSTVEK-SDTIAV 1230
Cdd:cd03220 139 PVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLkQGKTVILVSHDPSSIKRlCDRALV 214
|
250
....*....|
gi 1002260479 1231 VKDGRVAERG 1240
Cdd:cd03220 215 LEKGKIRFDG 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
364-588 |
1.29e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.57 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSrpDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMddHGIDTLN---VEWLRS 440
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV--SGIDTGDfskLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 441 QIGLVSQEP--VLFATSIRENILFGDETASLKQVVAAAKMANAHEFIvklphGYETHVGQFGTQLSGGQKQRIAIARALV 518
Cdd:PRK13644 78 LVGIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEI-----GLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 519 RDPRILLLDEATSALDAESERTVQDALDRA-SVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1020-1245 |
1.39e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 81.39 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYptRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVA 1099
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEP--TLFSGTIRDNIAYGAAEEHATEDEVAraaalanaHGFISAME----RGYDTRVGErgaQLSGGQRQRIALAR 1173
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVA--------HRVSSALHmlglEELRDRVPH---HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 1174 AVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTV-EKSDTIAVVKDGRVAERGRHHEL 1245
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1037-1247 |
1.42e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.37 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1037 VLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQ-----RGSVLVDGEDIRSYSLARLR----SQVALVSQEPtL 1107
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEP-M 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1108 FSGTIRDNIAYGAAE---------EHATEDEVaraaalanahgfISAMErgydtRVGERGA---------QLSGGQRQRI 1169
Cdd:PRK15134 103 VSLNPLHTLEKQLYEvlslhrgmrREAARGEI------------LNCLD-----RVGIRQAakrltdyphQLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1170 ALARAVLKDARILLLDEATSALDAAserlVQDAVDRMLR------GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRH 1242
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVS----VQAQILQLLRelqqelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRA 241
|
....*
gi 1002260479 1243 HELLA 1247
Cdd:PRK15134 242 ATLFS 246
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1031-1238 |
1.46e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.27 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1031 TRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLAR---LRSQVALVSQEPtl 1107
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkaFRRDIQMVFQDS-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1108 FSG-----TIRDNIA--------YGAAEEHATEDEVaraaalanahgfISAMERGyDTRVGERGAQLSGGQRQRIALARA 1174
Cdd:PRK10419 99 ISAvnprkTVREIIReplrhllsLDKAERLARASEM------------LRAVDLD-DSVLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 1175 VLKDARILLLDEATSALDaaseRLVQDAVDRML------RGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAE 1238
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLD----LVLQAGVIRLLkklqqqFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1038-1257 |
1.82e-16 |
|
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: 80.20 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1038 LAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLrsqvaLVSQEPTLFSG-TIRDNI 1116
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1117 AYG--AAEEHATEDEvarAAALANAHGFISAMERGYDTRVGergaQLSGGQRQRIALARAVLKDARILLLDEATSALDAA 1194
Cdd:TIGR01184 76 ALAvdRVLPDLSKSE---RRAIVEEHIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 1195 SERLVQDAVDRMLR--GRTCVVVAHRL-STVEKSDTIAVVKDGRVAERG--------RHHELLAVGRAGTYYNL 1257
Cdd:TIGR01184 149 TRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIGqilevpfpRPRDRLEVVEDPSYYDL 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
362-588 |
2.25e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.21 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 362 GEIVFKDVHFSYPSRP--DTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGI-----DTLN 434
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 435 VEWLRSQIGLVSQEP--VLFATSIRENILFG------DETASLKQVVAAAKManahefiVKLPHGYethVGQFGTQLSGG 506
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpvnlgeNKQEAYKKVPELLKL-------VQLPEDY---VKRSPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 507 QKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRL-STLRKADTIAVLDAGRVVEAGT 583
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
....*
gi 1002260479 584 HDELL 588
Cdd:PRK13645 235 PFEIF 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
371-592 |
2.36e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.91 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 371 FSYPSRPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEP- 449
Cdd:PRK13642 12 FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 450 -VLFATSIRENILFGDETAS------LKQVVAAAKMANAHEFIVKLPhgyethvgqfgTQLSGGQKQRIAIARALVRDPR 522
Cdd:PRK13642 92 nQFVGATVEDDVAFGMENQGipreemIKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 523 ILLLDEATSALD----AESERTVQDALDRASVgrTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDELLGMDD 592
Cdd:PRK13642 161 IIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
364-535 |
2.37e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 80.29 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYP-SRPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEwlRsqi 442
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 443 GLVSQEPVLFA-TSIRENILFGdetASLKQVVAAAKMANAHEFI--VKLpHGYETHvgqFGTQLSGGQKQRIAIARALVR 519
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFG---LRLRGVPKAERRARAEELLalVGL-ADFARR---RIWQLSGGMRQRVGIARALAA 151
|
170
....*....|....*.
gi 1002260479 520 DPRILLLDEATSALDA 535
Cdd:COG4525 152 DPRFLLMDEPFGALDA 167
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1019-1255 |
2.42e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.31 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPtrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRsyslARLRSQV 1098
Cdd:COG4152 1 MLELKGLTKRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQEPTLFSG-TIRDNIAY---------GAAEEHATEdevaraaalanahgfisAMER----GY-DTRVGErgaqLSG 1163
Cdd:COG4152 74 GYLPEERGLYPKmKVGEQLVYlarlkglskAEAKRRADE-----------------WLERlglgDRaNKKVEE----LSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1164 GQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAV-DRMLRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGR 1241
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIrELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
|
250
....*....|....
gi 1002260479 1242 HHELLAVGRAGTYY 1255
Cdd:COG4152 213 VDEIRRQFGRNTLR 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
417-582 |
2.75e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.84 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 417 SPDSGEISMDDHG-IDTLNVEWL---RSQIGLVSQEPVLFA-TSIRENILFGdetaslkqvvAAAKMANAHEFIVKLpHG 491
Cdd:PRK11144 49 RPQKGRIVLNGRVlFDAEKGICLppeKRRIGYVFQDARLFPhYKVRGNLRYG----------MAKSMVAQFDKIVAL-LG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 492 YETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRAS--VGRTTVIVAHRL-STLRKAD 568
Cdd:PRK11144 118 IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAreINIPILYVSHSLdEILRLAD 197
|
170
....*....|....
gi 1002260479 569 TIAVLDAGRVVEAG 582
Cdd:PRK11144 198 RVVVLEQGKVKAFG 211
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
730-981 |
3.04e-16 |
|
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: 80.76 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 730 RSKTRLYYFLFLGIAVVCITANIVQHYNFAVMGERLTERVRGQMLAKILSFEVGWFdeDENSSAAVCARLATQSSKVRSL 809
Cdd:cd18780 38 LRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFF--DVTRTGELLNRLSSDTQVLQNA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 810 VGDRMCLLVQAGATASLGFSLALAVSWRLATVMMAMQPLIIASF--YFKKVlmAAMSKKAKKAQVQGSQLASEAVVNHRT 887
Cdd:cd18780 116 VTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAviYGKYV--RKLSKKFQDALAAASTVAEESISNIRT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 888 ITAFSSQRRMLRLYEAAQQGP----KKDNVAHSWFSGFclclCQFSNTGSMAVALWYGGKLMAKGLITPTHLFQvfFMLM 963
Cdd:cd18780 194 VRSFAKETKEVSRYSEKINESyllgKKLARASGGFNGF----MGAAAQLAIVLVLWYGGRLVIDGELTTGLLTS--FLLY 267
|
250 260
....*....|....*....|
gi 1002260479 964 TM--GRVIADAGSLTSDLAQ 981
Cdd:cd18780 268 TLtvAMSFAFLSSLYGDFMQ 287
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1020-1238 |
3.89e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.19 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVdGEDIRsyslarlrsqVA 1099
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSG--TIRDNIAYGAaeEHATEDEVaraaalanahgfisameRGY-----------DTRVGErgaqLSGGQR 1166
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRDGA--PGGTEQEV-----------------RGYlgrflfsgddaFKPVGV----LSGGEK 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 1167 QRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRmLRGrTCVVVAH-R--LSTVekSDTIAVVKDGRVAE 1238
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-FPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1036-1236 |
6.41e-16 |
|
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: 77.09 E-value: 6.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1036 AVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYS-LARLRSQVALVSQEPT---LFSG- 1110
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPEDRKregLVLDl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1111 TIRDNIAYGAaeehatedevaraaalanahgfisamergydtrvgergaQLSGGQRQRIALARAVLKDARILLLDEATSA 1190
Cdd:cd03215 94 SVAENIALSS---------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 1191 LDAASERLVQDAVDRMLRGRTCVVVahrLST-----VEKSDTIAVVKDGRV 1236
Cdd:cd03215 135 VDVGAKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1031-1216 |
7.62e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.61 E-value: 7.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1031 TRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRsysLARLRSQVALVSQ----EPT 1106
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEACHYLGHrnamKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1107 LfsgTIRDNIA-----YGAAEEHATEDevaraaalanahgfISAMERGydtRVGERGAQ-LSGGQRQRIALARAVLKDAR 1180
Cdd:PRK13539 88 L---TVAENLEfwaafLGGEELDIAAA--------------LEAVGLA---PLAHLPFGyLSAGQKRRVALARLLVSNRP 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002260479 1181 ILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVA 1216
Cdd:PRK13539 148 IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
415-586 |
7.67e-16 |
|
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: 78.93 E-value: 7.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 415 FYSPDSGEISMDDHGIDTLNVeWLRSQIGLVS--QEPVLFAT-SIRENIL----------FGDETASLKQVVAAAKMAN- 480
Cdd:COG0411 53 FYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFPElTVLENVLvaaharlgrgLLAALLRLPRARREEREARe 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 481 -AHEFIVKLphGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSAL-DAESERTVQ--DALdRASVGRTTVI 556
Cdd:COG0411 132 rAEELLERV--GLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLnPEETEELAEliRRL-RDERGITILL 208
|
170 180 190
....*....|....*....|....*....|.
gi 1002260479 557 VAHRLSTLRK-ADTIAVLDAGRVVEAGTHDE 586
Cdd:COG0411 209 IEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
441-587 |
8.66e-16 |
|
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: 79.13 E-value: 8.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 441 QIGLVSQEPVLFATSIRENILFG---DETaSLKQVVAAAKManaHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARAL 517
Cdd:cd03291 99 RISFSSQFSWIMPGTIKENIIFGvsyDEY-RYKSVVKACQL---EEDITKFPEKDNTVLGEGGITLSGGQRARISLARAV 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 518 VRDPRILLLDEATSALDAESERTVQDA-LDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTHDEL 587
Cdd:cd03291 175 YKDADLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1023-1186 |
8.72e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.15 E-value: 8.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1023 KNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKST----VIGLIErfydAQRGSVLVDGEDIRSYSL-ARLRSQ 1097
Cdd:COG1137 7 ENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDITHLPMhKRARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQEPTLFSG-TIRDNIaYGAAEEHatedevaraaalanahgFISAMERgyDTRVGE-------------RGAQLSG 1163
Cdd:COG1137 80 IGYLPQEASIFRKlTVEDNI-LAVLELR-----------------KLSKKER--EERLEElleefgithlrksKAYSLSG 139
|
170 180
....*....|....*....|...
gi 1002260479 1164 GQRQRIALARAVLKDARILLLDE 1186
Cdd:COG1137 140 GERRRVEIARALATNPKFILLDE 162
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
438-588 |
9.48e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.55 E-value: 9.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 438 LRSQIGLVSQEPVLFA-TSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARA 516
Cdd:PRK14246 88 LRKEVGMVFQQPNPFPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARA 167
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 517 LVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHR-LSTLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1019-1251 |
1.13e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.61 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPtrpevAVLA--GFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGE--DIRSYSLARl 1094
Cdd:COG3845 5 ALELRGITKRFG-----GVVAndDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1095 RSQVALVSQEPTLFSG-TIRDNIAYGAaeehatEDEVARAAALANAHGFISAMERGY------DTRVGergaQLSGGQRQ 1167
Cdd:COG3845 79 ALGIGMVHQHFMLVPNlTVAENIVLGL------EPTKGGRLDRKAARARIRELSERYgldvdpDAKVE----DLSVGEQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1168 RIALARAVLKDARILLLDEATSAL-DAASERLVqdAVDRMLR--GRTCVVVAHRLSTV-EKSDTIAVVKDGRVAERGR-- 1241
Cdd:COG3845 149 RVEILKALYRGARILILDEPTAVLtPQEADELF--EILRRLAaeGKSIIFITHKLREVmAIADRVTVLRRGKVVGTVDta 226
|
250
....*....|....*
gi 1002260479 1242 ---HHEL--LAVGRA 1251
Cdd:COG3845 227 etsEEELaeLMVGRE 241
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
367-588 |
1.25e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.74 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 367 KDVHFSYPSrpDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGID--TLNVEWLRSQIGL 444
Cdd:PRK13636 9 EELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysRKGLMKLRESVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 445 VSQEP--VLFATSIRENILFGDETASL--KQVVAAAKMANAHEFIVKLPHGyETHVgqfgtqLSGGQKQRIAIARALVRD 520
Cdd:PRK13636 87 VFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-PTHC------LSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 521 PRILLLDEATSALD----AESERTVQDALDraSVGRTTVIVAHRLSTLR-KADTIAVLDAGRVVEAGTHDELL 588
Cdd:PRK13636 160 PKVLVLDEPTAGLDpmgvSEIMKLLVEMQK--ELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
503-566 |
1.27e-15 |
|
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: 75.65 E-value: 1.27e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 503 LSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASvgrTTVI-VAHRlSTLRK 566
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG---ITVIsVGHR-PSLWK 152
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
410-589 |
1.27e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 78.67 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 410 SLLQRF---YSPDSGEISMDD----HGIDTLNVEWLRSQIGLVSQ--EPVLFATSIRENILFGDET--ASLKQVvaaakM 478
Cdd:PRK13646 48 TLIQNInalLKPTTGTVTVDDititHKTKDKYIRPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNfkMNLDEV-----K 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 479 ANAHEFIVKLphGYETHVGQFGT-QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASV--GRTTV 555
Cdd:PRK13646 123 NYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTII 200
|
170 180 190
....*....|....*....|....*....|....*
gi 1002260479 556 IVAHRLSTL-RKADTIAVLDAGRVVEAGTHDELLG 589
Cdd:PRK13646 201 LVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
420-587 |
1.42e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 79.74 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 420 SGEISMddHGIDTLNVEWLRSQIGLVSQEPVLFA-TSIRENILFG---------DETASLKQVVAAA-KManahefiVKL 488
Cdd:PRK10851 56 SGHIRF--HGTDVSRLHARDRKVGFVFQHYALFRhMTVFDNIAFGltvlprrerPNAAAIKAKVTQLlEM-------VQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 489 PHGYEthvgQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAEsertVQDALDR------ASVGRTTVIVAH-RL 561
Cdd:PRK10851 127 AHLAD----RYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ----VRKELRRwlrqlhEELKFTSVFVTHdQE 198
|
170 180
....*....|....*....|....*.
gi 1002260479 562 STLRKADTIAVLDAGRVVEAGTHDEL 587
Cdd:PRK10851 199 EAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
67-295 |
1.80e-15 |
|
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: 78.35 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 67 SGAVDKFA---LRLLYVAVAVGACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDAApsspsspqaqaqaTTFRV 143
Cdd:cd18572 29 DGSREAFYravLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDAT-------------KTGEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 144 ISTVSDDADAIQDFLGEKLPMVLANATLFFGALAVSFVFAWRLALAGLpFTLLLFVTPSVLLAGRMAAAAGEARAAYEEA 223
Cdd:cd18572 96 TSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAF-ITVPVIALITKVYGRYYRKLSKEIQDALAEA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 224 GGIAQQAVSSIRTVASYTAERRTVERFRGAVARSAALGVRQGLikgAVIGSMGVIYAVWSFLS----WIGSLLVIH 295
Cdd:cd18572 175 NQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQAL---AYAGYVAVNTLLQNGTQvlvlFYGGHLVLS 247
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
364-583 |
2.01e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 78.25 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPS-RP-DTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGI--DTLN--VEW 437
Cdd:PRK13649 3 INLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItsTSKNkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 438 LRSQIGLVSQ--EPVLFATSIRENILFGDETASLKQvVAAAKMANAHEFIVKLPhgyETHVGQFGTQLSGGQKQRIAIAR 515
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQ-EEAEALAREKLALVGIS---ESLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 516 ALVRDPRILLLDEATSALDAESERTVQDALDRA-SVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGT 583
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1020-1247 |
2.13e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.14 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVAVLAGF--SLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVdGEDI-----RSYSLA 1092
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRALYdvNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1093 RLRSQVALVSQ--EPTLFSGTIRDNIAYGAAEEHATEDEvaraaalanahgfisAMER--------GYDTRVGERGA-QL 1161
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEED---------------AKQKaremielvGLPEELLARSPfEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1162 SGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAE 1238
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARyADQIVVMHKGTVFL 226
|
....*....
gi 1002260479 1239 RGRHHELLA 1247
Cdd:PRK13634 227 QGTPREIFA 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1025-1245 |
2.13e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 78.98 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1025 VHF------SYPTRPEVAVLA--GFSLEIGAGKTVALVGPSGSGKST----VIGLIErfydAQRGSVLVDGEDIRSYSLA 1092
Cdd:PRK15079 16 VHFdikdgkQWFWQPPKTLKAvdGVTLRLYEGETLGVVGESGCGKSTfaraIIGLVK----ATDGEVAWLGKDLLGMKDD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1093 RL---RSQVALVSQEPtLFSGTIRDNIAYGAAEE------HATEDEVARAaalanahgfISAMErgydTRVGERGA---- 1159
Cdd:PRK15079 92 EWravRSDIQMIFQDP-LASLNPRMTIGEIIAEPlrtyhpKLSRQEVKDR---------VKAMM----LKVGLLPNlinr 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1160 ---QLSGGQRQRIALARAVLKDARILLLDEATSALDAAserlVQDAVDRMLR------GRTCVVVAHRLSTVEK-SDTIA 1229
Cdd:PRK15079 158 yphEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS----IQAQVVNLLQqlqremGLSLIFIAHDLAVVKHiSDRVL 233
|
250
....*....|....*.
gi 1002260479 1230 VVKDGRVAERGRHHEL 1245
Cdd:PRK15079 234 VMYLGHAVELGTYDEV 249
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
445-566 |
2.42e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 80.62 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 445 VSQEPVLFATSIRENILF--GDETASLKQVVAAAKMANahefivkLPHgyetHVGQFGTQ------LSGGQKQRIAIARA 516
Cdd:COG4178 431 LPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVG-------LGH----LAERLDEEadwdqvLSLGEQQRLAFARL 499
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 517 LVRDPRILLLDEATSALDAESERTVQDALdRASVGRTTVI-VAHRlSTLRK 566
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLL-REELPGTTVIsVGHR-STLAA 548
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1032-1217 |
2.45e-15 |
|
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: 76.54 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1032 RPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIE---RFYDAQRGSVLVDGEDIRSYslaRLRSQVALVSQEPTLF 1108
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKPD---QFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1109 SG-TIRDNIAYGA---AEEHATEDEVARAAAlanahgfISAMERGYDTRVG-ERGAQLSGGQRQRIALARAVLKDARILL 1183
Cdd:cd03234 94 PGlTVRETLTYTAilrLPRKSSDAIRKKRVE-------DVLLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190
....*....|....*....|....*....|....*
gi 1002260479 1184 LDEATSALDAASE-RLVQDAVDRMLRGRTCVVVAH 1217
Cdd:cd03234 167 LDEPTSGLDSFTAlNLVSTLSQLARRNRIVILTIH 201
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
427-583 |
2.70e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.51 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 427 DHGIDTLNVewlRSQIGLVSQEPVLFATSIRENILFG----------DETA--SLKQVVAAAKMANahefivKLPhgyet 494
Cdd:PRK14243 81 APDVDPVEV---RRRIGMVFQKPNPFPKSIYDNIAYGaringykgdmDELVerSLRQAALWDEVKD------KLK----- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 495 hvgQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRL-STLRKADTIAVL 573
Cdd:PRK14243 147 ---QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMqQAARVSDMTAFF 223
|
170
....*....|
gi 1002260479 574 DAgRVVEAGT 583
Cdd:PRK14243 224 NV-ELTEGGG 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
418-592 |
3.42e-15 |
|
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: 76.56 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTLNVEWL-RSQIGLVSQEPVLFAT-SIRENILFGDETASLKQVVAAAKmanahEFIVKL-PHGYEt 494
Cdd:COG0410 55 PRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADL-----ERVYELfPRLKE- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 495 HVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALdaeSERTVQ---DALDR-ASVGRTTVIVAHRLSTLRK-ADT 569
Cdd:COG0410 129 RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL---APLIVEeifEIIRRlNREGVTILLVEQNARFALEiADR 205
|
170 180
....*....|....*....|...
gi 1002260479 570 IAVLDAGRVVEAGTHDELLGMDD 592
Cdd:COG0410 206 AYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1020-1245 |
3.75e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 3.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTrpeVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEdirsySLARLRSQVA 1099
Cdd:PRK15439 12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN-----PCARLTPAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 ------LVSQEPTLFSG-TIRDNIAYGAAEEHATEDEVARAAALANAHGFISAmergydtrvgeRGAQLSGGQRQRIALA 1172
Cdd:PRK15439 84 hqlgiyLVPQEPLLFPNlSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDS-----------SAGSLEVADRQIVEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 1173 RAVLKDARILLLDEATSALDAA-SERLVQDAvdRMLR--GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHEL 1245
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAeTERLFSRI--RELLaqGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
409-588 |
4.20e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 76.16 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 409 ISLLQRFYSPDSGEISMDdhGIDTLNVEWLRSQIGLVSQEPVLFA-TSIRENI---------LFGDETASLKQVvaAAKM 478
Cdd:PRK10771 42 LNLIAGFLTPASGSLTLN--GQDHTTTPPSRRPVSMLFQENNLFShLTVAQNIglglnpglkLNAAQREKLHAI--ARQM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 479 AnAHEFIVKLPHgyethvgqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSALD----AESERTVQDALDRASVgrTT 554
Cdd:PRK10771 118 G-IEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQL--TL 183
|
170 180 190
....*....|....*....|....*....|....*
gi 1002260479 555 VIVAHRLS-TLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:PRK10771 184 LMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1020-1235 |
4.96e-15 |
|
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: 73.25 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIerfydaqrgsvlvdgedirsyslarlrsqva 1099
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLI------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 lvSQEPTLFSGTIRdniaygaaeehatedevaraaalanahgFISAMERGYDtrvgergAQLSGGQRQRIALARAVLKDA 1179
Cdd:cd03221 47 --AGELEPDEGIVT----------------------------WGSTVKIGYF-------EQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 1180 RILLLDEATSALDAASerlvQDAVDRMLRG--RTCVVVAH-R--LSTVekSDTIAVVKDGR 1235
Cdd:cd03221 90 NLLLLDEPTNHLDLES----IEALEEALKEypGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
378-582 |
5.00e-15 |
|
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: 75.39 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 378 DTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNvewlRSQIGLVSQEPVLF-ATSI 456
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 457 RENILFgdeTASLKQVVAAAKMANAHEFIVKLphGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAE 536
Cdd:cd03269 88 IDQLVY---LAQLKGLKKEEARRRIDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1002260479 537 SERTVQDAL-DRASVGRTTVIVAHRLSTL-RKADTIAVLDAGRVVEAG 582
Cdd:cd03269 163 NVELLKDVIrELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
420-536 |
5.22e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 75.21 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 420 SGEISMDDHGIDTLNVEwlRSQIGLVSQEPVLFA-TSIRENILFG---DETASLKQVVAAAKMANAhefivKLPHGYETH 495
Cdd:COG4136 58 SGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPhLSVGENLAFAlppTIGRAQRRARVEQALEEA-----GLAGFADRD 130
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1002260479 496 VGQfgtqLSGGQKQRIAIARALVRDPRILLLDEATSALDAE 536
Cdd:COG4136 131 PAT----LSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
738-962 |
5.30e-15 |
|
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: 77.20 E-value: 5.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 738 FLFLGIAVVCITANIVQHYNFAVMGERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCLL 817
Cdd:cd18572 40 LLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDA--TKTGELTSRLTSDCQKVSDPLSTNLNVF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 818 VQAGATASLGFSLALAVSWRLATVMMAMQPLIIASF-----YFKKVlmaamskkakKAQVQ-----GSQLASEAVVNHRT 887
Cdd:cd18572 118 LRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITkvygrYYRKL----------SKEIQdalaeANQVAEEALSNIRT 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 888 ITAFSSQRRMLRLYEAAQQGPKKDNVAHSWFSGFCLCLCQFSNTGSMAVALWYGGKLMAKGLITPTHLfqVFFML 962
Cdd:cd18572 188 VRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQL--VTFML 260
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
417-582 |
5.70e-15 |
|
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: 75.48 E-value: 5.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 417 SPDSGEISMDdhGIDTL-NVEWLRSQIGLVSQEPVLFA-TSIRENILF--------GDE-TASLKQVVAAAKMAnahEFI 485
Cdd:cd03266 56 EPDAGFATVD--GFDVVkEPAEARRRLGFVSDSTGLYDrLTARENLEYfaglyglkGDElTARLEELADRLGME---ELL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 486 vklphgyETHVGQFGTqlsgGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLSTL 564
Cdd:cd03266 131 -------DRRVGGFST----GMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEV 199
|
170
....*....|....*....
gi 1002260479 565 -RKADTIAVLDAGRVVEAG 582
Cdd:cd03266 200 eRLCDRVVVLHRGRVVYEG 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1020-1191 |
5.85e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.69 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPtrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLAR-LRSQV 1098
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQEPTLFSG-TIRDNIAYGAAEEHATEdevaraaalanahgFISAMERGYD--TRVGERGAQ----LSGGQRQRIAL 1171
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMGGFFAERDQ--------------FQERIKWVYElfPRLHERRIQragtMSGGEQQMLAI 148
|
170 180
....*....|....*....|
gi 1002260479 1172 ARAVLKDARILLLDEATSAL 1191
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGL 168
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1022-1245 |
5.85e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.15 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1022 FKNVHFSYPtrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEdiRSYSLARLRSQVALV 1101
Cdd:PRK11000 6 LRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1102 SQEPTLFSG-TIRDNIAYGAAEEHATEDEVaraaalanahgfisamergyDTRVGE-------------RGAQLSGGQRQ 1167
Cdd:PRK11000 81 FQSYALYPHlSVAENMSFGLKLAGAKKEEI--------------------NQRVNQvaevlqlahlldrKPKALSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1168 RIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHrlSTVEK---SDTIAVVKDGRVAERGRH 1242
Cdd:PRK11000 141 RVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTH--DQVEAmtlADKIVVLDAGRVAQVGKP 218
|
...
gi 1002260479 1243 HEL 1245
Cdd:PRK11000 219 LEL 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1027-1245 |
5.99e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.58 E-value: 5.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1027 FSYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVI----GL---------IERFY-----DAQRGSVLVDGEDIRS 1088
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVthfnGLikskygtiqVGDIYigdkkNNHELITNPYSKKIKN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1089 YSlaRLRSQVALVSQEP--TLFSGTIRDNIAYGAAEEHATEDEVARAAALanahgFISAMerGYDTRVGERGA-QLSGGQ 1165
Cdd:PRK13631 111 FK--ELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLAKF-----YLNKM--GLDDSYLERSPfGLSGGQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1166 RQRIALARAVLKDARILLLDEATSALDAASER-LVQDAVDRMLRGRTCVVVAHRLSTV-EKSDTIAVVKDGRVAERGRHH 1243
Cdd:PRK13631 182 KRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPY 261
|
..
gi 1002260479 1244 EL 1245
Cdd:PRK13631 262 EI 263
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
434-588 |
6.40e-15 |
|
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: 75.89 E-value: 6.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 434 NVEWLRSQIGLVS---QEPVLFATSIRENILFGdETAS--LKQVVAAAKMANAHEFIVKLphGYETHVGQ-FGTqLSGGQ 507
Cdd:COG1119 72 DVWELRKRIGLVSpalQLRFPRDETVLDVVLSG-FFDSigLYREPTDEQRERARELLELL--GLAHLADRpFGT-LSQGE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 508 KQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVI-VAHRLSTLRKADT-IAVLDAGRVVEAGTH 584
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIPPGIThVLLLKDGRVVAAGPK 227
|
....
gi 1002260479 585 DELL 588
Cdd:COG1119 228 EEVL 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1049-1259 |
8.80e-15 |
|
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: 80.06 E-value: 8.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1049 KTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSySLARLRSQVALVSQEPTLFSG-TIRDNIAYGAAEEHATE 1127
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHILFYAQLKGRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1128 DEVARAaalanahgfISAM--ERGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDR 1205
Cdd:TIGR01257 1036 EEAQLE---------MEAMleDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK 1106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 1206 MLRGRTCVVVAHRLSTVE-KSDTIAVVKDGRVAERGRHHELLAVGRAGTYYNLIK 1259
Cdd:TIGR01257 1107 YRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVR 1161
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1038-1245 |
8.97e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.82 E-value: 8.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1038 LAGFSLEIGAGKTVALVGPSGSGKSTVI----GLIERfyDAQRGS-VLVDGEDI-RSYSLAR----LRSQVALVSQEPTL 1107
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITG--DKSAGShIELLGRTVqREGRLARdirkSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1108 FSG-TIRDNIAYGAAEEHATEDEVARAAALANAHGFISAMergydTRVG------ERGAQLSGGQRQRIALARAVLKDAR 1180
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 1181 ILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLS-TVEKSDTIAVVKDGRVAERGRHHEL 1245
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
418-583 |
1.24e-14 |
|
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: 74.78 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTLNVE----WLRSQIGLVSQEPVLFAT-SIRENILFGDETASLKQVVAAAKMANAHefiVKLPHgY 492
Cdd:COG4181 64 PTSGTVRLAGQDLFALDEDararLRARHVGFVFQSFQLLPTlTALENVMLPLELAGRRDARARARALLER---VGLGH-R 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 493 ETHvgqFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQD---ALDRASvGRTTVIVAHRLSTLRKADT 569
Cdd:COG4181 140 LDH---YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDllfELNRER-GTTLVLVTHDPALAARCDR 215
|
170
....*....|....
gi 1002260479 570 IAVLDAGRVVEAGT 583
Cdd:COG4181 216 VLRLRAGRLVEDTA 229
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1032-1246 |
1.26e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1032 RPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIErFYDAQ----RGSVLVDGEDIRSYSLARLRSQV--------A 1099
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKEMRAISAYVqqddlfipT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEPTLFSGTIRDNIAYGAAEEHATEDEVARAAalanahGFISAMergyDTRVGERGAQ--LSGGQRQRIALARAVLK 1177
Cdd:TIGR00955 114 LTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQAL------GLRKCA----NTRIGVPGRVkgLSGGERKRLAFASELLT 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 1178 DARILLLDEATSALDAASERLVQDAVDRM-LRGRTCVVVAHRLST--VEKSDTIAVVKDGRVAERGRHHELL 1246
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1037-1246 |
1.40e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.41 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1037 VLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSG-TIRDN 1115
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1116 IAYGAAEEHA------TEDEvARAAALANAHGFISAMERGYDTrvgergaqLSGGQRQRIALARAVLKDARILLLDEATS 1189
Cdd:PRK10253 102 VARGRYPHQPlftrwrKEDE-EAVTKAMQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1190 ALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTVEKSDT-IAVVKDGRVAERGRHHELL 1246
Cdd:PRK10253 173 WLDISHQIDLLELLSELNRekGYTLAAVLHDLNQACRYAShLIALREGKIVAQGAPKEIV 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1020-1241 |
1.50e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.21 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRP--------EVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQrGSVLVDGEDIRSYS- 1090
Cdd:PRK15134 276 LDVEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1091 --LARLRSQVALVSQEPTlFSGTIRDN----IAYGAAEEHAT------EDEVaraaalanahgfISAMER-GYDTRVGER 1157
Cdd:PRK15134 355 rqLLPVRHRIQVVFQDPN-SSLNPRLNvlqiIEEGLRVHQPTlsaaqrEQQV------------IAVMEEvGLDPETRHR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1158 -GAQLSGGQRQRIALARAVLKDARILLLDEATSALDaaseRLVQDAVDRMLRGrtcVVVAHRLSTVEKSDTIAVV----- 1231
Cdd:PRK15134 422 yPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAQILALLKS---LQQKHQLAYLFISHDLHVVralch 494
|
250
....*....|....*
gi 1002260479 1232 -----KDGRVAERGR 1241
Cdd:PRK15134 495 qvivlRQGEVVEQGD 509
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
415-585 |
1.58e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.76 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 415 FYSPDSGEISMDDHGIDTLN-VEWLRSQIGLVSQEPVLFAT-SIRENILFGDETASLKQVvaaaKMANAHEFIVKLPHGY 492
Cdd:COG3845 54 LYQPDSGEILIDGKPVRIRSpRDAIALGIGMVHQHFMLVPNlTVAENIVLGLEPTKGGRL----DRKAARARIRELSERY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 493 ------ETHVGQfgtqLSGGQKQRIAIARALVRDPRILLLDEATSAL-DAESERtVQDALDR-ASVGRTTVIVAHRLS-T 563
Cdd:COG3845 130 gldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADE-LFEILRRlAAEGKSIIFITHKLReV 204
|
170 180
....*....|....*....|..
gi 1002260479 564 LRKADTIAVLDAGRVVeaGTHD 585
Cdd:COG3845 205 MAIADRVTVLRRGKVV--GTVD 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
378-587 |
1.60e-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: 73.94 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 378 DTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGI--DTLNVewlRSQIGLVSQEPVL-FAT 454
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrEPREV---RRRIGIVFQDLSVdDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 455 SIRENILFGDETASLKQVVAAAKMANAHEFiVKLPHGYETHVGQFgtqlSGGQKQRIAIARALVRDPRILLLDEATSALD 534
Cdd:cd03265 89 TGWENLYIHARLYGVPGAERRERIDELLDF-VGLLEAADRLVKTY----SGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 535 AESERTVQDALDR--ASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDEL 587
Cdd:cd03265 164 PQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
381-582 |
1.76e-14 |
|
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: 73.79 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 381 VLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDdhGIDTLNVEWLRSQIGLVSQEPVLFAT-SIREN 459
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFD--GKSYQKNIEALRRIGALIEAPGFYPNlTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 460 ILfgdetasLKQVVAAAKMANAHEF--IVKLPHGYETHVGQFgtqlSGGQKQRIAIARALVRDPRILLLDEATSALDAES 537
Cdd:cd03268 93 LR-------LLARLLGIRKKRIDEVldVVGLKDSAKKKVKGF----SLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002260479 538 ERTVQDAL-DRASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAG 582
Cdd:cd03268 162 IKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
438-599 |
1.78e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.13 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 438 LRSQIGLVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARAL 517
Cdd:PRK14271 99 FRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 518 VRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLS-TLRKADTIAVLDAGRVVEAGTHDELLGMDDGGEG 596
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
...
gi 1002260479 597 GVY 599
Cdd:PRK14271 259 ARY 261
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1034-1238 |
1.97e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.05 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1034 EVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSY---SLARLRSQ-VALVSQE----P 1105
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhVGFVFQSfmliP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1106 TLfsgTIRDNIAY-----GAAEEHATEDEVARAAalanahgfisamERGYDTRVGERGAQLSGGQRQRIALARAVLKDAR 1180
Cdd:PRK10584 102 TL---NALENVELpallrGESSRQSRNGAKALLE------------QLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1181 ILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTVEKSDTIAVVKDGRVAE 1238
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1019-1240 |
2.05e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 74.35 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPT-------------------RPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSV 1079
Cdd:COG1134 4 MIEVENVSKSYRLyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1080 LVDGedirsyslaRLRSQVAL---VSQEptlFSGtiRDNIAYGAA-------EEHATEDEVARaaalanahgFiSAMERG 1149
Cdd:COG1134 84 EVNG---------RVSALLELgagFHPE---LTG--RENIYLNGRllglsrkEIDEKFDEIVE---------F-AELGDF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1150 YDTRVGergaQLSGGQRQRIALARAVLKDARILLLDEATSALDAA----SERLVQdavDRMLRGRTCVVVAHRLSTVEK- 1224
Cdd:COG1134 140 IDQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRl 212
|
250
....*....|....*.
gi 1002260479 1225 SDTIAVVKDGRVAERG 1240
Cdd:COG1134 213 CDRAIWLEKGRLVMDG 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
421-587 |
2.53e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.22 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 421 GEISMDDhgidtlnVEWLRSQIGLVSQEPVLFA-TSIRENILFGDETASLKQVVAAAKMANAHEfIVKLPHGYETHvgqf 499
Cdd:PRK11000 63 GEKRMND-------VPPAERGVGMVFQSYALYPhLSVAENMSFGLKLAGAKKEEINQRVNQVAE-VLQLAHLLDRK---- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 500 GTQLSGGQKQRIAIARALVRDPRILLLDEATSALDA--ESERTVQDALDRASVGRTTVIVAH-RLSTLRKADTIAVLDAG 576
Cdd:PRK11000 131 PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalRVQMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAG 210
|
170
....*....|.
gi 1002260479 577 RVVEAGTHDEL 587
Cdd:PRK11000 211 RVAQVGKPLEL 221
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
69-295 |
2.98e-14 |
|
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: 74.98 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 69 AVDKFALRLLYVAVAVGACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDaapsspsspqaqaQATTFRVISTVS 148
Cdd:cd18780 40 ALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFD-------------VTRTGELLNRLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 149 DDADAIQDFLGEKLPMVLANATLFFGALAVSFVFAWRLALaglpftLLLFVTPSVLLAGRM-----AAAAGEARAAYEEA 223
Cdd:cd18780 107 SDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTL------VMLSVVPPLSIGAVIygkyvRKLSKKFQDALAAA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 224 GGIAQQAVSSIRTVASYTAERRTVERFRGAVARSAALGVRQGLIKGAVIGSMGVIyavwSFLS-----WIGSLLVIH 295
Cdd:cd18780 181 STVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAA----AQLAivlvlWYGGRLVID 253
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1035-1246 |
3.23e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.81 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1035 VAV---LAGFSLEIGAGKTVALVGPSGSGKSTVI----GLIErfydaQRGSVLVDGEDIRSYSLARLRSQVA-LVSQEPT 1106
Cdd:PRK03695 6 VAVstrLGPLSAEVRAGEILHLVGPNGAGKSTLLarmaGLLP-----GSGSIQFAGQPLEAWSAAELARHRAyLSQQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1107 LFSGTIRDNIA-YGAAEEHATEDEvaraaalanahgfiSAMER-----GYDTRVGERGAQLSGGQRQRIALARAVLK--- 1177
Cdd:PRK03695 81 PFAMPVFQYLTlHQPDKTRTEAVA--------------SALNEvaealGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwp 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1178 ----DARILLLDEATSALDAASerlvQDAVDRMLR-----GRTCVVVAHRLS-TVEKSDTIAVVKDGRVAERGRHHELL 1246
Cdd:PRK03695 147 dinpAGQLLLLDEPMNSLDVAQ----QAALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
418-587 |
3.80e-14 |
|
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: 73.33 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTLNVEWL-RSQIGLVSQEPVLFAT-SIRENILFGdetaslkqvVAAAKMANAH--EFIVKLPHGYE 493
Cdd:TIGR03410 52 VKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPRlTVEENLLTG---------LAALPRRSRKipDEIYELFPVLK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 494 THVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALD----AESERTVQDAldRASVGRTTVIVAHRLS-TLRKAD 568
Cdd:TIGR03410 123 EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQpsiiKDIGRVIRRL--RAEGGMAILLVEQYLDfARELAD 200
|
170
....*....|....*....
gi 1002260479 569 TIAVLDAGRVVEAGTHDEL 587
Cdd:TIGR03410 201 RYYVMERGRVVASGAGDEL 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
434-587 |
3.80e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 74.74 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 434 NVEWLRSQIGLVSQ--EPVLFATSIRENILFGDETASLKQVvAAAKMANAHEFIVKLPhgyETHVGQFGTQLSGGQKQRI 511
Cdd:PRK13651 99 KIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKE-EAKKRAAKYIELVGLD---ESYLQRSPFELSGGQKRRV 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 512 AIARALVRDPRILLLDEATSALDAESERTVQDALDRA-SVGRTTVIVAHRL-STLRKADTIAVLDAGRVVEAG-THDEL 587
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGdTYDIL 253
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1020-1247 |
4.15e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 73.72 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTR------PEVAVLAGFSLEIGAGKTVALVGPSGSGKSTV----IGLIERfydaQRGSVLVDGEDIrSY 1089
Cdd:COG4167 5 LEVRNLSKTFKYRtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLakmlAGIIEP----TSGEILINGHKL-EY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1090 SLARLRSQ-VALVSQEP-TLFS-----GTIRD-----NIAYGAAEEHatedevaraaalanahgfisamERGYDT--RVG 1155
Cdd:COG4167 80 GDYKYRCKhIRMIFQDPnTSLNprlniGQILEeplrlNTDLTAEERE----------------------ERIFATlrLVG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1156 ERGAQ-------LSGGQRQRIALARAVLKDARILLLDEATSALDaASER-----LVQDAVDRMlrGRTCVVVAHRLSTVE 1223
Cdd:COG4167 138 LLPEHanfyphmLSSGQKQRVALARALILQPKIIIADEALAALD-MSVRsqiinLMLELQEKL--GISYIYVSQHLGIVK 214
|
250 260
....*....|....*....|....*
gi 1002260479 1224 K-SDTIAVVKDGRVAERGRHHELLA 1247
Cdd:COG4167 215 HiSDKVLVMHQGEVVEYGKTAEVFA 239
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
415-588 |
4.16e-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: 73.35 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 415 FYSPDSGEISMDDHGIDTLNVeWLRSQIGL--VSQEPVLFAT-SIRENILFGDETASLKQVVAAAKMANA-HEF-IVKLP 489
Cdd:cd03218 49 LVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFRKlTVEENILAVLEIRGLSKKEREEKLEELlEEFhITHLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 490 HgyethvgQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALD----AESERTVQDALDRasvGRTTVIVAHRLS-TL 564
Cdd:cd03218 128 K-------SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpiavQDIQKIIKILKDR---GIGVLITDHNVReTL 197
|
170 180
....*....|....*....|....
gi 1002260479 565 RKADTIAVLDAGRVVEAGTHDELL 588
Cdd:cd03218 198 SITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
410-585 |
5.38e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.10 E-value: 5.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 410 SLLQRFYS---PDSGEISMDDHGID----TLNVEWLRSQIGLVSQ--EPVLFATSIRENILFG-------DETASLKQVV 473
Cdd:PRK13641 48 TLMQHFNAllkPSSGTITIAGYHITpetgNKNLKKLRKKVSLVFQfpEAQLFENTVLKDVEFGpknfgfsEDEAKEKALK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 474 AAAKMANAHEFIVKLPHgyethvgqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDA-LDRASVGR 552
Cdd:PRK13641 128 WLKKVGLSEDLISKSPF-----------ELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLfKDYQKAGH 196
|
170 180 190
....*....|....*....|....*....|....
gi 1002260479 553 TTVIVAHRLSTLRK-ADTIAVLDAGRVVEagtHD 585
Cdd:PRK13641 197 TVILVTHNMDDVAEyADDVLVLEHGKLIK---HA 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
498-573 |
5.65e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.88 E-value: 5.65e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 498 QFGTqLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASV-GRTTVIVAHRLSTLRKADTIAVL 573
Cdd:NF040873 116 QLGE-LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
418-587 |
7.72e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 7.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTLNVEwLRSQIG--LVSQEPVLFAT-SIRENILFGDEtaslKQVVAAAKMAnahEFIVKLPHGYET 494
Cdd:PRK15439 63 PDSGTLEIGGNPCARLTPA-KAHQLGiyLVPQEPLLFPNlSVKENILFGLP----KRQASMQKMK---QLLAALGCQLDL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 495 HVgQFGTqLSGGQKQRIAIARALVRDPRILLLDEATSALD-AESERTVQ--DALDRASVGrtTVIVAHRLSTLRK-ADTI 570
Cdd:PRK15439 135 DS-SAGS-LEVADRQIVEILRGLMRDSRILILDEPTASLTpAETERLFSriRELLAQGVG--IVFISHKLPEIRQlADRI 210
|
170
....*....|....*..
gi 1002260479 571 AVLDAGRVVEAGTHDEL 587
Cdd:PRK15439 211 SVMRDGTIALSGKTADL 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1019-1193 |
9.76e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 74.11 E-value: 9.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYPTRpeVAVLAGFSLEIGAGKTVALVGPSGSGKST----VIGLiERFYDaqrGSVLVDGEDIRSYSLA-R 1093
Cdd:PRK11650 3 GLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTllrmVAGL-ERITS---GEIWIGGRVVNELEPAdR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1094 lrsQVALVSQEPTLFSG-TIRDNIAYGAAEEHATEDEVaraaalanahgfisamergyDTRVGE-------------RGA 1159
Cdd:PRK11650 77 ---DIAMVFQNYALYPHmSVRENMAYGLKIRGMPKAEI--------------------EERVAEaarileleplldrKPR 133
|
170 180 190
....*....|....*....|....*....|....
gi 1002260479 1160 QLSGGQRQRIALARAVLKDARILLLDEATSALDA 1193
Cdd:PRK11650 134 ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
418-588 |
9.80e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 72.95 E-value: 9.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTLNVEWL-----------------RSQIGLVSQEPVLFATSI----RENILFgdetASLKQVVAAA 476
Cdd:COG4167 65 PTSGEILINGHKLEYGDYKYRckhirmifqdpntslnpRLNIGQILEEPLRLNTDLtaeeREERIF----ATLRLVGLLP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 477 KMANAHefivklPHgyethvgqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAeSERT--------VQDALdra 548
Cdd:COG4167 141 EHANFY------PH-----------MLSSGQKQRVALARALILQPKIIIADEALAALDM-SVRSqiinlmleLQEKL--- 199
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1002260479 549 svGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDELL 588
Cdd:COG4167 200 --GISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVF 238
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
369-580 |
1.03e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.42 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 369 VHFSYPSRPdtlVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWlrsqiGLVSQ- 447
Cdd:PRK11248 7 LYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 448 EPVLFATSIRENILFGDETASlkqVVAAAKMANAHEFIVKLphGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLD 527
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAG---VEKMQRLEIAHQMLKKV--GLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 528 EATSALDAESERTVQDALDR--ASVGRTTVIVAHRLSTLRKADTIAVL---DAGRVVE 580
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLlspGPGRVVE 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
409-589 |
1.37e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 72.31 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 409 ISLLQRfysPDSGEISMDDHGI-------------DTLNVEWLRSQIGLVSQEPVLFA-TSIRENILfgdetASLKQVVA 474
Cdd:PRK10619 51 INFLEK---PSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRLLRTRLTMVFQHFNLWShMTVLENVM-----EAPIQVLG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 475 AAKmANAHEFIVKlphgYETHVG-------QFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR 547
Cdd:PRK10619 123 LSK-QEARERAVK----YLAKVGideraqgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQ 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1002260479 548 -ASVGRTTVIVAHRLSTLRKADT-IAVLDAGRVVEAGTHDELLG 589
Cdd:PRK10619 198 lAEEGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLFG 241
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
417-587 |
1.49e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.60 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 417 SPDSGEISMDdhGIDTLNVEWLRSQIGLVSQEPVLFA-TSIRENILFGDETASLKQVVAAAKMANAHEfIVKLPhGYETh 495
Cdd:PRK11432 57 KPTEGQIFID--GEDVTHRSIQQRDICMVFQSYALFPhMSLGENVGYGLKMLGVPKEERKQRVKEALE-LVDLA-GFED- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 496 vgQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALD--RASVGRTTVIVAHRLS-TLRKADTIAV 572
Cdd:PRK11432 132 --RYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRelQQQFNITSLYVTHDQSeAFAVSDTVIV 209
|
170
....*....|....*
gi 1002260479 573 LDAGRVVEAGTHDEL 587
Cdd:PRK11432 210 MNKGKIMQIGSPQEL 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1020-1247 |
1.56e-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: 74.84 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNV--HFSYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKST----VIGLIERF---YDAQRGSVLVDGEDIRSYS 1090
Cdd:TIGR03269 280 IKVRNVskRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTlskiIAGVLEPTsgeVNVRVGDEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1091 LARLRSQVALVSQEPTLFS-GTIRDNIAYGAAEEHATEDEVARAAALANAHGF-----ISAMERGYDtrvgergaQLSGG 1164
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPhRTVLDNLTEAIGLELPDELARMKAVITLKMVGFdeekaEEILDKYPD--------ELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1165 QRQRIALARAVLKDARILLLDEATSALDAASERLVQDAV--DRMLRGRTCVVVAHRLSTV-EKSDTIAVVKDGRVAERGR 1241
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGD 511
|
....*.
gi 1002260479 1242 HHELLA 1247
Cdd:TIGR03269 512 PEEIVE 517
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
364-587 |
1.57e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 72.53 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPDTlVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGE---ISMDdhGIdTLNVE--W- 437
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVD--GI-TLTAKtvWd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 438 LRSQIGLVSQEP--VLFATSIRENILFGDETASL---------KQVVAAAKMANaheFIVKLPhgyethvgqfgTQLSGG 506
Cdd:PRK13640 82 IREKVGIVFQNPdnQFVGATVGDDVAFGLENRAVprpemikivRDVLADVGMLD---YIDSEP-----------ANLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 507 QKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASV--GRTTVIVAHRLSTLRKADTIAVLDAGRVVEAGTH 584
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
...
gi 1002260479 585 DEL 587
Cdd:PRK13640 228 VEI 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1020-1240 |
1.63e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.46 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSY-PTRPEVA-VLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLAR---- 1093
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1094 LRSQVALVSQEP--TLFSGTIRDNIAYGAAEEHATEDEVARAaalanahgfisAMER----GYDTRVGERGA-QLSGGQR 1166
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKI-----------AAEKlemvGLADEFWEKSPfELSGGQM 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1167 QRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR-GRTCVVVAHRLSTV-EKSDTIAVVKDGRVAERG 1240
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCG 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1033-1258 |
2.13e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.65 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1033 PEVAVLAGFSLEIGAGKTVALVGPSGSGKS----TVIGLIERFYDAQRGSVLVDGEDIrsySLARLRSQ-VALVSQEP-T 1106
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV---APCALRGRkIATIMQNPrS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1107 LFSG--TIRDniaygaaeeHATEdEVARAAALANAHGFISAMER---GYDTRVGERGA-QLSGGQRQRIALARAVLKDAR 1180
Cdd:PRK10418 91 AFNPlhTMHT---------HARE-TCLALGKPADDATLTAALEAvglENAARVLKLYPfEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1181 ILLLDEATSALDAASERLVQDAVDRMLRGRT--CVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELLAVGRAGTYYNL 1257
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSL 240
|
.
gi 1002260479 1258 I 1258
Cdd:PRK10418 241 V 241
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
361-588 |
2.14e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 71.48 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 361 RGEIVFKDVHFSYPsrpDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYS--PD---SGEISMDDHGIDTLNV 435
Cdd:PRK14247 1 MNKIEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 436 EWLRSQIGLVSQEPVLFAT-SIRENILFGdetASLKQVVAAAK--MANAHEFIVK--LPHGYETHVGQFGTQLSGGQKQR 510
Cdd:PRK14247 78 IELRRRVQMVFQIPNPIPNlSIFENVALG---LKLNRLVKSKKelQERVRWALEKaqLWDEVKDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 511 IAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAH-RLSTLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
376-591 |
2.95e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.64 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 376 RPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEW---LRSQIGLVSQEP--- 449
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkaFRRDIQMVFQDSisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 450 VLFATSIRENIlfGDETASLKQVVAAAKMANAHEFI--VKLPhgyETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLD 527
Cdd:PRK10419 102 VNPRKTVREII--REPLRHLLSLDKAERLARASEMLraVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 528 EATSALDAESERTVQDALD--RASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDELLGMD 591
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLTFS 243
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1037-1236 |
4.00e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.23 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1037 VLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSL---ARLRSQ-VALVSQEPTLFSG-T 1111
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRNQkLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1112 IRDNIAY-----GAAEEHATEdevaraaalaNAHGFISAMerGYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDE 1186
Cdd:PRK11629 104 ALENVAMplligKKKPAEINS----------RALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1187 ATSALDAASerlvQDAVDRML------RGRTCVVVAHRLSTVEKSDTIAVVKDGRV 1236
Cdd:PRK11629 172 PTGNLDARN----ADSIFQLLgelnrlQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
66-295 |
4.14e-13 |
|
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: 71.36 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 66 SSGAVDKFALRLLYVAVAVGACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDaapsspsspqaqaQATTFRVIS 145
Cdd:cd18576 31 DTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFH-------------ERRVGELTS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 146 TVSDDADAIQDFLGEKLPMVLANATLFFGALAVSFVFAWRLALAGLpFTLLLFVTPSVLLAGRMAAAAGEARAAYEEAGG 225
Cdd:cd18576 98 RLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLML-ATVPVVVLVAVLFGRRIRKLSKKVQDELAEANT 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 226 IAQQAVSSIRTVASYTAERRTVERFRGAVARSAALGVRQGLIKGAVIGSMG-VIYAVWSFLSWIGSLLVIH 295
Cdd:cd18576 177 IVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIfLLFGAIVAVLWYGGRLVLA 247
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
442-589 |
6.03e-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: 72.91 E-value: 6.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 442 IGLVSQEPVLFA-TSIRENIL------FGDETASLKQVVAAaKMAN-----AHEFIVKLPHgyethvgqfgtQLSGGQKQ 509
Cdd:TIGR03269 367 IGILHQEYDLYPhRTVLDNLTeaigleLPDELARMKAVITL-KMVGfdeekAEEILDKYPD-----------ELSEGERH 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 510 RIAIARALVRDPRILLLDEATSALDAESERTVQDAL--DRASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDE 586
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEE 514
|
...
gi 1002260479 587 LLG 589
Cdd:TIGR03269 515 IVE 517
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
381-590 |
6.07e-13 |
|
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: 70.60 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 381 VLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEW---LRSQIGLVSQE---PVLFAT 454
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDspsAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 455 SIRENIlfGDETASLKQVVAAAKMANAHEFI--VKLPhgyETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSA 532
Cdd:TIGR02769 106 TVRQII--GEPLRHLTSLDESEQKARIAELLdmVGLR---SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 533 LDAESERTVQDALD--RASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDELLGM 590
Cdd:TIGR02769 181 LDMVLQAVILELLRklQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSF 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
375-588 |
8.01e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.80 E-value: 8.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 375 SRPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVL-FA 453
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 454 TSIRENILFGdETASLKQVvaaAKMANAHEFIVKLPHGyETHVGQFG----TQLSGGQKQRIAIARALVRDPRILLLDEA 529
Cdd:PRK09536 92 FDVRQVVEMG-RTPHRSRF---DTWTETDRAAVERAME-RTGVAQFAdrpvTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 530 TSALDAESE-RTVQDALDRASVGRTTVIVAHRLS-TLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:PRK09536 167 TASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
364-591 |
8.66e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.02 E-value: 8.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPSRPdtlVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTlNVEWLRSQIG 443
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 444 LVSQEPVL-FATSIRENIL-----FGDETASLKQVVAAAKmanahEFiVKLPHGYETHVgqfgTQLSGGQKQRIAIARAL 517
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLLvfgryFGMSTREIEAVIPSLL-----EF-ARLESKADARV----SDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 518 VRDPRILLLDEATSALDAESERTVQDALdRA--SVGRTTVIVAHRLSTL-RKADTIAVLDAGR-VVEAGTH---DELLGM 590
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERL-RSllARGKTILLTTHFMEEAeRLCDRLCVLEAGRkIAEGRPHaliDEHIGC 266
|
.
gi 1002260479 591 D 591
Cdd:PRK13536 267 Q 267
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1048-1239 |
1.06e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 67.01 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1048 GKTVALVGPSGSGKSTVIGLIERFYDAQRGSVL-VDGEDIRSYSLARLRsqvalvsqeptlfsgtirdniaygaaeehat 1126
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLL------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1127 edevaraaalanahgfisamergyDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRM 1206
Cdd:smart00382 51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELR 106
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002260479 1207 L------RGRTCVVVAHRLSTVEKSDTIAVVKDGRVAER 1239
Cdd:smart00382 107 LllllksEKNLTVILTTNDEKDLGPALLRRRFDRRIVLL 145
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
366-537 |
1.07e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 366 FKDVHFSYPSRPdtlVLNGFNLTISEGATvglvggsgsgkstvISL--------------LQRFYSPDSGEISMDDHgid 431
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDR--------------IGLvgrngagkstllkiLAGELEPDSGEVSIPKG--- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 432 tlnvewLRsqIGLVSQEPVLFAT-SIRENILFGD-ETASLKQVVAAA------------KMANAHEFIVKLpHGY--ETH 495
Cdd:COG0488 61 ------LR--IGYLPQEPPLDDDlTVLDTVLDGDaELRALEAELEELeaklaepdedleRLAELQEEFEAL-GGWeaEAR 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 496 VGQ------FGT--------QLSGGQKQRIAIARALVRDPRILLLDEATSALDAES 537
Cdd:COG0488 132 AEEilsglgFPEedldrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
364-588 |
1.38e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 69.76 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSY-PSRP-DTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLN----VEW 437
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 438 LRSQIGLVSQEP--VLFATSIRENILFGDETASLK----QVVAAAKMAN---AHEFIVKLPHgyethvgqfgtQLSGGQK 508
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPkekaEKIAAEKLEMvglADEFWEKSPF-----------ELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 509 QRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRA-SVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDE 586
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSD 230
|
..
gi 1002260479 587 LL 588
Cdd:PRK13643 231 VF 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
504-587 |
1.39e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 70.38 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 504 SGGQKQRIAIARALVRDPRILLLDEATSALDAESERTV-------QDALdrasvGRTTVIVAHRLSTLRK-ADTIAVLDA 575
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVlnlmmdlQQEL-----GLSYVFISHDLSVVEHiADEVMVMYL 230
|
90
....*....|..
gi 1002260479 576 GRVVEAGTHDEL 587
Cdd:PRK11308 231 GRCVEKGTKEQI 242
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1037-1247 |
1.53e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.77 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1037 VLAGFSLEIGAGKTVALVGPSGSGKST----VIGLIERfyDAqrGSVLVDGEDIRSYSL-ARLRSQVALVSQEPTLFSG- 1110
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR--DA--GNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1111 ----------TIRDNIAYGAAEEHATEdevaraaalanahgfisAMERGYDTRVGER-GAQLSGGQRQRIALARAVLKDA 1179
Cdd:PRK10895 94 svydnlmavlQIRDDLSAEQREDRANE-----------------LMEEFHIEHLRDSmGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 1180 RILLLDEATSALDAAS----ERLVQDAVDrmlRGRTCVVVAHRL-STVEKSDTIAVVKDGRVAERGRHHELLA 1247
Cdd:PRK10895 157 KFILLDEPFAGVDPISvidiKRIIEHLRD---SGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
409-583 |
1.77e-12 |
|
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: 72.35 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 409 ISLLQRFYSPDSGEISMDDHGIDTlNVEWLRSQIGLVSQEPVLFA-TSIRENILFGDETASLKQVVAAAKMANAHEfivk 487
Cdd:TIGR01257 973 LSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILFYAQLKGRSWEEAQLEMEAMLE---- 1047
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 488 lPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLR-K 566
Cdd:TIGR01257 1048 -DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlL 1126
|
170
....*....|....*..
gi 1002260479 567 ADTIAVLDAGRVVEAGT 583
Cdd:TIGR01257 1127 GDRIAIISQGRLYCSGT 1143
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
433-588 |
1.85e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.91 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 433 LNVEWLRSQIGLVSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIA 512
Cdd:PRK14258 81 VNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLC 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 513 IARALVRDPRILLLDEATSALDAES----ERTVQDALDRASVgrTTVIVAHRLSTL-RKADTIAVLDA-----GRVVEAG 582
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQSLRLRSEL--TMVIVSHNLHQVsRLSDFTAFFKGnenriGQLVEFG 238
|
....*.
gi 1002260479 583 THDELL 588
Cdd:PRK14258 239 LTKKIF 244
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
504-556 |
2.21e-12 |
|
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: 67.84 E-value: 2.21e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 504 SGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVI 556
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
461-587 |
2.31e-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: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 461 LFGDETA------SLKQVVAAAKMA--NAHEFI--VKLPHGYeTHVGQfgtQLSGGQKQRIAIARALVRDPRILLLDEAT 530
Cdd:TIGR03269 121 LYGDDTVldnvleALEEIGYEGKEAvgRAVDLIemVQLSHRI-THIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPT 196
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 531 SALDAESERTVQDALDRASV--GRTTVIVAHRLSTLRKADTIAV-LDAGRVVEAGTHDEL 587
Cdd:TIGR03269 197 GTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDLSDKAIwLENGEIKEEGTPDEV 256
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
416-582 |
3.11e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.33 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 416 YSPDsgeismddhgIDTLNVewlRSQIGLVSQEPVLFA-TSIRENILFGDETASLkqVVAAAKMANAHEFIVK---LPHG 491
Cdd:PRK14267 74 YSPD----------VDPIEV---RREVGMVFQYPNPFPhLTIYDNVAIGVKLNGL--VKSKKELDERVEWALKkaaLWDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 492 YETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHR-LSTLRKADTI 570
Cdd:PRK14267 139 VKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYV 218
|
170
....*....|..
gi 1002260479 571 AVLDAGRVVEAG 582
Cdd:PRK14267 219 AFLYLGKLIEVG 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1026-1236 |
3.21e-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: 67.74 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1026 HFSYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSlARLRSQVALV-SQE 1104
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRR-KKFLRRIGVVfGQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1105 PTL-FSGTIRDNIA-----YGAAEEHATE--DEvaraaalanahgfISAM---ERGYDTRVgergAQLSGGQRQRIALAR 1173
Cdd:cd03267 104 TQLwWDLPVIDSFYllaaiYDLPPARFKKrlDE-------------LSELldlEELLDTPV----RQLSLGQRMRAEIAA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1174 AVLKDARILLLDEATSALDAASERLVQDAVDRM--LRGRTCVVVAHRLSTVEK-SDTIAVVKDGRV 1236
Cdd:cd03267 167 ALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrERGTTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
364-588 |
3.22e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.06 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 364 IVFKDVHFSYPsrpDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTlNVEWLRSQIG 443
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 444 LVSQ----EPVLfatSIRENILFGDETASLKQVVAAAKMANAHEFiVKLPHGYETHVGQfgtqLSGGQKQRIAIARALVR 519
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 520 DPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLSTL-RKADTIAVLDAGRVVEAGTHDELL 588
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
66-295 |
3.62e-12 |
|
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: 68.66 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 66 SSGAVDKFALRLLYVAVAVGACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDAAPSSpsspqaqaqattfRVIS 145
Cdd:cd18575 31 NTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTG-------------EVLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 146 TVSDDADAIQDFLGEKLPMVLANATLFFGALAVSFVFAWRLA---LAGLPFTLLlfvtPSVLLAGRMAAAAGEARAAYEE 222
Cdd:cd18575 98 RLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTllvLLVIPLVVL----PIILFGRRVRRLSRASQDRLAD 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 223 AGGIAQQAVSSIRTVASYTAERRTVERFRGAVARSAALGVRQGLIKGAVIG-SMGVIYAVWSFLSWIGSLLVIH 295
Cdd:cd18575 174 LSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTAlVIFLVFGAIVFVLWLGAHDVLA 247
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
680-1186 |
4.64e-12 |
|
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: 70.21 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 680 LRLLKmnRPEWKQ----ALLGCVGAVVFGAVLPLYSYSLGSLPEVyfladdgqirskTRLYYFLFLGIAVVCITANIVQH 755
Cdd:COG4615 4 LRLLL--RESRWLlllaLLLGLLSGLANAGLIALINQALNATGAA------------LARLLLLFAGLLVLLLLSRLASQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 756 YNFAVMGERLTERVRGQMLAKILS-----FE-VGwfdedensSAAVCARLaTQSSKVRSLVGDRMCLLVQAGATASLGFS 829
Cdd:COG4615 70 LLLTRLGQHAVARLRLRLSRRILAaplerLErIG--------AARLLAAL-TEDVRTISQAFVRLPELLQSVALVLGCLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 830 -LALaVSWRLATVMMAMQPLIIASFYFKkvlmaamsKKAKKAQVQGSQLASEAVVNH-RTIT------AFSSQRRmLRLY 901
Cdd:COG4615 141 yLAW-LSPPLFLLTLVLLGLGVAGYRLL--------VRRARRHLRRAREAEDRLFKHfRALLegfkelKLNRRRR-RAFF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 902 E-----AAQQGPKKDNVAHSWFsgfcLCLCQFSNT---GSMAVALWYGGKLmakGLITPTHLFQ-VFFMLMTMGRVIADA 972
Cdd:COG4615 211 DedlqpTAERYRDLRIRADTIF----ALANNWGNLlffALIGLILFLLPAL---GWADPAVLSGfVLVLLFLRGPLSQLV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 973 GSLTSdLAQGGDAVRSvLDTLDREPTiKDDDNDNERKKKKRKEIKGAIEFKNVHFSYPTRPEvavLAGF-----SLEIGA 1047
Cdd:COG4615 284 GALPT-LSRANVALRK-IEELELALA-AAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDG---DEGFtlgpiDLTIRR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1048 GKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGTirdniaYGAAEEhATE 1127
Cdd:COG4615 358 GELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGLDGE-ADP 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 1128 DEVaraaalanaHGFISAMERGYDTRVgERGA----QLSGGQRQRIALARAVLKDARILLLDE 1186
Cdd:COG4615 431 ARA---------RELLERLELDHKVSV-EDGRfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1034-1240 |
5.18e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 5.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1034 EVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYS---LARLRSQVALVSQEPTLfSG 1110
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYA-SL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1111 TIRDNIAYGAAEEhatedevaraaalANAHGFI---SAMER--GYDTRVGERGA-------QLSGGQRQRIALARAVLKD 1178
Cdd:PRK10261 415 DPRQTVGDSIMEP-------------LRVHGLLpgkAAAARvaWLLERVGLLPEhawryphEFSGGQRQRICIARALALN 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 1179 ARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERG 1240
Cdd:PRK10261 482 PKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1027-1217 |
5.39e-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: 67.43 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1027 FSYPTRpeVAVLAGFSLEIGAG-----KTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIrSYSLARLRSQvalv 1101
Cdd:cd03237 1 YTYPTM--KKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKAD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1102 sqeptlFSGTIRD---NIAYGAAEEHATEDEVARAAAlanahgfisaMERGYDTRVGErgaqLSGGQRQRIALARAVLKD 1178
Cdd:cd03237 74 ------YEGTVRDllsSITKDFYTHPYFKTEIAKPLQ----------IEQILDREVPE----LSGGELQRVAIAACLSKD 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1002260479 1179 ARILLLDEATSALDAASERLVQDAVDR--MLRGRTCVVVAH 1217
Cdd:cd03237 134 ADIYLLDEPSAYLDVEQRLMASKVIRRfaENNEKTAFVVEH 174
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
493-588 |
5.40e-12 |
|
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: 70.10 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 493 ETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAeserTVQ----DALD--RASVGRTTVIVAHRLSTLRK 566
Cdd:COG4172 147 ERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaqilDLLKdlQRELGMALLLITHDLGVVRR 222
|
90 100
....*....|....*....|...
gi 1002260479 567 -ADTIAVLDAGRVVEAGTHDELL 588
Cdd:COG4172 223 fADRVAVMRQGEIVEQGPTAELF 245
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
367-588 |
5.48e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.49 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 367 KDVHFSYPSRPdtlVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVS 446
Cdd:PRK13548 6 RNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 447 QEPVL-FATSIRENILFG-----DETASLKQVVAAAkMAnahefIVKLPHgYEthvGQFGTQLSGGQKQRIAIARALVR- 519
Cdd:PRK13548 83 QHSSLsFPFTVEEVVAMGraphgLSRAEDDALVAAA-LA-----QVDLAH-LA---GRDYPQLSGGEQQRVQLARVLAQl 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 520 -----DPRILLLDEATSALD-AESERTVQDALDRASVGRTTVI-VAHRLS-TLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:PRK13548 153 wepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHERGLAVIvVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1034-1248 |
6.17e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.91 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1034 EVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQ--RGSVLVDGEDIRSYSLARlrsqVALVSQEPTLFSG- 1110
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKR----TGFVTQDDILYPHl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1111 TIRDNIAYGAA---EEHATEDEVARAAALANAHGFISAMErgyDTRVGE---RGaqLSGGQRQRIALARAVLKDARILLL 1184
Cdd:PLN03211 156 TVRETLVFCSLlrlPKSLTKQEKILVAESVISELGLTKCE---NTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 1185 DEATSALDA-ASERLVQDAVDRMLRGRTCVVVAHRLST--VEKSDTIAVVKDGRVAERGRHHELLAV 1248
Cdd:PLN03211 231 DEPTSGLDAtAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMAY 297
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
368-616 |
7.72e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.34 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 368 DVHFSYPSRPdtlVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGID--TLNVEWLRSQIGLV 445
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDysKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 446 SQEP--VLFATSIRENILFgdetaSLKQV-VAAAKMANAHEFIVKLPHGyeTHVGQFGTQ-LSGGQKQRIAIARALVRDP 521
Cdd:PRK13638 83 FQDPeqQIFYTDIDSDIAF-----SLRNLgVPEAEITRRVDEALTLVDA--QHFRHQPIQcLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 522 RILLLDEATSALDAESeRTVQDALDR--ASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDELLG----MDDGG 594
Cdd:PRK13638 156 RYLLLDEPTAGLDPAG-RTQMIAIIRriVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFActeaMEQAG 234
|
250 260
....*....|....*....|..
gi 1002260479 595 EGGVYARMVHLQKAPPVAAREE 616
Cdd:PRK13638 235 LTQPWLVKLHTQLGLPLCKTET 256
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1032-1198 |
9.60e-12 |
|
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: 65.46 E-value: 9.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1032 RPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQ---EPTLf 1108
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLpglKPEL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1109 sgTIRDNIAYGAAEeHATEDEVARAAAlanahgfisamergydTRVGERG------AQLSGGQRQRIALARAVLKDARIL 1182
Cdd:TIGR01189 89 --SALENLHFWAAI-HGGAQRTIEDAL----------------AAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLW 149
|
170
....*....|....*.
gi 1002260479 1183 LLDEATSALDAASERL 1198
Cdd:TIGR01189 150 ILDEPTTALDKAGVAL 165
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
739-975 |
1.10e-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: 350020 [Multi-domain] Cd Length: 289 Bit Score: 67.12 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 739 LFLGIAVVCITANIVQHYNFAVMGERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCLLV 818
Cdd:cd18576 41 LLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHE--RRVGELTSRLSNDVTQIQDTLTTTLAEFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 819 QAGATASLGFSLALAVSWRLATVMMAMQPLIIASF-----YFKKVlmaamskkakKAQVQgSQLAS------EAVVNHRT 887
Cdd:cd18576 119 RQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAvlfgrRIRKL----------SKKVQ-DELAEantiveETLQGIRV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 888 ITAFSS--------QRRMLRLYEAAQQGPKkdnvAHSWFSGFClclcQFSNTGSMAVALWYGGKLMAKGLITPTHLFQVF 959
Cdd:cd18576 188 VKAFTRedyeieryRKALERVVKLALKRAR----IRALFSSFI----IFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFL 259
|
250
....*....|....*.
gi 1002260479 960 FMLMTMGRVIADAGSL 975
Cdd:cd18576 260 LYTLFIAGSIGSLADL 275
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
502-630 |
1.27e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.42 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALD--RASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRV 578
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQqlQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHA 240
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 579 VEAGTHDEllgmddggeggVYARMVH-----LQKAPPVA-AREERHRAVDVVESEMVS 630
Cdd:PRK15079 241 VELGTYDE-----------VYHNPLHpytkaLMSAVPIPdPDLERNKTIQLLEGELPS 287
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
378-588 |
1.46e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.19 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 378 DTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVL-FATSI 456
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 457 RE---------NILFGDETASLKQVVAAAkMAnahefivklphgyETHVGQFG----TQLSGGQKQRIAIARALVRDPRI 523
Cdd:PRK11231 94 RElvaygrspwLSLWGRLSAEDNARVNQA-ME-------------QTRINHLAdrrlTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 524 LLLDEATSALDAESERTVQDAL-DRASVGRTTVIVAHRLS-TLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMrELNTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1032-1203 |
1.65e-11 |
|
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: 64.82 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1032 RPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGT 1111
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1112 IRDNIAYGAAeEHATEdevaraaalanahgfisAMERGYDtRVGERG------AQLSGGQRQRIALARAVLKDARILLLD 1185
Cdd:cd03231 90 VLENLRFWHA-DHSDE-----------------QVEEALA-RVGLNGfedrpvAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170
....*....|....*...
gi 1002260479 1186 EATSALDAASERLVQDAV 1203
Cdd:cd03231 151 EPTTALDKAGVARFAEAM 168
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
491-578 |
2.18e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.85 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 491 GYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLS-TLRKA 567
Cdd:PRK11247 122 GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMA 201
|
90
....*....|.
gi 1002260479 568 DTIAVLDAGRV 578
Cdd:PRK11247 202 DRVLLIEEGKI 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1038-1244 |
2.37e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.90 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1038 LAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDI---RSYSLARLRSQVALVSQEP-TLFSGTIR 1113
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1114 DNIAYGAAEEHATEDEVARAAAlanahgfiSAMER-GYDTRVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALD 1192
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIRRRVS--------AALDKvGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1193 AA-SERLVQ--DAVDRMlrGRTCVVVAHRLSTVEKSD-TIAVVKDGRVAErGRHHE 1244
Cdd:PRK10908 170 DAlSEGILRlfEEFNRV--GVTVLMATHDIGLISRRSyRMLTLSDGHLHG-GVGGE 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
417-578 |
2.69e-11 |
|
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: 63.61 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 417 SPDSGEISMDDHGIDTLNV-EWLRSQIGLVSQEPV---LFAT-SIRENILFGDetaslkqvvaaakmanahefivklphg 491
Cdd:cd03215 51 PPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRKregLVLDlSVAENIALSS--------------------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 492 yethvgqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVahrLST-----LRK 566
Cdd:cd03215 104 ----------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLL---ISSeldelLGL 170
|
170
....*....|..
gi 1002260479 567 ADTIAVLDAGRV 578
Cdd:cd03215 171 CDRILVMYEGRI 182
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
415-528 |
2.74e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.05 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 415 FY------SPDSGEISMDDHGIDTLNVeWLRSQ--IGLVSQEPVLFAT-SIRENILFGDETASLKQVVAAAKMAN-AHEF 484
Cdd:COG1137 46 FYmivglvKPDSGRIFLDGEDITHLPM-HKRARlgIGYLPQEASIFRKlTVEDNILAVLELRKLSKKEREERLEElLEEF 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1002260479 485 -IvklphgyeTHV-GQFGTQLSGGQKQRIAIARALVRDPRILLLDE 528
Cdd:COG1137 125 gI--------THLrKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1020-1186 |
3.55e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.30 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRpevavlaGFS-----LEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARL 1094
Cdd:PRK10522 323 LELRNVTFAYQDN-------GFSvgpinLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1095 RSQVALVSQEPTLFS------GTIRDNIAYGAAEEHatedeVARAAALANAHGFISAMergydtrvgergaQLSGGQRQR 1168
Cdd:PRK10522 396 RKLFSAVFTDFHLFDqllgpeGKPANPALVEKWLER-----LKMAHKLELEDGRISNL-------------KLSKGQKKR 457
|
170
....*....|....*...
gi 1002260479 1169 IALARAVLKDARILLLDE 1186
Cdd:PRK10522 458 LALLLALAEERDILLLDE 475
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1020-1240 |
4.75e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.11 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVA---VLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYS-LARLR 1095
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1096 SQVALVSQEP--TLFSGTIRDNIAYGAAEEHATEDEVARAAAlanahgfiSAMER--GYDTRvgeRGAQ--LSGGQRQRI 1169
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENLGIPPEEIRERVD--------ESLKKvgMYEYR---RHAPhlLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 1170 ALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTVEKSDTIAVVKDGRVAERG 1240
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1048-1231 |
5.54e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1048 GKTVALVGPSGSGKSTVI---------------------GLIERFydaqRGSVLVDgedirsYsLARLRSQ---VAL--- 1100
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVkilsgelipnlgdyeeepswdEVLKRF----RGTELQN------Y-FKKLYNGeikVVHkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1101 -VSQEPTLFSGTIRDNIAygAAEEHATEDEVARAAalanahGFISAMERGYDtrvgergaQLSGGQRQRIALARAVLKDA 1179
Cdd:PRK13409 168 yVDLIPKVFKGKVRELLK--KVDERGKLDEVVERL------GLENILDRDIS--------ELSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 1180 RILLLDEATSALDaASERL-VQDAVDRMLRGRTCVVVAHRLSTVEK-SDTIAVV 1231
Cdd:PRK13409 232 DFYFFDEPTSYLD-IRQRLnVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
501-592 |
5.61e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.56 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 501 TQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLSTLRK-ADTIAVLDAGR 577
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlvRELGLAVVIVTHDLAVARLlAHRLLVMKQGR 229
|
90
....*....|....*
gi 1002260479 578 VVEAGTHDELLgmDD 592
Cdd:PRK11701 230 VVESGLTDQVL--DD 242
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1042-1240 |
6.10e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.18 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1042 SLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARL---------RSQVALVSQEPtlfsgti 1112
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHP------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1113 RD----------NIA----------YGAAEEHATEdevaraaalanahgFISAMERGYDtRVGERGAQLSGGQRQRIALA 1172
Cdd:PRK11701 99 RDglrmqvsaggNIGerlmavgarhYGDIRATAGD--------------WLERVEIDAA-RIDDLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 1173 RAVLKDARILLLDEATSALDAAserlVQDAVDRMLRGRT------CVVVAHRLSTVEK-SDTIAVVKDGRVAERG 1240
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVS----VQARLLDLLRGLVrelglaVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1040-1231 |
7.77e-11 |
|
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: 66.35 E-value: 7.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1040 GFSL----EIGAGKTVALVGPSGSGKSTVIGL---------------------IERFydaqRGSVLVDgedirsYsLARL 1094
Cdd:COG1245 87 GFRLyglpVPKKGKVTGILGPNGIGKSTALKIlsgelkpnlgdydeepswdevLKRF----RGTELQD------Y-FKKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1095 RSQ---VAL----VSQEPTLFSGTIRDNIAygAAEEHATEDEVARAAalanahgfisAMERGYDTRVGErgaqLSGGQRQ 1167
Cdd:COG1245 156 ANGeikVAHkpqyVDLIPKVFKGTVRELLE--KVDERGKLDELAEKL----------GLENILDRDISE----LSGGELQ 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1168 RIALARAVLKDARILLLDEATSALDaASERLvqdAVDRMLR-----GRTCVVVAHRLSTVEK-SDTIAVV 1231
Cdd:COG1245 220 RVAIAAALLRDADFYFFDEPSSYLD-IYQRL---NVARLIRelaeeGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1036-1246 |
9.24e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 9.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1036 AVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQ--------RGSVLVDGEDIRSYS---LARLRSQVALVSQE 1104
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDaprLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1105 PTLFSgtIRDNIAYGAAEEHATEDEVARAAALANAHgfisAMER-GYDTRVGERGAQLSGGQRQRIALARAVLK------ 1177
Cdd:PRK13547 95 AFAFS--AREIVLLGRYPHARRAGALTHRDGEIAWQ----ALALaGATALVGRDVTTLSGGELARVQFARVLAQlwpphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 1178 ---DARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVA--HRLSTVEK-SDTIAVVKDGRVAERGRHHELL 1246
Cdd:PRK13547 169 aaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAivHDPNLAARhADRIAMLADGAIVAHGAPADVL 243
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
503-582 |
1.07e-10 |
|
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: 62.54 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 503 LSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAH--RLSTLRKADTIAVLDAGRVV 579
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIV 184
|
...
gi 1002260479 580 EAG 582
Cdd:cd03217 185 KSG 187
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
694-965 |
1.17e-10 |
|
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: 63.98 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 694 LLGCVGAVVFGAVLPLYSYSLGslpevyFLADDGQIRSKTRLYYFLFLGIAVVCITANI---VQHYNFAVMGERLTERVR 770
Cdd:cd18552 2 ALAILGMILVAATTAALAWLLK------PLLDDIFVEKDLEALLLVPLAIIGLFLLRGLasyLQTYLMAYVGQRVVRDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 771 GQMLAKILSFEVGWFdeDENSSAAVCARLATQSSKVRSLVGDRMCLLVQAGATASLGFSLALAVSWRLATVMMAMQPLII 850
Cdd:cd18552 76 NDLFDKLLRLPLSFF--DRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 851 ASFYF--KKVLMAAMSKKAKKAQVqgSQLASEAVVNHRTITAFSSQRRMLRLYEAAQQGPKKDNVAHSWFSGFCLCLCQF 928
Cdd:cd18552 154 LPIRRigKRLRKISRRSQESMGDL--TSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMEL 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 1002260479 929 SNTGSMAVALWYGGKLMAKGLITPTHLFqVFFMLMTM 965
Cdd:cd18552 232 LGAIAIALVLWYGGYQVISGELTPGEFI-SFITALLL 267
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
416-583 |
1.51e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 62.78 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 416 YSPDSGEISMDDHGIDTLNVEwLRSQ--IGLVSQEPVLF------------ATSIRENILfgDETASLKQVVAAAKMana 481
Cdd:COG0396 52 YEVTSGSILLDGEDILELSPD-ERARagIFLAFQYPVEIpgvsvsnflrtaLNARRGEEL--SAREFLKLLKEKMKE--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 482 hefiVKLPHGY---ETHVGqfgtqLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIV 557
Cdd:COG0396 126 ----LGLDEDFldrYVNEG-----FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKlRSPDRGILII 196
|
170 180
....*....|....*....|....*...
gi 1002260479 558 AH--RLSTLRKADTIAVLDAGRVVEAGT 583
Cdd:COG0396 197 THyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
499-588 |
1.61e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 499 FGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALD--RASVGRTTVIVAHRLSTLRK-ADTIAVLDA 575
Cdd:PRK15134 153 YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQN 232
|
90
....*....|...
gi 1002260479 576 GRVVEAGTHDELL 588
Cdd:PRK15134 233 GRCVEQNRAATLF 245
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
382-579 |
1.71e-10 |
|
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: 62.48 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 382 LNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLrsqigLVSQEPVLFA-TSIRENI 460
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 461 -LFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQfgtqLSGGQKQRIAIARALVRDPRILLLDEATSALDAESER 539
Cdd:TIGR01184 76 aLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002260479 540 TVQDALDR--ASVGRTTVIVAHRLSTlrkadtiAVLDAGRVV 579
Cdd:TIGR01184 152 NLQEELMQiwEEHRVTVLMVTHDVDE-------ALLLSDRVV 186
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1033-1239 |
1.76e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1033 PEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDiRSYSLARlRSQVALVS---QEPTLFS 1109
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE-VTFNGPK-SSQEAGIGiihQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1110 G-TIRDNI--------AYGA---AEEHATEDEVARAAAlanahgfisaMERGYDTRVGErgaqLSGGQRQRIALARAVLK 1177
Cdd:PRK10762 93 QlTIAENIflgrefvnRFGRidwKKMYAEADKLLARLN----------LRFSSDKLVGE----LSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 1178 DARILLLDEATSAL-DAASERLVQdaVDRMLRGRTC--VVVAHRLSTV-EKSDTIAVVKDGR-VAER 1239
Cdd:PRK10762 159 ESKVIIMDEPTDALtDTETESLFR--VIRELKSQGRgiVYISHRLKEIfEICDDVTVFRDGQfIAER 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
367-579 |
2.17e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.13 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 367 KDVHFSYPSRPDTL-VLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWL----RSQ 441
Cdd:PRK10535 8 KDIRRSYPSGEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 442 IGLVSQEPVLFA-TSIRENIlfgDETASLKQVVAAAKMANAHEFIVKLphGYETHVGQFGTQLSGGQKQRIAIARALVRD 520
Cdd:PRK10535 88 FGFIFQRYHLLShLTAAQNV---EVPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 521 PRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLSTLRKADTIAVLDAGRVV 579
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1031-1238 |
2.30e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.81 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1031 TRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDA--QRGSVLVDGE-----DIRSySLAR----LRSQVA 1099
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGEvcrfkDIRD-SEALgiviIHQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVsqePTLfsgTIRDNIAYGaaEEHATedevaraaalanaHGFISAMERGYDT-----RVG------ERGAQLSGGQRQR 1168
Cdd:NF040905 89 LI---PYL---SIAENIFLG--NERAK-------------RGVIDWNETNRRArellaKVGldespdTLVTDIGVGKQQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1169 IALARAVLKDARILLLDEATSAL-DAASERLvqdaVDRML----RGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAE 1238
Cdd:NF040905 148 VEIAKALSKDVKLLILDEPTAALnEEDSAAL----LDLLLelkaQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
501-583 |
3.20e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.34 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 501 TQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALD--RASVGRTTVIVAHRLS-TLRKADTIAVLDAGR 577
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGH 230
|
....*.
gi 1002260479 578 VVEAGT 583
Cdd:PRK09984 231 VFYDGS 236
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
72-293 |
3.22e-10 |
|
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: 62.53 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 72 KFALRLLYVAVAVGACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDAAPSSpsspqaqaqattfRVISTVSDDA 151
Cdd:cd18573 42 TFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTG-------------ELVSRLSSDT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 152 DAIQDFLGEKLPMVLANATLFFGALAVSFVFAWRLALAGLPFTLLLFVTpSVLLAGRMAAAAGEARAAYEEAGGIAQQAV 231
Cdd:cd18573 109 SVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVG-AVFYGRYVRKLSKQVQDALADATKVAEERL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 232 SSIRTVASYTAERRTVERFRGAVARSAALGVRQGLIKGAVIGSMGVIYAVwSFLS--WIGSLLV 293
Cdd:cd18573 188 SNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNL-SLLSvlYYGGSLV 250
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
418-581 |
3.32e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.43 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTLN---VEWLRSQIGLVSQEP-VLFATSIREN-----ILFGDETASLKQVVAAAkmanahefIVKL 488
Cdd:PRK10908 54 PSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHhLLMDRTVYDNvaiplIIAGASGDDIRRRVSAA--------LDKV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 489 phGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALD-AESERTVQDALDRASVGRTTVIVAHRLSTL-RK 566
Cdd:PRK10908 126 --GLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdALSEGILRLFEEFNRVGVTVLMATHDIGLIsRR 203
|
170
....*....|....*
gi 1002260479 567 ADTIAVLDAGRVVEA 581
Cdd:PRK10908 204 SYRMLTLSDGHLHGG 218
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
77-295 |
3.46e-10 |
|
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: 62.45 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 77 LLYVAVAV--GACSFLEGLCWTRTAERQASKMR-RLYlEAVLSQEVAFFDaapsspsspqaqaQATTFRVISTVSDDADA 153
Cdd:cd18542 43 LLILGVALlrGVFRYLQGYLAEKASQKVAYDLRnDLY-DHLQRLSFSFHD-------------KARTGDLMSRCTSDVDT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 154 IQDFLGEKLPMVLANATLFFGALAVSFVFAWRLALAGLPFTLLLFVTpSVLLAGRMAAAAGEARAAYEEAGGIAQQAVSS 233
Cdd:cd18542 109 IRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALF-SYVFFKKVRPAFEEIREQEGELNTVLQENLTG 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 234 IRTVASYTAERRTVERFRGAVARSAALGVRQGLIKGAVIGSMGVI-YAVWSFLSWIGSLLVIH 295
Cdd:cd18542 188 VRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLsGLQIVLVLWVGGYLVIN 250
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
362-578 |
4.02e-10 |
|
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: 62.18 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 362 GEIVFKDVHFSYpSRPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDsGEISMDDHGIDTLNVEWLRSQ 441
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 442 IGLVSQEPVLFATSIRENiLFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDP 521
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKN-LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 522 RILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAGRV 578
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1037-1237 |
4.09e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.88 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1037 VLAGFSLEIGAGKTVALVGPSGSGKS----TVIGLierfYDAQRGSVLVDGE--DIRSYSlARLRSQVALVSQE------ 1104
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTelarALFGA----DPADSGEIRLDGKpvRIRSPR-DAIRAGIAYVPEDrkgegl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1105 -PTLfsgTIRDNIAYGAAEEHATedevaraaalanaHGFIS-AMER---------------GYDTRVGergaQLSGGQRQ 1167
Cdd:COG1129 342 vLDL---SIRENITLASLDRLSR-------------GGLLDrRRERalaeeyikrlriktpSPEQPVG----NLSGGNQQ 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1168 RIALARAVLKDARILLLDEATSALD--AASE--RLVQDAVDrmlRGRTCVVVahrlST-----VEKSDTIAVVKDGRVA 1237
Cdd:COG1129 402 KVVLAKWLATDPKVLILDEPTRGIDvgAKAEiyRLIRELAA---EGKAVIVI----SSelpelLGLSDRILVMREGRIV 473
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1040-1235 |
7.57e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.16 E-value: 7.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1040 GFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDI--------------RSYSLARLRSQVA-----L 1100
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFQHVRLFREMTvienlL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1101 VSQ----EPTLFSGTIRdNIAYGAAEEHATEDEVARaaalanahgfisaMERGYDTRVGERGA-QLSGGQRQRIALARAV 1175
Cdd:PRK11300 103 VAQhqqlKTGLFSGLLK-TPAFRRAESEALDRAATW-------------LERVGLLEHANRQAgNLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 1176 LKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTV-EKSDTIAVVKDGR 1235
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVmGISDRIYVVNQGT 231
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
503-588 |
8.19e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.14 E-value: 8.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 503 LSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLST--LRKADTIAVLDAGRVV 579
Cdd:TIGR00955 167 LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSelFELFDKIILMAEGRVA 246
|
....*....
gi 1002260479 580 EAGTHDELL 588
Cdd:TIGR00955 247 YLGSPDQAV 255
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
758-989 |
9.67e-10 |
|
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: 61.17 E-value: 9.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 758 FAVMGERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCL----LVQAGATASLGFSLala 833
Cdd:cd18784 60 FTLAMARLNIRIRNLLFRSIVSQEIGFFDT--VKTGDITSRLTSDTTTMSDTVSLNLNIflrsLVKAIGVIVFMFKL--- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 834 vSWRLATVMMAMQPLI--IASFY---FKKVlmaamskkakKAQVQGS-----QLASEAVVNHRTITAFSSQRRMLRLYEA 903
Cdd:cd18784 135 -SWQLSLVTLIGLPLIaiVSKVYgdyYKKL----------SKAVQDSlakanEVAEETISSIRTVRSFANEDGEANRYSE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 904 AQQGPKKDNVAHSWFSGFCLCLCQFSNTGSMAVALWYGGKLMAKGLITPTHLFQVFFMLMTMGRVIADAGSLTSDLAQGG 983
Cdd:cd18784 204 KLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAV 283
|
....*.
gi 1002260479 984 DAVRSV 989
Cdd:cd18784 284 GAAEKV 289
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1035-1253 |
1.03e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.22 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1035 VAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIerfydA-----QRGSVLVDGEDIRSyslARLRSQV----ALVSQ-- 1103
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-----AgarkiQQGRVEVLGGDMAD---ARHRRAVcpriAYMPQgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1104 ----EPTLfsgTIRDNIAY-------GAAEEHATEDEVAraaalanahgfisamergydTRVG-----ERGA-QLSGGQR 1166
Cdd:NF033858 86 gknlYPTL---SVFENLDFfgrlfgqDAAERRRRIDELL--------------------RATGlapfaDRPAgKLSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1167 QRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRT--CVVVAhrlsT-----VEKSDTIAVVKDGRVAER 1239
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmSVLVA----TaymeeAERFDWLVAMDAGRVLAT 218
|
250
....*....|....
gi 1002260479 1240 GRHHELLAVGRAGT 1253
Cdd:NF033858 219 GTPAELLARTGADT 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
494-582 |
1.09e-09 |
|
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: 59.98 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 494 THVG-QFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVA-H--RLSTLRKADT 569
Cdd:cd03234 134 TRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTiHqpRSDLFRLFDR 213
|
90
....*....|...
gi 1002260479 570 IAVLDAGRVVEAG 582
Cdd:cd03234 214 ILLLSSGEIVYSG 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
502-587 |
1.17e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.78 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDA--------ESERtvqdaLDRaSVGRTTVIVAH---RLSTLrkADTI 570
Cdd:PRK11650 134 ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAklrvqmrlEIQR-----LHR-RLKTTSLYVTHdqvEAMTL--ADRV 205
|
90
....*....|....*..
gi 1002260479 571 AVLDAGRVVEAGTHDEL 587
Cdd:PRK11650 206 VVMNGGVAEQIGTPVEV 222
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
74-295 |
1.23e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 60.99 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 74 ALRLLYVAVAVGACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDAAPSSPsspqaqaqattfrVISTVSDDADA 153
Cdd:cd18564 57 AAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGD-------------LLSRLTGDVGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 154 IQDFLGEKLPMVLANATLFFGALAVSFVFAWRLALAGLPFTLLLFVTpSVLLAGRMAAAAGEARAAYEEAGGIAQQAVSS 233
Cdd:cd18564 124 IQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLA-ARRFSRRIKEASREQRRREGALASVAQESLSA 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 234 IRTVASYTAERRTVERFRGAVARSAALGVRQGLIKGAVIGSMGVIYAVWSFLS-WIGSLLVIH 295
Cdd:cd18564 203 IRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVlWFGAWLVLA 265
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
485-577 |
1.45e-09 |
|
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: 57.84 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 485 IVKLPHGYEthVGQFgTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALdrASVGRTTVIVAHRLSTL 564
Cdd:cd03221 56 IVTWGSTVK--IGYF-EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL--KEYPGTVILVSHDRYFL 130
|
90
....*....|....
gi 1002260479 565 RK-ADTIAVLDAGR 577
Cdd:cd03221 131 DQvATKIIELEDGK 144
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
502-588 |
1.50e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 60.10 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRAS--VGRTTVIVAHRL---STLrkADTIAVLDAG 576
Cdd:COG4604 135 ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDInfaSCY--ADHIVAMKDG 212
|
90
....*....|..
gi 1002260479 577 RVVEAGTHDELL 588
Cdd:COG4604 213 RVVAQGTPEEII 224
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
24-278 |
1.65e-09 |
|
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: 60.52 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 24 MALGVLGSFGdGMMQPLsmlVLGDIVNSyggaggagsarsaFSSGAVDKFALRLLYVAVAVGAcsFLEGLCW---TRTAE 100
Cdd:cd18551 5 LLLSLLGTAA-SLAQPL---LVKNLIDA-------------LSAGGSSGGLLALLVALFLLQA--VLSALSSyllGRTGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 101 RQASKMRRLYLEAVLSQEVAFFDAAPSSpsspqaqaqattfRVISTVSDDADAIQDFLGEKLPMVLANATLFFGALAVSF 180
Cdd:cd18551 66 RVVLDLRRRLWRRLLRLPVSFFDRRRSG-------------DLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 181 VFAWRLA---LAGLPFTLLLFVtpsvLLAGRMAAAAGEARAAYEEAGGIAQQAVSSIRTVASYTAERRTVERFRGAVARS 257
Cdd:cd18551 133 LLDWVLTlvtLAVVPLAFLIIL----PLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERL 208
|
250 260
....*....|....*....|.
gi 1002260479 258 AALGVRQGLIKGAVIGSMGVI 278
Cdd:cd18551 209 YRAGLKAAKIEALIGPLMGLA 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
501-582 |
1.91e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.64 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 501 TQLSGGQKQRIAIARALVRDPRILLLDEATSALDaeseRTVQD---ALDRASVGR---TTVIVAHRLSTLRK-ADTIAVL 573
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVL 499
|
....*....
gi 1002260479 574 DAGRVVEAG 582
Cdd:PRK15134 500 RQGEVVEQG 508
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
418-579 |
1.99e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.57 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTLNV-EWLRSQIGLVS----QEPVLFATSIRENILFgdetASLKQVV------AAAKMANAHEFIV 486
Cdd:COG1129 304 ADSGEIRLDGKPVRIRSPrDAIRAGIAYVPedrkGEGLVLDLSIRENITL----ASLDRLSrgglldRRRERALAEEYIK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 487 KL---PHGYETHVGQfgtqLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAhrlST 563
Cdd:COG1129 380 RLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI---SS 452
|
170 180
....*....|....*....|.
gi 1002260479 564 -----LRKADTIAVLDAGRVV 579
Cdd:COG1129 453 elpelLGLSDRILVMREGRIV 473
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1028-1236 |
2.72e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.20 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1028 SYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKS----TVIGLIErfydAQRGSVLVDGEDIRSYS-LARLRSQVALVS 1102
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSelaeALAGLRP----PASGSIRLDGEDITGLSpRERRRLGVAYIP 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1103 QE-------PTLfsgTIRDNIA----------------YGAAEEHATEdevaraaalanahgfisAMERgYDTRVGERGA 1159
Cdd:COG3845 340 EDrlgrglvPDM---SVAENLIlgryrrppfsrggfldRKAIRAFAEE-----------------LIEE-FDVRTPGPDT 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1160 ---QLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVahrLST-----VEKSDTIAVV 1231
Cdd:COG3845 399 parSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL---ISEdldeiLALSDRIAVM 475
|
....*
gi 1002260479 1232 KDGRV 1236
Cdd:COG3845 476 YEGRI 480
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1020-1247 |
2.89e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.42 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVH--FSYPT----RPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIrSYSLAR 1093
Cdd:PRK15112 5 LEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1094 LRSQ-VALVSQEPT-----------LFSGTIRDNIAYGAAEEHATEDEVARAAALANAH-GFISAMergydtrvgergaq 1160
Cdd:PRK15112 84 YRSQrIRMIFQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHaSYYPHM-------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1161 LSGGQRQRIALARAVLKDARILLLDEATSALDAAserLVQDAVDRML-----RGRTCVVVAHRLSTVEK-SDTIAVVKDG 1234
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMS---MRSQLINLMLelqekQGISYIYVTQHLGMMKHiSDQVLVMHQG 226
|
250
....*....|...
gi 1002260479 1235 RVAERGRHHELLA 1247
Cdd:PRK15112 227 EVVERGSTADVLA 239
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1024-1226 |
3.19e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1024 NVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSySLARLRSQVALVSQ 1103
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1104 E----PTLfsgTIRDNIAYgaaEEHATEDEVARAAALAnahgfISAMERGYDTRVGergaQLSGGQRQRIALARAVLKDA 1179
Cdd:PRK13540 82 RsginPYL---TLRENCLY---DIHFSPGAVGITELCR-----LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1002260479 1180 RILLLDEATSALDAAS-ERLVQDAVDRMLRGRTCVVVAHRLSTVEKSD 1226
Cdd:PRK13540 147 KLWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
439-603 |
3.30e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 439 RSQIGLVSQEPVLFAT-SIRENILFGDETASLKQVVAAAKMANAHEFI--VKLPHGYETHVGQFGtqlsGGQKQRIAIAR 515
Cdd:PRK13549 81 RAGIAIIHQELALVKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLaqLKLDINPATPVGNLG----LGQQQLVEIAK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 516 ALVRDPRILLLDEATSALDAESERTVQDAL-DRASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVeaGTHDellgMDDG 593
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIrDLKAHGIACIYISHKLNEVKAiSDTICVIRDGRHI--GTRP----AAGM 230
|
170
....*....|
gi 1002260479 594 GEGGVYARMV 603
Cdd:PRK13549 231 TEDDIITMMV 240
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
759-955 |
3.38e-09 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 59.48 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 759 AVMGERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVgdRMCL---LVQAGATASLGFSLALaVS 835
Cdd:cd18574 67 SVVGERVAARLRNDLFSSLLRQDIAFFDT--HRTGELVNRLTADVQEFKSSF--KQCVsqgLRSVTQTVGCVVSLYL-IS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 836 WRLATVMMAMQPLIIA--SFYFKKVLMAAMSKKAKKAQVQGsqLASEAVVNHRTITAFSSQRRMLRLYEAAQQGPKKDNV 913
Cdd:cd18574 142 PKLTLLLLVIVPVVVLvgTLYGSFLRKLSRRAQAQVAKATG--VADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNE 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1002260479 914 AhswfSGFCLCLCQ-FSNT--GSMA-VALWYGGKLMAKGLITPTHL 955
Cdd:cd18574 220 K----LGLGIGIFQgLSNLalNGIVlGVLYYGGSLVSRGELTAGDL 261
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
736-977 |
3.90e-09 |
|
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: 59.42 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 736 YYFLFLGIAVVCITANIVQHYNFAVMGERLTERVRGQMLAKILSFEVGWFdeDENSSAAVCARLATQSSKVRSLVGDRMC 815
Cdd:cd18575 38 AFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFF--ETTRTGEVLSRLTTDTTLIQTVVGSSLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 816 LLVQAGATASLGFSLALAVSWRLATVMMAMQPLIIASFYF--KKVLMAAMSKKAKKAQVqgSQLASEAVVNHRTITAFSS 893
Cdd:cd18575 116 IALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILfgRRVRRLSRASQDRLADL--SAFAEETLSAIKTVQAFTR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 894 QRRMLRLY----EAAQQGPKKDNVAHSWFSGFCLCLCQfsntGSMAVALWYGGKLMAKGLITPTHLFQ-VFFMLMTmgrv 968
Cdd:cd18575 194 EDAERQRFatavEAAFAAALRRIRARALLTALVIFLVF----GAIVFVLWLGAHDVLAGRMSAGELSQfVFYAVLA---- 265
|
....*....
gi 1002260479 969 iadAGSLTS 977
Cdd:cd18575 266 ---AGSVGA 271
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
333-588 |
5.38e-09 |
|
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: 61.08 E-value: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 333 AASRMQEMIEMlPPLEGAEKKGATMERIRGEIVFKDVHFS--YPSRPDTLV--------------LNGFNLTISEGATVG 396
Cdd:TIGR01271 1171 SVSRVFKFIDL-PQEEPRPSGGGGKYQLSTVLVIENPHAQkcWPSGGQMDVqgltakyteagravLQDLSFSVEGGQRVG 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 397 LVGGSGSGKSTVISLLQRFYSPDsGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENiLFGDETASLKQVVAAA 476
Cdd:TIGR01271 1250 LLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN-LDPYEQWSDEEIWKVA 1327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 477 KMANAHEFIVKLPHGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVI 556
Cdd:TIGR01271 1328 EEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVIL 1407
|
250 260 270
....*....|....*....|....*....|..
gi 1002260479 557 VAHRLSTLRKADTIAVLDAGRVVEAGTHDELL 588
Cdd:TIGR01271 1408 SEHRVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
403-587 |
6.66e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 58.58 E-value: 6.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 403 SGKSTVISLLQRFYSPDSGEISMDDHGIDTLNvewlRSQIGLVSQEPVLFA-TSIRENILFgdeTASLKQVVAAAKMANA 481
Cdd:COG4152 38 AGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYPkMKVGEQLVY---LARLKGLSKAEAKRRA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 482 HEFIVKLphgyetHVGQFGT----QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDAL-DRASVGRTTVI 556
Cdd:COG4152 111 DEWLERL------GLGDRANkkveELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIrELAAKGTTVIF 184
|
170 180 190
....*....|....*....|....*....|..
gi 1002260479 557 VAHRLSTL-RKADTIAVLDAGRVVEAGTHDEL 587
Cdd:COG4152 185 SSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
455-585 |
6.79e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.80 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 455 SIRENILFGDETASLKQVVAAAKMANAHEFI--VKLPHGYETHVGQFGTqlsgGQKQRIAIARALVRDPRILLLDEATSA 532
Cdd:NF040905 94 SIAENIFLGNERAKRGVIDWNETNRRARELLakVGLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLILDEPTAA 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 533 L-DAESERTVQDALDRASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEagTHD 585
Cdd:NF040905 170 LnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE--TLD 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1042-1240 |
7.15e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 58.36 E-value: 7.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1042 SLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSyslARLRSQVALVSQEPTL---FSGTIRDNIAY 1118
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLVAYVPQSEEVdwsFPVLVEDVVMM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1119 G-----------AAEEHATEDEVARAAAlanahgfisaMERGYDTRVGErgaqLSGGQRQRIALARAVLKDARILLLDEA 1187
Cdd:PRK15056 104 GryghmgwlrraKKRDRQIVTAALARVD----------MVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1188 TSALDAASE-RLVqdAVDRMLR--GRTCVVVAHRLSTVEKSDTIAVVKDGRVAERG 1240
Cdd:PRK15056 170 FTGVDVKTEaRII--SLLRELRdeGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1020-1248 |
7.61e-09 |
|
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: 59.82 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPtrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERF--YDAQRGSVL----------------- 1080
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1081 ----------------VDGEDIRSYSLARLRSQVALVSQEPTLFSG--TIRDNIaYGAAEEHATEDEvaraaalanahgf 1142
Cdd:TIGR03269 78 vgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNV-LEALEEIGYEGK------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1143 iSAMERGYD----TRVGER----GAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTC 1212
Cdd:TIGR03269 144 -EAVGRAVDliemVQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISM 222
|
250 260 270
....*....|....*....|....*....|....*..
gi 1002260479 1213 VVVAHRLSTVEKSDTIAV-VKDGRVAERGRHHELLAV 1248
Cdd:TIGR03269 223 VLTSHWPEVIEDLSDKAIwLENGEIKEEGTPDEVVAV 259
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
412-582 |
7.65e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.87 E-value: 7.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 412 LQRFYSPDSGEISMDDHGIDTLN---VEWLRSQIGLVSQEPvlFAT---------SIRE-----NILFGDEtaslkqvvA 474
Cdd:PRK10261 370 LLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDP--YASldprqtvgdSIMEplrvhGLLPGKA--------A 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 475 AAKMANAHEFIVKLPHgyetHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAE-SERTVQDALD-RASVGR 552
Cdd:PRK10261 440 AARVAWLLERVGLLPE----HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSiRGQIINLLLDlQRDFGI 515
|
170 180 190
....*....|....*....|....*....|.
gi 1002260479 553 TTVIVAHRLSTL-RKADTIAVLDAGRVVEAG 582
Cdd:PRK10261 516 AYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
738-973 |
9.32e-09 |
|
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: 58.21 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 738 FLFLGIAVVCITANIVQHYNFAVMGERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCLL 817
Cdd:cd18542 43 LLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDK--ARTGDLMSRCTSDVDTIRRFLAFGLVEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 818 VQAGATASLGFSLALAVSWRLATVMMAMQPLI--IASFYFKKVlmaamSKKAKKAQVQGSQLAS---EAVVNHRTITAFS 892
Cdd:cd18542 121 VRAVLLFIGALIIMFSINWKLTLISLAIIPFIalFSYVFFKKV-----RPAFEEIREQEGELNTvlqENLTGVRVVKAFA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 893 SQRRMLRLYEAAQQGPKKDNV----AHSWFSGFCLCLCQFsntgSMAVALWYGGKLMAKGLITPTHLFqVFFMLMTM--- 965
Cdd:cd18542 196 REDYEIEKFDKENEEYRDLNIklakLLAKYWPLMDFLSGL----QIVLVLWVGGYLVINGEITLGELV-AFISYLWMliw 270
|
250
....*....|...
gi 1002260479 966 -----GRVIADAG 973
Cdd:cd18542 271 pvrqlGRLINDMS 283
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1033-1235 |
9.59e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 9.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1033 PEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIR-SYSLARLRSQVALVSQEPTLF-SG 1110
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVlQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1111 TIRDNIAYGaaeehatedevaraaaLANAHGFISAMERGY-DTRV-----------GERGAQLSGGQRQRIALARAVLKD 1178
Cdd:PRK10982 89 SVMDNMWLG----------------RYPTKGMFVDQDKMYrDTKAifdeldididpRAKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 1179 ARILLLDEATSALdaaSERLVQD--AVDRMLRGRTC--VVVAHRLSTVEK-SDTIAVVKDGR 1235
Cdd:PRK10982 153 AKIVIMDEPTSSL---TEKEVNHlfTIIRKLKERGCgiVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1020-1234 |
1.17e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTrpeVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGediRSYSlaRLRSQVA 1099
Cdd:PRK09700 6 ISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN---INYN--KLDHKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 ------LVSQEPTLFSG-TIRDNIAYGaaeEHATED-------EVARAAALANAHGFISAMERGYDTRVGErgaqLSGGQ 1165
Cdd:PRK09700 78 aqlgigIIYQELSVIDElTVLENLYIG---RHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISH 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 1166 RQRIALARAVLKDARILLLDEATSAL-DAASERLVqdAVDRMLR--GRTCVVVAHRLSTVEK-SDTIAVVKDG 1234
Cdd:PRK09700 151 KQMLEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLF--LIMNQLRkeGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1032-1216 |
1.20e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1032 RPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRsyslaRLRSQVAlvsQEpTLFSG- 1110
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR-----RQRDEYH---QD-LLYLGh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1111 --------TIRDNIAYGAAEEHATEDEVAraaalanahgfISAMERgydtrVGERG------AQLSGGQRQRIALARAVL 1176
Cdd:PRK13538 82 qpgiktelTALENLRFYQRLHGPGDDEAL-----------WEALAQ-----VGLAGfedvpvRQLSAGQQRRVALARLWL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1002260479 1177 KDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVVVA 1216
Cdd:PRK13538 146 TRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILT 185
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1048-1231 |
1.84e-08 |
|
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: 56.99 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1048 GKTVALVGPSGSGKSTVIGLIE--------RFYDAQRGSVLVD---GEDIRSYsLARLRS-------QVALVSQEPTLFS 1109
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNY-FTKLLEgdvkvivKPQYVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1110 GTIRDNIAygAAEEHATEDEVARAAalanahGFISAMERGYDtrvgergaQLSGGQRQRIALARAVLKDARILLLDEATS 1189
Cdd:cd03236 105 GKVGELLK--KKDERGKLDELVDQL------ELRHVLDRNID--------QLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1002260479 1190 ALDaASERLVQDAVDRML--RGRTCVVVAHRLSTVEK-SDTIAVV 1231
Cdd:cd03236 169 YLD-IKQRLNAARLIRELaeDDNYVLVVEHDLAVLDYlSDYIHCL 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1037-1218 |
1.88e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1037 VLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLRSQVALVsqeptlfsGTIRDNI 1116
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRK--------GDFKDAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1117 AYGAAEehatedevaraaalanahGFISA--MERGYDtrvgergaQLSGGQRQRIALARAVLKDARILLLDEATSALDAA 1194
Cdd:COG2401 117 ELLNAV------------------GLSDAvlWLRRFK--------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*.
gi 1002260479 1195 SERLVQDAVDRMLR--GRTCVVVAHR 1218
Cdd:COG2401 171 TAKRVARNLQKLARraGITLVVATHH 196
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
381-579 |
1.90e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.02 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 381 VLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNvEWLRSQ-IGLVSQEPVL---FATSI 456
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRAKyIGRVFQDPMMgtaPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 457 RENILFGD---ETASLKQVVAAAKMANAHEFIVKLPHGYE----THVGqfgtQLSGGQKQRIAIARALVRDPRILLLDEA 529
Cdd:COG1101 100 EENLALAYrrgKRRGLRRGLTKKRRELFRELLATLGLGLEnrldTKVG----LLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 530 TSALDAESERTVQDALDRAsVGR---TTVIVAHRLS-TLRKADTIAVLDAGRVV 579
Cdd:COG1101 176 TAALDPKTAALVLELTEKI-VEEnnlTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
496-590 |
2.13e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.50 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 496 VGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVI--VAHRLSTLRK-ADTIAV 572
Cdd:PRK15093 152 MRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLSQwADKINV 231
|
90
....*....|....*...
gi 1002260479 573 LDAGRVVEAGTHDELLGM 590
Cdd:PRK15093 232 LYCGQTVETAPSKELVTT 249
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1020-1228 |
2.29e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.66 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRpevAVLAGFSLEIGAGKTVALVGPSGSGKST----VIGLIErfydAQRGSVLVDGEDIRSYSLARLR 1095
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTlvrvVLGLVA----PDEGVIKRNGKLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1096 SQVAL---VSQEPTLFSGTIRDNIaygaaeehatedevaraaalanahgfISAMERGYDTRVGERGAQ-LSGGQRQRIAL 1171
Cdd:PRK09544 78 LDTTLpltVNRFLRLRPGTKKEDI--------------------------LPALKRVQAGHLIDAPMQkLSGGETQRVLL 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1172 ARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVV--VAHRLSTV-EKSDTI 1228
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVlmVSHDLHLVmAKTDEV 191
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
418-588 |
2.51e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.72 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPvlfATSIRENILFG-------------DETASLKQVVAAAKMANAhef 484
Cdd:PRK15112 65 PTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STSLNPRQRISqildfplrlntdlEPEQREKQIIETLRQVGL--- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 485 ivkLPHgyetHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAeSERT--VQDALD-RASVGRTTVIVAHRL 561
Cdd:PRK15112 139 ---LPD----HASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM-SMRSqlINLMLElQEKQGISYIYVTQHL 210
|
170 180
....*....|....*....|....*...
gi 1002260479 562 STLRK-ADTIAVLDAGRVVEAGTHDELL 588
Cdd:PRK15112 211 GMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1020-1237 |
4.14e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.56 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVAVLAGFSLEIGAgkTVALVGPSGSGKSTVIGLIERFYDAQRGSVLvdgediRSyslARLRsqVA 1099
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDS--RIAMVGPNGIGKSTILKLISGELQPSSGTVF------RS---AKVR--MA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEptlfsgtirdniaygaaeeHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQ----------LSGGQRQRI 1169
Cdd:PLN03073 576 VFSQH-------------------HVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSRV 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1170 ALARAVLKDARILLLDEATSALDA-ASERLVQDAVdrMLRGRTCvVVAHRLSTVEKS-DTIAVVKDGRVA 1237
Cdd:PLN03073 637 AFAKITFKKPHILLLDEPSNHLDLdAVEALIQGLV--LFQGGVL-MVSHDEHLISGSvDELWVVSEGKVT 703
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
420-595 |
4.62e-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: 57.14 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 420 SGEISMDDHGIDTLNV-EWLRSQIGLVSQEPVLFAT-SIRENILFGDETASLKQVVAAAKMA-NAHEFI--VKLPHGYET 494
Cdd:TIGR02633 57 DGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVPElSVAENIFLGNEITLPGGRMAYNAMYlRAKNLLreLQLDADNVT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 495 -HVGQFGtqlsGGQKQRIAIARALVRDPRILLLDEATSAL-DAESERTVQDALDRASVGRTTVIVAHRLSTLRK-ADTIA 571
Cdd:TIGR02633 137 rPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTIC 212
|
170 180
....*....|....*....|....*....
gi 1002260479 572 VLDAGRVV-----EAGTHDELLGMDDGGE 595
Cdd:TIGR02633 213 VIRDGQHVatkdmSTMSEDDIITMMVGRE 241
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
24-337 |
4.78e-08 |
|
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: 55.89 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 24 MALGVLGSFGDGMMQPLSMLVLGDIVNSyggaggagsarsafssGAVDKFALRLLYVAVAV-------GACSFLEGLCWT 96
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDD----------------IFVEKDLEALLLVPLAIiglfllrGLASYLQTYLMA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 97 RTAERQASKMRRLYLEAVLSQEVAFFDAAPSSpsspqaqaqattfRVISTVSDDADAIQDFLGEKLPMVLANATLFFGAL 176
Cdd:cd18552 65 YVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSG-------------DLISRITNDVNQVQNALTSALTVLVRDPLTVIGLL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 177 AVSFVFAWRLALAGLpFTLLLFVTPSVLLAGRMAAAAGEARAAYEEAGGIAQQAVSSIRTVASYTAERRTVERFRGAVAR 256
Cdd:cd18552 132 GVLFYLDWKLTLIAL-VVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANER 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 257 SAALGVRQGLIKGA------VIGSMGViyavwSFLSWIGSLLVIHLHAQGGHvFVAsiciVLAGMSIMM----ALPNLRY 326
Cdd:cd18552 211 LRRLSMKIARARALssplmeLLGAIAI-----ALVLWYGGYQVISGELTPGE-FIS----FITALLLLYqpikRLSNVNA 280
|
330
....*....|..
gi 1002260479 327 FI-DATAAASRM 337
Cdd:cd18552 281 NLqRGLAAAERI 292
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
502-582 |
4.90e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.48 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRLSTL-RKADTIAVLDAGRV 578
Cdd:PRK10418 140 EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRI 219
|
....
gi 1002260479 579 VEAG 582
Cdd:PRK10418 220 VEQG 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
419-588 |
5.49e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 55.28 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 419 DSGEISMDDHGIDTLNV-EWLRSQIGLVSQEPVLFAT-SIRENILF-----GDETASLKQVVAAAKMANAHefIVKLPHg 491
Cdd:PRK10895 56 DAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlSVYDNLMAvlqirDDLSAEQREDRANELMEEFH--IEHLRD- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 492 yethvgQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAES----ERTVQDALDRasvGRTTVIVAHRL-STLRK 566
Cdd:PRK10895 133 ------SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISvidiKRIIEHLRDS---GLGVLITDHNVrETLAV 203
|
170 180
....*....|....*....|..
gi 1002260479 567 ADTIAVLDAGRVVEAGTHDELL 588
Cdd:PRK10895 204 CERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
442-543 |
5.93e-08 |
|
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: 56.87 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 442 IGLVSQEPVLFAT-SIRENI-------------------LFGDETASLKQVvaAAKMA---------NAHEFIVKL---- 488
Cdd:TIGR03719 70 VGYLPQEPQLDPTkTVRENVeegvaeikdaldrfneisaKYAEPDADFDKL--AAEQAelqeiidaaDAWDLDSQLeiam 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 489 -----PHGyETHVgqfgTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAES----ERTVQD 543
Cdd:TIGR03719 148 dalrcPPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1038-1241 |
7.20e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1038 LAGFSLEIGAGK-----TVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDgEDIrSYSLARLRSQvalvsqeptlFSGTI 1112
Cdd:PRK13409 350 LGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKI-SYKPQYIKPD----------YDGTV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1113 RDNIAyGAAEEHAT---EDEVAraaalanaHGFisAMERGYDTRVGErgaqLSGGQRQRIALARAVLKDARILLLDEATS 1189
Cdd:PRK13409 418 EDLLR-SITDDLGSsyyKSEII--------KPL--QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 1190 ALDaASERL-VQDAVDRMLRGR--TCVVVAHRLSTVEK-SDTIaVVKDGRVAERGR 1241
Cdd:PRK13409 483 HLD-VEQRLaVAKAIRRIAEEReaTALVVDHDIYMIDYiSDRL-MVFEGEPGKHGH 536
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1038-1241 |
7.27e-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: 56.72 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1038 LAGFSLEIGAGK-----TVALVGPSGSGKSTVI----GLIErfydAQRGSVlvdGEDIR-SYSLARLRSQvalvsqeptl 1107
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAkilaGVLK----PDEGEV---DEDLKiSYKPQYISPD---------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1108 FSGTIRDNIAYGAAEEHAT---EDEVARAAalanahgfisAMERGYDTRVGErgaqLSGGQRQRIALARAVLKDARILLL 1184
Cdd:COG1245 414 YDGTVEEFLRSANTDDFGSsyyKTEIIKPL----------GLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 1185 DEATSALDaASERL-VQDAVDRML--RGRTCVVVAHRLSTVEK-SDTIaVVKDGRVAERGR 1241
Cdd:COG1245 480 DEPSAHLD-VEQRLaVAKAIRRFAenRGKTAMVVDHDIYLIDYiSDRL-MVFEGEPGVHGH 538
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
409-558 |
7.50e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.11 E-value: 7.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 409 ISLLQRfysPDSGEISMDDHGIDTLNVewlRSQIGLVSQ----EPVLfatSIRENILF-----GDETASLkqVVAAAKMA 479
Cdd:PRK13539 48 IAGLLP---PAAGTIKLDGGDIDDPDV---AEACHYLGHrnamKPAL---TVAENLEFwaaflGGEELDI--AAALEAVG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 480 NAHefIVKLPHGYethvgqfgtqLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVA 558
Cdd:PRK13539 117 LAP--LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
503-591 |
7.69e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 503 LSGGQKQRIAIARALVRDPRILLLDEATSALDA-ESER--TVQDALdRASvGRTTVIVAHRLSTL-RKADTIAVLDAGRV 578
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQlfRVIREL-RAE-GRVILYVSHRMEEIfALCDAITVFKDGRY 218
|
90
....*....|...
gi 1002260479 579 VEagTHDELLGMD 591
Cdd:PRK11288 219 VA--TFDDMAQVD 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1022-1195 |
7.78e-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: 54.19 E-value: 7.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1022 FKNVHF-SYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKST---VIGLIERFYDAQRGSVLVDGEDIRSYSlARLRSQ 1097
Cdd:cd03233 6 WRNISFtTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFA-EKYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 VALVSQE----PTLfsgTIRDNIAYgAAEEHATEdevaraaalanahgfisaMERGydtrvgergaqLSGGQRQRIALAR 1173
Cdd:cd03233 85 IIYVSEEdvhfPTL---TVRETLDF-ALRCKGNE------------------FVRG-----------ISGGERKRVSIAE 131
|
170 180
....*....|....*....|..
gi 1002260479 1174 AVLKDARILLLDEATSALDAAS 1195
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSST 153
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1020-1240 |
7.97e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERF--YDAQRGSVLVDGEDIRSYSlARLRSQ 1097
Cdd:CHL00131 8 LEIKNLHASVNENE---ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1098 --VALVSQEPTLFSGTirDN-----IAYGAAEEHATEDEVARAAALanahGFIS------AMERGYDTRVGERGaqLSGG 1164
Cdd:CHL00131 84 lgIFLAFQYPIEIPGV--SNadflrLAYNSKRKFQGLPELDPLEFL----EIINeklklvGMDPSFLSRNVNEG--FSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1165 QRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGRTCVV-VAH--RLSTVEKSDTIAVVKDGRVAERG 1240
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTG 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
502-579 |
7.99e-08 |
|
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: 54.65 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGR-TTVIV-AHRLSTLRK-ADTIAVLDAGRV 578
Cdd:cd03267 153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgTTVLLtSHYMKDIEAlARRVLVIDKGRL 232
|
.
gi 1002260479 579 V 579
Cdd:cd03267 233 L 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
502-573 |
8.05e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 8.05e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVIVAHRLSTLRK-ADTIAVL 573
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
501-562 |
8.13e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.44 E-value: 8.13e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 501 TQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTT--VIVAHRLS 562
Cdd:PRK11629 144 SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQ 207
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
28-280 |
8.61e-08 |
|
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: 55.24 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 28 VLGSFGDGMMQPLSMLVLGDIVNSYGGAGGAGSARSAfssGAVDKFALRLLYVAVAVGACSFLEGLCWTRTAERQASKMR 107
Cdd:cd18574 2 VLSALAAALVNIQIPLLLGDLVNVISRSLKETNGDFI---EDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 108 RLYLEAVLSQEVAFFDAAPSSpsspqaqaqattfRVISTVSDDadaIQDF---------LGeklpmvLANATLFFGALAV 178
Cdd:cd18574 79 NDLFSSLLRQDIAFFDTHRTG-------------ELVNRLTAD---VQEFkssfkqcvsQG------LRSVTQTVGCVVS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 179 SFVFAWRLALaglpftLLLFVTPSV-----LLAGRMAAAAGEARAAYEEAGGIAQQAVSSIRTVASYTAERRTVERFRGA 253
Cdd:cd18574 137 LYLISPKLTL------LLLVIVPVVvlvgtLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEE 210
|
250 260 270
....*....|....*....|....*....|....*....
gi 1002260479 254 VARSAAL--------GVRQGL----IKGAVigsMGVIYA 280
Cdd:cd18574 211 VEKAAKLneklglgiGIFQGLsnlaLNGIV---LGVLYY 246
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
367-588 |
9.52e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.79 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 367 KDVHFSYPSRpdTLvLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNvewlrsqiglvs 446
Cdd:PRK10575 15 RNVSFRVPGR--TL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 447 qepvlfatsireNILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQ------------------------ 502
Cdd:PRK10575 80 ------------SKAFARKVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGRFGAAdrekveeaislvglkplahrlvds 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 503 LSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGR--TTVIVAHRLS-TLRKADTIAVLDAGRVV 579
Cdd:PRK10575 148 LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMI 227
|
....*....
gi 1002260479 580 EAGTHDELL 588
Cdd:PRK10575 228 AQGTPAELM 236
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
455-595 |
1.13e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 455 SIRENILFGDETASLkqvvaaAKMANAHEFIVKLPhGYethvgqfgTQLSGGQKQRIAIARALVRDPRILLLDEATSALD 534
Cdd:PLN03140 987 SKEEKMMFVDEVMEL------VELDNLKDAIVGLP-GV--------TGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 535 AESE----RTVQDALDrasVGRTTVIVAHRLStlrkadtIAVLDAgrvveagtHDELLGMDDGGE 595
Cdd:PLN03140 1052 ARAAaivmRTVRNTVD---TGRTVVCTIHQPS-------IDIFEA--------FDELLLMKRGGQ 1098
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
493-574 |
1.29e-07 |
|
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: 52.38 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 493 ETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALD------RASVGRTTVIVA-HRLSTLR 565
Cdd:smart00382 51 LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllllLKSEKNLTVILTtNDEKDLG 130
|
....*....
gi 1002260479 566 KADTIAVLD 574
Cdd:smart00382 131 PALLRRRFD 139
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
375-576 |
1.32e-07 |
|
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: 53.27 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 375 SRPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFAT 454
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 455 SIRENILFGDETASLKQVVAAAKMANAhefivklpHGYEtHVGqfGTQLSGGQKQRIAIARALVRDPRILLLDEATSALD 534
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGL--------NGFE-DRP--VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002260479 535 AESERTVQDALDRASVGRTTVIVAHRLSTLRKADTIAVLDAG 576
Cdd:cd03231 158 KAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
501-543 |
1.79e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 1.79e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1002260479 501 TQLSGGQKQRIAIARALVRDPRILLLDEATSALDAES----ERTVQD 543
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawlEQFLHD 208
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
441-577 |
1.93e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.66 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 441 QIGLVSQEPVLFA-TSIRENILFGDETASLKQVVAAAKMANAHEFIVKL--PHGYETHVGQ-FGTQLSGGQKQRIAIARA 516
Cdd:PLN03211 141 RTGFVTQDDILYPhLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELglTKCENTIIGNsFIRGISGGERKRVSIAHE 220
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 517 LVRDPRILLLDEATSALDAESE-RTVQDALDRASVGRTTVIVAHRLST--LRKADTIAVLDAGR 577
Cdd:PLN03211 221 MLINPSLLILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
68-295 |
1.97e-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: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 68 GAVDKFALRLLYVAVAVGACSFLEGLCWTRTAERQASKMR-RLYlEAVLSQEVAFFdaapsspsspqaqAQATTFRVIST 146
Cdd:cd18550 36 GLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRvQLY-AHLQRMSLAFF-------------TRTRTGEIQSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 147 VSDDADAIQDFLGEKLPMVLANATLFFGALAVSFVFAWRLALAGLPFtLLLFVTPSVLLAGRMAAAAGEARAAYEEAGGI 226
Cdd:cd18550 102 LNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVL-LPLFVLPTRRVGRRRRKLTREQQEKLAELNSI 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 227 AQQ--AVSSIRTVASYTAERRTVERFRGAVARSAALGVRQGLIKGAVIGSMGVIYAVWS-FLSWIGSLLVIH 295
Cdd:cd18550 181 MQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPaLVYWVGGLLVIG 252
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1052-1192 |
2.09e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.50 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1052 ALVGPSGSGKSTVIGLIERFYDAQRGS------VLVDGEdiRSYSLARLRSQVALVSQEPTLFSG-TIRDNIAYGAAEEh 1124
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRivlngrVLFDAE--KGICLPPEKRRIGYVFQDARLFPHyKVRGNLRYGMAKS- 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 1125 atedevaraaalanahgfisaMERGYDTRVGERG---------AQLSGGQRQRIALARAVLKDARILLLDEATSALD 1192
Cdd:PRK11144 105 ---------------------MVAQFDKIVALLGieplldrypGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
420-583 |
2.41e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.68 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 420 SGEISMDD---HGIDTLNVEWLRSQIGLVSQEPvlFATSIRENILFG--------DETASLKQVVAAAKMANAhefivkl 488
Cdd:PRK13547 63 TGDVTLNGeplAAIDAPRLARLRAVLPQAAQPA--FAFSAREIVLLGrypharraGALTHRDGEIAWQALALA------- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 489 phGYETHVGQFGTQLSGGQKQRIAIARAL---------VRDPRILLLDEATSALD-AESER---TVQDALDRASVGRTTV 555
Cdd:PRK13547 134 --GATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDlAHQHRlldTVRRLARDWNLGVLAI 211
|
170 180
....*....|....*....|....*...
gi 1002260479 556 IVAHRLSTlRKADTIAVLDAGRVVEAGT 583
Cdd:PRK13547 212 VHDPNLAA-RHADRIAMLADGAIVAHGA 238
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
504-586 |
2.55e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 53.16 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 504 SGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDAL-DRASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEA 581
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIrELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMD 227
|
....*
gi 1002260479 582 GTHDE 586
Cdd:COG1134 228 GDPEE 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
418-537 |
2.83e-07 |
|
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: 52.36 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATSIRENI-----LFGDETASLKQVVAAAKMANAHEFIVKlphgy 492
Cdd:TIGR01189 52 PDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLhfwaaIHGGAQRTIEDALAAVGLTGFEDLPAA----- 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1002260479 493 ethvgqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAES 537
Cdd:TIGR01189 127 ---------QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
73-295 |
3.19e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 53.67 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 73 FALRLLYVAVAVGACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDAAPSSpsspqaqaqattfRVISTVSDDAD 152
Cdd:cd18563 45 LVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTG-------------SLMSRVTSDTD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 153 AIQDFLGEKLPMVLANATLFFGALAVSFVFAWRLALAGL---PFTLLLfvtpSVLLAGRMAAAAGEARAAYEEAGGIAQQ 229
Cdd:cd18563 112 RLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLipvPLVVWG----SYFFWKKIRRLFHRQWRRWSRLNSVLND 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 230 AVSSIRTVASYTAERRTVERFRGAVARSAALGVRQGLIKGAVIGSMGVI-----YAVWsflsWIGSLLVIH 295
Cdd:cd18563 188 TLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLtslgtLIVW----YFGGRQVLS 254
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1020-1234 |
3.40e-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: 51.86 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPT-RPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIerfydAQR-------GSVLVDGEDIRSYsl 1091
Cdd:cd03232 4 LTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL-----AGRktagvitGEILINGRPLDKN-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1092 arLRSQVALVSQEPTLFSG-TIRDNIAYgaaeehatedevaraaalanahgfiSAMERGydtrvgergaqLSGGQRQRIA 1170
Cdd:cd03232 77 --FQRSTGYVEQQDVHSPNlTVREALRF-------------------------SALLRG-----------LSVEQRKRLT 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 1171 LARAVLKDARILLLDEATSALDAASERLVQDAVDRM-LRGRTCVVVAHRLSTV--EKSDTIAVVKDG 1234
Cdd:cd03232 119 IGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
420-588 |
3.41e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.96 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 420 SGEISMDDHGIdtlnVEW-----LRSQIGLVSQEPVLFA-TSIRENILFGDETASLKQVvaAAKMANAHEFIVKLphgYE 493
Cdd:PRK11614 59 SGRIVFDGKDI----TDWqtakiMREAVAIVPEGRRVFSrMTVEENLAMGGFFAERDQF--QERIKWVYELFPRL---HE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 494 THVGQFGTqLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLS-TLRKADTIA 571
Cdd:PRK11614 130 RRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQlREQGMTIFLVEQNANqALKLADRGY 208
|
170
....*....|....*..
gi 1002260479 572 VLDAGRVVEAGTHDELL 588
Cdd:PRK11614 209 VLENGHVVLEDTGDALL 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
330-586 |
3.50e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 54.30 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 330 ATAAASRM---QEMIEMLPPLEGAEKKGATMERIR-GEIVF--KDVHFSYPSRPdtlVLNGFNLTISEGA---------- 393
Cdd:COG0488 276 AKQAQSRIkalEKLEREEPPRRDKTVEIRFPPPERlGKKVLelEGLSKSYGDKT---LLDDLSLRIDRGDrigligpnga 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 394 ---TVglvggsgsgkstvISLLQRFYSPDSGEIsmdDHGiDTLnvewlrsQIGLVSQEpvlfatsiRENIlfgDETASLK 470
Cdd:COG0488 353 gksTL-------------LKLLAGELEPDSGTV---KLG-ETV-------KIGYFDQH--------QEEL---DPDKTVL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 471 QVVAAAKmanahefivklPHGYETHV----GQFG----------TQLSGGQKQRIAIARALVRDPRILLLDEATSALDAE 536
Cdd:COG0488 398 DELRDGA-----------PGGTEQEVrgylGRFLfsgddafkpvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIE 466
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 537 SERTVQDALDRASvGrTTVIVAH-R--LSTLrkADTIAVLDAGRVVE-AGTHDE 586
Cdd:COG0488 467 TLEALEEALDDFP-G-TVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGGYDD 516
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
502-573 |
3.63e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.41 E-value: 3.63e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALD----AESERTVQDAldrASVGRTTVIVAHRLSTLRK-ADTIAVL 573
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1028-1201 |
4.12e-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: 54.17 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1028 SYPtrPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVI----GLIERFydaqrgsvlvDGEdirsyslARLRS--QVALV 1101
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLrimaGVDKDF----------NGE-------ARPQPgiKVGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1102 SQEPTL-FSGTIRDNIAYGAAE-------------EHATED-----------EVARAAALANAHGFISAMERG------- 1149
Cdd:TIGR03719 74 PQEPQLdPTKTVRENVEEGVAEikdaldrfneisaKYAEPDadfdklaaeqaELQEIIDAADAWDLDSQLEIAmdalrcp 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 1150 -YDTRVgergAQLSGGQRQRIALARAVLKDARILLLDEATSALDAAS----ERLVQD 1201
Cdd:TIGR03719 154 pWDADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
723-969 |
5.14e-07 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 52.80 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 723 LADDGQIRSKTRLYYFLFLGIAVVCITANIVQHYNFAVMGERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQ 802
Cdd:cd18541 29 LTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQK--NRTGDLMARATND 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 803 SSKVRSLVGDRMCLLVQAGATASLGFSLALAVSWRLATVMMAMQPLIIASFY---------FKKVlmaamskkakkaQVQ 873
Cdd:cd18541 107 LNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYrlgkkihkrFRKV------------QEA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 874 GSQLAS---EAVVNHRTITAFSSQRRMLRLYEAAQQGPKKDNVAHSWFSGFCLCLCQFSNTGSMAVALWYGGKLMAKGLI 950
Cdd:cd18541 175 FSDLSDrvqESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTI 254
|
250 260
....*....|....*....|....*.
gi 1002260479 951 TPTHL--FQVFFMLMT-----MGRVI 969
Cdd:cd18541 255 TLGDLvaFNSYLGMLIwpmmaLGWVI 280
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
475-587 |
5.75e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.19 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 475 AAKMANAHEFIVKLPHgyethvgqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSALDAeserTVQ-------DALDR 547
Cdd:PRK09473 145 AVKMPEARKRMKMYPH-----------EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV----TVQaqimtllNELKR 209
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1002260479 548 aSVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGTHDEL 587
Cdd:PRK09473 210 -EFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV 249
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1020-1242 |
6.39e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.10 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPtrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLI--ERFYDAQRGSVLVDGEDIRSYSLA-RLRS 1096
Cdd:PRK09580 2 LSIKDLHVSVE---DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEdRAGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEPTLFSGTIRD---NIAYGAAEEHATEDEVARAAALANAHGFISAMERGYDTRVGERGAQLSGGQRQRIALAR 1173
Cdd:PRK09580 79 GIFMAFQYPVEIPGVSNQfflQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 1174 AVLKDARILLLDEATSALDAASERLVQDAVDRMLRG-RTCVVVAH--RLSTVEKSDTIAVVKDGRVAERGRH 1242
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
501-579 |
6.50e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 6.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 501 TQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALdrASVGRTTVIVAHRLSTLRKADT-IAVLDAGRVV 579
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL--KTFQGSIIFISHDRSFIRNMATrIVDLDRGKLV 232
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
502-587 |
6.83e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.82 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDAL----DRASVGrtTVIVAHRLSTLRK-ADTIAVLDAG 576
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLlelqQKENMA--LVLITHDLALVAEaAHKIIVMYAG 230
|
90
....*....|.
gi 1002260479 577 RVVEAGTHDEL 587
Cdd:PRK11022 231 QVVETGKAHDI 241
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
484-582 |
7.62e-07 |
|
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: 50.78 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 484 FIVKLPHGYEThVGQFGTQLSGGQKQRIAIARAL-VRDPRIL-LLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHR 560
Cdd:cd03238 70 FLIDVGLGYLT-LGQKLSTLSGGELQRVKLASELfSEPPGTLfILDEPSTGLHQQDINQLLEVIKGlIDLGNTVILIEHN 148
|
90 100
....*....|....*....|....*...
gi 1002260479 561 LSTLRKADTI------AVLDAGRVVEAG 582
Cdd:cd03238 149 LDVLSSADWIidfgpgSGKSGGKVVFSG 176
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
420-559 |
1.02e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 51.32 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 420 SGEISMDDHGIDTLNVEW---LRSQ-IGLVSQEPVLFAT-SIRENILFgdeTASLKQVVAAAKMANAHEFIVKLphGYET 494
Cdd:PRK10584 64 SGEVSLVGQPLHQMDEEArakLRAKhVGFVFQSFMLIPTlNALENVEL---PALLRGESSRQSRNGAKALLEQL--GLGK 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 495 HVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQD---ALDRaSVGRTTVIVAH 559
Cdd:PRK10584 139 RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADllfSLNR-EHGTTLILVTH 205
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1021-1192 |
1.03e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1021 EFKNVHFSYPTRpevAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVdGEDIrsyslarlrsQVAL 1100
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKL----------EVAY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1101 VSQ-----EPtlfSGTIRDNIAYGaaeehatEDEVARAAALANAHGFIS--------AMergydTRVgergAQLSGGQRQ 1167
Cdd:PRK11147 387 FDQhraelDP---EKTVMDNLAEG-------KQEVMVNGRPRHVLGYLQdflfhpkrAM-----TPV----KALSGGERN 447
|
170 180
....*....|....*....|....*
gi 1002260479 1168 RIALARAVLKDARILLLDEATSALD 1192
Cdd:PRK11147 448 RLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1020-1204 |
1.21e-06 |
|
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: 52.63 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPevaVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVdGEDIrsyslarlrsQVA 1099
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 LVSQEptlfsgtiRDNIAYGAA--EEHATEDEVARAaalanahGFISAMERGYDTRVGERGA-------QLSGGQRQRIA 1170
Cdd:TIGR03719 389 YVDQS--------RDALDPNKTvwEEISGGLDIIKL-------GKREIPSRAYVGRFNFKGSdqqkkvgQLSGGERNRVH 453
|
170 180 190
....*....|....*....|....*....|....
gi 1002260479 1171 LARAVLKDARILLLDEATSALDAASERLVQDAVD 1204
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1020-1220 |
1.37e-06 |
|
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: 52.83 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTrpEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYslarlrsqva 1099
Cdd:TIGR00954 452 IKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFY---------- 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1100 lVSQEPTLFSGTIRDNIAYGAAEEHATE----DEVARAAALANAHGFISAMERGYDTrVGERGAQLSGGQRQRIALARAV 1175
Cdd:TIGR00954 520 -VPQRPYMTLGTLRDQIIYPDSSEDMKRrglsDKDLEQILDNVQLTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARLF 597
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002260479 1176 LKDARILLLDEATSALDAAserlVQDAVDRMLR--GRTCVVVAHRLS 1220
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVD----VEGYMYRLCRefGITLFSVSHRKS 640
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1020-1241 |
1.46e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 51.65 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTrPEVAVLA----GFSLEigAGKTVALVGPSGSGKS-TVIGLIERFYDAQR--GSVLVDGEDI---RSY 1089
Cdd:PRK09473 13 LDVKDLRVTFST-PDGDVTAvndlNFSLR--AGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREIlnlPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1090 SLARLRS-QVALVSQEP-TLFSGTIR--DNIA--------YGAAEehATEDEVaraaalanahgfisameRGYDT----- 1152
Cdd:PRK09473 90 ELNKLRAeQISMIFQDPmTSLNPYMRvgEQLMevlmlhkgMSKAE--AFEESV-----------------RMLDAvkmpe 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1153 ---RVGERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAAserlVQDAVDRMLR------GRTCVVVAHRLSTVE 1223
Cdd:PRK09473 151 arkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVT----VQAQIMTLLNelkrefNTAIIMITHDLGVVA 226
|
250
....*....|....*....
gi 1002260479 1224 KS-DTIAVVKDGRVAERGR 1241
Cdd:PRK09473 227 GIcDKVLVMYAGRTMEYGN 245
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
420-582 |
1.46e-06 |
|
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: 50.32 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 420 SGEISMDDHGIDtlnvEWLRSQIGLVSQEPVLFATS-IRENILFgdeTASLKQvvaaakmanahefivklphgyethvgq 498
Cdd:cd03232 63 TGEILINGRPLD----KNFQRSTGYVEQQDVHSPNLtVREALRF---SALLRG--------------------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 499 fgtqLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLS--TLRKADTIAVLD- 574
Cdd:cd03232 109 ----LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKr 184
|
....*...
gi 1002260479 575 AGRVVEAG 582
Cdd:cd03232 185 GGKTVYFG 192
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
242-528 |
1.70e-06 |
|
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: 52.11 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 242 AERRtvERFRGAVARSAALGVRQGLIKGAVIGSMGVIYAVWSFLSWIGSLLVIHLHAQGGHVFVASIcIVLAGM------ 315
Cdd:COG4615 203 RRRR--RAFFDEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGWADPAVLSG-FVLVLLflrgpl 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 316 -SIMMALPNLryfIDATAAASRMQEMIEMLPPLEGAEKKGATMERIRG--EIVFKDVHFSYPSRPDTlvlNGF-----NL 387
Cdd:COG4615 280 sQLVGALPTL---SRANVALRKIEELELALAAAEPAAADAAAPPAPADfqTLELRGVTYRYPGEDGD---EGFtlgpiDL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 388 TISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFATsireniLFGDETA 467
Cdd:COG4615 354 TIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LLGLDGE 427
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 468 SLKQVVAA--AKMANAHefivklphgyETHV--GQFGT-QLSGGQKQRIAIARALVRDPRILLLDE 528
Cdd:COG4615 428 ADPARAREllERLELDH----------KVSVedGRFSTtDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
382-595 |
1.90e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.09 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 382 LNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEwLRSQ--IGLVSQE-PVLFATSIRE 458
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQlgIGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 459 NILFGdeTASLKQV-----VAAAKM-ANAHEFIVKLphGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSA 532
Cdd:PRK09700 100 NLYIG--RHLTKKVcgvniIDWREMrVRAAMMLLRV--GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 533 L-DAESERTVQDALDRASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVVEAG-----THDELLGMDDGGE 595
Cdd:PRK09700 176 LtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGmvsdvSNDDIVRLMVGRE 245
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
481-583 |
1.94e-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: 50.69 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 481 AHEFIVKLPH-------------GYeTHVGQFGTQLSGGQKQRIAIARALVRDPR---ILLLDEATSALDAESERTVQDA 544
Cdd:cd03271 136 ALEFFENIPKiarklqtlcdvglGY-IKLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEV 214
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1002260479 545 LDR-ASVGRTTVIVAHRLSTLRKADTIavLD--------AGRVVEAGT 583
Cdd:cd03271 215 LQRlVDKGNTVVVIEHNLDVIKCADWI--IDlgpeggdgGGQVVASGT 260
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
739-952 |
2.04e-06 |
|
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: 50.93 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 739 LFLGIAVVCITANIVQHYNFAVMGERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARL-----ATQ---SSKVRSLV 810
Cdd:cd18545 45 LFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDS--RPVGKILSRVindvnSLSdllSNGLINLI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 811 GDrMCLLVqaGATASLgfslaLAVSWRLATVMMAMQP-LIIASFYFKKVLMAAMSKKAKKAQVQGSQLAsEAVVNHRTIT 889
Cdd:cd18545 123 PD-LLTLV--GIVIIM-----FSLNVRLALVTLAVLPlLVLVVFLLRRRARKAWQRVRKKISNLNAYLH-ESISGIRVIQ 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 890 AFSSQRRMLRLYEAAQQGPKKDNVAHSWFSGFCLCLCQFSNTGSMAVALWYGGKLMAKGLITP 952
Cdd:cd18545 194 SFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAITV 256
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
418-579 |
2.67e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 418 PDSGEISMDDHGIDTLNVEWLRSQ-IGLVSQEPVLFAT----SIRENILFG--DETASLKQVV----AAAKMANA--HEF 484
Cdd:COG3845 310 PASGSIRLDGEDITGLSPRERRRLgVAYIPEDRLGRGLvpdmSVAENLILGryRRPPFSRGGFldrkAIRAFAEEliEEF 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 485 IVKLPhGYETHVGQfgtqLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDAL-DRASVGRTTVIVAHRLST 563
Cdd:COG3845 390 DVRTP-GPDTPARS----LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLlELRDAGAAVLLISEDLDE 464
|
170
....*....|....*..
gi 1002260479 564 LRK-ADTIAVLDAGRVV 579
Cdd:COG3845 465 ILAlSDRIAVMYEGRIV 481
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
347-582 |
3.26e-06 |
|
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: 49.45 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 347 LEGAEKKGATMERIRGEIVFKDVHFSYPSRPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMd 426
Cdd:cd03220 3 LENVSKSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 427 dHGidtlNVEWLrsqIGL-VSQEPVLfatSIRENILFGDETASLKQVVAAAKMANAHEFivklphgyeTHVGQFGTQ--- 502
Cdd:cd03220 82 -RG----RVSSL---LGLgGGFNPEL---TGRENIYLNGRLLGLSRKEIDEKIDEIIEF---------SELGDFIDLpvk 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 503 -LSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDAL-DRASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRVV 579
Cdd:cd03220 142 tYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIR 221
|
...
gi 1002260479 580 EAG 582
Cdd:cd03220 222 FDG 224
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1155-1245 |
3.63e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.50 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1155 GERGAQLSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR-GRTCVVVAHRLSTVEK-SDTIAVVK 1232
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQlAHELTVID 218
|
90
....*....|...
gi 1002260479 1233 DGRVAERGRHHEL 1245
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
497-587 |
3.86e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.50 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 497 GQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALdRASV--GRTTVIVAHRLSTLRK-ADTIAVL 573
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV-RSMVrdGATVLLTTQYMEEAEQlAHELTVI 217
|
90
....*....|....
gi 1002260479 574 DAGRVVEAGTHDEL 587
Cdd:NF000106 218 DRGRVIADGKVDEL 231
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
74-252 |
4.18e-06 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 50.16 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 74 ALRLLYVAVAVgaCSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDaapsspsspqaqaQATTFRVISTVSDDADA 153
Cdd:cd18589 41 VMSLLTIASAV--SEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD-------------SNQTGDIVSRVTTDTED 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 154 IQDFLGEKLPMVLANATLFFGALAVSFVFAWRLAL---AGLPftlLLFVTPSvLLAGRMAAAAGEARAAYEEAGGIAQQA 230
Cdd:cd18589 106 MSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALltaLGLP---LLLLVPK-FVGKFQQSLAVQVQKSLARANQVAVET 181
|
170 180
....*....|....*....|..
gi 1002260479 231 VSSIRTVASYTAERRTVERFRG 252
Cdd:cd18589 182 FSAMKTVRSFANEEGEAQRYRQ 203
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1030-1247 |
4.81e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 50.09 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1030 PTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVI----GLIErfydAQRGSVLVDGEDI--RSYSLARlrsQVALV-- 1101
Cdd:COG4586 30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIkmltGILV----PTSGEVRVLGYVPfkRRKEFAR---RIGVVfg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1102 --SQ----EPTLFSGTIRDNIaYG--AAEEHATEDEvaraaalanahgFISAMERG--YDTRVgeRgaQLSGGQRQRIAL 1171
Cdd:COG4586 103 qrSQlwwdLPAIDSFRLLKAI-YRipDAEYKKRLDE------------LVELLDLGelLDTPV--R--QLSLGQRMRCEL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 1172 ARAVLKDARILLLDEATSALDAASERLVQDAVDRM--LRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHELLA 1247
Cdd:COG4586 166 AAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1043-1192 |
6.86e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1043 LEIGAGKTVALVGPSGSGKSTVIGLIErfydaqrGSVLVD-GEDIRSYSLArlrsqVALVSQEPTL-FSGTIRDNIAYGA 1120
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDdGRIIYEQDLI-----VARLQQDPPRnVEGTVYDFVAEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1121 AEE-------HATEDEVARAAALANahgfISAMER-----------GYDTRVGERGAQ-----------LSGGQRQRIAL 1171
Cdd:PRK11147 92 EEQaeylkryHDISHLVETDPSEKN----LNELAKlqeqldhhnlwQLENRINEVLAQlgldpdaalssLSGGWLRKAAL 167
|
170 180
....*....|....*....|.
gi 1002260479 1172 ARAVLKDARILLLDEATSALD 1192
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1042-1232 |
7.15e-06 |
|
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: 47.35 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1042 SLEIGAGKTVALVGPSGSGKSTV---IGLIerfydaqrgsVLVDGEDIRSYSLARLRSQVALVSQEPTLFSGtirdniay 1118
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTIldaIGLA----------LGGAQSATRRRSGVKAGCIVAAVSAELIFTRL-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1119 gaaeehatedevaraaalanahgfisamergydtrvgergaQLSGGQRQRIALARAV----LKDARILLLDEATSALDAA 1194
Cdd:cd03227 77 -----------------------------------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPR 115
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002260479 1195 SERLVQDAVDRML-RGRTCVVVAHRLSTVEKSDTIAVVK 1232
Cdd:cd03227 116 DGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHIK 154
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
486-578 |
8.95e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 486 VKLPhGYETHVGQfgtqLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTV-QDALDRASVGRTTVIVAHRLSTL 564
Cdd:PRK10982 380 VKTP-GHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPEL 454
|
90
....*....|....*
gi 1002260479 565 RK-ADTIAVLDAGRV 578
Cdd:PRK10982 455 LGiTDRILVMSNGLV 469
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
415-587 |
1.12e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.45 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 415 FYSPDSGEISMDDHGIDTLNVEWLrSQIGLVS--QEPVLFA--TSIrENILFGD-------------ETASLKQVVAAAk 477
Cdd:PRK11300 54 FYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFRemTVI-ENLLVAQhqqlktglfsgllKTPAFRRAESEA- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 478 MANAHEFIVKLphGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALD--RASVGRTTV 555
Cdd:PRK11300 131 LDRAATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAelRNEHNVTVL 208
|
170 180 190
....*....|....*....|....*....|...
gi 1002260479 556 IVAHRLS-TLRKADTIAVLDAGRVVEAGTHDEL 587
Cdd:PRK11300 209 LIEHDMKlVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
502-588 |
1.14e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRT--TVIV-------AHRLstlrkaDTIAV 572
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmSVLVataymeeAERF------DWLVA 209
|
90
....*....|....*.
gi 1002260479 573 LDAGRVVEAGTHDELL 588
Cdd:NF033858 210 MDAGRVLATGTPAELL 225
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
764-965 |
1.16e-05 |
|
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: 48.62 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 764 RLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCLLVQAGATASLGFSLALAVSWRLATVMM 843
Cdd:cd18589 66 RIHSRLQGLVFAAVLRQEIAFFDS--NQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 844 AMQPLIIASFYFKKVLMAAMSKKAKKAQVQGSQLASEAVVNHRTITAFSSQRRMLRLYEAAQQGP----KKDNVAH---S 916
Cdd:cd18589 144 LGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTyrlnKKEAAAYavsM 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 917 W---FSGFCLCLCqfsntgsmavALWYGGKLMAKGLITPTHLfqVFFMLMTM 965
Cdd:cd18589 224 WtssFSGLALKVG----------ILYYGGQLVTAGTVSSGDL--VTFVLYEL 263
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1019-1240 |
1.18e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.47 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1019 AIEFKNVHFSYpTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGE----------DIRS 1088
Cdd:PRK10261 14 AVENLNIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1089 YSLARLR----SQVALVSQEPT-----LFsgTIRDNIA------YGAAEEHAtedevaraaalanahgfISAMERGYD-T 1152
Cdd:PRK10261 93 QSAAQMRhvrgADMAMIFQEPMtslnpVF--TVGEQIAesirlhQGASREEA-----------------MVEAKRMLDqV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1153 RVGERGA-------QLSGGQRQRIALARAVLKDARILLLDEATSALDAASE----RLVQDAVDRMLRGrtCVVVAHRLST 1221
Cdd:PRK10261 154 RIPEAQTilsryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilQLIKVLQKEMSMG--VIFITHDMGV 231
|
250 260
....*....|....*....|
gi 1002260479 1222 V-EKSDTIAVVKDGRVAERG 1240
Cdd:PRK10261 232 VaEIADRVLVMYQGEAVETG 251
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
445-573 |
1.19e-05 |
|
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: 48.52 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 445 VSQEPVLFATSIRENILFGDETASLKQVVAAakmanahefiVKLPHGYETHVgqfgTQLSGGQKQRIAIARALVRDPRIL 524
Cdd:cd03236 96 VDLIPKAVKGKVGELLKKKDERGKLDELVDQ----------LELRHVLDRNI----DQLSGGELQRVAIAAALARDADFY 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 525 LLDEATSALDAESERTVQDAL-DRASVGRTTVIVAHRLSTLRK-ADTIAVL 573
Cdd:cd03236 162 FFDEPSSYLDIKQRLNAARLIrELAEDDNYVLVVEHDLAVLDYlSDYIHCL 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1041-1237 |
1.21e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1041 FSLEIGAGKTVALVGPSGSGKSTVIGLIerfYDAQR---GSVLVDGE--DIRSYSLArLRSQVALV----SQEPTLFSGT 1111
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLL---YGATRrtaGQVYLDGKpiDIRSPRDA-IRAGIMLCpedrKAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1112 IRDNIAYGAAEEHAT---------EDEVARAaalanahgFISAMergydtRVGERGAQ-----LSGGQRQRIALARAVLK 1177
Cdd:PRK11288 348 VADNINISARRHHLRagclinnrwEAENADR--------FIRSL------NIKTPSREqlimnLSGGNQQKAILGRWLSE 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002260479 1178 DARILLLDEATSALD--AASE--RLVQDAVDrmlRGRTCVVVAHRLSTVEK-SDTIAVVKDGRVA 1237
Cdd:PRK11288 414 DMKVILLDEPTRGIDvgAKHEiyNVIYELAA---QGVAVLFVSSDLPEVLGvADRIVVMREGRIA 475
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1025-1245 |
1.22e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.97 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1025 VHFSYPTRPEVAVlAGFSLEIGAGKTVALVGPSGSGKS----TVIGLIERFYDAQRGSVLVDGEDIRSYSLARLR----S 1096
Cdd:PRK11022 11 VHFGDESAPFRAV-DRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRnlvgA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQEPTlfsgtIRDNIAYGAAEEHATEDEVARAAALANAHgfisamERGYD-----------TRVGERGAQLSGGQ 1165
Cdd:PRK11022 90 EVAMIFQDPM-----TSLNPCYTVGFQIMEAIKVHQGGNKKTRR------QRAIDllnqvgipdpaSRLDVYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1166 RQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLRGR--TCVVVAHRLSTV-EKSDTIAVVKDGRVAERGRH 1242
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVaEAAHKIIVMYAGQVVETGKA 238
|
...
gi 1002260479 1243 HEL 1245
Cdd:PRK11022 239 HDI 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1020-1245 |
1.57e-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: 49.05 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQ-RGSVLVDGE--DIRSYSLArLRS 1096
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNPAQA-IRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1097 QVALVSQE-------PTLFSGtirDNIAYGAAEEHATEDEVARAAALANAHGFISAME---RGYDTRVGergaQLSGGQR 1166
Cdd:TIGR02633 337 GIAMVPEDrkrhgivPILGVG---KNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKvktASPFLPIG----RLSGGNQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1167 QRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR-GRTCVVVAHRLSTVEK-SDTIAVVKDGRVAERGRHHE 1244
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQeGVAIIVVSSELAEVLGlSDRVLVIGEGKLKGDFVNHA 489
|
.
gi 1002260479 1245 L 1245
Cdd:TIGR02633 490 L 490
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
445-562 |
1.65e-05 |
|
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: 49.36 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 445 VSQEPVLFATSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYETHVGQFGTQ-----LSGGQKQRIAIARALVR 519
Cdd:TIGR00954 520 VPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQdwmdvLSGGEKQRIAMARLFYH 599
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1002260479 520 DPRILLLDEATSALDAESERTVQDALDRasVGRTTVIVAHRLS 562
Cdd:TIGR00954 600 KPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKS 640
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
502-588 |
1.69e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 48.54 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGR-TTVIVA-HRLSTLRK-ADTIAVLDAGRV 578
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIEAlCDRVIVIDHGRI 233
|
90
....*....|
gi 1002260479 579 VEAGTHDELL 588
Cdd:COG4586 234 IYDGSLEELK 243
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
738-951 |
1.87e-05 |
|
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: 48.15 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 738 FLFLGIAVVCITANIVQHYNFAVMGERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLA--TQ------SSKVRSL 809
Cdd:cd18544 45 LLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDR--TPVGRLVTRVTndTEalnelfTSGLVTL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 810 VGDrmcLLVQAGATASLgfslaLAVSWRLATVMMAMQPLII-ASFYFKKVLmaamskkAKKAQVQGSQLA------SEAV 882
Cdd:cd18544 123 IGD---LLLLIGILIAM-----FLLNWRLALISLLVLPLLLlATYLFRKKS-------RKAYREVREKLSrlnaflQESI 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 883 VNHRTITAFSSQRRMLRLYEAAQQGPKKDNVAHSWFSGFCLCLCQFSNTGSMAVALWYGGKLMAKGLIT 951
Cdd:cd18544 188 SGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVT 256
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
502-582 |
1.88e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.96 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDAL-DRASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVE 580
Cdd:PRK15056 142 ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLrELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLA 221
|
..
gi 1002260479 581 AG 582
Cdd:PRK15056 222 SG 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
442-587 |
1.98e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 442 IGLVSQEPVL-----------FATSIRENILFGDETA--SLKQVVAAAKMANAHEFIVKLPHgyethvgqfgtQLSGGQK 508
Cdd:PRK10261 106 MAMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAmvEAKRMLDQVRIPEAQTILSRYPH-----------QLSGGMR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 509 QRIAIARALVRDPRILLLDEATSALD----AESERTVQDALDRASVGrtTVIVAHRLSTLRK-ADTIAVLDAGRVVEAGT 583
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMG--VIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
....
gi 1002260479 584 HDEL 587
Cdd:PRK10261 253 VEQI 256
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
381-588 |
2.35e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 47.98 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 381 VLNGFNLTISEGATVGLVGGSGSGKstviSLLQRF---YSPDSGEISMDD---HGIDTLNV------EWLRSQIGLVSQE 448
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGK----SLIAKAicgITKDNWHVTADRfrwNGIDLLKLsprerrKIIGREIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 449 P-------VLFATSIRENILFGDETASLKQVVAAAKMANA----------HEFIVK-LPHgyethvgqfgtQLSGGQKQR 510
Cdd:COG4170 98 PsscldpsAKIGDQLIEAIPSWTFKGKWWQRFKWRKKRAIellhrvgikdHKDIMNsYPH-----------ELTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 511 IAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGRTTVI--VAHRLSTLRK-ADTIAVLDAGRVVEAGTHDEL 587
Cdd:COG4170 167 VMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSIllISHDLESISQwADTITVLYCGQTVESGPTEQI 246
|
.
gi 1002260479 588 L 588
Cdd:COG4170 247 L 247
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1031-1209 |
2.36e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.77 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1031 TRPEVAVLAGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGEDIRSYSLARLrsqVALVSQEPTLFSG 1110
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRF---MAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1111 -TIRDNIAY--GAAEEHATEDEVARAAalanahgfISAMERGYDTRVgergAQLSGGQRQRIALARAVLKDARILLLDEA 1187
Cdd:PRK13543 97 lSTLENLHFlcGLHGRRAKQMPGSALA--------IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180
....*....|....*....|..
gi 1002260479 1188 TSALDAASERLVQDAVDRMLRG 1209
Cdd:PRK13543 165 YANLDLEGITLVNRMISAHLRG 186
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1161-1231 |
2.36e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.41 E-value: 2.36e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 1161 LSGGQRQRIALARAVLKDARILLLDEATSALDAASERLVQDAVDRMLR--GRTCVVVAHRLSTVEK-SDTIAVV 1231
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVF 145
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
497-587 |
3.15e-05 |
|
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: 48.47 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 497 GQFGTQLSGGQKQRIAIARALVRD---PRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLSTLRKADTIAV 572
Cdd:TIGR00630 824 GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRlVDKGNTVVVIEHNLDVIKTADYIID 903
|
90 100
....*....|....*....|.
gi 1002260479 573 L------DAGRVVEAGTHDEL 587
Cdd:TIGR00630 904 LgpeggdGGGTVVASGTPEEV 924
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
412-591 |
3.33e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 46.90 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 412 LQRFYSPDSGEISMDDHGIDTLNVEWLRSQIGLVSQEPVLFA-TSIRENI---------LFGDETASLKQVVAAAKMANa 481
Cdd:PRK10253 53 LSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQELVargryphqpLFTRWRKEDEEAVTKAMQAT- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 482 hefivklphGYETHVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRAS--VGRTTVIVAH 559
Cdd:PRK10253 132 ---------GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNreKGYTLAAVLH 202
|
170 180 190
....*....|....*....|....*....|...
gi 1002260479 560 RLS-TLRKADTIAVLDAGRVVEAGTHDELLGMD 591
Cdd:PRK10253 203 DLNqACRYASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
420-534 |
3.79e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 420 SGEISMDDHGIDTLN-VEWLRSQIGLVSQE-------PVLfatSIRENILFgdetASLKQVV------AAAKMANAHEFI 485
Cdd:PRK13549 317 EGEIFIDGKPVKIRNpQQAIAQGIAMVPEDrkrdgivPVM---GVGKNITL----AALDRFTggsridDAAELKTILESI 389
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 486 ----VKLPHGyETHVGQfgtqLSGGQKQRIAIARALVRDPRILLLDEATSALD 534
Cdd:PRK13549 390 qrlkVKTASP-ELAIAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
71-302 |
3.88e-05 |
|
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: 46.92 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 71 DKFALRLLY---VAVAVGACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDaapsspsspqaqaQATTFRVISTV 147
Cdd:cd18784 33 DKFSRAIIImglLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFD-------------TVKTGDITSRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 148 SDDADAIQDFLGEKLPMVLANATLFFGALAVSFVFAWRLALA---GLPFTLLLfvtpSVLLAGRMAAAAGEARAAYEEAG 224
Cdd:cd18784 100 TSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVtliGLPLIAIV----SKVYGDYYKKLSKAVQDSLAKAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 225 GIAQQAVSSIRTVASYTAERRTVERFRGAVARSAALGVRQGLIKGAVIGSMGVIY-AVWSFLSWIGSLLVIHLHAQGGH 302
Cdd:cd18784 176 EVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTElALTVSTLYYGGHLVITGQISGGN 254
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1053-1195 |
4.02e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1053 LVGPSGSGKSTVI----GLIERFydaqrgsvlvDGEdirsyslARLRS--QVALVSQEPTL-FSGTIRDNIAYGAAE--- 1122
Cdd:PRK11819 38 VLGLNGAGKSTLLrimaGVDKEF----------EGE-------ARPAPgiKVGYLPQEPQLdPEKTVRENVEEGVAEvka 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1123 ----------EHATED-----------EVARAAALANAHGFISAMERG--------YDTRVGergaQLSGGQRQRIALAR 1173
Cdd:PRK11819 101 aldrfneiyaAYAEPDadfdalaaeqgELQEIIDAADAWDLDSQLEIAmdalrcppWDAKVT----KLSGGERRRVALCR 176
|
170 180
....*....|....*....|..
gi 1002260479 1174 AVLKDARILLLDEATSALDAAS 1195
Cdd:PRK11819 177 LLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
73-263 |
4.08e-05 |
|
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: 47.09 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 73 FALRLLYVAVAVGACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDAAPSSpsspqaqaqattfRVISTVSDDAD 152
Cdd:cd18543 41 LVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSG-------------QLLSRATSDLS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 153 AIQDFLGeKLPMVLANATLFFGALAVSFVFAWRLALAGLPFTLLLFVTpSVLLAGRMAAAAGEARAAYEEAGGIAQQAVS 232
Cdd:cd18543 108 LVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLV-ARRFRRRYFPASRRAQDQAGDLATVVEESVT 185
|
170 180 190
....*....|....*....|....*....|.
gi 1002260479 233 SIRTVASYTAERRTVERFRGAVARSAALGVR 263
Cdd:cd18543 186 GIRVVKAFGRERRELDRFEAAARRLRATRLR 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
503-559 |
4.21e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.86 E-value: 4.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 503 LSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAH 559
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRfaENRGKTAMVVDH 514
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
503-564 |
4.39e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.64 E-value: 4.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 503 LSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASV--GRTTVIVAHRLSTL 564
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVL 135
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
503-559 |
6.18e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 6.18e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 503 LSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVGR--TTVIVAH 559
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
504-596 |
6.94e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.94 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 504 SGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASVG-RTTVIVAH--RLSTLRKADTIAVLDAGRVVE 580
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVK 226
|
90
....*....|....*.
gi 1002260479 581 AGTHDELLGMDDGGEG 596
Cdd:PRK09580 227 SGDFTLVKQLEEQGYG 242
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
502-573 |
6.96e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 45.88 E-value: 6.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALD--RASVGRTTVIVAHRLStLRKADTIAVL 573
Cdd:PRK09544 120 KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDqlRRELDCAVLMVSHDLH-LVMAKTDEVL 192
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
142-263 |
7.48e-05 |
|
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: 46.33 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 142 RVISTVSDDADAIQDFLGEKLPMVLANATLFFGALAVSFVFAWRLALAGLPFTLLLFVTpSVLLAGRMAAAAGEARAAYE 221
Cdd:cd18546 97 RIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALA-TRWFRRRSSRAYRRARERIA 175
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1002260479 222 EAGGIAQQAVSSIRTVASYTAERRTVERFRGAVARSAALGVR 263
Cdd:cd18546 176 AVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLR 217
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1048-1234 |
8.81e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1048 GKTVALVGPSGSGKSTVI---------GLIErfydaqrGSVLVDGEDIRSYSLARLRS----------QVALvsQEPTLF 1108
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMdvlagrktgGYIE-------GDIRISGFPKKQETFARISGyceqndihspQVTV--RESLIY 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1109 SGTIRDNIAYGAAEEHATEDEVARaaalanahgfISAMERGYDTRVGERGAQ-LSGGQRQRIALARAVLKDARILLLDEA 1187
Cdd:PLN03140 977 SAFLRLPKEVSKEEKMMFVDEVME----------LVELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 1188 TSALDAASE----RLVQDAVDrmlRGRTCVVVAHRLS--TVEKSDTIAVVKDG 1234
Cdd:PLN03140 1047 TSGLDARAAaivmRTVRNTVD---TGRTVVCTIHQPSidIFEAFDELLLMKRG 1096
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
420-579 |
1.07e-04 |
|
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: 44.95 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 420 SGEISMDDHGIDTlNVEWLRSQIGLVSQEPVLFAT-SIRENILFgdetaslkqvvaAAKMaNAHEFIVKLphgyethvgq 498
Cdd:cd03233 64 EGDIHYNGIPYKE-FAEKYPGEIIYVSEEDVHFPTlTVRETLDF------------ALRC-KGNEFVRGI---------- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 499 fgtqlSGGQKQRIAIARALVRDPRILLLDEATSALDAESE-------RTVQDALdrasvgRTTVIVAhrLS-----TLRK 566
Cdd:cd03233 120 -----SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAleilkciRTMADVL------KTTTFVS--LYqasdeIYDL 186
|
170
....*....|...
gi 1002260479 567 ADTIAVLDAGRVV 579
Cdd:cd03233 187 FDKVLVLYEGRQI 199
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
501-547 |
1.11e-04 |
|
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: 45.09 E-value: 1.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1002260479 501 TQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR 547
Cdd:cd03237 114 PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
502-560 |
1.15e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.95 E-value: 1.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAES----ERTVQDALDRAsvGRTTVIVAHR 560
Cdd:COG2401 136 ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTakrvARNLQKLARRA--GITLVVATHH 196
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1149-1228 |
1.35e-04 |
|
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: 45.30 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1149 GYdTRVGERGAQLSGGQRQRIALARAVLKDAR---ILLLDEATSALDAASERLVQDAVDRML-RGRTCVVVAHRLSTVEK 1224
Cdd:cd03271 159 GY-IKLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIKC 237
|
....
gi 1002260479 1225 SDTI 1228
Cdd:cd03271 238 ADWI 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
475-586 |
1.63e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 475 AAKMANAHEFIVKLPHGYETHVG-QFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDAL-DRASVGR 552
Cdd:TIGR00956 181 AKHIADVYMATYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALkTSANILD 260
|
90 100 110
....*....|....*....|....*....|....*..
gi 1002260479 553 TTVIVA-HRLS--TLRKADTIAVLDAGRVVEAGTHDE 586
Cdd:TIGR00956 261 TTPLVAiYQCSqdAYELFDKVIVLYEGYQIYFGPADK 297
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
502-571 |
1.78e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.50 E-value: 1.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 502 QLSGGQKQRIAIA-----RALVRDPrILLLDEATSALDAESERTVQDALDRASVGRTTVIVA-HRLSTLRKADTIA 571
Cdd:cd03227 77 QLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVItHLPELAELADKLI 151
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1033-1195 |
1.81e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1033 PEVAVLAGFSLEIGAGKTVALVGPSGSGKST----VIGLIERFYDAQRGSVLVDG---EDIRSyslaRLRSQVALVSQEP 1105
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGitpEEIKK----HYRGDVVYNAETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1106 TLF-SGTIRDNIAYGAA-------EEHATEDEVARAAALANAHGFisAMERGYDTRVGE---RGaqLSGGQRQRIALARA 1174
Cdd:TIGR00956 148 VHFpHLTVGETLDFAARcktpqnrPDGVSREEYAKHIADVYMATY--GLSHTRNTKVGNdfvRG--VSGGERKRVSIAEA 223
|
170 180
....*....|....*....|.
gi 1002260479 1175 VLKDARILLLDEATSALDAAS 1195
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSAT 244
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
378-568 |
1.89e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.17 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 378 DTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWlRSQIGLVSQE----PVLfa 453
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGHRsginPYL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 454 tSIRENILFGDETASLKQVVAAAKMANAHEFIVKLPHGYethvgqfgtqLSGGQKQRIAIARALVRDPRILLLDEATSAL 533
Cdd:PRK13540 90 -TLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1002260479 534 DAESERTVQDALD--RASvGRTTVIVAHRLSTLRKAD 568
Cdd:PRK13540 159 DELSLLTIITKIQehRAK-GGAVLLTSHQDLPLNKAD 194
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
421-578 |
1.91e-04 |
|
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: 45.59 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 421 GEISMDDHGIDTLN-VEWLRSQIGLVSQE-------PVLfatSIRENILFG--DETASLKQVVAAAKMANAHEFIVKLph 490
Cdd:TIGR02633 316 GNVFINGKPVDIRNpAQAIRAGIAMVPEDrkrhgivPIL---GVGKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRL-- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 491 gyetHVGQFG-----TQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLS-T 563
Cdd:TIGR02633 391 ----KVKTASpflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAeV 466
|
170
....*....|....*
gi 1002260479 564 LRKADTIAVLDAGRV 578
Cdd:TIGR02633 467 LGLSDRVLVIGEGKL 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
502-563 |
2.17e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 45.31 E-value: 2.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDraSVGRTTVIVAH------RLST 563
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL--NFAGCAVVISHdrwfldRIAT 508
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
504-583 |
2.61e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.25 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 504 SGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAH--RLSTLRKADTIAVLDAGRVVE 580
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
...
gi 1002260479 581 AGT 583
Cdd:CHL00131 233 TGD 235
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
738-981 |
2.70e-04 |
|
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: 44.35 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 738 FLFLGIAVVCITANIVQHYNFAVMGERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKVRSLVGDRMCLL 817
Cdd:cd18551 40 ALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDR--RRSGDLVSRVTNDTTLLRELITSGLPQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 818 VQAGATASLGFSLALAVSWRLATVMMAMQPLIIASFYfkkVLMAAMSKKAKKAQVQGSQLAS---EAVVNHRTITAFSSQ 894
Cdd:cd18551 118 VTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIIL---PLGRRIRKASKRAQDALGELSAaleRALSAIRTVKASNAE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 895 RRMLRLYEAAQQGPKKDNVAHSWFSGFCLCLCQFSNTGSMAVALWYGGKLMAKGLITPTHLFQvFFMLMTMgrVIADAGS 974
Cdd:cd18551 195 ERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVA-FLLYLFQ--LITPLSQ 271
|
....*..
gi 1002260479 975 LTSDLAQ 981
Cdd:cd18551 272 LSSFFTQ 278
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
367-592 |
2.89e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 44.37 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 367 KDVHFSypsRPDTLVLNGFNLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEWL---RSQIG 443
Cdd:PRK11831 11 RGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 444 LVSQEPVLFA-TSIRENILFG--DETASLKQVVAAAKManahefiVKLphgyeTHVGQFG------TQLSGGQKQRIAIA 514
Cdd:PRK11831 88 MLFQSGALFTdMNVFDNVAYPlrEHTQLPAPLLHSTVM-------MKL-----EAVGLRGaaklmpSELSGGMARRAALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 515 RALVRDPRILLLDEATSALDAESERTVQDALDR--ASVGRTTVIVAHRL-STLRKADTIAVLDAGRVVEAGTHDELLGMD 591
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISElnSALGVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
.
gi 1002260479 592 D 592
Cdd:PRK11831 236 D 236
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1048-1222 |
3.24e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1048 GKTVALVGPSGSGKSTVIGLIerfydAQR--------GSVLVDGEDIRSySLARLRSQVAlvSQEPTLFSGTIRDNIAYG 1119
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVL-----AERvttgvitgGDRLVNGRPLDS-SFQRSIGYVQ--QQDLHLPTSTVRESLRFS 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1120 A----------AEEHATEDEVARaaalanahgfISAMERGYDTRVGERGAQLSGGQRQRIALA-RAVLKDARILLLDEAT 1188
Cdd:TIGR00956 861 AylrqpksvskSEKMEYVEEVIK----------LLEMESYADAVVGVPGEGLNVEQRKRLTIGvELVAKPKLLLFLDEPT 930
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002260479 1189 SALDAASE----RLVQDAVDrmlRGRTCVVVAHRLSTV 1222
Cdd:TIGR00956 931 SGLDSQTAwsicKLMRKLAD---HGQAILCTIHQPSAI 965
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1038-1228 |
3.36e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 42.70 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1038 LAGFSLEIGAGKTVALVGPSGSGKSTVigLIERFYDAQRgsvlvdgedirsyslARLRSQVALVSQEPTLFSGTIRdnia 1117
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGK---------------ARLISFLPKFSRNKLIFIDQLQ---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1118 ygaaeehatedevaraaalanahgFISAMERGYDTrVGERGAQLSGGQRQRIALARAVLKDAR--ILLLDEATSALDAAS 1195
Cdd:cd03238 70 ------------------------FLIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190
....*....|....*....|....*....|....
gi 1002260479 1196 ERLVQDAVDRML-RGRTCVVVAHRLSTVEKSDTI 1228
Cdd:cd03238 125 INQLLEVIKGLIdLGNTVILIEHNLDVLSSADWI 158
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
24-253 |
3.56e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 44.09 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 24 MALGVLGSFGDGMMQPLSMLVLG---DIVNSYGGAGGAGSARSAFSSGAVDKFALRLLYVAVAVGACSFLE---GLCWTR 97
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGvaiDAVFNGEASFLPLVPASLGPADPRGQLWLLGGLTVAAFLLESLFQylsGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 98 TAERQASKMRRLYLEAVLSQEVAFFDAAPsspsspqaqaqatTFRVISTVSDDADAIQDFLGEKLPMVLANATLFFGALA 177
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQ-------------TGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002260479 178 VSFVFAWRLAL-AGLPFTLLLFVTpsVLLAGRMAAAAGEARAAYEEAGGIAQQAVSSIRTVASYTAERRTVERFRGA 253
Cdd:cd18565 148 ILFYLNWQLALvALLPVPLIIAGT--YWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADA 222
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
24-200 |
3.59e-04 |
|
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: 43.93 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 24 MALGVLGSFGDGMMQPLSMLVLGDIVNSYGGAGGAGSArsaFSSGAVDKFALRLLYVAVAVGACSFLEGLCWTRTAERQA 103
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGG---VDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 104 SKMRRLYLEAVLSQEVAFFDaapsspsspqaqaQATTFRVISTVSDDADAIQDFLGEKLPMVLANATLFFGALAVSFVFA 183
Cdd:cd18547 78 YDLRKDLFEKLQRLPLSYFD-------------THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYIS 144
|
170
....*....|....*..
gi 1002260479 184 WRLALAGLPFTLLLFVT 200
Cdd:cd18547 145 PLLTLIVLVTVPLSLLV 161
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
363-580 |
4.33e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.58 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 363 EIVFKDVHFSYPSrpdtlvlNGF-----NLTISEGATVGLVGGSGSGKSTVISLLQRFYSPDSGEISMDDHGIDTLNVEW 437
Cdd:PRK10522 322 TLELRNVTFAYQD-------NGFsvgpiNLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 438 LRSQIGLVSQEPVLFatsirENILFGDETASLKQVVAA----AKMANAhefiVKLPHGYETHvgqfgTQLSGGQKQRIAI 513
Cdd:PRK10522 395 YRKLFSAVFTDFHLF-----DQLLGPEGKPANPALVEKwlerLKMAHK----LELEDGRISN-----LKLSKGQKKRLAL 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 514 ARALVRDPRILLLDEATSALDAESERTV-QDALDR-ASVGRTTVIVAHRLSTLRKADTIAVLDAGRVVE 580
Cdd:PRK10522 461 LLALAEERDILLLDEWAADQDPHFRREFyQVLLPLlQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
77-306 |
4.49e-04 |
|
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: 43.61 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 77 LLYVAVAVG--ACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDAAPSSpsspqaqaqattfRVISTVSDDADAI 154
Cdd:cd18545 44 LLFLALNLVnwVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVG-------------KILSRVINDVNSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 155 QDFLGEKLPMVLANATLFFGALAVSFVFAWRLAL---AGLPFtLLLFVTpsvLLAGRMAAAAGEARAAYEEAGGIAQQAV 231
Cdd:cd18545 111 SDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALvtlAVLPL-LVLVVF---LLRRRARKAWQRVRKKISNLNAYLHESI 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002260479 232 SSIRTVASYTAERRTVERFRGAVARSAALGVRQGLIKGAVIGSMGVIYAVWSFLS-WIGSLLVIHLHAQGGhVFVA 306
Cdd:cd18545 187 SGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVyWYGGKLVLGGAITVG-VLVA 261
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
503-534 |
6.34e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.84 E-value: 6.34e-04
10 20 30
....*....|....*....|....*....|..
gi 1002260479 503 LSGGQKQRIAIARALVRDPRILLLDEATSALD 534
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
501-589 |
6.83e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 501 TQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDR-ASVGRTTVIVAHRLSTLRK-ADTIAVLDAGRV 578
Cdd:PRK10938 134 KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTL 213
|
90
....*....|.
gi 1002260479 579 VEAGTHDELLG 589
Cdd:PRK10938 214 AETGEREEILQ 224
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1045-1192 |
7.48e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1045 IGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVDGedirSYSLarlrsqvALVSQEPTLFSGTIRDNIAYGAAEEH 1124
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----NWQL-------AWVNQETPALPQPALEYVIDGDREYR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1125 ATEDEVARAAALANAHGfISAMERGYDT----RVGERGAQL------------------SGGQRQRIALARAVLKDARIL 1182
Cdd:PRK10636 93 QLEAQLHDANERNDGHA-IATIHGKLDAidawTIRSRAASLlhglgfsneqlerpvsdfSGGWRMRLNLAQALICRSDLL 171
|
170
....*....|
gi 1002260479 1183 LLDEATSALD 1192
Cdd:PRK10636 172 LLDEPTNHLD 181
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
495-534 |
8.32e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 8.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1002260479 495 HVGQFGTQ----------LSGGQKQRIAIARALVRDPRILLLDEATSALD 534
Cdd:PLN03073 610 HLGSFGVTgnlalqpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
502-534 |
8.39e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 8.39e-04
10 20 30
....*....|....*....|....*....|...
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALD 534
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
493-559 |
9.10e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 9.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 493 ETHVGQFgTQLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDAL-DRASvgrTTVIVAH 559
Cdd:PRK15064 147 EQHYGLM-SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLnERNS---TMIIISH 210
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1159-1236 |
9.78e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.38 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1159 AQLSGGQRQRIALARAVLKDARILLLDEATSALD--AASE--RLVQDAVDrmlRGRTCVVVAHRLSTV-EKSDTIAVVKD 1233
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgAKYEiyKLINQLVQ---QGVAIIVISSELPEVlGLSDRVLVMHE 480
|
...
gi 1002260479 1234 GRV 1236
Cdd:PRK13549 481 GKL 483
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
738-969 |
9.78e-04 |
|
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: 42.77 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 738 FLFLGIAVVCITANIVQHYNFAVMGERLTERVRGQMLAKILSFEVGWFDEDENSSAAVcaRLATQSSKVRSLVGdrMCL- 816
Cdd:cd18548 43 LLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLIT--RLTNDVTQVQNFVM--MLLr 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 817 -LVQAGATASLGFSLALAVSWRLATVMMAMQPLIIASFYF--KKVLmaamskkAKKAQVQGS-----QLASEAVVNHRTI 888
Cdd:cd18548 119 mLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLimKKAI-------PLFKKVQKKldrlnRVVRENLTGIRVI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 889 TAFSSQRRMLRLYEAAQQGPKKDNVAHSWFSGFCLCLCQFSNTGSMAVALWYGGKLMAKGLITP-------THLFQVFFM 961
Cdd:cd18548 192 RAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVgdlvafiNYLMQILMS 271
|
....*...
gi 1002260479 962 LMTMGRVI 969
Cdd:cd18548 272 LMMLSMVF 279
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
725-850 |
1.03e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 42.47 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 725 DDGQIRSKTRLYYFLFLG-IAVVCITA--NIVQHYNFAVMGERLTERVRGQMLAKILSFEVGWFdeDENSSAAVCARLAT 801
Cdd:cd18550 27 DDALPQGDLGLLVLLALGmVAVAVASAllGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFF--TRTRTGEIQSRLNN 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1002260479 802 QSSKVRSLVGDRMCLLVQAGATASLGFSLALAVSWRLATVMMAMQPLII 850
Cdd:cd18550 105 DVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFV 153
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1149-1228 |
1.09e-03 |
|
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: 43.46 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1149 GYdTRVGERGAQLSGGQRQRIALARAVLKDAR---ILLLDEATSALDAASERLVQDAVDRML-RGRTCVVVAHRLSTVEK 1224
Cdd:TIGR00630 819 GY-IRLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVdKGNTVVVIEHNLDVIKT 897
|
....
gi 1002260479 1225 SDTI 1228
Cdd:TIGR00630 898 ADYI 901
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1020-1192 |
1.21e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.18 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1020 IEFKNVHFSYPTRpevaVL-AGFSLEIGAGKTVALVGPSGSGKSTVIGLIERFYDAQRGSVLVdGEDIrsyslarlrsQV 1098
Cdd:PRK11819 325 IEAENLSKSFGDR----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 1099 ALVSQ-------EPTLF---SGTiRDNIAYGAAEEHAtedevaraaalanahgfisameRGYDTRVGERGA-------QL 1161
Cdd:PRK11819 390 AYVDQsrdaldpNKTVWeeiSGG-LDIIKVGNREIPS----------------------RAYVGRFNFKGGdqqkkvgVL 446
|
170 180 190
....*....|....*....|....*....|.
gi 1002260479 1162 SGGQRQRIALARAVLKDARILLLDEATSALD 1192
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
442-537 |
1.42e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 442 IGLVSQEPVLFATS-IRENILFgdeTASLKQ---VVAAAKMANAHEFI--VKLPHGYETHVGQFGTQLSGGQKQRIAIAR 515
Cdd:TIGR00956 838 IGYVQQQDLHLPTStVRESLRF---SAYLRQpksVSKSEKMEYVEEVIklLEMESYADAVVGVPGEGLNVEQRKRLTIGV 914
|
90 100
....*....|....*....|...
gi 1002260479 516 ALVRDPRILL-LDEATSALDAES 537
Cdd:TIGR00956 915 ELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
502-547 |
1.43e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 39.14 E-value: 1.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002260479 502 QLSGGQKQR---IAIARALV----------RDPRILLLDEATSALDAESERTVQDALDR 547
Cdd:pfam13558 32 GLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
496-580 |
1.92e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.46 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 496 VGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALD--AESE-RTVQDALdrASVGRTTVIVAHRL-STLRKADTIA 571
Cdd:PRK09700 403 VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvgAKAEiYKVMRQL--ADDGKVILMVSSELpEIITVCDRIA 480
|
....*....
gi 1002260479 572 VLDAGRVVE 580
Cdd:PRK09700 481 VFCEGRLTQ 489
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
502-537 |
1.92e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 40.94 E-value: 1.92e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAES 537
Cdd:PRK13538 129 QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1160-1192 |
2.29e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.29e-03
10 20 30
....*....|....*....|....*....|...
gi 1002260479 1160 QLSGGQRQRIALARAVLKDARILLLDEATSALD 1192
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
503-588 |
3.20e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 503 LSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALDRASvGrTTVIVAH-R--LSTLrkADTIAVLDAGRVV 579
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYE-G-TLIFVSHdRefVSSL--ATRIIEITPDGVV 514
|
90
....*....|
gi 1002260479 580 E-AGTHDELL 588
Cdd:PRK15064 515 DfSGTYEEYL 524
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
758-969 |
3.78e-03 |
|
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: 40.78 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 758 FAVMGERLTERVRGQMLAKILSFEVGWFDEdeNSSAAVCARLATQSSKV-RSLVGDRMCLLVQAGATASLgFSLALAVSW 836
Cdd:cd18590 60 FMCTLSRLNLRLRHQLFSSLVQQDIGFFEK--TKTGDLTSRLSTDTTLMsRSVALNANVLLRSLVKTLGM-LGFMLSLSW 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 837 RLATVMMAMQPLIIASfyfKKVLMAAMSKKAKKAQ---VQGSQLASEAVVNHRTITAFSSQRRMLRLYEAAQQGPKKDNV 913
Cdd:cd18590 137 QLTLLTLIEMPLTAIA---QKVYNTYHQKLSQAVQdsiAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKD 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002260479 914 AHSWFSGFCLCLCQFSNTGSMAVALWYGGKLMAKGLITPTHLfqVFFML--MTMGRVI 969
Cdd:cd18590 214 RRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSL--VSFILyqKNLGSYV 269
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
87-273 |
3.88e-03 |
|
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: 40.78 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 87 CSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDaapsspsspqaqaQATTFRVISTVSDDADAIQDFLGEKLPMVL 166
Cdd:cd18590 52 SAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFE-------------KTKTGDLTSRLSTDTTLMSRSVALNANVLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 167 ANATLFFGALAVSFVFAWRLALAGLPFTLLLFVTPSVLlAGRMAAAAGEARAAYEEAGGIAQQAVSSIRTVASYTAERRT 246
Cdd:cd18590 119 RSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVY-NTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEE 197
|
170 180
....*....|....*....|....*..
gi 1002260479 247 VERFRGAVARSAALGVRQGLIKGAVIG 273
Cdd:cd18590 198 ACRYSEALERTYNLKDRRDTVRAVYLL 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
479-586 |
4.05e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.44 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 479 ANAHEFI----VKLPHGyETHVGQfgtqLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDAL-DRASVGRT 553
Cdd:PRK11288 374 ENADRFIrslnIKTPSR-EQLIMN----LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIyELAAQGVA 448
|
90 100 110
....*....|....*....|....*....|....
gi 1002260479 554 TVIVAHRL-STLRKADTIAVLDAGRVVEAGTHDE 586
Cdd:PRK11288 449 VLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
403-590 |
4.32e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 403 SGKSTVISLLQRFYSPDSGEIsmddhgidtlnvEWL----------RSQ---IGLVSQEPVLFAT-SIRENILFGDETAS 468
Cdd:PRK10762 41 AGKSTMMKVLTGIYTRDAGSI------------LYLgkevtfngpkSSQeagIGIIHQELNLIPQlTIAENIFLGREFVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 469 LKQVVAAAKM-ANAHEFIVKL--PHGYETHVGqfgtQLSGGQKQRIAIARALVRDPRILLLDEATSAL-DAESERTVQDA 544
Cdd:PRK10762 109 RFGRIDWKKMyAEADKLLARLnlRFSSDKLVG----ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRVI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002260479 545 LDRASVGRTTVIVAHRLSTLRK-ADTIAVLDAG-----RVVEAGTHDELLGM 590
Cdd:PRK10762 185 RELKSQGRGIVYISHRLKEIFEiCDDVTVFRDGqfiaeREVADLTEDSLIEM 236
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
145-294 |
5.35e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 40.21 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 145 STVSDDADAIQDFLGEKLPMVLANATLFFGALAVSFVFAWRLALAGL-PFTLLLFVTpsVLLAGRMAAAAGEARAAYEEA 223
Cdd:cd18778 101 SRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLiPIPFLALGA--WLYSKKVRPRYRKVREALGEL 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002260479 224 GGIAQQAVSSIRTVASYTAERRTVERFRGavarsAALGVRQGLIKGAVIgsMGVIYAVWSFLSWIGSLLVI 294
Cdd:cd18778 179 NALLQDNLSGIREIQAFGREEEEAKRFEA-----LSRRYRKAQLRAMKL--WAIFHPLMEFLTSLGTVLVL 242
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
1048-1087 |
6.30e-03 |
|
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
Pssm-ID: 396247 [Multi-domain] Cd Length: 154 Bit Score: 38.84 E-value: 6.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1002260479 1048 GKTVALVGPSGSGKSTVIGLIERFYDAQRGSV-LVDGEDIR 1087
Cdd:pfam01583 2 GCTIWLTGLSGAGKSTIANALERKLFEQGRSVyVLDGDNVR 42
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
78-199 |
6.52e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 40.15 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002260479 78 LYVA--VAVGACSFLEGLCWTRTAERQASKMRRLYLEAVLSQEVAFFDAAPsspsspqaqaqatTFRVISTVSDDADAIQ 155
Cdd:cd18606 40 IYAGlgVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTP-------------LGRILNRFSKDTDVLD 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1002260479 156 DFLGEKLPMVLANATLFFGALAVSFVFAWRLALAgLPFTLLLFV 199
Cdd:cd18606 107 NELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIA-LPPLLVLYY 149
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
502-546 |
7.85e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 7.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1002260479 502 QLSGGQKQRIAIARALVRDPRILLLDEATSALDAESERTVQDALD 546
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
494-534 |
8.72e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.03 E-value: 8.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1002260479 494 THVGQFGTQLSGGQKQRIAIARALVRDPRILLLDEATSALD 534
Cdd:PRK15439 395 NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
503-534 |
9.49e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.00 E-value: 9.49e-03
10 20 30
....*....|....*....|....*....|...
gi 1002260479 503 LSGGQkQRIA-IARALVRDPRILLLDEATSALD 534
Cdd:PRK10938 402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433
|
|
| |
