|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
10-574 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 628.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 10 SFKKLWLLTNPPTGKLLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQ----LIAGLLVLFAAQMVTSAVSLYLLAQ 85
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSalllLLLLLLGLALLRALLSYLQRYLLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 86 VGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLIL 165
Cdd:COG1132 88 LAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 166 LAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAII 245
Cdd:COG1132 168 LLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 246 TPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIFDILAEKEENYEN 325
Cdd:COG1132 248 FPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 326 GEVLEQV---GSLRFDKVAFQY-EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNV 401
Cdd:COG1132 328 PGAVPLPpvrGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 402 NLRSWRHLFSYVQQDSPILAGTIRENLIYGLErHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIA 481
Cdd:COG1132 408 TLESLRRQIGVVPQDTFLFSGTIRENIRYGRP-DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 482 IARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASHS 561
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGG 566
|
570
....*....|...
gi 1265182468 562 FYRRLVEQQFQTS 574
Cdd:COG1132 567 LYARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-570 |
2.15e-171 |
|
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: 502.83 E-value: 2.15e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 9 FSFKKLWLLTNPPTGKLLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQ----LIAGLLVLFAAQMVTSAVSLYLLA 84
Cdd:COG2274 142 FGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLStlwvLAIGLLLALLFEGLLRLLRSYLLL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 85 QVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRItNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLI 164
Cdd:COG2274 222 RLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALV 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 165 LLAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAI 244
Cdd:COG2274 301 VLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNL 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 245 ITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIFDILAEKEENYE 324
Cdd:COG2274 381 LSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 325 NGEVLEQV---GSLRFDKVAFQY--EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQ 399
Cdd:COG2274 461 GRSKLSLPrlkGDIELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 400 NVNLRSWRHLFSYVQQDSPILAGTIRENLIYGLErHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQR 479
Cdd:COG2274 541 QIDPASLRRQIGVVLQDVFLFSGTIRENITLGDP-DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 480 IAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLAS 559
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
570
....*....|.
gi 1265182468 560 HSFYRRLVEQQ 570
Cdd:COG2274 700 KGLYAELVQQQ 710
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
13-571 |
1.40e-150 |
|
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: 444.91 E-value: 1.40e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 13 KLWLLTNPPTGKLLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQLI----AGLLVLFAAQMVTSAVSLYLLAQVGQ 88
Cdd:TIGR02204 8 ALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLnryfAFLLVVALVLALGTAARFYLVTWLGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 89 GVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAV 168
Cdd:TIGR02204 88 RVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 169 IPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPI 248
Cdd:TIGR02204 168 VPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 249 ISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIFDILAEKEE--NYENG 326
Cdd:TIGR02204 248 VIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDikAPAHP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 327 EVLEQ--VGSLRFDKVAFQYE---DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNV 401
Cdd:TIGR02204 328 KTLPVplRGEIEFEQVNFAYParpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 402 NLRSWRHLFSYVQQDSPILAGTIRENLIYGlERHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIA 481
Cdd:TIGR02204 408 DPAELRARMALVPQDPVLFAASVMENIRYG-RPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 482 IARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASHS 561
Cdd:TIGR02204 487 IARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGG 566
|
570
....*....|
gi 1265182468 562 FYRRLVEQQF 571
Cdd:TIGR02204 567 LYARLARLQF 576
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
10-573 |
1.13e-142 |
|
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: 424.51 E-value: 1.13e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 10 SFKKLWLLTNPPTGKLLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQLI----AGLLVLFAAQMVTSAVSLYLLAQ 85
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLwwvpLVVIGLAVLRGICSFVSTYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 86 VGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLIL 165
Cdd:TIGR02203 81 VSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 166 LAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAII 245
Cdd:TIGR02203 161 VVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 246 TPI---ISTVMTAVMIAIVGFGAyrvSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIFDILAEKEEN 322
Cdd:TIGR02203 241 SPItqlIASLALAVVLFIALFQA---QAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 323 YENGEVLEQV-GSLRFDKVAFQY--EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQ 399
Cdd:TIGR02203 318 DTGTRAIERArGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 400 NVNLRSWRHLFSYVQQDSPILAGTIRENLIYGLERHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQR 479
Cdd:TIGR02203 398 DYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 480 IAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLAS 559
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
570
....*....|....
gi 1265182468 560 HSFYRRLVEQQFQT 573
Cdd:TIGR02203 558 NGLYAQLHNMQFRE 571
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-571 |
1.48e-119 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 365.50 E-value: 1.48e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 11 FKKLWLLTNPPTGKLLISFILALINTGA-----SLSIPLvIKEVMEKIAIGVS---PQLIAGLLVLfaaQMVTSAVSLYL 82
Cdd:PRK11176 13 FRRLWPTIAPFKAGLIVAGVALILNAASdtfmlSLLKPL-LDDGFGKADRSVLkwmPLVVIGLMIL---RGITSFISSYC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 83 LAQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMT 162
Cdd:PRK11176 89 ISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 163 LILLAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIE 242
Cdd:PRK11176 169 LILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSAS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 243 AIITPIIStVMTAVMIAIVGFGAYRVS-EGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIFDILAEKEE 321
Cdd:PRK11176 249 SISDPIIQ-LIASLALAFVLYAASFPSvMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 322 NYENGEVLEQV-GSLRFDKVAFQYE--DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDS 398
Cdd:PRK11176 328 KDEGKRVIERAkGDIEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 399 QNVNLRSWRHLFSYVQQDSPILAGTIRENLIYGLERHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQ 478
Cdd:PRK11176 408 RDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQ 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 479 RIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLA 558
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLA 567
|
570
....*....|...
gi 1265182468 559 SHSFYRRLVEQQF 571
Cdd:PRK11176 568 QNGVYAQLHKMQF 580
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-560 |
7.75e-116 |
|
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: 355.22 E-value: 7.75e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 12 KKLWLLTNPPTGKLLISFILALINTGASLSIPLVIKEVMEKIAIGVSP-----QLIAGLLVLFAAQMVTSAVSLYLLAQV 86
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPlsallPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 87 GQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSritndttivmnlLSTEMIDFVKN---------ILSIIVAIVIL--- 154
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELAT------------LLTEGVEALDGyfarylpqlFLAALVPLLILvav 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 155 FTLDVPMTLILLA---VIPVMFVLVMPLARKIhkiSREQQDKMSKLTA-FL--AQMLSEIRLIKVSGSEKKEVDSGLQSF 228
Cdd:COG4988 154 FPLDWLSGLILLVtapLIPLFMILVGKGAAKA---SRRQWRALARLSGhFLdrLRGLTTLKLFGRAKAEAERIAEASEDF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 229 QSLYLFGVKRAKIEAIITPIISTVMTAVMIAIVGFgayRVSEGFITAGELVaFVLYL----FQimvPvgsLTRFVTSFQQ 304
Cdd:COG4988 231 RKRTMKVLRVAFLSSAVLEFFASLSIALVAVYIGF---RLLGGSLTLFAAL-FVLLLapefFL---P---LRDLGSFYHA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 305 T---KGASERIFDILAEKEENYENGEV---LEQVGSLRFDKVAFQYED-KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVF 377
Cdd:COG4988 301 RangIAAAEKIFALLDAPEPAAPAGTAplpAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 378 SLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTIRENLIYGlERHVTDEEIEEAAKLANAHHFIQSF 457
Cdd:COG4988 381 NLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLG-RPDASDEELEAALEAAGLDEFVAAL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 458 EAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINAD 537
Cdd:COG4988 460 PDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQAD 539
|
570 580
....*....|....*....|...
gi 1265182468 538 QIVVIEEGQVTGSGTHKELLASH 560
Cdd:COG4988 540 RILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
336-570 |
6.55e-113 |
|
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: 336.05 E-value: 6.55e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 336 RFDKVAFQYEDKP---VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSY 412
Cdd:cd03249 2 EFKNVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 413 VQQDSPILAGTIRENLIYGLERhVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQF 492
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPD-ATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 493 LLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASHSFYRRLVEQQ 570
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
25-312 |
5.10e-112 |
|
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: 335.56 E-value: 5.10e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKI-AIGVSPQLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLI 103
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALsAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 104 KLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKI 183
Cdd:cd18551 81 RLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 184 HKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAIVGF 263
Cdd:cd18551 161 RKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1265182468 264 GAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18551 241 GGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-567 |
1.60e-111 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 348.64 E-value: 1.60e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 13 KLWLLTNPPTGKLLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQLIAGLLVLFAAQMVTSAVS--------LYLLA 84
Cdd:TIGR00958 151 RLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSaglrggsfNYTMA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 85 QVgqgvVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLI 164
Cdd:TIGR00958 231 RI----NLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMV 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 165 LLAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAI 244
Cdd:TIGR00958 307 TLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAG 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 245 ITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIFDILAEKEENYE 324
Cdd:TIGR00958 387 YLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 325 NGEV--LEQVGSLRFDKVAFQY---EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQ 399
Cdd:TIGR00958 467 TGTLapLNLEGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 400 NVNLRSWRHLFSYVQQDSPILAGTIRENLIYGLERhVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQR 479
Cdd:TIGR00958 547 QYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD-TPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 480 IAIARALLRNPQFLLLDEATASLDSESEKLVQESLEtvMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLAS 559
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMED 703
|
....*...
gi 1265182468 560 HSFYRRLV 567
Cdd:TIGR00958 704 QGCYKHLV 711
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
335-566 |
1.87e-110 |
|
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: 329.58 E-value: 1.87e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDK--PVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSY 412
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 413 VQQDSPILAGTIRENLIYGLERhVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQF 492
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPG-ATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 493 LLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASHSFYRRL 566
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
90-569 |
2.00e-107 |
|
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: 333.66 E-value: 2.00e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 90 VVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDttivmnllstemIDFVKN------------ILSIIVAIVILFTL 157
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVAD------------VDALDNlylrvllpllvaLLVILAAVAFLAFF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 158 DVPMTLILLAVIpVMFVLVMPL--ARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFG 235
Cdd:COG4987 154 SPALALVLALGL-LLAGLLLPLlaARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 236 VKRAKIEAIITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIFDI 315
Cdd:COG4987 233 RRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNEL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 316 LAEKEENYE--NGEVLEQVGSLRFDKVAFQY--EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRI 391
Cdd:COG4987 313 LDAPPAVTEpaEPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 392 FLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTIRENLIYGLERhVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGIN 471
Cdd:COG4987 393 TLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD-ATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRR 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 472 LSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSG 551
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQG 551
|
490
....*....|....*...
gi 1265182468 552 THKELLASHSFYRRLVEQ 569
Cdd:COG4987 552 THEELLAQNGRYRQLYQR 569
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-570 |
2.04e-107 |
|
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: 334.87 E-value: 2.04e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMekIAIGVSPQLIA---GLLVLFAAQMVTSAVSLYL----LAQVGQGVVKELRHK 97
Cdd:COG5265 39 LAALLLLLLAAALALVVPPLLKDAID--ALLSGAAALLVvpvGLLLAYGLLRLLSVLFGELrdalFARVTQRAVRRLALE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 98 VWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTL-DVPMTLILLAVIPVMFVLV 176
Cdd:COG5265 117 VFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNILPTLLEIALVAGILLVKyDWWFALITLVTVVLYIAFT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 177 MPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEV-----------DSGLQSFQSLYLFGVKRAKIeaii 245
Cdd:COG5265 197 VVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREArrydealaryeRAAVKSQTSLALLNFGQALI---- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 246 tpiISTVMTAVMIaivgFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTrFVtsFQQTKGAS---ERIFDILAEKEEN 322
Cdd:COG5265 273 ---IALGLTAMML----MAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLG-FV--YREIRQALadmERMFDLLDQPPEV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 323 YENGEVLEQV---GSLRFDKVAFQYE-DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDS 398
Cdd:COG5265 343 ADAPDAPPLVvggGEVRFENVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 399 QNVNLRSWRHLFSYVQQDSPILAGTIRENLIYGLErHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQ 478
Cdd:COG5265 423 RDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP-DASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQ 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 479 RIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLA 558
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLA 581
|
570
....*....|..
gi 1265182468 559 SHSFYRRLVEQQ 570
Cdd:COG5265 582 QGGLYAQMWARQ 593
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
25-570 |
1.12e-99 |
|
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: 317.45 E-value: 1.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALIntgaSLSIPLVIKEVMEKIAIGVSPQ----LIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWN 100
Cdd:TIGR01846 145 LLISLALQLF----ALVTPLLFQVVIDKVLVHRGLStlsvLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 101 KLIKLPVSFYDQNRSGEMVSRITNDTTIvMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLA 180
Cdd:TIGR01846 221 HLLGLPLGYFESRRVGDTVARVRELEQI-RNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 181 RKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAI 260
Cdd:TIGR01846 300 PILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAIL 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 261 VGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIFDILAEKEENYENGEVL--EQVGSLRFD 338
Cdd:TIGR01846 380 LWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEPRSAGLAAlpELRGAITFE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 339 KVAFQY-EDKP-VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQD 416
Cdd:TIGR01846 460 NIRFRYaPDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 417 SPILAGTIRENLIYGlERHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLD 496
Cdd:TIGR01846 540 NVLFSRSIRDNIALC-NPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFD 618
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 497 EATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASHSFYRRLVEQQ 570
Cdd:TIGR01846 619 EATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
335-570 |
1.83e-99 |
|
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: 301.46 E-value: 1.83e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYED-KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYV 413
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 414 QQDSPILAGTIRENLIYGLErHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFL 493
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRP-DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 494 LLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASHSFYRRLVEQQ 570
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
333-560 |
5.39e-97 |
|
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: 294.90 E-value: 5.39e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 333 GSLRFDKVAFQY-EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFS 411
Cdd:cd03254 1 GEIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 412 YVQQDSPILAGTIRENLIYGLERhVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQ 491
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPN-ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265182468 492 FLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASH 560
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
61-568 |
6.17e-94 |
|
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: 302.63 E-value: 6.17e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 61 LIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRI-TNDTtiVMNLLSTEMID 139
Cdd:TIGR03796 196 LLLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVqLNDQ--VAEFLSGQLAT 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 140 FVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKk 219
Cdd:TIGR03796 274 TALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLES- 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 220 EVDSGLQSFQSLYLFGVKR-AKIEAIITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRF 298
Cdd:TIGR03796 353 DFFSRWAGYQAKLLNAQQElGVLTQILGVLPTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGF 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 299 VTSFQQTKGASERIFDIL----AEKEENYENGEVLEQ-----VGSLRFDKVAFQYE--DKPVLQEVSFSAKKGEVTAFVG 367
Cdd:TIGR03796 433 GGTLQELEGDLNRLDDVLrnpvDPLLEEPEGSAATSEpprrlSGYVELRNITFGYSplEPPLIENFSLTLQPGQRVALVG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 368 PSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTIRENLIYgLERHVTDEEIEEAAKL 447
Cdd:TIGR03796 513 GSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTL-WDPTIPDADLVRACKD 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 448 ANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLetvmKER--TSLV 525
Cdd:TIGR03796 592 AAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL----RRRgcTCII 667
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1265182468 526 IAHRLSTVINADQIVVIEEGQVTGSGTHKELLASHSFYRRLVE 568
Cdd:TIGR03796 668 VAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
101-571 |
3.88e-90 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 289.17 E-value: 3.88e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 101 KLIKLPVSFYDQNRSGEMVSRITNDTtivmNLLSTEMIDFVKNILSIIVAIVIL----FTLDVPMTLIL--LAVIPVMF- 173
Cdd:PRK13657 98 RIIQLPLAWHSQRGSGRALHTLLRGT----DALFGLWLEFMREHLATLVALVVLlplaLFMNWRLSLVLvvLGIVYTLIt 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 174 VLVMplaRKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVdSGLQSFQSlylfgvkraKIEAIITPIIS--- 250
Cdd:PRK13657 174 TLVM---RKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAET-QALRDIAD---------NLLAAQMPVLSwwa 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 251 --TVM-----TAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIFDIL---AEKE 320
Cdd:PRK13657 241 laSVLnraasTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEdavPDVR 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 321 ENYENGEVLEQVGSLRFDKVAFQYEDK-PVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQ 399
Cdd:PRK13657 321 DPPGAIDLGRVKGAVEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 400 NVNLRSWRHLFSYVQQDSPILAGTIRENLIYGLErHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQR 479
Cdd:PRK13657 401 TVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRP-DATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQR 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 480 IAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLAS 559
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR 559
|
490
....*....|..
gi 1265182468 560 HSFYRRLVEQQF 571
Cdd:PRK13657 560 GGRFAALLRAQG 571
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-570 |
1.26e-80 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 264.27 E-value: 1.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 10 SFKKLWlltnpPTGKLLISF------------ILALINTGASLSIPLVIKEVME-KIAIGVSP-QLIAGLLVLFAAQMVT 75
Cdd:PRK10790 3 SFSQLW-----PTLKRLLAYgspwrkplglavLMLWVAAAAEVSGPLLISYFIDnMVAKGNLPlGLVAGLAAAYVGLQLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 76 SAVSLY----LLAQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAI 151
Cdd:PRK10790 78 AAGLHYaqslLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 152 VILFTLDVPMTLILLAVIPVMFVLVM-------PLARKIHKISREQQDK-------MSKLTAFLAQMLSEIRLIKVSGSE 217
Cdd:PRK10790 158 VAMFSLDWRMALVAIMIFPAVLVVMViyqrystPIVRRVRAYLADINDGfnevingMSVIQQFRQQARFGERMGEASRSH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 218 KkevdsgLQSFQSLYLFGVkrakieaIITPIISTVMTAVMIAIV---GFGayrvSEGFITAGELVAFVLYLFQIMVPVGS 294
Cdd:PRK10790 238 Y------MARMQTLRLDGF-------LLRPLLSLFSALILCGLLmlfGFS----ASGTIEVGVLYAFISYLGRLNEPLIE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 295 LTRFVTSFQQTKGASERIFDILAEKEENYENGEVLEQVGSLRFDKVAFQY-EDKPVLQEVSFSAKKGEVTAFVGPSGAGK 373
Cdd:PRK10790 301 LTTQQSMLQQAVVAGERVFELMDGPRQQYGNDDRPLQSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 374 STVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTIRENLIYGleRHVTDEEIEEAAKLANAHHF 453
Cdd:PRK10790 381 STLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG--RDISEEQVWQALETVQLAEL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 454 IQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTV 533
Cdd:PRK10790 459 ARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTI 538
|
570 580 590
....*....|....*....|....*....|....*..
gi 1265182468 534 INADQIVVIEEGQVTGSGTHKELLASHSFYRRLVEQQ 570
Cdd:PRK10790 539 VEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
28-567 |
7.96e-80 |
|
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: 265.06 E-value: 7.96e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 28 SFILALINTGASLSIPLVIKEVMEKIAIGVSPQLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPV 107
Cdd:TIGR01193 165 AIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPM 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 108 SFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFtLDVPMTLILLAVIPVMFVLVMPLARKIHKIS 187
Cdd:TIGR01193 245 SFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVR-QNMLLFLLSLLSIPVYAVIIILFKRTFNKLN 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 188 REQQDKMSKLTAFLAQMLSEIRLIKVSGSE---KKEVDSglqSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAIVGFG 264
Cdd:TIGR01193 324 HDAMQANAVLNSSIIEDLNGIETIKSLTSEaerYSKIDS---EFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTG 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 265 AYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIFDIL---AEKEENYENGEVLEQVGSLRFDKVA 341
Cdd:TIGR01193 401 AYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYlvdSEFINKKKRTELNNLNGDIVINDVS 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 342 FQYE-DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPIL 420
Cdd:TIGR01193 481 YSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIF 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 421 AGTIRENLIYGLERHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATA 500
Cdd:TIGR01193 561 SGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 501 SLDSESEKLVQESLeTVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASHSFYRRLV 567
Cdd:TIGR01193 641 NLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
337-570 |
1.09e-79 |
|
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: 250.48 E-value: 1.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 337 FDKVAFQYE-DKP-VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQ 414
Cdd:cd03252 3 FEHVRFRYKpDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QDSPILAGTIRENLIYGLErHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLL 494
Cdd:cd03252 83 QENVLFNRSIRDNIALADP-GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 495 LDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASHSFYRRLVEQQ 570
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
335-546 |
3.13e-78 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 244.21 E-value: 3.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYED--KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSY 412
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 413 VQQDSPILAGTIRENLiyglerhvtdeeieeaaklanahhfiqsfeaqyetmigerginLSGGQRQRIAIARALLRNPQF 492
Cdd:cd03228 81 VPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 493 LLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQ 546
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
23-570 |
1.66e-77 |
|
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: 258.35 E-value: 1.66e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 23 GKLLISFILALINTGASLSIPLVIKEVMEK-IAIGVSPQLIAGLLVLFAAQMVTSAVSL---YLLAQVGQGVVKELRHKV 98
Cdd:TIGR03797 136 RDLLAILAMGLLGTLLGMLVPIATGILIGTaIPDADRSLLVQIALALLAAAVGAAAFQLaqsLAVLRLETRMDASLQAAV 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 99 WNKLIKLPVSFYDQNRSGEMVSRITNDTTIvMNLLSTEMidfVKNILSIIVAI---VILFTLDVPMTL----ILLAVIPV 171
Cdd:TIGR03797 216 WDRLLRLPVSFFRQYSTGDLASRAMGISQI-RRILSGST---LTTLLSGIFALlnlGLMFYYSWKLALvavaLALVAIAV 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 172 MFVLVMPLARKIHKISREQqDKMSKLTAFLAQMLSEIRlikVSGSEKKEVD--SGLQSFQSLYLFGVKRAK-IEAIITPI 248
Cdd:TIGR03797 292 TLVLGLLQVRKERRLLELS-GKISGLTVQLINGISKLR---VAGAENRAFArwAKLFSRQRKLELSAQRIEnLLTVFNAV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 249 ISTVMTAVMIAIVGFGayrVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIFDILAEKEENYEN--- 325
Cdd:TIGR03797 368 LPVLTSAALFAAAISL---LGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALPEVDEAktd 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 326 -GEVleqVGSLRFDKVAFQYEDK--PVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVN 402
Cdd:TIGR03797 445 pGKL---SGAIEVDRVTFRYRPDgpLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLD 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 403 LRSWRHLFSYVQQDSPILAGTIRENLIYGLErhVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAI 482
Cdd:TIGR03797 522 VQAVRRQLGVVLQNGRLMSGSIFENIAGGAP--LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 483 ARALLRNPQFLLLDEATASLDSESEKLVQESLETVmkERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASHSF 562
Cdd:TIGR03797 600 ARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGL 677
|
....*...
gi 1265182468 563 YRRLVEQQ 570
Cdd:TIGR03797 678 FAQLARRQ 685
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
333-547 |
3.17e-75 |
|
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: 238.52 E-value: 3.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 333 GSLRFDKVAFQYEDKP---VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHL 409
Cdd:cd03248 10 GIVKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 410 FSYVQQDSPILAGTIRENLIYGLERhVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRN 489
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGLQS-CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 490 PQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQV 547
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-542 |
7.70e-73 |
|
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: 242.19 E-value: 7.70e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 23 GKLLISFILALINTGASLSIPLVIKEVMEKIAIGVSP-QLIAGLLVLFAAQMVTSAVSLYLLAQVGQ----GVVKELRHK 97
Cdd:TIGR02857 3 RALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPlAELLPALGALALVLLLRALLGWLQERAAAraaaAVKSQLRER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 98 VWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLS---TEMIDFVknILSIIVAIVIlFTLDVPMTLILLAVIPVMFV 174
Cdd:TIGR02857 83 LLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFArylPQLVLAV--IVPLAILAAV-FPQDWISGLILLLTAPLIPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 175 LVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLylfgvKRAKIEAIITPIIST--- 251
Cdd:TIGR02857 160 FMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEY-----RERTMRVLRIAFLSSavl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 252 -VMTAVMIAIVGfgayrVSEGFITAGELVAFVLYLFQ-IMVP--VGSLTRFVTSF---QQTKGASERIFDILAEKE-ENY 323
Cdd:TIGR02857 235 eLFATLSVALVA-----VYIGFRLLAGDLDLATGLFVlLLAPefYLPLRQLGAQYharADGVAAAEALFAVLDAAPrPLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 324 ENGEVLEQV-GSLRFDKVAFQYEDK-PVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNV 401
Cdd:TIGR02857 310 GKAPVTAAPaSSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 402 NLRSWRHLFSYVQQDSPILAGTIRENLIYGlERHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIA 481
Cdd:TIGR02857 390 DADSWRDQIAWVPQHPFLFAGTIAENIRLA-RPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLA 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265182468 482 IARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVI 542
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
44-575 |
1.75e-71 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 239.61 E-value: 1.75e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 44 LVIKEVMEKIAIGVSPQ-LIAGLLVLFAAQMVTSAVSLYLLAQVG---------QGVVkELRHKVWNKLIKLPVSFYDQN 113
Cdd:PRK10789 12 LIPPKVVGIIVDGVTEQhMTTGQILMWIGTMVLIAVVVYLLRYVWrvllfgasyQLAV-ELREDFYRQLSRQHPEFYLRH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 114 RSGEMVSRITNDTTIVMNLLSTEMIDFVKN-ILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKIHKISREQQD 192
Cdd:PRK10789 91 RTGDLMARATNDVDRVVFAAGEGVLTLVDSlVMGCAVLIVMSTQISWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 193 KMSKLTAFLAQMLSEIRLIKVSGSEKKE--------VDSGLQSfqslylfgVKRAKIEAIITPIIS-TVMTAVMIAIVGf 263
Cdd:PRK10789 171 AFSSLNDRTQESLTSIRMIKAFGLEDRQsalfaadaEDTGKKN--------MRVARIDARFDPTIYiAIGMANLLAIGG- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 264 GAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIFDILAEKEENYENGEVL-EQVGSLRFDKVAF 342
Cdd:PRK10789 242 GSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVpEGRGELDVNIRQF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 343 QY--EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPIL 420
Cdd:PRK10789 322 TYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 421 AGTIRENLIYGlERHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATA 500
Cdd:PRK10789 402 SDTVANNIALG-RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 501 SLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASHSFYRRLVE-QQFQTSL 575
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRyQQLEAAL 556
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
25-312 |
3.35e-70 |
|
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: 227.82 E-value: 3.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIK----EVMEKIAIGVSPQLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWN 100
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKllidDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 101 KLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLA 180
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 181 RKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAI 260
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 261 VGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
30-567 |
2.13e-68 |
|
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: 231.70 E-value: 2.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 30 ILALIntgaSLSIPLVIKEVMEKIAIGVSpqlIAGLLVLFAAQMVTSAVSLYLLAQ----VGQGVVKELRHKVWNKLIKL 105
Cdd:TIGR01192 30 TLAAI----TIAEPILFGRIIDAISSKSD---VLPTLALWAGFGVFNTIAYVLVAReadrLAHGRRATLLTEAFGRIISM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 106 PVSFYDQNRSGEMVSRITNDTtivmNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKIHK 185
Cdd:TIGR01192 103 PLSWHQQRGTSNALHTLLRAT----ETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRLSIVLMVLGILYILIAKLVMQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 186 ISREQQDKMS----KLTAFLAQMLSEIRLIKvSGSEKKEVDSGLQSF-QSLYLFGVKRAKIEAIITPIISTVMTAVMIAI 260
Cdd:TIGR01192 179 RTKNGQAAVEhhyhNVFKHVSDSISNVSVVH-SYNRIEAETSALKQFtNNLLSAQYPVLDWWALASGLNRMASTISMMCI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 261 VGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIFDI---LAEKEENYENGEVLEQVGSLRF 337
Cdd:TIGR01192 258 LVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLedsVFQREEPADAPELPNVKGAVEF 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 338 DKVAFQYED-KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQD 416
Cdd:TIGR01192 338 RHITFEFANsSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQD 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 417 SPILAGTIRENLIYGLErHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLD 496
Cdd:TIGR01192 418 AGLFNRSIRENIRLGRE-GATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLD 496
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265182468 497 EATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASHSFYRRLV 567
Cdd:TIGR01192 497 EATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
25-312 |
9.76e-67 |
|
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: 218.83 E-value: 9.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQLI----AGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWN 100
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALllvpLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 101 KLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLA 180
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 181 RKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAI 260
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 261 VGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18552 241 LWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
28-312 |
1.03e-65 |
|
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: 215.81 E-value: 1.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 28 SFILALINTGASLSIPLVIKEVMEKIAIGVSP----QLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLI 103
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTaslnQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 104 KLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKI 183
Cdd:cd18576 81 RLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 184 HKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAIVGF 263
Cdd:cd18576 161 RKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1265182468 264 GAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18576 241 GGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
333-551 |
1.82e-65 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 212.83 E-value: 1.82e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 333 GSLRFDKVAFQY--EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLF 410
Cdd:cd03245 1 GRIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 411 SYVQQDSPILAGTIRENLIYGLeRHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNP 490
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGA-PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265182468 491 QFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSG 551
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
32-558 |
3.99e-64 |
|
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: 219.53 E-value: 3.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 32 ALINTGAsLSIPLVIKEVMEKI-AIGVSPQLIA---GLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPV 107
Cdd:TIGR01842 16 FVINILM-LAPPLYMLQVYDRVlTSGSVPTLLMltvLALGLYLFLGLLDALRSFVLVRIGEKLDGALNQPIFAASFSATL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 108 sfydqNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKIHKIS 187
Cdd:TIGR01842 95 -----RRGSGDGLQALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLLHPWIGILALGGAVVLVGLALLNNRATKKPL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 188 REQQDKMSKLTAFLAQMLSEIRLIKVSGSeKKEVDSGLQSFQSLYLFGVKRAKIEAI-ITPIISTVMTAVMIAIVGFGAY 266
Cdd:TIGR01842 170 KEATEASIRANNLADSALRNAEVIEAMGM-MGNLTKRWGRFHSKYLSAQSAASDRAGmLSNLSKYFRIVLQSLVLGLGAY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 267 RVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIFDILAEKEENYENGEVLEQVGSLRFDKVAFQY-- 344
Cdd:TIGR01842 249 LAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPLPEPEGHLSVENVTIVPpg 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 345 EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTI 424
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 425 RENlIYGLERHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDS 504
Cdd:TIGR01842 409 AEN-IARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 505 ESEKLVQESLETVMKER-TSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLA 558
Cdd:TIGR01842 488 EGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
333-552 |
1.62e-63 |
|
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: 207.73 E-value: 1.62e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 333 GSLRFDKVAFQYED--KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLF 410
Cdd:cd03244 1 GDIEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 411 SYVQQDSPILAGTIRENL-IYGlerHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRN 489
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLdPFG---EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 490 PQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGT 552
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
243-559 |
3.39e-62 |
|
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: 214.61 E-value: 3.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 243 AIITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIFDILAEKEEN 322
Cdd:COG4618 239 GGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIAASILMGRALAPIEQAIGGWKQFVSARQAYRRLNELLAAVPAE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 323 YENGEVLEQVGSLRFDKVAFQY--EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDsqn 400
Cdd:COG4618 319 PERMPLPRPKGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAD--- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 401 vnLRSW------RHLfSYVQQDSPILAGTIRENlIYGLERhVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSG 474
Cdd:COG4618 396 --LSQWdreelgRHI-GYLPQDVELFDGTIAEN-IARFGD-ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSG 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 475 GQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETvMKER--TSLVIAHRLSTVINADQIVVIEEGQVTGSGT 552
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRA-LKARgaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
....*..
gi 1265182468 553 HKELLAS 559
Cdd:COG4618 550 RDEVLAR 556
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-530 |
5.00e-62 |
|
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: 213.38 E-value: 5.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 17 LTNPPTGKLLISFILALINTGASLSIplvikevmekiaIGVSPQLIAGllvlfAAQM-----------------VTSAVS 79
Cdd:TIGR02868 7 LLKPRRRRLALAVLLGALALGSAVAL------------LGVSAWLISR-----AAEMppvlylsvaavavrafgIGRAVF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 80 LYLLAQVGQGVV----KELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILF 155
Cdd:TIGR02868 70 RYLERLVGHDAAlrslGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 156 TLDVPMTLILlAVIPVMFVLVMPL-----ARKIHKISREQQDKMSKLTAFLAQMLSEIRlikVSGSEKKEVDSGLQSFQS 230
Cdd:TIGR02868 150 VLSVPAALIL-AAGLLLAGFVAPLvslraARAAEQALARLRGELAAQLTDALDGAAELV---ASGALPAALAQVEEADRE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 231 LYLFGVKRAKIEAIITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASE 310
Cdd:TIGR02868 226 LTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 311 RIFDILAEKEENYE-----NGEVLEQVGSLRFDKVAFQYED-KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFY 384
Cdd:TIGR02868 306 RIVEVLDAAGPVAEgsapaAGAVGLGKPTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 385 EPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTIRENLIYGLErHVTDEEIEEAAKLANAHHFIQSFEAQYETM 464
Cdd:TIGR02868 386 DPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARP-DATDEELWAALERVGLADWLRALPDGLDTV 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 465 IGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRL 530
Cdd:TIGR02868 465 LGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
25-312 |
3.51e-60 |
|
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: 201.51 E-value: 3.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQLIAGLLVLFAAQMVTSAVSLY----LLAQVGQGVVKELRHKVWN 100
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYlqgyLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 101 KLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLA 180
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 181 RKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAI 260
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 261 VGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
90-570 |
6.61e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 208.53 E-value: 6.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 90 VVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDT----TIVMNLLSTemidFVKNILSIIVAIVILFTLDVPMTLIL 165
Cdd:PRK11160 91 VLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVdtldHLYLRLISP----LVAALVVILVLTIGLSFFDLTLALTL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 166 -------LAVIPVMFVLvmpLARKI-HKISREQQDKMSKLTAFLaQMLSEIRLIKVSGSEKKEVD---SGLQSFQSlylf 234
Cdd:PRK11160 167 ggillllLLLLPLLFYR---LGKKPgQDLTHLRAQYRVQLTEWL-QGQAELTLFGAEDRYRQQLEqteQQWLAAQR---- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 235 gvKRAKIEAIITP--IISTVMTAVMI---AIVGFGAYRVSEGFITageLVAF-VLYLFQIMVPVGsltrfvTSFQ---QT 305
Cdd:PRK11160 239 --RQANLTGLSQAlmILANGLTVVLMlwlAAGGVGGNAQPGALIA---LFVFaALAAFEALMPVA------GAFQhlgQV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 306 KGASERIFDILAEKEE---NYENGEVLEQvGSLRFDKVAFQYEDK--PVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLI 380
Cdd:PRK11160 308 IASARRINEITEQKPEvtfPTTSTAAADQ-VSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 381 ERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTIRENLIYGLErHVTDEEIEEAAKLANAHHFIQSFEAq 460
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAP-NASDEALIEVLQQVGLEKLLEDDKG- 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 461 YETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIV 540
Cdd:PRK11160 465 LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRIC 544
|
490 500 510
....*....|....*....|....*....|
gi 1265182468 541 VIEEGQVTGSGTHKELLASHSFYRRLVEQQ 570
Cdd:PRK11160 545 VMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
303-570 |
7.82e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 206.23 E-value: 7.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 303 QQTKGASERIFDILAEKEENYENGEV-LEQVGSLRF---DKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFS 378
Cdd:PRK11174 315 AQAVGAAESLVTFLETPLAHPQQGEKeLASNDPVTIeaeDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 379 LIERFYePSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTIRENLIYGlERHVTDEEIEEAAKLANAHHFIQSFE 458
Cdd:PRK11174 395 ALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG-NPDASDEQLQQALENAWVSEFLPLLP 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 459 AQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQ 538
Cdd:PRK11174 473 QGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQ 552
|
250 260 270
....*....|....*....|....*....|..
gi 1265182468 539 IVVIEEGQVTGSGTHKELLASHSFYRRLVEQQ 570
Cdd:PRK11174 553 IWVMQDGQIVQQGDYAELSQAGGLFATLLAHR 584
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
25-312 |
4.93e-58 |
|
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: 195.68 E-value: 4.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKIAIGVSP------QLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKV 98
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGdlqgllLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 99 WNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMP 178
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 179 LARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEvdsgLQSF----QSLYLFGVKRAKIEAIITPIISTVMT 254
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKRE----FEEFdeinQEYRKANLKSIKLFALFRPLVELLSS 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 255 AVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18544 237 LALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
25-312 |
1.58e-56 |
|
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: 191.95 E-value: 1.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQ--------LIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRH 96
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGgntsllllLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 97 KVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLV 176
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 177 MPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAV 256
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 257 MIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
25-312 |
6.53e-56 |
|
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: 190.05 E-value: 6.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKIAIG-----VSPQLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVW 99
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGskslgLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 100 NKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPL 179
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 180 ARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIA 259
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 260 IVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18778 241 VLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
25-312 |
3.24e-54 |
|
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: 185.68 E-value: 3.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKIAIGVSP----------QLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKEL 94
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGgggvdfsgllRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 95 RHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFV 174
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 175 LVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEvdsgLQSF----QSLYLFGVKRAKIEAIITPIIS 250
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEA----IEEFdeinEELYKASFKAQFYSGLLMPIMN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 251 TVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18547 237 FINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
24-312 |
3.31e-54 |
|
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: 185.75 E-value: 3.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 24 KLLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQLIAGLLVLFAA----QMVTSAVSLYLLAQVGQGVVKELRHKVW 99
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLAlnlvNWVASRLRIYLMAKVGQRILYDLRQDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 100 NKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPL 179
Cdd:cd18545 81 SHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 180 ARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEvdsgLQSFQSL----YLFGVKRAKIEAIITPIISTVMTA 255
Cdd:cd18545 161 RRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDEN----EEIFDELnrenRKANMRAVRLNALFWPLVELISAL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 256 VMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18545 237 GTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
65-568 |
2.64e-53 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 196.40 E-value: 2.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 65 LLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPVSFYDQ--NRSGEMVSRITNDTTIVMNLLSTEMIDFVK 142
Cdd:PTZ00265 872 ILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkHAPGLLSAHINRDVHLLKTGLVNNIVIFTH 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 143 NILSIIVAIVILFTLdVPMTLILLAVIPVMFVLVMPLARKIHKiSREQQDKMSKL--TAFLAQMLSEIR-----LIKVSG 215
Cdd:PTZ00265 952 FIVLFLVSMVMSFYF-CPIVAAVLTGTYFIFMRVFAIRARLTA-NKDVEKKEINQpgTVFAYNSDDEIFkdpsfLIQEAF 1029
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 216 SEKKEV-DSGLQSF-----QSLYLFGVKRAKIEAIITPIISTVMTAVMIAIVGF----GAYRVSEGFITAGElvaFVLYL 285
Cdd:PTZ00265 1030 YNMNTViIYGLEDYfcnliEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFaywfGSFLIRRGTILVDD---FMKSL 1106
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 286 FQIMVP---VGSLTRFVTSFQQTKGASERIFDILAEKE--ENYENGEVLEQ-----VGSLRFDKVAFQYEDKP---VLQE 352
Cdd:PTZ00265 1107 FTFLFTgsyAGKLMSLKGDSENAKLSFEKYYPLIIRKSniDVRDNGGIRIKnkndiKGKIEIMDVNFRYISRPnvpIYKD 1186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 353 VSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYE----------------------------------------------- 385
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggs 1266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 386 -------PSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTIRENLIYGLErHVTDEEIEEAAKLANAHHFIQSFE 458
Cdd:PTZ00265 1267 gedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE-DATREDVKRACKFAAIDEFIESLP 1345
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 459 AQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMK--ERTSLVIAHRLSTVINA 536
Cdd:PTZ00265 1346 NKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRS 1425
|
570 580 590
....*....|....*....|....*....|....*...
gi 1265182468 537 DQIVVIEEGQVTGS-----GTHKELLASHS-FYRRLVE 568
Cdd:PTZ00265 1426 DKIVVFNNPDRTGSfvqahGTHEELLSVQDgVYKKYVK 1463
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
25-312 |
3.97e-51 |
|
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: 177.70 E-value: 3.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQ-------------------LIAGLLVLFAAQMVTSAVSLYLLAQ 85
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPgllglapllgpdplallllAAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 86 VGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLIL 165
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 166 LAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVD----SGLQSFQSlylfGVKRAKI 241
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERrfarENRKSLRA----GLRAARL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265182468 242 EAIITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18564 237 QALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
335-547 |
3.71e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.92 E-value: 3.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQ 414
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QDSPILAGTIRENLIYGLERHVTDEEIEEAAKLANAHHFIQSF-EAQYEtmigergiNLSGGQRQRIAIARALLRNPQFL 493
Cdd:COG4619 81 QEPALWGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDIlDKPVE--------RLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 494 LLDEATASLDSESEKLVQESLETVMKE--RTSLVIAH------RLstvinADQIVVIEEGQV 547
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEegRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
28-312 |
6.72e-50 |
|
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: 174.24 E-value: 6.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 28 SFILALINTGASLSIPLVI--------KEVMEKIAIGVS-PQLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKV 98
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIgklidvasKESGDIEIFGLSlKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 99 WNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMP 178
Cdd:cd18573 81 FKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 179 LARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMI 258
Cdd:cd18573 161 YGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 259 AIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18573 241 SVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-542 |
1.26e-49 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 185.23 E-value: 1.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 20 PPTGK--LLISFILALINTGaslSIPL---VIKEVMEKIAIG--VSPqLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVK 92
Cdd:PTZ00265 55 PASHRklLGVSFVCATISGG---TLPFfvsVFGVIMKNMNLGenVND-IIFSLVLIGIFQFILSFISSFCMDVVTTKILK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 93 ELRHKVWNKLIKLPVSFYDQNRSgemvSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTL----DVPMTLILLAV 168
Cdd:PTZ00265 131 TLKLEFLKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWslfkNARLTLCITCV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 169 IPVMFVLVMPLARKIhKISREQQDKMSKLT-AFLAQMLSEIRLIkVSGSEKKEVDSGLQSFQSLYL-FGVKRAKIEAIIT 246
Cdd:PTZ00265 207 FPLIYICGVICNKKV-KINKKTSLLYNNNTmSIIEEALVGIRTV-VSYCGEKTILKKFNLSEKLYSkYILKANFMESLHI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 247 PIIStvmtAVMIAIVGFGAYRVSEGFIT------------AGELVAFVL----YLFQIMVPVGSLTRFVTSFQqtkgASE 310
Cdd:PTZ00265 285 GMIN----GFILASYAFGFWYGTRIIISdlsnqqpnndfhGGSVISILLgvliSMFMLTIILPNITEYMKSLE----ATN 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 311 RIFDILAEKE--ENYENGEVLEQVGSLRFDKVAFQYE---DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYE 385
Cdd:PTZ00265 357 SLYEIINRKPlvENNDDGKKLKDIKKIQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 386 PSSGRIFL-DGTDSQNVNLRSWRHLFSYVQQDSPILAGTIRENLIYGLE------------------------------- 433
Cdd:PTZ00265 437 PTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYslkdlealsnyynedgndsqenknkrnscra 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 434 -------------------------RHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLR 488
Cdd:PTZ00265 517 kcagdlndmsnttdsneliemrknyQTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIR 596
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 489 NPQFLLLDEATASLDSESEKLVQESLETVM--KERTSLVIAHRLSTVINADQIVVI 542
Cdd:PTZ00265 597 NPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVL 652
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
29-312 |
1.52e-49 |
|
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: 173.13 E-value: 1.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 29 FILALINTGASLSIPLV----IKEVMEKIAIGVSPQLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIK 104
Cdd:cd18557 2 LLFLLISSAAQLLLPYLigrlIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 105 LPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKIH 184
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 185 KISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAIVGFG 264
Cdd:cd18557 162 KLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1265182468 265 AYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18557 242 GYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
331-547 |
9.06e-49 |
|
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: 168.36 E-value: 9.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 331 QVGSLRFDKVAFQY--EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRH 408
Cdd:cd03369 3 EHGEIEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 409 LFSYVQQDSPILAGTIRENL-IYGlerHVTDEEIEEAAKlanahhfiqsfeaqyetmIGERGINLSGGQRQRIAIARALL 487
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFD---EYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 488 RNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQV 547
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
25-312 |
4.89e-48 |
|
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: 169.20 E-value: 4.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKiAIGVSPQ-----LIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVW 99
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDG-PIAHGDRsalwpLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 100 NKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIdFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPL 179
Cdd:cd18543 80 AHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPF-LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 180 ARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIA 259
Cdd:cd18543 159 RRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 260 IVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18543 239 VLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
335-547 |
4.48e-47 |
|
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: 162.39 E-value: 4.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYED--KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSY 412
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 413 VQQDSPILAGTIRENLiyglerhvtdeeieeaaklanahhfiqsfeaqyetmigerginLSGGQRQRIAIARALLRNPQF 492
Cdd:cd03246 81 LPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 493 LLLDEATASLDSESEKLVQESLETV-MKERTSLVIAHRLSTVINADQIVVIEEGQV 547
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
25-312 |
9.09e-47 |
|
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: 165.66 E-value: 9.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQ----LIAGLLVLFA-AQMVTSAVSLYLLAQVGQGVVKELRHKVW 99
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTAsqllRYALLILLLAlLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 100 NKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPL 179
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 180 ARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIA 259
Cdd:cd18541 161 GKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 260 IVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18541 241 VLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
28-312 |
5.87e-46 |
|
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: 163.42 E-value: 5.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 28 SFILALINTGASLSIPLVIKEVMEKIAIGVSPQLI----AGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLI 103
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLnrafLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 104 KLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKI 183
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 184 HKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITpiiSTVMTAVMIAIVG- 262
Cdd:cd18575 161 RRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLT---ALVIFLVFGAIVFv 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 263 --FGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18575 238 lwLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
335-558 |
5.89e-45 |
|
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: 5.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYED-KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYV 413
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 414 QQDsP---ILAGTIRENLIYGLERH-VTDEEI----EEAAKLANAHHFiqsfeaqyetmiGERGI-NLSGGQRQRIAIAR 484
Cdd:COG1122 81 FQN-PddqLFAPTVEEDVAFGPENLgLPREEIrervEEALELVGLEHL------------ADRPPhELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 485 ALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIA-HRLSTVI-NADQIVVIEEGQVTGSGTHKELLA 558
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAeLADRVIVLDDGRIVADGTPREVFS 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
335-570 |
1.06e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.61 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNvNLRSWRHLFSYVQ 414
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QDSPILAG-TIRENL-----IYGLERHVTDEEIEEAAKLANAHHFIqsfeaqyETMIGergiNLSGGQRQRIAIARALLR 488
Cdd:COG1131 80 QEPALYPDlTVRENLrffarLYGLPRKEARERIDELLELFGLTDAA-------DRKVG----TLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 489 NPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIA-HRLSTVIN-ADQIVVIEEGQVTGSGTHKELLASH--SFYR 564
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKARLleDVFL 228
|
....*.
gi 1265182468 565 RLVEQQ 570
Cdd:COG1131 229 ELTGEE 234
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
336-546 |
1.53e-43 |
|
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: 154.16 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 336 RFDKVAFQYED--KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYV 413
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 414 QQ--DSPILAGTIRENLIYGLE-RHVTDEEIEEAAKLANAHHFIQSFEaqyetmigERGI-NLSGGQRQRIAIARALLRN 489
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLEnLGLPEEEIEERVEEALELVGLEGLR--------DRSPfTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265182468 490 PQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIA-HRLSTVIN-ADQIVVIEEGQ 546
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
77-563 |
7.59e-43 |
|
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: 165.12 E-value: 7.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 77 AVSLYLLAQVGQGVV--KELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVIL 154
Cdd:TIGR00957 1021 AVFGYSMAVSIGGIQasRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVI 1100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 155 FtLDVPMTLILLAVIPVMFVLVMPL-ARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKV-SGSEKKEVDSGLQSfqsly 232
Cdd:TIGR00957 1101 L-LATPIAAVIIPPLGLLYFFVQRFyVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAfEEQERFIHQSDLKV----- 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 233 lfgvkRAKIEAIITPIISTVMTAVMIAIVG-----FGAY--RVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQT 305
Cdd:TIGR00957 1175 -----DENQKAYYPSIVANRWLAVRLECVGncivlFAALfaVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETN 1249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 306 KGASERIFDIL-AEKE-----ENYENGEVLEQVGSLRFDKVAFQYED--KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVF 377
Cdd:TIGR00957 1250 IVAVERLKEYSeTEKEapwqiQETAPPSGWPPRGRVEFRNYCLRYREdlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLT 1329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 378 SLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTIRENL-IYGlerHVTDEEIEEAAKLANAHHFIQS 456
Cdd:TIGR00957 1330 LGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFS---QYSDEEVWWALELAHLKTFVSA 1406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 457 FEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINA 536
Cdd:TIGR00957 1407 LPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDY 1486
|
490 500
....*....|....*....|....*...
gi 1265182468 537 DQIVVIEEGQVTGSGTHKELLASHS-FY 563
Cdd:TIGR00957 1487 TRVIVLDKGEVAEFGAPSNLLQQRGiFY 1514
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
25-292 |
1.06e-42 |
|
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: 153.95 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKIAIGVSP------QLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKV 98
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPetqalnVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 99 WNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMP 178
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 179 LARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMI 258
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 1265182468 259 AIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPV 292
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
25-312 |
2.32e-42 |
|
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: 153.80 E-value: 2.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEK-IAIGVSPQLI---AGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWN 100
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSgVRAGDLGVLLlaaAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 101 KLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLA 180
Cdd:cd18546 81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 181 RKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEkkevDSGLQSFQSL---YLFGVKRA-KIEAIITPIISTVMTAV 256
Cdd:cd18546 161 RRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRE----RRNAERFAELsddYRDARLRAqRLVAIYFPGVELLGNLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 257 MIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18546 237 TAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
25-312 |
3.60e-42 |
|
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: 153.32 E-value: 3.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQLI---AGLLVLFAA-QMVTSAVSLYLLAQVGQGVVKELRHKVWN 100
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYIlrtGLLMLLLALlGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 101 KLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLA 180
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 181 RKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAI 260
Cdd:cd18548 161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 261 VGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18548 241 LWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
25-312 |
5.71e-42 |
|
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: 152.64 E-value: 5.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQLIAGL-LVLFAAQMVTSAVSL---YLLAQVGQGVVKELRHKVWN 100
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLaLGMVAVAVASALLGVvqtYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 101 KLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLA 180
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 181 RKIHKISREQQDKMSKLTAFLAQMLSE--IRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMI 258
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 259 AIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
350-500 |
1.12e-41 |
|
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: 147.02 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAG-TIRENL 428
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 429 IYGLE-----RHVTDEEIEEAAKLANAHHFIqsfeaqyETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATA 500
Cdd:pfam00005 81 RLGLLlkglsKREKDARAEEALEKLGLGDLA-------DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
23-304 |
1.64e-41 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 151.45 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 23 GKLLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQLI----AGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKV 98
Cdd:cd18549 2 KLFFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLIliigAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 99 WNKLIKLPVSFYDQNRSGEMVSRITNDTTIVmnllsTEMI-----DFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMF 173
Cdd:cd18549 82 FEHLQKLSFSFFDNNKTGQLMSRITNDLFDI-----SELAhhgpeDLFISIITIIGSFIILLTINVPLTLIVFALLPLMI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 174 VLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEvdsgLQSFQSL--YLFGVKRA--KIEAIITPII 249
Cdd:cd18549 157 IFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYE----IEKFDEGndRFLESKKKayKAMAYFFSGM 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 250 STVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQ 304
Cdd:cd18549 233 NFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQK 287
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
333-546 |
2.02e-41 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 148.39 E-value: 2.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 333 GSLRFDKVafQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLI--ErfYEPSSGRIFLDGTdsqnvnlrswrhlF 410
Cdd:cd03250 6 ASFTWDSG--EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS-------------I 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 411 SYVQQDSPILAGTIRENLIYGLERhvtDEE-----IEEAAKLANahhfIQSFEAQYETMIGERGINLSGGQRQRIAIARA 485
Cdd:cd03250 69 AYVSQEPWIQNGTIRENILFGKPF---DEEryekvIKACALEPD----LEILPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 486 LLRNPQFLLLDEATASLDSESEKLVQES--LETVMKERTSLVIAHRLSTVINADQIVVIEEGQ 546
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
24-312 |
8.94e-41 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 149.58 E-value: 8.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 24 KLLIS-FILALINTGASLSIPLVIKEVMEKIAIGVSPQ----LIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKV 98
Cdd:cd18555 2 KLLISiLLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNllnvLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 99 WNKLIKLPVSFYDQNRSGEMVSRItNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMP 178
Cdd:cd18555 82 FEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 179 LARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMI 258
Cdd:cd18555 161 TRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 259 AIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18555 241 LILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
335-551 |
9.47e-41 |
|
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: 145.53 E-value: 9.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQY--EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNlRSWRHLFSY 412
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 413 VQQDSPILAGTIRENLiyglerhvtdeeieeaaklanahhfiqsfeaqyetmigerGINLSGGQRQRIAIARALLRNPQF 492
Cdd:cd03247 80 LNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265182468 493 LLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSG 551
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
66-568 |
1.80e-40 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 157.83 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 66 LVLFAAQMVTSAVSLYLLAQvGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVK--- 142
Cdd:PLN03232 958 LLGFGQVAVTFTNSFWLISS-SLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNqlw 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 143 NILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIK----VSGSEK 218
Cdd:PLN03232 1037 QLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKaydrMAKING 1116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 219 KEVDSGLQsfqslylFGVKRAKIEAIITpIISTVMTAVMI------AIVGFGAYRVSEGFI-TAGELVAFVLYLFQIMVP 291
Cdd:PLN03232 1117 KSMDNNIR-------FTLANTSSNRWLT-IRLETLGGVMIwltatfAVLRNGNAENQAGFAsTMGLLLSYTLNITTLLSG 1188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 292 VgslTRFVTSFQQTKGASERI---FDILAEKEENYENGEVLE---QVGSLRFDKVAFQY--EDKPVLQEVSFSAKKGEVT 363
Cdd:PLN03232 1189 V---LRQASKAENSLNSVERVgnyIDLPSEATAIIENNRPVSgwpSRGSIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKV 1265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 364 AFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTIRENLIYGLERHvtDEEIEE 443
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHN--DADLWE 1343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 444 AAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTS 523
Cdd:PLN03232 1344 ALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTM 1423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1265182468 524 LVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASH-SFYRRLVE 568
Cdd:PLN03232 1424 LVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDtSAFFRMVH 1469
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
335-557 |
2.65e-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: 147.11 E-value: 2.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQ 414
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QDSPILAG-TIRENLIYGLERHVT--------DEEI-EEAAKLANAHHFIqsfeaqyetmigERGIN-LSGGQRQRIAIA 483
Cdd:COG1120 82 QEPPAPFGlTVRELVALGRYPHLGlfgrpsaeDREAvEEALERTGLEHLA------------DRPVDeLSGGERQRVLIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265182468 484 RALLRNPQFLLLDEATASLD----SESEKLVQEslETVMKERTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELL 557
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDlahqLEVLELLRR--LARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
24-312 |
1.48e-39 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 146.09 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 24 KLLISFILALINTGASLSI-PLVIKEVMEKIAIGVSPQLIAGLLVLFAAQMVTSAVSLYLL----AQVGQGVVKELRHKV 98
Cdd:cd18540 2 KLLILLIILMLLVALLDAVfPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFirlaGKIEMGVSYDLRKKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 99 WNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMP 178
Cdd:cd18540 82 FEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 179 LARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMI 258
Cdd:cd18540 162 FQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 259 AIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18540 242 LVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
33-312 |
3.43e-39 |
|
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: 145.09 E-value: 3.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 33 LINTGASLSIPLVIKEVMEKIAIGVSP----------QLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKL 102
Cdd:cd18780 6 LVSSGTNLALPYFFGQVIDAVTNHSGSggeealralnQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 103 IKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARK 182
Cdd:cd18780 86 IAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 183 IHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAIVG 262
Cdd:cd18780 166 VRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLW 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1265182468 263 FGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18780 246 YGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
28-312 |
7.21e-39 |
|
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: 144.22 E-value: 7.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 28 SFILALINTGASLSIPLVIKEVMEKIAIGVSPQL----IAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLI 103
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAfyraVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 104 KLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKI 183
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 184 HKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAIVGF 263
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1265182468 264 GAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18572 241 GGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
336-546 |
1.23e-38 |
|
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: 139.30 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 336 RFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQ 415
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 416 dspilagtirenliyglerhvtdeeieeaaklanahhfiqsfeaqyetmigerginLSGGQRQRIAIARALLRNPQFLLL 495
Cdd:cd00267 81 --------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 496 DEATASLDSESEKLVQESLETVMKE-RTSLVIAHRLSTVINA-DQIVVIEEGQ 546
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
335-559 |
2.74e-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: 140.89 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVN---LRSWRHLFS 411
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 412 YV-QQ----DSpiLagTIRENLIYGLERH--VTDEEIEEAAK-------LANAHHFiqsfeaqyetMIGErginLSGGQR 477
Cdd:COG1127 86 MLfQGgalfDS--L--TVFENVAFPLREHtdLSEAEIRELVLeklelvgLPGAADK----------MPSE----LSGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 478 QRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHK 554
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPE 227
|
....*
gi 1265182468 555 ELLAS 559
Cdd:COG1127 228 ELLAS 232
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
25-312 |
4.19e-38 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 142.20 E-value: 4.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQL----IAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWN 100
Cdd:cd18570 4 LILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLlniiSIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 101 KLIKLPVSFYDQNRSGEMVSRItNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLA 180
Cdd:cd18570 84 HLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 181 RKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAI 260
Cdd:cd18570 163 KPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLI 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 261 VGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18570 243 LWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
335-561 |
4.70e-38 |
|
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: 140.38 E-value: 4.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFsYVQ 414
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIG-VLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QDSPILAG-TIRENL-----IYGLERHVTDEEIEEAAKLANahhfiqsFEAQYETMIGErginLSGGQRQRIAIARALLR 488
Cdd:COG4555 81 DERGLYDRlTVRENIryfaeLYGLFDEELKKRIEELIELLG-------LEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 489 NPQFLLLDEATASLDSESEKLVQESLETVMKE-RTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLASHS 561
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
335-556 |
6.29e-38 |
|
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: 139.62 E-value: 6.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYE-----PSSGRIFLDGTD--SQNVNLRSWR 407
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 408 HLFSYVQQDSPILAGTIRENLIYGL------ERHVTDEEIEEAAKLA--------NAHhfiqsfeaqyetmigerGINLS 473
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLrlhgikLKEELDERVEEALRKAalwdevkdRLH-----------------ALGLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 474 GGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGT 552
Cdd:cd03260 144 GGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGP 223
|
....
gi 1265182468 553 HKEL 556
Cdd:cd03260 224 TEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-568 |
8.58e-38 |
|
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: 146.20 E-value: 8.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQY-----EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHL 409
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 410 FSYVQ---QD-----SPILagTIRENLIYGLERH--VTDEEIEE-AAKLANAHHFIQSFEAQYetmIGErginLSGGQRQ 478
Cdd:COG1123 341 RRRVQmvfQDpysslNPRM--TVGDIIAEPLRLHglLSRAERRErVAELLERVGLPPDLADRY---PHE----LSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 479 RIAIARALLRNPQFLLLDEATASLDseseKLVQESLETVMKE------RTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSG 551
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALD----VSVQAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
250
....*....|....*....
gi 1265182468 552 THKELLAS--HSFYRRLVE 568
Cdd:COG1123 488 PTEEVFANpqHPYTRALLA 506
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-564 |
1.18e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.45 E-value: 1.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDsqnvnLRSWRHLFSYVQ 414
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 Q------DSPI------LAGTIRENLIYGLERHVTDEEIEEAAKLANAHHFIQsfeaqyeTMIGErginLSGGQRQRIAI 482
Cdd:COG1121 82 QraevdwDFPItvrdvvLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLAD-------RPIGE----LSGGQQQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 483 ARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKE-RTSLVIAHRLSTVI-NADQIVVIEEGQVTgSGTHKELLASH 560
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVReYFDRVLLLNRGLVA-HGPPEEVLTPE 229
|
....
gi 1265182468 561 SFYR 564
Cdd:COG1121 230 NLSR 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
333-568 |
2.74e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 148.35 E-value: 2.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 333 GSLRFDKVAFQY--EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLF 410
Cdd:PLN03130 1236 GSIKFEDVVLRYrpELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 411 SYVQQdSPIL-AGTIRENLIYGLERHvtDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRN 489
Cdd:PLN03130 1316 GIIPQ-APVLfSGTVRFNLDPFNEHN--DADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRR 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 490 PQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLAS-HSFYRRLVE 568
Cdd:PLN03130 1393 SKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNeGSAFSKMVQ 1472
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
335-547 |
9.70e-37 |
|
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: 135.72 E-value: 9.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSwRHLfSYVQ 414
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER-RNI-GMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QDS---PILagTIRENLIYGLERHVTDEE-----IEEAAKLANAHHFIQSFEAQyetmigerginLSGGQRQRIAIARAL 486
Cdd:cd03259 79 QDYalfPHL--TVAENIAFGLKLRGVPKAeirarVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 487 LRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQV 547
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALAlADRIAVMNEGRI 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
335-549 |
1.36e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 135.94 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQY----EDKPVLQEVSFSAKKGEVTAFVGPSGAGKST---VFSLIERfyePSSGRIFLDGTD------SQNV 401
Cdd:COG1136 5 LELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDisslseRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 402 NLRswRHLFSYVQQDS---PILagTIREN-----LIYGLERHVTDEEIEEAAKLANAHHFIQSFEAQyetmigerginLS 473
Cdd:COG1136 82 RLR--RRHIGFVFQFFnllPEL--TALENvalplLLAGVSRKERRERARELLERVGLGDRLDHRPSQ-----------LS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 474 GGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER-TSLVIA-HRLSTVINADQIVVIEEGQVTG 549
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVtHDPELAARADRVIRLRDGRIVS 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
334-568 |
1.49e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 136.47 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 334 SLRFDKvafQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYV 413
Cdd:COG1124 8 SVSYGQ---GGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 414 QQDSP-------ILAGTIRENL-IYGLERHvtDEEIEEAAKLAN-AHHFIQSFEAQyetmigerginLSGGQRQRIAIAR 484
Cdd:COG1124 85 FQDPYaslhprhTVDRILAEPLrIHGLPDR--EERIAELLEQVGlPPSFLDRYPHQ-----------LSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 485 ALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLStVIN--ADQIVVIEEGQVTGSGTHKELL--A 558
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADLLagP 230
|
250
....*....|
gi 1265182468 559 SHSFYRRLVE 568
Cdd:COG1124 231 KHPYTRELLA 240
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
335-560 |
1.97e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 135.65 E-value: 1.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVlqEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTD--SQNVNLRSWRHLFsy 412
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDltALPPAERPVSMLF-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 413 vqQDS---PILagTIRENLIYGLE--RHVTDEE---IEEAAKLANAHHFIQSFEAQyetmigerginLSGGQRQRIAIAR 484
Cdd:COG3840 78 --QENnlfPHL--TVAQNIGLGLRpgLKLTAEQraqVEQALERVGLAGLLDRLPGQ-----------LSGGQRQRVALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 485 ALLRNPQFLLLDEATASLD----SESEKLVQEsletVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELL 557
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDpalrQEMLDLVDE----LCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
...
gi 1265182468 558 ASH 560
Cdd:COG3840 219 DGE 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
335-558 |
2.55e-36 |
|
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: 135.40 E-value: 2.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDK----PVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVN---LRSWR 407
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 408 HLFSYVQQDSPILAG-TIRENLIYGLE-RHVTDEEIEEAA----KLANAHHFIQSFEAQyetmigerginLSGGQRQRIA 481
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEiAGVPKAEIEERVlellELVGLEDKADAYPAQ-----------LSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 482 IARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTV--InADQIVVIEEGQVTGSGTHKELL 557
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVkrI-CDRVAVMEKGEVVEEGTVEEVF 229
|
.
gi 1265182468 558 A 558
Cdd:cd03258 230 A 230
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
335-546 |
2.90e-36 |
|
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: 133.47 E-value: 2.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTD--SQNVNLRSWRHLFSY 412
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 413 VQQDSPILAG-TIRENLIYGlerhvtdeeieeaaklanahhfiqsfeaqyetmigerginLSGGQRQRIAIARALLRNPQ 491
Cdd:cd03229 81 VFQDFALFPHlTVLENIALG----------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 492 FLLLDEATASLDSESEKLVQESLETVMKE--RTSLVIAHRLSTVIN-ADQIVVIEEGQ 546
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
335-559 |
5.40e-36 |
|
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: 134.55 E-value: 5.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVN---LRSWRHLFS 411
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 412 YVQQDSPILAG-TIRENLIYGLERH--VTDEEIEEAA--KLAnahhfiqsfeaqyetMIGERGI------NLSGGQRQRI 480
Cdd:cd03261 81 MLFQSGALFDSlTVFENVAFPLREHtrLSEEEIREIVleKLE---------------AVGLRGAedlypaELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 481 AIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELL 557
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELR 225
|
..
gi 1265182468 558 AS 559
Cdd:cd03261 226 AS 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
336-542 |
5.77e-36 |
|
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: 133.81 E-value: 5.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 336 RFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsqnVNLRSWRHLFSYVQQ 415
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 416 ------DSPIlagTIRENLIYGLERHV---------TDEEIEEAAKLANAHHFIQSfeaqyetMIGErginLSGGQRQRI 480
Cdd:cd03235 76 rrsidrDFPI---SVRDVVLMGLYGHKglfrrlskaDKAKVDEALERVGLSELADR-------QIGE----LSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 481 AIARALLRNPQFLLLDEATASLDSESEKLVQESLETV-MKERTSLVIAHRLSTVIN-ADQIVVI 542
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLL 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
348-547 |
7.54e-36 |
|
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: 133.79 E-value: 7.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 348 PVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVN---LRSWRHLFSYVQQDS-----PI 419
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDPmsslnPR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 420 LagTIRENLIYGLERH--VTDEEIEEAAKLANAHHFIQSfeaqyETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDE 497
Cdd:cd03257 99 M--TIGEQIAEPLRIHgkLSKKEARKEAVLLLLVGVGLP-----EEVLNRYPHELSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 498 ATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQV 547
Cdd:cd03257 172 PTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
340-551 |
9.00e-36 |
|
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: 9.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 340 VAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQdspi 419
Cdd:cd03214 5 LSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 420 lagtirenliyglerhvtdeeieeAAKLANAHHFIqsfeaqyetmigERGIN-LSGGQRQRIAIARALLRNPQFLLLDEA 498
Cdd:cd03214 81 ------------------------ALELLGLAHLA------------DRPFNeLSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 499 TASLDSESEKLVQESLETVMKERTSLVIA--HRLSTVIN-ADQIVVIEEGQVTGSG 551
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMvlHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
335-542 |
9.48e-36 |
|
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: 133.37 E-value: 9.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDK----PVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRswrhlF 410
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 411 SYV-QQDS--PILagTIRENLIYGLE-RHVTDEEIEEAaklanAHHFI-----QSFEAQYETMigerginLSGGQRQRIA 481
Cdd:cd03293 76 GYVfQQDAllPWL--TVLDNVALGLElQGVPKAEARER-----AEELLelvglSGFENAYPHQ-------LSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 482 IARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVI 542
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDEAVFlADRVVVL 205
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
333-558 |
1.76e-35 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 133.88 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 333 GSLRFDKVAFQYED--KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLF 410
Cdd:cd03288 18 GEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 411 SYVQQDSPILAGTIRENLiyGLERHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNP 490
Cdd:cd03288 98 SIILQDPILFSGSIRFNL--DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 491 QFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLA 558
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLA 243
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
335-556 |
8.87e-35 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 131.54 E-value: 8.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYED-KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNV---NLRSWRHLF 410
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 411 SYVQQDSP----------ILAGTI-RENLIYGLERHVTDEEIEEAAKLANahhfiqsfEAQYETMIGERGINLSGGQRQR 479
Cdd:cd03256 81 GMIFQQFNlierlsvlenVLSGRLgRRSTWRSLFGLFPKEEKQRALAALE--------RVGLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 480 IAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIA--HRLSTVI-NADQIVVIEEGQVTGSGTHKEL 556
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVslHQVDLAReYADRIVGLKDGRIVFDGPPAEL 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
335-559 |
2.04e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 130.11 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDG---TDS------------- 398
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedlTDSkkdinklrrkvgm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 399 --QNVNLrsWRHLfsyvqqdspilagTIRENLIYGLE--RHVTDEEIEEAAK-------LAnahHFIQSFEAQyetmige 467
Cdd:COG1126 82 vfQQFNL--FPHL-------------TVLENVTLAPIkvKKMSKAEAEERAMellervgLA---DKADAYPAQ------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 468 rginLSGGQRQRIAIARALLRNPQFLLLDEATASLDSEsekLVQESLEtVMKE-----RTSLVIAHRLS---TVinADQI 539
Cdd:COG1126 137 ----LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLD-VMRDlakegMTMVVVTHEMGfarEV--ADRV 206
|
250 260
....*....|....*....|
gi 1265182468 540 VVIEEGQVTGSGTHKELLAS 559
Cdd:COG1126 207 VFMDGGRIVEEGPPEEFFEN 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
335-547 |
2.50e-34 |
|
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: 129.53 E-value: 2.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQY----EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHL- 409
Cdd:cd03255 1 IELKNLSKTYggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 410 ---FSYVQQDS---PILagTIRENLIYGLE-RHVTDEEIEEAAK-------LAN-AHHFIQsfeaqyetmigergiNLSG 474
Cdd:cd03255 81 rrhIGFVFQSFnllPDL--TALENVELPLLlAGVPKKERRERAEellervgLGDrLNHYPS---------------ELSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 475 GQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVINADQIVVIEEGQV 547
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
335-547 |
5.81e-34 |
|
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: 126.74 E-value: 5.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNvNLRSWRHLFSYVQ 414
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QDSPILAG-TIRENLIYglerhvtdeeieeaaklanahhfiqsfeaqyetmigerginlSGGQRQRIAIARALLRNPQFL 493
Cdd:cd03230 80 EEPSLYENlTVRENLKL------------------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 494 LLDEATASLDSESEKLVQESLETVMKE-RTSLVIAHRLSTVIN-ADQIVVIEEGQV 547
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
335-547 |
5.96e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 129.41 E-value: 5.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQY-EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVN---LRSWRHLF 410
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 411 SYVQQDSP----------ILAGTI-RENLIYGLERHVTDEEIEEAAKLAN----AHHfiqsfeaqyetmIGERGINLSGG 475
Cdd:COG3638 83 GMIFQQFNlvprlsvltnVLAGRLgRTSTWRSLLGLFPPEDRERALEALErvglADK------------AYQRADQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 476 QRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQV 547
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
335-541 |
7.52e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 129.44 E-value: 7.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYE----DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRswrhlF 410
Cdd:COG1116 8 LELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 411 SYV-QQDS--PILagTIRENLIYGLE-RHVTDEEIEEAAK-------LAnahHFIQSFEAQyetmigerginLSGGQRQR 479
Cdd:COG1116 83 GVVfQEPAllPWL--TVLDNVALGLElRGVPKAERRERARellelvgLA---GFEDAYPHQ-----------LSGGMRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 480 IAIARALLRNPQFLLLDEATASLDSES-EKLVQESLETVMKERTSLV-IAH------RLstvinADQIVV 541
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTrERLQDELLRLWQETGKTVLfVTHdvdeavFL-----ADRVVV 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
107-568 |
1.22e-33 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 137.22 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 107 VSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFtldVPMTLILLAVIPVMFV---LVMPLARKI 183
Cdd:PTZ00243 1046 MSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTS---ASQPFVLVALVPCGYLyyrLMQFYNSAN 1122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 184 HKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQS----FQSLYL-------FGVKrakIEAIITPIISTV 252
Cdd:PTZ00243 1123 REIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRldvvYSCSYLenvanrwLGVR---VEFLSNIVVTVI 1199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 253 mtaVMIAIVG--FGAYRVSEGFITAGELVAFvlylfQIMVPVGSLTRFVTSFQQTKGASERIFDIL--AEKEENYENGE- 327
Cdd:PTZ00243 1200 ---ALIGVIGtmLRATSQEIGLVSLSLTMAM-----QTTATLNWLVRQVATVEADMNSVERLLYYTdeVPHEDMPELDEe 1271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 328 ------------------VLE------------QVGSLRFDKVAFQY-EDKP-VLQEVSFSAKKGEVTAFVGPSGAGKST 375
Cdd:PTZ00243 1272 vdalerrtgmaadvtgtvVIEpasptsaaphpvQAGSLVFEGVQMRYrEGLPlVLRGVSFRIAPREKVGIVGRTGSGKST 1351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 376 VFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTIRENLIYGLErhVTDEEIEEAAKLANAHHFIQ 455
Cdd:PTZ00243 1352 LLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLE--ASSAEVWAALELVGLRERVA 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 456 SFEAQYETMIGERGINLSGGQRQRIAIARALL-RNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVI 534
Cdd:PTZ00243 1430 SESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVA 1509
|
490 500 510
....*....|....*....|....*....|....*
gi 1265182468 535 NADQIVVIEEGQVTGSGTHKEL-LASHSFYRRLVE 568
Cdd:PTZ00243 1510 QYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMVE 1544
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
344-558 |
4.12e-33 |
|
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: 126.01 E-value: 4.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 344 YEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTD--SQNVNLRSwRHLFSYVQQDSPILA 421
Cdd:cd03224 10 YGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDitGLPPHERA-RAGIGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 422 G-TIRENL---IYGLERHVTDEEIEEAAKLanahhfiqsFEAQYEtMIGERGINLSGGQRQRIAIARALLRNPQFLLLDE 497
Cdd:cd03224 89 ElTVEENLllgAYARRRAKRKARLERVYEL---------FPRLKE-RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 498 ATASLdseSEKLVQESLETVMKER----TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLA 558
Cdd:cd03224 159 PSEGL---APKIVEEIFEAIRELRdegvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-560 |
6.82e-33 |
|
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: 132.33 E-value: 6.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQY--EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPS---SGRIFLDGTDSQNVNLRSWRHL 409
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 410 FSYVQQD--SPILAGTIRENLIYGLE-RHVTDEEIEEAAKLANAHHFIQSFEAQYETmigergiNLSGGQRQRIAIARAL 486
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEALEnLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 487 LRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLASH 560
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
334-565 |
6.89e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 129.06 E-value: 6.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 334 SLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNV--NLRSwrhlFS 411
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppEKRN----VG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 412 YVQQDS---PILagTIRENLIYGLE-RHVTDEEI----EEAAKLANahhfIQSFEAQYetmIGErginLSGGQRQRIAIA 483
Cdd:COG3842 81 MVFQDYalfPHL--TVAENVAFGLRmRGVPKAEIrarvAELLELVG----LEGLADRY---PHQ----LSGGQQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 484 RALLRNPQFLLLDEATASLDSeseKL---VQESLETVMKER--TSLVIAHRLS---TVinADQIVVIEEGQVTGSGTHKE 555
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDA---KLreeMREELRRLQRELgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEE 222
|
250
....*....|
gi 1265182468 556 LlashsfYRR 565
Cdd:COG3842 223 I------YER 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
335-559 |
3.02e-32 |
|
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: 124.34 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYED-KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYV 413
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 414 QQDSPILAG-TIREN--LIYGLErHVTDEEIEEAAK--LANAHHFIQSFEAQYETmigergiNLSGGQRQRIAIARALLR 488
Cdd:cd03295 81 IQQIGLFPHmTVEENiaLVPKLL-KWPKEKIRERADelLALVGLDPAEFADRYPH-------ELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 489 NPQFLLLDEATASLDSESEKLVQESLETVMKE--RTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLAS 559
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-558 |
3.23e-32 |
|
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: 132.76 E-value: 3.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 10 SFKKLWLLTNPPTgkLLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQ----LIAGLLVLfAAQMVTSAVSLY--LL 83
Cdd:TIGR00957 306 SLFKVLYKTFGPY--FLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDwqgyFYTGLLFV-CACLQTLILHQYfhIC 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 84 AQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLStemidFVKNI----LSIIVAIVILFTLDV 159
Cdd:TIGR00957 383 FVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLAT-----YINMIwsapLQVILALYFLWLNLG 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 160 PMTLILLAVIPVMFVL--VMPLARKIHKISR-EQQDKMSKLtafLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGV 236
Cdd:TIGR00957 458 PSVLAGVAVMVLMVPLnaVMAMKTKTYQVAHmKSKDNRIKL---MNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLK 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 237 KRAKIEAIITpiISTVMTAVMIAIVGFGAY-RVSEGFITAGELVAFVLYLFQIM-VPVGSLTRFVTSFQQTKGASERIFD 314
Cdd:TIGR00957 535 KSAYLHAVGT--FTWVCTPFLVALITFAVYvTVDENNILDAEKAFVSLALFNILrFPLNILPMVISSIVQASVSLKRLRI 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 315 ILAEKE---ENYENGEVLEQVG-SLRFDKVAFQY--EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSS 388
Cdd:TIGR00957 613 FLSHEElepDSIERRTIKPGEGnSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVE 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 389 GRIFLDGTdsqnvnlrswrhlFSYVQQDSPILAGTIRENLIYG--LERHVTDEEIEEAAKLANahhfIQSFEAQYETMIG 466
Cdd:TIGR00957 693 GHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGkaLNEKYYQQVLEACALLPD----LEILPSGDRTEIG 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 467 ERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESL---ETVMKERTSLVIAHRLSTVINADQIVVIE 543
Cdd:TIGR00957 756 EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMS 835
|
570
....*....|....*
gi 1265182468 544 EGQVTGSGTHKELLA 558
Cdd:TIGR00957 836 GGKISEMGSYQELLQ 850
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
337-564 |
4.68e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 124.72 E-value: 4.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 337 FDKVAFQY--EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQ 414
Cdd:PRK13632 10 VENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 Q--DSPILAGTIRENLIYGLE-RHVTDEE----IEEAAKLANAHHFIQsFEAQyetmigergiNLSGGQRQRIAIARALL 487
Cdd:PRK13632 90 QnpDNQFIGATVEDDIAFGLEnKKVPPKKmkdiIDDLAKKVGMEDYLD-KEPQ----------NLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265182468 488 RNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIA--HRLSTVINADQIVVIEEGQVTGSGTHKELLASHSFYR 564
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEILE 237
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
352-559 |
9.68e-32 |
|
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: 125.98 E-value: 9.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 352 EVSFSAKKGEVTAFVGPSGAGKSTVFSLI---ERfyePSSGRIFLDGT----DSQNVNLRSWRHLFSYVQQDS---PILa 421
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEArlfPHL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 422 gTIRENLIYGLERHVTDE---EIEEAAKLANAHHFIQSFEAQyetmigerginLSGGQRQRIAIARALLRNPQFLLLDEA 498
Cdd:COG4148 93 -SVRGNLLYGRKRAPRAErriSFDEVVELLGIGHLLDRRPAT-----------LSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265182468 499 TASLDSES--------EKLVQE----------SLETVMkertslviahRLstvinADQIVVIEEGQVTGSGTHKELLAS 559
Cdd:COG4148 161 LAALDLARkaeilpylERLRDEldipilyvshSLDEVA----------RL-----ADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
333-556 |
1.15e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.57 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 333 GSLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDsqnVN-LRSWRHLFS 411
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD---VTdLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 412 YVQQdSPIL--AGTIRENLIYGLE-RHVTDEEIE----EAAKLANAHHFIQSFEAQyetmigerginLSGGQRQRIAIAR 484
Cdd:COG3839 79 MVFQ-SYALypHMTVYENIAFPLKlRKVPKAEIDrrvrEAAELLGLEDLLDRKPKQ-----------LSGGQRQRVALGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 485 ALLRNPQFLLLDEATASLDSE------SE-KLVQESLETvmkerTSLVIAH------RLstvinADQIVVIEEGQVTGSG 551
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDAKlrvemrAEiKRLHRRLGT-----TTIYVTHdqveamTL-----ADRIAVMNDGRIQQVG 216
|
....*
gi 1265182468 552 THKEL 556
Cdd:COG3839 217 TPEEL 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
349-557 |
1.33e-31 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 122.44 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 349 VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSqnVNLRSWRHLFSYVQQDSPILAG-TIREN 427
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--TNLPPEKRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 428 LIYGL-----ERHVTDEEIEEAAKLANAHHFIQSFEAqyetmigergiNLSGGQRQRIAIARALLRNPQFLLLDEATASL 502
Cdd:cd03299 92 IAYGLkkrkvDKKEIERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 503 DSESEKLVQESLETVMKER--TSLVIAHRLSTV-INADQIVVIEEGQVTGSGTHKELL 557
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
25-312 |
1.52e-31 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 124.07 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQLIAGLLVLFAAQMVTSAVSL-----------YLLAQVGQGVVKE 93
Cdd:cd18554 1 IIITIVIGLVRFGIPLLLPLILKYIVDDVIQGSSLTLDEKVYKLFTIIGIMFFIFLilrppveyyrqYFAQWIANKILYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 94 LRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMF 173
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 174 VLVMPLARKIHKISREQQDKMSKLTAFL---AQMLSEIRLIKVSGSEKKEVDSGLQSFQSLylfGVKRAKIEAIITPIIS 250
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLherIQGMSVIKSFALEKHEQKQFDKRNGHFLTR---ALKHTRWNAKTFSAVN 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 251 TVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18554 238 TITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
334-559 |
2.36e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 124.49 E-value: 2.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 334 SLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLI---ERfyePSSGRIFLDGTDSqNVNLRS----- 405
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIaglET---PDSGRIVLNGRDL-FTNLPPrerrv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 406 ---------WRHLfsyvqqdspilagTIRENLIYGLE-RHVTDEEIEEAA----KLANAHHFIQSFEAQyetmigergin 471
Cdd:COG1118 78 gfvfqhyalFPHM-------------TVAENIAFGLRvRPPSKAEIRARVeellELVQLEGLADRYPSQ----------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 472 LSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKE--RTSLVIAH------RLstvinADQIVVIE 543
Cdd:COG1118 134 LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElgGTTVFVTHdqeealEL-----ADRVVVMN 208
|
250
....*....|....*.
gi 1265182468 544 EGQVTGSGTHKELLAS 559
Cdd:COG1118 209 QGRIEQVGTPDEVYDR 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
115-568 |
8.33e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 128.56 E-value: 8.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 115 SGEMVSRITNDTTiVMNLLSTEMIDFVKNILSIIVAIVILFT-LDVPM---TLILLAVIPVMFVLVmplaRKIHKISREQ 190
Cdd:PLN03232 397 SGKVTNMITTDAN-ALQQIAEQLHGLWSAPFRIIVSMVLLYQqLGVASlfgSLILFLLIPLQTLIV----RKMRKLTKEG 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 191 QDKMSKLTAFLAQMLSEIRLIKVSGSEKkEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTvMTAVMIAIVGFGAYRVSE 270
Cdd:PLN03232 472 LQWTDKRVGIINEILASMDTVKCYAWEK-SFESRIQGIRNEELSWFRKAQLLSAFNSFILN-SIPVVVTLVSFGVFVLLG 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 271 GFITAGElvAFV-LYLFQIM-VPVGSLTRFVTSFQQTKGASERIFDILAEKEENYENGEVLEQ-VGSLRFDKVAFQYE-- 345
Cdd:PLN03232 550 GDLTPAR--AFTsLSLFAVLrSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPgAPAISIKNGYFSWDsk 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 346 -DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSsgrifldgtDSQNVNLRSwrhLFSYVQQDSPILAGTI 424
Cdd:PLN03232 628 tSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA---------ETSSVVIRG---SVAYVPQVSWIFNATV 695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 425 RENLIYGlerhvTDEEIEEAAKLANA---HHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATAS 501
Cdd:PLN03232 696 RENILFG-----SDFESERYWRAIDVtalQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 502 LDSESEKLVQES-LETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASHSFYRRLVE 568
Cdd:PLN03232 771 LDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLME 838
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
14-548 |
1.03e-30 |
|
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: 126.07 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 14 LWLLTNPPTGKLLISFILALINTGASLSIPLVIKEVMEKIAiGVSPQLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKE 93
Cdd:COG4615 4 LRLLLRESRWLLLLALLLGLLSGLANAGLIALINQALNATG-AALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 94 LRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTeMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPV-- 171
Cdd:COG4615 83 LRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLgv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 172 -MFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLikvsGSEKKE--VDSGLQSFQSLYlfgvKRAKIEAIITPI 248
Cdd:COG4615 162 aGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKL----NRRRRRafFDEDLQPTAERY----RDLRIRADTIFA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 249 ISTVMTAVM----IAIVGFGAYRVSEgfITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIfDILAEKEENYE 324
Cdd:COG4615 234 LANNWGNLLffalIGLILFLLPALGW--ADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKI-EELELALAAAE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 325 NGEVLEQVG-------SLRFDKVAFQY----EDKP-VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIF 392
Cdd:COG4615 311 PAAADAAAPpapadfqTLELRGVTYRYpgedGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEIL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 393 LDGTDSQNVNLRSWRHLFSYVQQDspilaGTIRENLiYGLERHVTDEEieeaaklanAHHFIQSFEAQYETMIgERG--- 469
Cdd:COG4615 391 LDGQPVTADNREAYRQLFSAVFSD-----FHLFDRL-LGLDGEADPAR---------ARELLERLELDHKVSV-EDGrfs 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 470 -INLSGGQRQRIAIARALLRNPQFLLLDEATASLDSE-----SEKLVQEsletvMKER--TSLVIAH--RLSTVinADQI 539
Cdd:COG4615 455 tTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvfYTELLPE-----LKARgkTVIAISHddRYFDL--ADRV 527
|
....*....
gi 1265182468 540 VVIEEGQVT 548
Cdd:COG4615 528 LKMDYGKLV 536
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
352-559 |
1.46e-30 |
|
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: 122.53 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 352 EVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGT----DSQNVNLRSWRHLFSYVQQDS---PILagTI 424
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdSRKGIFLPPEKRRIGYVFQEArlfPHL--SV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 425 RENLIYGL------ERHVTDEEIEEaakLANAHHFIQsfeaqyetmigeRGIN-LSGGQRQRIAIARALLRNPQFLLLDE 497
Cdd:TIGR02142 93 RGNLRYGMkrarpsERRISFERVIE---LLGIGHLLG------------RLPGrLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 498 ATASLDSESEKLVQESLETVMKERT--SLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLAS 559
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAEFGipILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
350-559 |
1.96e-30 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 120.06 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVN------LRswRHLFSYVQQDSPILAG- 422
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelreLR--RKKISMVFQSFALLPHr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 423 TIRENLIYGLE-RHVTDEEIEEAAKLANAHHFIQSFEAQYetmIGErginLSGGQRQRIAIARALLRNPQFLLLDEATAS 501
Cdd:cd03294 118 TVLENVAFGLEvQGVPRAEREERAAEALELVGLEGWEHKY---PDE----LSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265182468 502 LDSESEKLVQESLETVMKE--RTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLAS 559
Cdd:cd03294 191 LDPLIRREMQDELLRLQAElqKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
335-551 |
2.15e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 118.62 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYE-DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVN------LRswR 407
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreipyLR--R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 408 HLfSYVQQDSPILAG-TIRENL-----IYGLERHVTDEEIEEAAKLANAHHFIQSFEAQyetmigerginLSGGQRQRIA 481
Cdd:COG2884 80 RI-GVVFQDFRLLPDrTVYENValplrVTGKSRKEIRRRVREVLDLVGLSDKAKALPHE-----------LSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 482 IARALLRNPQFLLLDEATASLDSE-SEKLVqESLETVMKERTSLVIA-HRLSTVINADQ-IVVIEEGQVTGSG 551
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
90-565 |
2.77e-30 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 126.95 E-value: 2.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 90 VVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIvilFTLDVPMTLILLAVI 169
Cdd:TIGR01271 956 VSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAI---FVVSVLQPYIFIAAI 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 170 PVMFVLVMPLA---RKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEK-------KEVDSGLQSFqSLYLFGVK-- 237
Cdd:TIGR01271 1033 PVAVIFIMLRAyflRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSyfetlfhKALNLHTANW-FLYLSTLRwf 1111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 238 RAKIEAIITPIISTVmTAVMIAIVGFGAYRVseGFITAgeLVAFVLYLFQIMV----PVGSLTRFVTsfqqtkgaseRIF 313
Cdd:TIGR01271 1112 QMRIDIIFVFFFIAV-TFIAIGTNQDGEGEV--GIILT--LAMNILSTLQWAVnssiDVDGLMRSVS----------RVF 1176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 314 ---DILAEKEE------NYENGEVL-----------EQVGSLRFDKVAFQYED--KPVLQEVSFSAKKGEVTAFVGPSGA 371
Cdd:TIGR01271 1177 kfiDLPQEEPRpsggggKYQLSTVLvienphaqkcwPSGGQMDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGS 1256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 372 GKSTVFSLIERFYEpSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTIRENLiyGLERHVTDEEIEEAAKLANAH 451
Cdd:TIGR01271 1257 GKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL--DPYEQWSDEEIWKVAEEVGLK 1333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 452 HFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLS 531
Cdd:TIGR01271 1334 SVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
490 500 510
....*....|....*....|....*....|....
gi 1265182468 532 TVINADQIVVIEEGQVTGSGTHKELLASHSFYRR 565
Cdd:TIGR01271 1414 ALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
344-551 |
3.18e-30 |
|
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: 117.70 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 344 YEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNvNLRSWRHLFSYVqqDSPILAG- 422
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALI--EAPGFYPn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 423 -TIRENL-IYGLERHVTDEEIEEAAKLANAHHfiqsfeaqyetmIGERGI-NLSGGQRQRIAIARALLRNPQFLLLDEAT 499
Cdd:cd03268 87 lTARENLrLLARLLGIRKKRIDEVLDVVGLKD------------SAKKKVkGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 500 ASLDSESEKLVQESLETVMKE-RTSLVIAHRLSTV-INADQIVVIEEGQVTGSG 551
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQgITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
335-559 |
5.00e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 119.35 E-value: 5.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYED--KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGT--DSQNVnlrsW--RH 408
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlSEETV----WdvRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 409 LFSYVQQ--DSPILAGTIRENLIYGLERH-VTDEE----IEEAAKLANahhfIQSFeAQYETMigergiNLSGGQRQRIA 481
Cdd:PRK13635 82 QVGMVFQnpDNQFVGATVQDDVAFGLENIgVPREEmverVDQALRQVG----MEDF-LNREPH------RLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 482 IARALLRNPQFLLLDEATASLDSESEklvQESLETV--MKER---TSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKEL 556
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGR---REVLETVrqLKEQkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
...
gi 1265182468 557 LAS 559
Cdd:PRK13635 228 FKS 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
335-559 |
5.08e-30 |
|
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: 117.64 E-value: 5.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTD--SQNVNLRSWRHLfSY 412
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitKLPMHKRARLGI-GY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 413 VQQDSPILAG-TIRENLIYGLE-RHVTDEEIEEAAKlanahHFIQSFeaQYETMIGERGINLSGGQRQRIAIARALLRNP 490
Cdd:cd03218 80 LPQEASIFRKlTVEENILAVLEiRGLSKKEREEKLE-----ELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 491 QFLLLDEATASLD----SESEKLVQEsletvMKERT--SLVIAHRLS-TVINADQIVVIEEGQVTGSGTHKELLAS 559
Cdd:cd03218 153 KFLLLDEPFAGVDpiavQDIQKIIKI-----LKDRGigVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
344-559 |
5.77e-30 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 117.78 E-value: 5.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 344 YEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQnvNLRSW---RHLFSYVQQDSPIL 420
Cdd:COG0410 13 YGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT--GLPPHriaRLGIGYVPEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 421 AG-TIRENLIYGLERHVTDEEIEEAaklanahhfiqsFEAQYET------MIGERGINLSGGQRQRIAIARALLRNPQFL 493
Cdd:COG0410 91 PSlTVEENLLLGAYARRDRAEVRAD------------LERVYELfprlkeRRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 494 LLDEATASLdseSEKLVQESLETVM---KERTSLVI----AHRLSTVinADQIVVIEEGQVTGSGTHKELLAS 559
Cdd:COG0410 159 LLDEPSLGL---APLIVEEIFEIIRrlnREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLAD 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
335-559 |
9.11e-30 |
|
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: 117.49 E-value: 9.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSG---RIFldGTDSQNVNLRSWRHLFS 411
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 412 YVqqdSPILAGTIRENL------------IYGLERHVTDEEIEEAAKLanahhfIQSFEAQYetmIGERGIN-LSGGQRQ 478
Cdd:COG1119 82 LV---SPALQLRFPRDEtvldvvlsgffdSIGLYREPTDEQRERAREL------LELLGLAH---LADRPFGtLSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 479 RIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKE--RTSLVIAHRLSTVINA-DQIVVIEEGQVTGSGTHKE 555
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEE 229
|
....
gi 1265182468 556 LLAS 559
Cdd:COG1119 230 VLTS 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
349-552 |
1.33e-29 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 116.77 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 349 VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTD------SQNVNL---RSWrhlfsyvQQDSPI 419
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitglppHEIARLgigRTF-------QIPRLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 420 LAGTIRENLIYGLERH---------VTDEEIEEAAKlanAHHFIQSF--EAQYETMIGergiNLSGGQRQRIAIARALLR 488
Cdd:cd03219 88 PELTVLENVMVAAQARtgsglllarARREEREARER---AEELLERVglADLADRPAG----ELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 489 NPQFLLLDEATASL-DSESEKLVQESLETVMKERTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGT 552
Cdd:cd03219 161 DPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
335-540 |
1.64e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 116.35 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQ 414
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QdSPILAG-TIRENLIYGLE-RHVTDEEIEEAAKLANahhfiqsFEAQYETMigERGIN-LSGGQRQRIAIARALLRNPQ 491
Cdd:PRK10247 88 Q-TPTLFGdTVYDNLIFPWQiRNQQPDPAIFLDDLER-------FALPDTIL--TKNIAeLSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1265182468 492 FLLLDEATASLDSESEKLVQESLETVMKERTSLVI--AHRLSTVINADQIV 540
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVI 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
346-556 |
2.23e-29 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 115.68 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 346 DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDsQNVNLRSWRHLFSYVQQDSPILAG-TI 424
Cdd:cd03263 14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS-IRTDRKAARQSLGYCPQFDALFDElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 425 RENL-IYGLERHVTDEEIEEaakLANAHHFIQSFEAQYETMIGergiNLSGGQRQRIAIARALLRNPQFLLLDEATASLD 503
Cdd:cd03263 93 REHLrFYARLKGLPKSEIKE---EVELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 504 SESEKLVQESLETVMKERTSLVIAHRLSTV-INADQIVVIEEGQVTGSGTHKEL 556
Cdd:cd03263 166 PASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
335-544 |
6.16e-29 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 114.11 E-value: 6.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFsYVQ 414
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLA-YLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QDSPILAG-TIRENL-----IYGLerHVTDEEIEEAAKLANahhfIQSFEaqyETMIGergiNLSGGQRQRIAIARALLR 488
Cdd:COG4133 82 HADGLKPElTVRENLrfwaaLYGL--RADREAIDEALEAVG----LAGLA---DLPVR----QLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 489 NPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEE 544
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGD 204
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
334-556 |
1.06e-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: 114.36 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 334 SLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRS-------- 405
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnvgfvfq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 406 ----WRHLfsyvqqdspilagTIRENLIYGLERHVTDEEIEEAAKLANAHHFIQ-----SFEAQYETmigergiNLSGGQ 476
Cdd:cd03296 82 hyalFRHM-------------TVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKlvqldWLADRYPA-------QLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 477 RQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTH 553
Cdd:cd03296 142 RQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTP 221
|
...
gi 1265182468 554 KEL 556
Cdd:cd03296 222 DEV 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
352-551 |
1.36e-28 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 113.16 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 352 EVSFSAKkGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGT---DS-QNVNLRSWRHLFSYVQQDS---PILagTI 424
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSrKKINLPPQQRKIGLVFQQYalfPHL--NV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 425 RENLIYGLERHVTDEE---IEEAAKLANAHHFIQSFEAQyetmigerginLSGGQRQRIAIARALLRNPQFLLLDEATAS 501
Cdd:cd03297 93 RENLAFGLKRKRNREDrisVDELLDLLGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 502 LDSESEKLVQESLETVMKE--RTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSG 551
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
335-556 |
1.40e-28 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 113.87 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNV--NLRSWRHLF-S 411
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLppHKRPVNTVFqN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 412 YVQqdSPILagTIRENLIYGLERHVTDEEiEEAAKLANAHHFIQsFEAQYETMIGErginLSGGQRQRIAIARALLRNPQ 491
Cdd:cd03300 81 YAL--FPHL--TVFENIAFGLRLKKLPKA-EIKERVAEALDLVQ-LEGYANRKPSQ----LSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 492 FLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKEL 556
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
65-312 |
1.82e-28 |
|
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: 115.26 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 65 LLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNI 144
Cdd:cd18577 53 FVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 145 LSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSG 224
Cdd:cd18577 133 STFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRY 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 225 LQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQ 304
Cdd:cd18577 213 SKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAK 292
|
....*...
gi 1265182468 305 TKGASERI 312
Cdd:cd18577 293 ARAAAAKI 300
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
343-547 |
2.14e-28 |
|
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: 112.62 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 343 QYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGT----DSQNVN-LRS-----------W 406
Cdd:cd03262 9 SFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltdDKKNINeLRQkvgmvfqqfnlF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 407 RHLfsyvqqdspilagTIRENLIYGLE--RHVTDEEIEEAAK-------LAnahHFIQSFEAQyetmigerginLSGGQR 477
Cdd:cd03262 89 PHL-------------TVLENITLAPIkvKGMSKAEAEERALellekvgLA---DKADAYPAQ-----------LSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 478 QRIAIARALLRNPQFLLLDEATASLDSEsekLVQESLEtVMKE-----RTSLVIAHRLSTVIN-ADQIVVIEEGQV 547
Cdd:cd03262 142 QRVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLD-VMKDlaeegMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
348-556 |
2.47e-28 |
|
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: 114.57 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 348 PVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTdsqnvnlrswrhlFSYVQQDSPILAGTIREN 427
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 428 LIYGLErhvTDE-EIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSES 506
Cdd:cd03291 118 IIFGVS---YDEyRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1265182468 507 EKLVQES-LETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKEL 556
Cdd:cd03291 195 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
335-547 |
2.80e-28 |
|
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: 112.35 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNV------------N 402
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLppkdrdiamvfqN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 403 LRSWRHLfsyvqqdspilagTIRENLIYGLE-RHVTDEEIEE----AAKLANAHHFIQSFEAQyetmigerginLSGGQR 477
Cdd:cd03301 81 YALYPHM-------------TVYDNIAFGLKlRKVPKDEIDErvreVAELLQIEHLLDRKPKQ-----------LSGGQR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265182468 478 QRIAIARALLRNPQFLLLDEATASLD--------SESEKLvQESLETvmkerTSLVIAHRLSTVIN-ADQIVVIEEGQV 547
Cdd:cd03301 137 QRVALGRAIVREPKVFLMDEPLSNLDaklrvqmrAELKRL-QQRLGT-----TTIYVTHDQVEAMTmADRIAVMNDGQI 209
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
335-556 |
5.95e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.92 E-value: 5.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYE-DKP-VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSY 412
Cdd:PRK13648 8 IVFKNVSFQYQsDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 413 VQQ--DSPILAGTIRENLIYGLERH---------VTDEEIEEAAKLANAHHFIQSfeaqyetmigerginLSGGQRQRIA 481
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGLENHavpydemhrRVSEALKQVDMLERADYEPNA---------------LSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265182468 482 IARALLRNPQFLLLDEATASLDSESEK----LVQESLETvmKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKEL 556
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQnlldLVRKVKSE--HNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
339-547 |
6.82e-28 |
|
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: 113.99 E-value: 6.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 339 KVAFQYEDKPV--LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEP---SSGRIFLDGTDSQNVNLRSWRHL---- 409
Cdd:COG0444 8 KVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIrgre 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 410 FSYVQQDS-----PILagTIRENLIYGLERH--VTDEEIEEAAK-------LANAHHFIQSFEAQyetmigerginLSGG 475
Cdd:COG0444 88 IQMIFQDPmtslnPVM--TVGDQIAEPLRIHggLSKAEARERAIellervgLPDPERRLDRYPHE-----------LSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 476 QRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER-TSLV-IAHRLSTVIN-ADQIVV------IEEGQ 546
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELgLAILfITHDLGVVAEiADRVAVmyagriVEEGP 234
|
.
gi 1265182468 547 V 547
Cdd:COG0444 235 V 235
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
339-558 |
7.35e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 112.90 E-value: 7.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 339 KVAFQY---EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQ 415
Cdd:PRK13650 9 NLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 416 --DSPILAGTIRENLIYGLERHVTD-----EEIEEAAKLANAHHFIQSFEAQyetmigerginLSGGQRQRIAIARALLR 488
Cdd:PRK13650 89 npDNQFVGATVEDDVAFGLENKGIPheemkERVNEALELVGMQDFKEREPAR-----------LSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 489 NPQFLLLDEATASLDSESEklvQESLETVMKER-----TSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLA 558
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGR---LELIKTIKGIRddyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
335-547 |
7.89e-28 |
|
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: 111.11 E-value: 7.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVlqEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDsqNVNLRSWRHLFSYVQ 414
Cdd:TIGR01277 1 LALDKVRYEYEHLPM--EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS--HTGLAPYQRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QDSPILAG-TIRENLIYGLE-----RHVTDEEIEEAAKLANAHHFIQSFEAQyetmigerginLSGGQRQRIAIARALLR 488
Cdd:TIGR01277 77 QENNLFAHlTVRQNIGLGLHpglklNAEQQEKVVDAAQQVGIADYLDRLPEQ-----------LSGGQRQRVALARCLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 489 NPQFLLLDEATASLDsesEKLVQESLETVM-----KERTSLVIAHRLSTVIN-ADQIVVIEEGQV 547
Cdd:TIGR01277 146 PNPILLLDEPFSALD---PLLREEMLALVKqlcseRQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
349-552 |
9.40e-28 |
|
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: 112.05 E-value: 9.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 349 VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTD-----------------SQNVNLrsWRHLfs 411
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitglpphriarlgiartFQNPRL--FPEL-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 412 yvqqdspilagTIRENLIYGLERHVTDEEI-----------EEAAKLANAHHFIQSF--EAQYETMIGergiNLSGGQRQ 478
Cdd:COG0411 95 -----------TVLENVLVAAHARLGRGLLaallrlprarrEEREARERAEELLERVglADRADEPAG----NLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 479 RIAIARALLRNPQFLLLDEATASL-DSESEKLVqESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGT 552
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLnPEETEELA-ELIRRLRDERgiTILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
347-551 |
1.78e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 109.56 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 347 KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLI--ERFYEPSSGRIFLDGTdsqNVNLRSWRHLFSYVQQDSPILAG-T 423
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQDDILHPTlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 424 IRENLIYglerhvtdeeieeAAKLanahhfiqsfeaqyetmigeRGInlSGGQRQRIAIARALLRNPQFLLLDEATASLD 503
Cdd:cd03213 99 VRETLMF-------------AAKL--------------------RGL--SGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 504 SESEKLVqesLETVMKE----RTSLVIAHRLSTVI--NADQIVVIEEGQVTGSG 551
Cdd:cd03213 144 SSSALQV---MSLLRRLadtgRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
353-541 |
1.87e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 112.90 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 353 VSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQ---QDS-----PILagTI 424
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQmvfQDPyaslnPRM--TV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 425 RENLIYGLERH--VTDEEIEEAAklanahhfiqsfeaqyETMIGERGIN----------LSGGQRQRIAIARALLRNPQF 492
Cdd:COG4608 115 GDIIAEPLRIHglASKAERRERV----------------AELLELVGLRpehadrypheFSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 493 LLLDEATASLD-SeseklVQES----LETVMKER--TSLVIAHRLSTV--InADQIVV 541
Cdd:COG4608 179 IVCDEPVSALDvS-----IQAQvlnlLEDLQDELglTYLFISHDLSVVrhI-SDRVAV 230
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
121-546 |
2.15e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 116.45 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 121 RITND----TTIVMNLLstemIDFVKNILSIIVAIVILFTLDVPMTLILL---AVIPVMFVLVMPL------------AR 181
Cdd:COG4178 129 RIAEDirlfTETTLSLS----LGLLSSVVTLISFIGILWSLSGSLTFTLGgysITIPGYMVWAALIyaiigtllthliGR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 182 KIHKISREQQdkmsKLTA-FLAQMlseIRL------IKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMT 254
Cdd:COG4178 205 PLIRLNFEQQ----RREAdFRFAL---VRVrenaesIALYRGEAAERRRLRRRFDAVIANWRRLIRRQRNLTFFTTGYGQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 255 AVMIAIVGFGAYRVSEGFITAGELV----AFvlylFQIMvpvGSLTRFVTSFQQT---KGASERI---FDILAEKEENYE 324
Cdd:COG4178 278 LAVIFPILVAAPRYFAGEITLGGLMqaasAF----GQVQ---GALSWFVDNYQSLaewRATVDRLagfEEALEAADALPE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 325 NGEVLEQV--GSLRFDKVAFQ-YEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDgtdsqnv 401
Cdd:COG4178 351 AASRIETSedGALALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP------- 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 402 nlRSWRHLF----SYVQQdspilaGTIRENLIY-GLERHVTDEEIEEAAKLANAHHFIQSFEAQyetmiGERGINLSGGQ 476
Cdd:COG4178 424 --AGARVLFlpqrPYLPL------GTLREALLYpATAEAFSDAELREALEAVGLGHLAERLDEE-----ADWDQVLSLGE 490
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 477 RQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQ 546
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
335-561 |
3.57e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 109.67 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVlqEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDS--------------QN 400
Cdd:PRK10771 2 LKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHtttppsrrpvsmlfQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 401 VNLRSwrHLfsyvqqdspilagTIRENLIYGLE-----RHVTDEEIEEAAKLANAHHFIQSFEAQyetmigerginLSGG 475
Cdd:PRK10771 80 NNLFS--HL-------------TVAQNIGLGLNpglklNAAQREKLHAIARQMGIEDLLARLPGQ-----------LSGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 476 QRQRIAIARALLRNPQFLLLDEATASLDSeseKLVQESL---ETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTG 549
Cdd:PRK10771 134 QRQRVALARCLVREQPILLLDEPFSALDP---ALRQEMLtlvSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAW 210
|
250
....*....|..
gi 1265182468 550 SGTHKELLASHS 561
Cdd:PRK10771 211 DGPTDELLSGKA 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
341-551 |
5.11e-27 |
|
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: 108.99 E-value: 5.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 341 AFQYEDKPV--LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSP 418
Cdd:cd03266 10 RFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 419 ILAGTIRENL-----IYGLERHVTDEEIEEAAKLANAHHFIQsfeaqyetmigERGINLSGGQRQRIAIARALLRNPQFL 493
Cdd:cd03266 90 YDRLTARENLeyfagLYGLKGDELTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 494 LLDEATASLDSESEKLVQESLETVMKERTSLVIA-HRLSTVIN-ADQIVVIEEGQVTGSG 551
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
342-566 |
6.79e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 116.42 E-value: 6.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 342 FQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDgtdsqnvnlRSwrhlFSYVQQDSPILA 421
Cdd:PTZ00243 668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE---------RS----IAYVPQQAWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 422 GTIRENLIYglerhvTDEEieEAAKLANAHHFIQsFEAQ-------YETMIGERGINLSGGQRQRIAIARALLRNPQFLL 494
Cdd:PTZ00243 735 ATVRGNILF------FDEE--DAARLADAVRVSQ-LEADlaqlgggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYL 805
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 495 LDEATASLDSE-SEKLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLAShSFYRRL 566
Cdd:PTZ00243 806 LDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRT-SLYATL 877
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
336-548 |
6.82e-27 |
|
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: 108.11 E-value: 6.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 336 RFDKVAFQYEDKP-VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsQNVNLRSWRHLFSYVQ 414
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QDS--PILAGTIRENLIYGLERhvTDEEIEEAAK---------LANAHHFIqsfeaqyetmigerginLSGGQRQRIAIA 483
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKE--LDAGNEQAETvlkdldlyaLKERHPLS-----------------LSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265182468 484 RALLRNPQFLLLDEATASLDSESEKLVQESLETVMKE-RTSLVIAHR---LSTVinADQIVVIEEGQVT 548
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQgKAVIVITHDyefLAKV--CDRVLLLANGAIV 205
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
342-575 |
8.79e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 111.32 E-value: 8.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 342 FQYEDKPV--LQEVSFSAKKGEVTAFVGPSGAGKST---VFSLIERfyePSSGRIFLDGTDSQNVN---LRSWRHLFSYV 413
Cdd:COG1135 11 FPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSereLRAARRKIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 414 QQDSPILAG-TIRENLIYGLER-HVTDEEIEEAAK-------LANAHHfiqSFEAQyetmigerginLSGGQRQRIAIAR 484
Cdd:COG1135 88 FQHFNLLSSrTVAENVALPLEIaGVPKAEIRKRVAellelvgLSDKAD---AYPSQ-----------LSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 485 ALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTV--InADQIVVIEEGQVTGSGTHKELLAS- 559
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVrrI-CDRVAVLENGRIVEQGPVLDVFANp 232
|
250
....*....|....*..
gi 1265182468 560 -HSFYRRLVEQQFQTSL 575
Cdd:COG1135 233 qSELTRRFLPTVLNDEL 249
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
349-567 |
9.00e-27 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 109.94 E-value: 9.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 349 VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEpSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTIRENL 428
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 429 -IYGlerHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESE 507
Cdd:cd03289 98 dPYG---KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 508 KLVQESLETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASHSFYRRLV 567
Cdd:cd03289 175 QVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-526 |
9.46e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 109.36 E-value: 9.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYE--PS---SGRIFLDGTD--SQNVNLRSWR 407
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDiyDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 408 HLFSYV-QQDSPiLAGTIRENLIYGLERH------VTDEEIEEAAKLAnahhfiqsfeAQYETM---IGERGINLSGGQR 477
Cdd:COG1117 92 RRVGMVfQKPNP-FPKSIYDNVAYGLRLHgiksksELDEIVEESLRKA----------ALWDEVkdrLKKSALGLSGGQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 478 QRIAIARALLRNPQFLLLDEATASLDSES----EKLVQEsletvMKERTSLVI 526
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPIStakiEELILE-----LKKDYTIVI 208
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
25-312 |
1.19e-26 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 109.96 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALIntgaSLSIPLVIKEVMEKIAIGVSPQL----IAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWN 100
Cdd:cd18568 8 LLASLLLQLL----GLALPLFTQIILDRVLVHKNISLlnliLIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 101 KLIKLPVSFYDQNRSGEMVSRITNDTTIvMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLA 180
Cdd:cd18568 84 HLLSLPLSFFASRKVGDIITRFQENQKI-RRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 181 RKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAI 260
Cdd:cd18568 163 PKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 261 VGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18568 243 LWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
337-548 |
1.46e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 113.62 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 337 FDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsqnvNLRswrhlFSYVQQD 416
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR-----IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 417 SPILAG-TIRENLIYGLER------------HVTDEEIEEAAKLANAHHFIQ-----SFEAQYETMIGERGI-------- 470
Cdd:COG0488 70 PPLDDDlTVLDTVLDGDAElraleaeleeleAKLAEPDEDLERLAELQEEFEalggwEAEARAEEILSGLGFpeedldrp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 471 --NLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESeklvQESLETVMKERTS--LVIAH-R--LSTVinADQIVVIE 543
Cdd:COG0488 150 vsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKNYPGtvLVVSHdRyfLDRV--ATRILELD 223
|
....*
gi 1265182468 544 EGQVT 548
Cdd:COG0488 224 RGKLT 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
335-551 |
1.46e-26 |
|
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: 107.58 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSakKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSqnVNLRSWRHLFSYVQ 414
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV--TAAPPADRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QDSPILAG-TIRENLIYGLER--HVTDEEiEEAAKLANAHHFIQSFEAQyetmigeRGINLSGGQRQRIAIARALLRNPQ 491
Cdd:cd03298 77 QENNLFAHlTVEQNVGLGLSPglKLTAED-RQAIEVALARVGLAGLEKR-------LPGELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 492 FLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSG 551
Cdd:cd03298 149 VLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
344-550 |
1.46e-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: 105.97 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 344 YEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDsqnvnlrswrhlfsyVQQDSPIlagt 423
Cdd:cd03216 10 FGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE---------------VSFASPR---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 424 irenliyglerhvtdeeieeaaklanahhfiqsfEAQyetmigERGIN----LSGGQRQRIAIARALLRNPQFLLLDEAT 499
Cdd:cd03216 71 ----------------------------------DAR------RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 500 ASL-DSESEKLvqesLETV--MKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGS 550
Cdd:cd03216 111 AALtPAEVERL----FKVIrrLRAQgvAVIFISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
338-551 |
2.38e-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: 106.89 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 338 DKVAFQYEDKPVLQEVSFSAKKGeVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTD--SQNVNLRswRHLfSYVQQ 415
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDvlKQPQKLR--RRI-GYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 416 DSPILAG-TIRENLIY-----GLERHVTDEEIEEAAKLANAHHFiqsfeaqYETMIGErginLSGGQRQRIAIARALLRN 489
Cdd:cd03264 80 EFGVYPNfTVREFLDYiawlkGIPSKEVKARVDEVLELVNLGDR-------AKKKIGS----LSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 490 PQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTV-INADQIVVIEEGQVTGSG 551
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFEG 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
343-555 |
3.20e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.42 E-value: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 343 QYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSwRHLFSYVQQDSPILAG 422
Cdd:PRK09452 23 SFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RHVNTVFQSYALFPHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 423 TIRENLIYGLE-RHVTDEEIE----EAAKLAnahhfiqsfeaQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDE 497
Cdd:PRK09452 102 TVFENVAFGLRmQKTPAAEITprvmEALRMV-----------QLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265182468 498 ATASLDSESEKLVQESLETVMKER--TSLVIAH-RLSTVINADQIVVIEEGQVTGSGTHKE 555
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
337-547 |
4.45e-26 |
|
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: 105.95 E-value: 4.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 337 FDKVAFQY-EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRS---WRHLFSY 412
Cdd:cd03292 3 FINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 413 VQQDSPILAG-TIRENLIYGLErhVTDEEIEEAAK-------LANAHHFIQSFEAQyetmigerginLSGGQRQRIAIAR 484
Cdd:cd03292 83 VFQDFRLLPDrNVYENVAFALE--VTGVPPREIRKrvpaaleLVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 485 ALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVINADQ--IVVIEEGQV 547
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
61-312 |
6.73e-26 |
|
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: 108.04 E-value: 6.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 61 LIAGLLVL-FAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMID 139
Cdd:cd18565 55 LLGGLTVAaFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 140 FVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKK 219
Cdd:cd18565 135 IIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDF 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 220 EVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAIVGFGAYRVSEGF------ITAGELVAFVLYLFQIMVPVG 293
Cdd:cd18565 215 ERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGPplftgtLTVGTLVTFLFYTQRLLWPLT 294
|
250
....*....|....*....
gi 1265182468 294 SLTRFVTSFQQTKGASERI 312
Cdd:cd18565 295 RLGDLIDQYQRAMASAKRV 313
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
338-556 |
9.82e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.10 E-value: 9.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 338 DKVAFQYED------KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNV-NLRSWRHLF 410
Cdd:PRK13633 8 KNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 411 SYVQQ--DSPILAGTIRENLIYGLER-HVTDEEI----EEAAKLANAHHFiqsfeAQYETMIgerginLSGGQRQRIAIA 483
Cdd:PRK13633 88 GMVFQnpDNQIVATIVEEDVAFGPENlGIPPEEIrervDESLKKVGMYEY-----RRHAPHL------LSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 484 RALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKEL 556
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
145-568 |
1.04e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 112.52 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 145 LSIIVAIVILF-TLDVPM---TLILLAVIPVMFVLVmplaRKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKkE 220
Cdd:PLN03130 426 FRIIIAMVLLYqQLGVASligSLMLVLMFPIQTFII----SKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWEN-S 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 221 VDSGLQSFQSLYLFGVKRAK-IEAIITPIISTVmtAVMIAIVGFGAYRVSEGFITAGElvAFV-LYLFQIM-VPVGSLTR 297
Cdd:PLN03130 501 FQSKVQTVRDDELSWFRKAQlLSAFNSFILNSI--PVLVTVVSFGVFTLLGGDLTPAR--AFTsLSLFAVLrFPLFMLPN 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 298 FVTSFQQTKGASERIFDILAEKEENYENGEVLEQV--------GSLRFDKVAfqyeDKPVLQEVSFSAKKGEVTAFVGPS 369
Cdd:PLN03130 577 LITQAVNANVSLKRLEELLLAEERVLLPNPPLEPGlpaisiknGYFSWDSKA----ERPTLSNINLDVPVGSLVAIVGST 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 370 GAGKSTVFSLIERFYEP-SSGRIFLDGTdsqnvnlrswrhlFSYVQQDSPILAGTIRENLIYGLErhVTDEEIEEAAKLA 448
Cdd:PLN03130 653 GEGKTSLISAMLGELPPrSDASVVIRGT-------------VAYVPQVSWIFNATVRDNILFGSP--FDPERYERAIDVT 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 449 NAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQES-LETVMKERTSLVIA 527
Cdd:PLN03130 718 ALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVT 797
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1265182468 528 HRLSTVINADQIVVIEEGQVTGSGTHKELLASHSFYRRLVE 568
Cdd:PLN03130 798 NQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLME 838
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
61-556 |
1.17e-25 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 112.31 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 61 LIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDttivMNLL--STEMI 138
Cdd:TIGR01271 124 LALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNN----LNKFdeGLALA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 139 DFV-KNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSE 217
Cdd:TIGR01271 200 HFVwIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 218 KKevdsglqsfqslylfgvkrakIEAIITPIISTVMTavMIAIVGFGAYRVSEGFITAGELVAFV----------LYLFQ 287
Cdd:TIGR01271 280 EA---------------------MEKIIKNIRQDELK--LTRKIAYLRYFYSSAFFFSGFFVVFLsvvpyalikgIILRR 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 288 I-------MVPVGSLTR-FVTSFQ---QTKGASERIFDILAEKEE-----NYENGEVL---------EQVGSLrFDKVA- 341
Cdd:TIGR01271 337 IfttisycIVLRMTVTRqFPGAIQtwyDSLGAITKIQDFLCKEEYktleyNLTTTEVEmvnvtaswdEGIGEL-FEKIKq 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 342 ------------------FQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTdsqnvnl 403
Cdd:TIGR01271 416 nnkarkqpngddglffsnFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR------- 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 404 rswrhlFSYVQQDSPILAGTIRENLIYGLErhvTDE-EIEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAI 482
Cdd:TIGR01271 489 ------ISFSPQTSWIMPGTIKDNIIFGLS---YDEyRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISL 559
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 483 ARALLRNPQFLLLDEATASLDSESEKLVQES-LETVMKERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKEL 556
Cdd:TIGR01271 560 ARAVYKDADLYLLDSPFTHLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
337-556 |
2.73e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 105.65 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 337 FDKVAFQYED--KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEP---SSGRIFLDGTDSQNVNLRSWRHLFS 411
Cdd:PRK13640 8 FKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 412 YVQQ--DSPILAGTIRENLIYGLE-RHVTDEEIEEAAKLANAH----HFIQSFEAqyetmigergiNLSGGQRQRIAIAR 484
Cdd:PRK13640 88 IVFQnpDNQFVGATVGDDVAFGLEnRAVPRPEMIKIVRDVLADvgmlDYIDSEPA-----------NLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 485 ALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKEL 556
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
340-557 |
2.89e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.20 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 340 VAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDsqnvnLRSW------RHLfSYV 413
Cdd:COG4559 7 LSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRP-----LAAWspwelaRRR-AVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 414 QQDSPI-LAGTIRENLIYGLERHVT-----DEEIEEAAKLANAHHFIQSFeaqYETmigerginLSGGQRQRIAIARALL 487
Cdd:COG4559 81 PQHSSLaFPFTVEEVVALGRAPHGSsaaqdRQIVREALALVGLAHLAGRS---YQT--------LSGGEQQRVQLARVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 488 -------RNPQFLLLDEATASLDsesekLV-QESLETVMKERTS-----LVIAHRLstviN-----ADQIVVIEEGQVTG 549
Cdd:COG4559 150 qlwepvdGGPRWLFLDEPTSALD-----LAhQHAVLRLARQLARrgggvVAVLHDL----NlaaqyADRILLLHQGRLVA 220
|
....*...
gi 1265182468 550 SGTHKELL 557
Cdd:COG4559 221 QGTPEEVL 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
334-503 |
3.81e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 103.33 E-value: 3.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 334 SLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEP---SSGRIFLDGTDSQNVNLRSwRHLf 410
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ-RRI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 411 SYVQQDS---PILagTIRENLIYGLERHVTDEE----IEEAAKLANAHHFIQSFEAQyetmigerginLSGGQRQRIAIA 483
Cdd:COG4136 79 GILFQDDllfPHL--SVGENLAFALPPTIGRAQrrarVEQALEEAGLAGFADRDPAT-----------LSGGQRARVALL 145
|
170 180
....*....|....*....|
gi 1265182468 484 RALLRNPQFLLLDEATASLD 503
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLD 165
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
349-548 |
1.40e-24 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 102.51 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 349 VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLI---ERfyePSSGRIFLDGTDSQNVN------LRSwRHLfSYVQQDSPI 419
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLaglDR---PTSGTVRLAGQDLFALDedararLRA-RHV-GFVFQSFQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 420 LAG-TIRENLIYGLERHVTDEEIEEAAKL-------ANAHHFiqsfEAQyetmigerginLSGGQRQRIAIARALLRNPQ 491
Cdd:COG4181 102 LPTlTALENVMLPLELAGRRDARARARALlervglgHRLDHY----PAQ-----------LSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 492 FLLLDEATASLDSESEKLVQESLETVMKER-TSLVI-------AHRlstvinADQIVVIEEGQVT 548
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERgTTLVLvthdpalAAR------CDRVLRLRAGRLV 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
337-557 |
1.62e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.48 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 337 FDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTD--SQNVNLRSWRHLFSYV- 413
Cdd:PRK09493 4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvnDPKVDERLIRQEAGMVf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 414 QQDSPILAGTIRENLIYGlERHVTDEEIEEAAKLA-----------NAHHFIQSfeaqyetmigerginLSGGQRQRIAI 482
Cdd:PRK09493 84 QQFYLFPHLTALENVMFG-PLRVRGASKEEAEKQArellakvglaeRAHHYPSE---------------LSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 483 ARALLRNPQFLLLDEATASLDSEsekLVQESLeTVMKE-----RTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKEL 556
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPE---LRHEVL-KVMQDlaeegMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVL 223
|
.
gi 1265182468 557 L 557
Cdd:PRK09493 224 I 224
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
335-556 |
2.27e-24 |
|
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: 101.83 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTD------SQNVnlrswRH 408
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDitklppHERA-----RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 409 LFSYVQQDSPILAG-TIRENLIYGLERhvtdeeieeaakLANAHHFIQsfEAQYE------TMIGERGINLSGGQRQRIA 481
Cdd:TIGR03410 76 GIAYVPQGREIFPRlTVEENLLTGLAA------------LPRRSRKIP--DEIYElfpvlkEMLGRRGGDLSGGQQQQLA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 482 IARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKEL 556
Cdd:TIGR03410 142 IARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
328-528 |
2.56e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 102.25 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 328 VLEQVgSLRFDKVAfqyEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDS--------- 398
Cdd:COG4525 5 TVRHV-SVRYPGGG---QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadrgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 399 --QNVNLRSWRhlfsyvqqdspilagTIRENLIYGL--------ERHVTDEEIEEAAKLANAH-HFIqsfeaqYEtmige 467
Cdd:COG4525 81 vfQKDALLPWL---------------NVLDNVAFGLrlrgvpkaERRARAEELLALVGLADFArRRI------WQ----- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 468 rginLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKE--RTSLVIAH 528
Cdd:COG4525 135 ----LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtgKGVFLITH 193
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
342-558 |
2.63e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.85 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 342 FQYED-KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGT--DSQNVNLRSWRHLFSYVQQ--D 416
Cdd:PRK13639 9 YSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpiKYDKKSLLEVRKTVGIVFQnpD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 417 SPILAGTIRENLIYG-LERHVTDEEIEEAAKLANAHHFIQSFEAQYETmigergiNLSGGQRQRIAIARALLRNPQFLLL 495
Cdd:PRK13639 89 DQLFAPTVEEDVAFGpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPH-------HLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 496 DEATASLDSESEKLVQESLETVMKERTSLVIA-HRLSTV-INADQIVVIEEGQVTGSGTHKELLA 558
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
344-497 |
4.13e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 101.26 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 344 YEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTD--SQNVNLRSWRHLfSYVQQDSPILA 421
Cdd:COG1137 13 YGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDitHLPMHKRARLGI-GYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 422 G-TIRENLIYGLE-RHVTDEEIEEaaKLanahhfiqsfeaqyETMIGE---------RGINLSGGQRQRIAIARALLRNP 490
Cdd:COG1137 92 KlTVEDNILAVLElRKLSKKEREE--RL--------------EELLEEfgithlrksKAYSLSGGERRRVEIARALATNP 155
|
....*..
gi 1265182468 491 QFLLLDE 497
Cdd:COG1137 156 KFILLDE 162
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
344-556 |
4.29e-24 |
|
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: 100.52 E-value: 4.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 344 YEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTD----SQNVnlrswRHLFSYVQQDS-- 417
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvvrePREV-----RRRIGIVFQDLsv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 418 -PILAGtiRENL-----IYGLERHVTDEEIEEAAKlanahhFIQSFEAQyetmiGERGINLSGGQRQRIAIARALLRNPQ 491
Cdd:cd03265 85 dDELTG--WENLyiharLYGVPGAERRERIDELLD------FVGLLEAA-----DRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 492 FLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKEL 556
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
346-545 |
4.65e-24 |
|
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: 100.48 E-value: 4.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 346 DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIF----LDGTDSQNVNLRSWRHLFSYVQQDSPILA 421
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 422 GTIRENLIYGL----ERHvtdEEIEEAAKLANAhhfIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDE 497
Cdd:cd03290 93 ATVEENITFGSpfnkQRY---KAVTDACSLQPD---IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1265182468 498 ATASLDSE-SEKLVQESLETVMKE--RTSLVIAHRLSTVINADQIVVIEEG 545
Cdd:cd03290 167 PFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
334-557 |
4.82e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.39 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 334 SLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDsqnvnLRSW------R 407
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-----LADWspaelaR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 408 HLFSYVQQDSPILAGTIRE-----NLIYGLERHVTDEEIEEAAKLANAHHFIQSFeaqYETmigerginLSGGQRQRIAI 482
Cdd:PRK13548 77 RRAVLPQHSSLSFPFTVEEvvamgRAPHGLSRAEDDALVAAALAQVDLAHLAGRD---YPQ--------LSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 483 ARALLR------NPQFLLLDEATASLDsesekLV-QESLETVMKERTS------LVIAHRLstviN-----ADQIVVIEE 544
Cdd:PRK13548 146 ARVLAQlwepdgPPRWLLLDEPTSALD-----LAhQHHVLRLARQLAHerglavIVVLHDL----NlaaryADRIVLLHQ 216
|
250
....*....|...
gi 1265182468 545 GQVTGSGTHKELL 557
Cdd:PRK13548 217 GRLVADGTPAEVL 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
347-547 |
5.20e-24 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 101.81 E-value: 5.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 347 KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVN---LRSWRHLFSYVQQDSPILAG- 422
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDSPSAVNp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 423 --TIRENLIYGLeRHVTDeeIEEAAKLANAHHFIQSFEAQYETMiGERGINLSGGQRQRIAIARALLRNPQFLLLDEATA 500
Cdd:TIGR02769 104 rmTVRQIIGEPL-RHLTS--LDESEQKARIAELLDMVGLRSEDA-DKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1265182468 501 SLDSESEKLVQESLETVMKE--RTSLVIAHRLSTVIN-ADQIVVIEEGQV 547
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLQQAfgTAYLFITHDLRLVQSfCQRVAVMDKGQI 229
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
366-558 |
5.20e-24 |
|
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: 102.96 E-value: 5.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 366 VGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNV--NLRSWRHLFsyvQQDSPILAGTIRENLIYGLE-RHVTDEEIE 442
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVppHLRHINMVF---QSYALFPHMTVEENVAFGLKmRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 443 EAAKLANAhhfiqsfEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER- 521
Cdd:TIGR01187 79 PRVLEALR-------LVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLg 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 1265182468 522 -TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLA 558
Cdd:TIGR01187 152 iTFVFVTHDQEEAMTmSDRIAIMRKGKIAQIGTPEEIYE 190
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
334-572 |
5.62e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 101.24 E-value: 5.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 334 SLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSW-RHLfSY 412
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLaRRL-AL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 413 VQQDSPILAG-TIRENLIYGLERHVT--------DEEIEEAAklanahhfIQsfEAQYETMIGERGINLSGGQRQRIAIA 483
Cdd:PRK11231 81 LPQHHLTPEGiTVRELVAYGRSPWLSlwgrlsaeDNARVNQA--------ME--QTRINHLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 484 RALLRNPQFLLLDEATASLD----SESEKLVQEsLETvmKERTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLA 558
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDinhqVELMRLMRE-LNT--QGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
|
250
....*....|....
gi 1265182468 559 SHsfyrrLVEQQFQ 572
Cdd:PRK11231 228 PG-----LLRTVFD 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
344-530 |
7.42e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.01 E-value: 7.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 344 YEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYE--PS---SGRIFLDGTD-----SQNVNLRswRHLFSYV 413
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNiysprTDTVDLR--KEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 414 QQDSPiLAGTIRENLIYGL------ERHVTDEEIEEAAKLAnahhfiqSFEAQYETMIGERGINLSGGQRQRIAIARALL 487
Cdd:PRK14239 93 QQPNP-FPMSIYENVVYGLrlkgikDKQVLDEAVEKSLKGA-------SIWDEVKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1265182468 488 RNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRL 530
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
335-528 |
1.58e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.16 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDS-----------QNVNL 403
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegpgaergvvfQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 404 RSWRhlfsyvqqdspilagTIRENLIYGLE-RHVTDEEIEEAAKLANAHHFIQSFEAQYetmIGErginLSGGQRQRIAI 482
Cdd:PRK11248 82 LPWR---------------NVQDNVAFGLQlAGVEKMQRLEIAHQMLKKVGLEGAEKRY---IWQ----LSGGQRQRVGI 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1265182468 483 ARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKE--RTSLVIAH 528
Cdd:PRK11248 140 ARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITH 187
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
340-559 |
1.75e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.00 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 340 VAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPI 419
Cdd:PRK09536 9 LSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 420 -LAGTIRENLIYGLERHVT-----DEEIEEAAKLANAHHFIQSFEAQYETmigergiNLSGGQRQRIAIARALLRNPQFL 493
Cdd:PRK09536 89 sFEFDVRQVVEMGRTPHRSrfdtwTETDRAAVERAMERTGVAQFADRPVT-------SLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 494 LLDEATASLDSESEKLVQESLETVMKE-RTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLAS 559
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTA 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
348-556 |
1.80e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.94 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 348 PVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsQNVNLRS----WRHLFSYVQQD-SPILAG 422
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSprdaQAAGIAIIHQElNLVPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 423 TIRENLIYGLE---RHVTD--EEIEEAAKLanahhfIQSFEAQY--ETMIGErginLSGGQRQRIAIARALLRNPQFLLL 495
Cdd:COG1129 95 SVAENIFLGREprrGGLIDwrAMRRRAREL------LARLGLDIdpDTPVGD----LSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 496 DEATASL-DSESEKLvqesLETV--MKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKEL 556
Cdd:COG1129 165 DEPTASLtEREVERL----FRIIrrLKAQgvAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
94-312 |
1.88e-23 |
|
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: 100.46 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 94 LRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMF 173
Cdd:cd18784 71 IRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 174 VLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVM 253
Cdd:cd18784 151 IVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTE 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265182468 254 TAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18784 231 LALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
350-568 |
2.45e-23 |
|
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: 103.61 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKST----VFSLIerfyePSSGRIFLDGTDSQNVNLRSWRHLFSYVQ---QD-----S 417
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSRRALRPLRRRMQvvfQDpfgslS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 418 PILagTIRENLIYGLERH---VTDEEIEEAAklanahhfIQSFEaqyetmigERGIN----------LSGGQRQRIAIAR 484
Cdd:COG4172 377 PRM--TVGQIIAEGLRVHgpgLSAAERRARV--------AEALE--------EVGLDpaarhrypheFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 485 ALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLStVINA--DQIVVIEEGQVTGSGTHKELLAS- 559
Cdd:COG4172 439 ALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDLA-VVRAlaHRVMVMKDGKVVEQGPTEQVFDAp 517
|
250
....*....|
gi 1265182468 560 -HSFYRRLVE 568
Cdd:COG4172 518 qHPYTRALLA 527
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
25-312 |
4.14e-23 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 99.50 E-value: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALIntgaSLSIPLVIKEVMEKIAIGVSPQ----LIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWN 100
Cdd:cd18588 8 LLASLFLQLF----ALVTPLFFQVIIDKVLVHRSLStldvLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 101 KLIKLPVSFYDQNRSGEMVSRITNDTTIvMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLA 180
Cdd:cd18588 84 HLLRLPLSYFESRQVGDTVARVRELESI-RQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 181 RKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAI 260
Cdd:cd18588 163 PILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAI 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 261 VGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18588 243 LWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
25-312 |
4.25e-23 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 99.47 E-value: 4.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINtgasLSIPLVIKEVMEKIAIGVSPQ----LIAGLLVLFAAQMVTSAVSLYLLAQvgqgvvkeLRHKV-- 98
Cdd:cd18569 8 VLAGLLLVIPG----LVIPVFSRIFIDDILVGGLPDwlrpLLLGMALTALLQGLLTWLQQYYLLR--------LETKLal 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 99 -------WnKLIKLPVSFYDQNRSGEMVSRI-TNDTtiVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIP 170
Cdd:cd18569 76 ssssrffW-HVLRLPVEFFSQRYAGDIASRVqSNDR--VANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 171 VMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKkevD-----SGLQSfqSLYLFGVKRAKIEAII 245
Cdd:cd18569 153 LNLLVLRLVSRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAES---DffsrwAGYQA--KVLNAQQELGRTNQLL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 246 TPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18569 228 GALPTLLSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
338-557 |
4.53e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 98.62 E-value: 4.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 338 DKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDsqnvnLRSW------RHLfS 411
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLD-----VATTpsrelaKRL-A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 412 YVQQDSPILAG-TIRENLIYGleRH--------VTDEE-IEEAAKLANahhfIQSFEAQYetmIGErginLSGGQRQRIA 481
Cdd:COG4604 79 ILRQENHINSRlTVRELVAFG--RFpyskgrltAEDREiIDEAIAYLD----LEDLADRY---LDE----LSGGQRQRAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 482 IARALLRNPQFLLLDEATASLDseseklVQESLEtVMKERTSLVIAHRLSTV-----IN-----ADQIVVIEEGQVTGSG 551
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLD------MKHSVQ-MMKLLRRLADELGKTVVivlhdINfascyADHIVAMKDGRVVAQG 218
|
....*.
gi 1265182468 552 THKELL 557
Cdd:COG4604 219 TPEEII 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
347-547 |
6.18e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.62 E-value: 6.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 347 KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsQNV-NLRSWR--HLFSYVQQDsPiLAGT 423
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG---KDVtKLPEYKraKYIGRVFQD-P-MMGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 424 -----IRENLI--------YGLERHVTDEEI----EEAAKLANahhfiqSFEAQYETMIGergiNLSGGQRQRIAIARAL 486
Cdd:COG1101 94 apsmtIEENLAlayrrgkrRGLRRGLTKKRRelfrELLATLGL------GLENRLDTKVG----LLSGGQRQALSLLMAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 487 LRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQV 547
Cdd:COG1101 164 LTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEQALDyGNRLIMMHEGRI 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
348-546 |
8.65e-23 |
|
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: 97.12 E-value: 8.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 348 PVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLD----------GTDSQNVNLRswRHLFSYVQQ-- 415
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqASPREILALR--RRTIGYVSQfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 416 ---------DspILAGTIRENliyGLERhvtDEEIEEAAKLanAHHFiqsfeaqyetMIGERGINL-----SGGQRQRIA 481
Cdd:COG4778 103 rviprvsalD--VVAEPLLER---GVDR---EEARARAREL--LARL----------NLPERLWDLppatfSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 482 IARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLV-IAHRLSTV-INADQIVVIEEGQ 546
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVReAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
335-562 |
8.86e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.14 E-value: 8.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYED-KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVN-LRSWRHLFSY 412
Cdd:PRK13644 2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 413 VQQ--DSPILAGTIRENLIYGLE---------RHVTDEEIEEAAKLANAHHFIQSfeaqyetmigerginLSGGQRQRIA 481
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPEnlclppieiRKRVDRALAEIGLEKYRHRSPKT---------------LSGGQGQCVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 482 IARALLRNPQFLLLDEATASLDSESEKLVQESLETVM-KERTSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASH 560
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
..
gi 1265182468 561 SF 562
Cdd:PRK13644 227 SL 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
349-565 |
1.14e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.41 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 349 VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDsqnVNLRSWRH-----------LFSYVqqds 417
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED---VTHRSIQQrdicmvfqsyaLFPHM---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 418 pilagTIRENLIYGLE-RHVTDEEIEEAAKLANAHHFIQSFEAQYETMIgerginlSGGQRQRIAIARALLRNPQFLLLD 496
Cdd:PRK11432 94 -----SLGENVGYGLKmLGVPKEERKQRVKEALELVDLAGFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 497 EATASLD-----SESEKL--VQESLETvmkerTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELlashsfYRR 565
Cdd:PRK11432 162 EPLSNLDanlrrSMREKIreLQQQFNI-----TSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQEL------YRQ 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
343-559 |
1.22e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.13 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 343 QYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRI-----FLDGTDS---QNVNLRSWRHLFSYVQ 414
Cdd:PRK11264 12 KFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSlsqQKGLIRQLRQHVGFVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QDSPILAG-TIRENLIYGlERHVTDEEIEEAAKLANAHhFIQSFEAQYETMIGERginLSGGQRQRIAIARALLRNPQFL 493
Cdd:PRK11264 92 QNFNLFPHrTVLENIIEG-PVIVKGEPKEEATARAREL-LAKVGLAGKETSYPRR---LSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265182468 494 LLDEATASLDSEsekLVQESLETVM----KERTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLAS 559
Cdd:PRK11264 167 LFDEPTSALDPE---LVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
340-560 |
1.42e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 99.13 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 340 VAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNvNLRSWRHLFSYVQQ-DSP 418
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQfDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 419 ILAGTIRENLI-YGLERHVTDEEIEEAakLANAHHFiqsfeAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDE 497
Cdd:PRK13536 126 DLEFTVRENLLvFGRYFGMSTREIEAV--IPSLLEF-----ARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 498 ATASLDSESEKLVQESLETVM-KERTSLVIAH------RLstvinADQIVVIEEGQVTGSGTHKELLASH 560
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
335-548 |
2.72e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.52 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLdgtdSQNVNLrswrhlfSYVQ 414
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL----GETVKI-------GYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QDSPILAG--TIRENLiygleRHVTDEEIEeaaklANAHHFIQSF----EAQYeTMIGergiNLSGGQRQRIAIARALLR 488
Cdd:COG0488 385 QHQEELDPdkTVLDEL-----RDGAPGGTE-----QEVRGYLGRFlfsgDDAF-KPVG----VLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 489 NPQFLLLDEATASLDSESEKLVQESLE----TVmkertsLVIAH-R--LSTVinADQIVVIEEGQVT 548
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEALDdfpgTV------LLVSHdRyfLDRV--ATRILEFEDGGVR 508
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
346-555 |
3.00e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.04 E-value: 3.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 346 DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTD--SQNVNLRSWRHLFSYVQQ--DSPILA 421
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIRKKVGLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 422 GTIRENLIYGLER-HVTDEEIEEAAKLAnahhfIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATA 500
Cdd:PRK13637 99 ETIEKDIAFGPINlGLSEEEIENRVKRA-----MNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 501 SLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKE 555
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
350-552 |
7.64e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 96.79 E-value: 7.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVN---LRSWRHLFSYVQQDSPILAG-TIR 425
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKARRQIGMIFQHFNLLSSrTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 426 ENLIYGLE-RHVTDEEIE-------EAAKLANAHHFIQSfeaqyetmigergiNLSGGQRQRIAIARALLRNPQFLLLDE 497
Cdd:PRK11153 101 DNVALPLElAGTPKAEIKarvtellELVGLSDKADRYPA--------------QLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 498 ATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGT 552
Cdd:PRK11153 167 ATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
63-319 |
8.62e-22 |
|
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: 96.37 E-value: 8.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 63 AGLLVLFA-AQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPVSFYDQ--NRSGEMVSRITNDTTIVMNLLSTEMID 139
Cdd:cd18578 55 ALMFLVLAiVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDpeNSTGALTSRLSTDASDVRGLVGDRLGL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 140 FVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKK 219
Cdd:cd18578 135 ILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDY 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 220 EVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAIVGFGAYRVSEGFITAGE-LVAFVLYLFQIMVpVGSLTRF 298
Cdd:cd18578 215 FLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQfFIVFMALIFGAQS-AGQAFSF 293
|
250 260
....*....|....*....|.
gi 1265182468 299 VTSFQQTKGASERIFDILAEK 319
Cdd:cd18578 294 APDIAKAKAAAARIFRLLDRK 314
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
342-571 |
9.59e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 94.90 E-value: 9.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 342 FQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGT--DSQNVNLRSwrHLFSYVQQDS-- 417
Cdd:COG4167 21 FRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHklEYGDYKYRC--KHIRMIFQDPnt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 418 ---PILagTIRENLIYGLeRHVTDEEIEEAAKLANA----------HHFIqsfeaqYETMigerginLSGGQRQRIAIAR 484
Cdd:COG4167 99 slnPRL--NIGQILEEPL-RLNTDLTAEEREERIFAtlrlvgllpeHANF------YPHM-------LSSGQKQRVALAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 485 ALLRNPQFLLLDEATASLD-SESEKLVQESLEtvMKERTSL---VIAHRLSTV--InADQIVVIEEGQVTGSGTHKELLA 558
Cdd:COG4167 163 ALILQPKIIIADEALAALDmSVRSQIINLMLE--LQEKLGIsyiYVSQHLGIVkhI-SDKVLVMHQGEVVEYGKTAEVFA 239
|
250
....*....|....*
gi 1265182468 559 S--HSFYRRLVEQQF 571
Cdd:COG4167 240 NpqHEVTKRLIESHF 254
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
345-557 |
1.01e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 94.36 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 345 EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLI---ERfYEPSSGRIFLDGTD--SQNVNLRSWRHLFSYVQQDSPI 419
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDilELSPDERARAGIFLAFQYPVEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 420 -----------LAGTIRENLIYGLErhvTDEEIEEAAKLAN-AHHFIqsfeaqyetmigERGIN--LSGGQRQRIAIARA 485
Cdd:COG0396 90 pgvsvsnflrtALNARRGEELSARE---FLKLLKEKMKELGlDEDFL------------DRYVNegFSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 486 LLRNPQFLLLDEATASLDSESEKLVQESLETVM-KERTSLVIAH--RLSTVINADQIVVIEEGQVTGSGThKELL 557
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG-KELA 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
343-560 |
1.09e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.56 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 343 QYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNlrswRHLFSYVQQDSpilaG 422
Cdd:COG4152 10 RFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEER----G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 423 -----TIRENLIY-----GLERHVTDEEIEEaaklanahhFIQSFEaqyetmIGERG---I-NLSGGQRQRIAIARALLR 488
Cdd:COG4152 82 lypkmKVGEQLVYlarlkGLSKAEAKRRADE---------WLERLG------LGDRAnkkVeELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 489 NPQFLLLDEATASLDSES-EKLVQESLEtvMKERTSLVI--AHRLSTV--InADQIVVIEEGQVTGSGTHKELLASH 560
Cdd:COG4152 147 DPELLILDEPFSGLDPVNvELLKDVIRE--LAAKGTTVIfsSHQMELVeeL-CDRIVIINKGRKVLSGSVDEIRRQF 220
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
25-312 |
1.35e-21 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 95.35 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQ----LIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWN 100
Cdd:cd18782 4 LIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLAtlyvIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 101 KLIKLPVSFYDQNRSGEMVSRItNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLA 180
Cdd:cd18782 84 HLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 181 RKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEvdsgLQSFQSLYLF----GVKRAKIEAIITPIISTVMTAV 256
Cdd:cd18782 163 PILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKA----RWRWQNRYARslgeGFKLTVLGTTSGSLSQFLNKLS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 257 MIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18782 239 SLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
342-569 |
2.02e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.42 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 342 FQYED-KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQD--SP 418
Cdd:PRK13647 12 FRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDpdDQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 419 ILAGTIRENLIYG-----LERHVTDEEIEEAAKLANAHHFIQsfEAQYetmigergiNLSGGQRQRIAIARALLRNPQFL 493
Cdd:PRK13647 92 VFSSTVWDDVAFGpvnmgLDKDEVERRVEEALKAVRMWDFRD--KPPY---------HLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 494 LLDEATASLDSESEKLVQESLETVMKERTSLVIA-HRLSTVIN-ADQIVVIEEGQVTGSGThKELLAShsfyRRLVEQ 569
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGD-KSLLTD----EDIVEQ 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
335-564 |
2.07e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.53 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYED-KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDG--TDSQNVNLRSWRHLFS 411
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 412 YVQQ--DSPILAGTIRENLIYG-LERHVTDEEIEEAAKLANAHHFIQSFEAQYETMigerginLSGGQRQRIAIARALLR 488
Cdd:PRK13636 86 MVFQdpDNQLFSASVYQDVSFGaVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 489 NPQFLLLDEATASLD----SESEKLVQESLETVmkERTSLVIAHRLSTV-INADQIVVIEEGQVTGSGTHKELLASHSFY 563
Cdd:PRK13636 159 EPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAEKEML 236
|
.
gi 1265182468 564 R 564
Cdd:PRK13636 237 R 237
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
334-553 |
2.10e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 93.54 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 334 SLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKST---VFSLIERfyePSSGRIFLDGTD---SQNVNLRSWR 407
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSllrVLNLLET---PDSGQLNIAGHQfdfSQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 408 HLFSYV----QQDS--PILagTIRENLI------YGLERhvtDEEIEEAAKLANahhfiqsfEAQYETMIGERGINLSGG 475
Cdd:COG4161 79 LLRQKVgmvfQQYNlwPHL--TVMENLIeapckvLGLSK---EQAREKAMKLLA--------RLRLTDKADRFPLHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 476 QRQRIAIARALLRNPQFLLLDEATASLDSESE----KLVQESLETvmkERTSLVIAHRLSTVIN-ADQIVVIEEGQVTGS 550
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITaqvvEIIRELSQT---GITQVIVTHEVEFARKvASQVVYMEKGRIIEQ 222
|
...
gi 1265182468 551 GTH 553
Cdd:COG4161 223 GDA 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
362-575 |
2.47e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 95.71 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 362 VTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGT---DS-QNVNLRSWRHLFSYVQQDSPILAG-TIRENLIYGLeRHV 436
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDARLFPHyKVRGNLRYGM-AKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 437 TDEEIEEAAKLANAHHFIQSFEaqyetmigergINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLET 516
Cdd:PRK11144 105 MVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 517 VMKERTS--LVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLASHSFYRRLVEQQfQTSL 575
Cdd:PRK11144 174 LAREINIpiLYVSHSLDEILRlADRVVVLEQGKVKAFGPLEEVWASSAMRPWLPKEE-QSSI 234
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
334-553 |
3.05e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.16 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 334 SLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKST---VFSLIERfyePSSGRIFLDGTD---SQNVNLRSWR 407
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLEM---PRSGTLNIAGNHfdfSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 408 HLFSYV----QQDS--PILagTIRENLI------YGLERhvtDEEIEEAAKLANAHH---FIQSFEAQyetmigerginL 472
Cdd:PRK11124 79 ELRRNVgmvfQQYNlwPHL--TVQQNLIeapcrvLGLSK---DQALARAEKLLERLRlkpYADRFPLH-----------L 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 473 SGGQRQRIAIARALLRNPQFLLLDEATASLDSESE----KLVQESLETVMkerTSLVIAHRLSTVIN-ADQIVVIEEGQV 547
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITaqivSIIRELAETGI---TQVIVTHEVEVARKtASRVVYMENGHI 219
|
....*.
gi 1265182468 548 TGSGTH 553
Cdd:PRK11124 220 VEQGDA 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
343-557 |
3.37e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.05 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 343 QYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFS----LIERFYEPS-SGRIFLDGTDSQNVNLRSWRHLFSYV-QQD 416
Cdd:PRK14247 12 SFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEARvSGEVYLDGQDIFKMDVIELRRRVQMVfQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 417 SPILAGTIRENLIYGLE-RHVTDEEIEEAAKLANAHHFIQSFEaQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLL 495
Cdd:PRK14247 92 NPIPNLSIFENVALGLKlNRLVKSKKELQERVRWALEKAQLWD-EVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 496 DEATASLDSESEKLVQESLETVMKERTSLVIAH------RLStvinaDQIVVIEEGQVTGSGTHKELL 557
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGPTREVF 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
332-559 |
3.63e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.49 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 332 VGSLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsQNVNLRSwRHLFS 411
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG---EPVPSRA-RHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 412 YV----QQDSPILAGTIRENLI-----YGLERHVTDEEIE---EAAKLanahhfiqsfEAQYETMIGErginLSGGQRQR 479
Cdd:PRK13537 81 RVgvvpQFDNLDPDFTVRENLLvfgryFGLSAAAARALVPpllEFAKL----------ENKADAKVGE----LSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 480 IAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVM-KERTSLVIAH------RLstvinADQIVVIEEGQVTGSGT 552
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGA 221
|
....*..
gi 1265182468 553 HKELLAS 559
Cdd:PRK13537 222 PHALIES 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
350-555 |
5.04e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 96.25 E-value: 5.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsQNVNLRSWR------------HlFSYVqqds 417
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSPRdaialgigmvhqH-FMLV---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 418 PILagTIRENLIYGLERHV-----TDEEIEEAAKLANAHHFiqsfEAQYETMIGErginLSGGQRQRIAIARALLRNPQF 492
Cdd:COG3845 93 PNL--TVAENIVLGLEPTKggrldRKAARARIRELSERYGL----DVDPDAKVED----LSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265182468 493 LLLDEATASL-DSESEKLvqesLETV--MKE--RTSLVIAHRLSTVI-NADQIVVIEEGQVTGSGTHKE 555
Cdd:COG3845 163 LILDEPTAVLtPQEADEL----FEILrrLAAegKSIIFITHKLREVMaIADRVTVLRRGKVVGTVDTAE 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
334-556 |
5.20e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.77 E-value: 5.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 334 SLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSwRHLFSYV 413
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-RKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 414 QQDSPILAGTIRENLIYGL------ER---HVTDEEIEEAAKLANAHHFIQSFEAQyetmigerginLSGGQRQRIAIAR 484
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLtvlprrERpnaAAIKAKVTQLLEMVQLAHLADRYPAQ-----------LSGGQKQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 485 ALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKEL 556
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
344-551 |
5.27e-21 |
|
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: 92.01 E-value: 5.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 344 YEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsqnvnLRSWRHLFSYVQQDSPILAGt 423
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-------LVPWKRRKKFLRRIGVVFGQ- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 424 iRENLI--------YGLERHVTDeeIEEAAKLANAHHFIQSFEAQYETMIGERgiNLSGGQRQRIAIARALLRNPQFLLL 495
Cdd:cd03267 103 -KTQLWwdlpvidsFYLLAAIYD--LPPARFKKRLDELSELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265182468 496 DEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSG 551
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
347-569 |
8.87e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.44 E-value: 8.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 347 KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQ---QDSP----- 418
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQmvfQDSIsavnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 419 --ILAGTIRENLiygleRHVTDeeIEEAAKLANAHHFIQSFEAQYETMiGERGINLSGGQRQRIAIARALLRNPQFLLLD 496
Cdd:PRK10419 105 rkTVREIIREPL-----RHLLS--LDKAERLARASEMLRAVDLDDSVL-DKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 497 EATASLDseseKLVQESLETVMK---ERTS---LVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLASHSFYRRLVEQ 569
Cdd:PRK10419 177 EAVSNLD----LVLQAGVIRLLKklqQQFGtacLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLTFSSPAGRVLQN 252
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
349-504 |
1.00e-20 |
|
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: 91.18 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 349 VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPS---SGRIFLDGtdsQNVNLRSWRHLFSYVQQDSPILAG-TI 424
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 425 RENLIYG----LERHVTD---EEIEEAAKLANAHHfiqsfeaqyeTMIGERGI-NLSGGQRQRIAIARALLRNPQFLLLD 496
Cdd:cd03234 99 RETLTYTailrLPRKSSDairKKRVEDVLLRDLAL----------TRIGGNLVkGISGGERRRVSIAVQLLWDPKVLILD 168
|
....*...
gi 1265182468 497 EATASLDS 504
Cdd:cd03234 169 EPTSGLDS 176
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
25-312 |
1.74e-20 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 91.88 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALIntgaSLSIPLVIKEVMEKI----AIGVSPQLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWN 100
Cdd:cd18566 8 LLASLFINIL----ALATPLFILQVYDRVipneSIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 101 KLIKLPVSFYDQNRSGEMVSRItNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLA 180
Cdd:cd18566 84 HLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 181 RKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSgLQSFQSLYLFGV-KRAKIEAIITPIISTVMTAVMIA 259
Cdd:cd18566 163 PILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRR-YERLQANAAYAGfKVAKINAVAQTLGQLFSQVSMVA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 260 IVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18566 242 VVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
350-545 |
2.30e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 90.22 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDS-----------QNVNLRSWRhlfsyvqqdsp 418
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItepgpdrmvvfQNYSLLPWL----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 419 ilagTIRENLIYGLERHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGErginLSGGQRQRIAIARALLRNPQFLLLDEA 498
Cdd:TIGR01184 70 ----TVRENIALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1265182468 499 TASLDSESEKLVQESLETVMKER--TSLVIAHRL-STVINADQIVVIEEG 545
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
28-283 |
2.41e-20 |
|
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: 91.45 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 28 SFILALINtgasLSIPLVIKEVMEKIAIGVSPQLIAG----------LLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHK 97
Cdd:cd18574 5 ALAAALVN----IQIPLLLGDLVNVISRSLKETNGDFiedlkkpalkLLGLYLLQSLLTFAYISLLSVVGERVAARLRND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 98 VWNKLIKLPVSFYDQNRSGEMVSRITNDttiVMNLLSTemidF-------VKNILSIIVAIVILFTLDVPMTLILLAVIP 170
Cdd:cd18574 81 LFSSLLRQDIAFFDTHRTGELVNRLTAD---VQEFKSS----FkqcvsqgLRSVTQTVGCVVSLYLISPKLTLLLLVIVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 171 VMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDsglqsfqsLYLFGVKRAKIEA------- 243
Cdd:cd18574 154 VVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELE--------LYEEEVEKAAKLNeklglgi 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1265182468 244 -IITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVL 283
Cdd:cd18574 226 gIFQGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFLV 266
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
344-556 |
2.67e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 92.98 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 344 YEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVN--LRSWRHLFsyvQQDSPILA 421
Cdd:PRK11607 29 FDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPpyQRPINMMF---QSYALFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 422 GTIRENLIYGLE-----RHVTDEEIEEAAKLANAHHFIQSFEAQyetmigerginLSGGQRQRIAIARALLRNPQFLLLD 496
Cdd:PRK11607 106 MTVEQNIAFGLKqdklpKAEIASRVNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 497 EATASLDSESEKLVQesLETV-MKER---TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKEL 556
Cdd:PRK11607 175 EPMGALDKKLRDRMQ--LEVVdILERvgvTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEI 237
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
353-556 |
2.78e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.43 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 353 VSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTD-----SQNVN----LRSWRH--LFSYVqqdspila 421
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpGHQIArmgvVRTFQHvrLFREM-------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 422 gTIRENLIYGLERHVTDEEI-----------EEAAKLANAHHFIQSfeaqyetmIGERGI------NLSGGQRQRIAIAR 484
Cdd:PRK11300 96 -TVIENLLVAQHQQLKTGLFsgllktpafrrAESEALDRAATWLER--------VGLLEHanrqagNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 485 ALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKEL 556
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
346-565 |
2.86e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.02 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 346 DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQ--DSPILAGT 423
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpDDQIFSPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 424 IRENLIY-----GLERHVTDEEIEEAAKLANAHHFIQSFEAqyetmigergiNLSGGQRQRIAIARALLRNPQFLLLDEA 498
Cdd:PRK13652 96 VEQDIAFgpinlGLDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 499 TASLDSESEKLVQESLETVMKERTSLVI--AHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLASHSFYRR 565
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDLLAR 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
344-542 |
5.18e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.06 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 344 YEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSqnvnlrswrhlFSYVQQDSPI---L 420
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGAR-----------VAYVPQRSEVpdsL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 421 AGTIRENLIYGLERH-------------VTDEEIEE--AAKLANAHhfiqsfeaqyetmIGErginLSGGQRQRIAIARA 485
Cdd:NF040873 71 PLTVRDLVAMGRWARrglwrrltrddraAVDDALERvgLADLAGRQ-------------LGE----LSGGQRQRALLAQG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 486 LLRNPQFLLLDEATASLDSESEKLVQESL-ETVMKERTSLVIAHRLSTVINADQIVVI 542
Cdd:NF040873 134 LAQEADLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
335-547 |
5.71e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.74 E-value: 5.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIfLDGTDSQNVNLRSWRHLFsyvq 414
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTRLMF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QDSPILA-GTIRENLIYGLERHVTDEEIE--EAAKLANahhfiqsfeaqyetMIGERGINLSGGQRQRIAIARALLRNPQ 491
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLGLKGQWRDAALQalAAVGLAD--------------RANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265182468 492 FLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLS-TVINADQIVVIEEGQV 547
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
334-556 |
6.95e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.80 E-value: 6.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 334 SLRFDKVAFQYE-----DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGT----DSQNVNLR 404
Cdd:PRK13649 2 GINLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitsTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 405 SWRHLFSYVQQ--DSPILAGTIRENLIYGLERH-VTDEEIEEAAKLANAHHFIQsfeaqyETMIGERGINLSGGQRQRIA 481
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNFgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 482 IARALLRNPQFLLLDEATASLDSESEKlvqeSLETVMKE-----RTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKE 555
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRK----ELMTLFKKlhqsgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKD 231
|
.
gi 1265182468 556 L 556
Cdd:PRK13649 232 I 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
335-559 |
8.39e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.77 E-value: 8.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYE---DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFS 411
Cdd:PRK13642 5 LEVENLVFKYEkesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 412 YVQQ--DSPILAGTIRENLIYGLE-----RHVTDEEIEEAAKLANAHHFIQSFEAQyetmigerginLSGGQRQRIAIAR 484
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFGMEnqgipREEMIKRVDEALLAVNMLDFKTREPAR-----------LSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 485 ALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLAS 559
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFAT 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
332-572 |
9.00e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.80 E-value: 9.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 332 VGSLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRS-WRHLF 410
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 411 SYVQQDSPILAG-TIRENLIYGLE--RHVTDEEIEEAAKlanahHFIQSFEAQYetMIGERGINLSGGQRQRIAIARALL 487
Cdd:PRK10895 81 GYLPQEASIFRRlSVYDNLMAVLQirDDLSAEQREDRAN-----ELMEEFHIEH--LRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 488 RNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIA-HRLSTVINA-DQIVVIEEGQVTGSGTHKELLASHSFYRR 565
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVRETLAVcERAYIVSQGHLIAHGTPTEILQDEHVKRV 233
|
....*..
gi 1265182468 566 LVEQQFQ 572
Cdd:PRK10895 234 YLGEDFR 240
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
335-546 |
9.03e-20 |
|
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: 85.96 E-value: 9.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSqnvnlrswrhlFSYVQ 414
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK-----------IGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QdspilagtirenliyglerhvtdeeieeaaklanahhfiqsfeaqyetmigerginLSGGQRQRIAIARALLRNPQFLL 494
Cdd:cd03221 70 Q--------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 495 LDEATASLDSESeklvQESLETVMKE--RTSLVIAH-R--LSTVinADQIVVIEEGQ 546
Cdd:cd03221 94 LDEPTNHLDLES----IEALEEALKEypGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
347-553 |
1.33e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.42 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 347 KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIErFYEPS----SGRIFLDGTdsqNVNLRSWRHLFSYVQQDSpILAG 422
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGM---PIDAKEMRAISAYVQQDD-LFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 423 --TIRENLIYG----LERHVTD-------EEIEEAAKLANAHHfiqsfeaqyeTMIGERGI--NLSGGQRQRIAIARALL 487
Cdd:TIGR00955 113 tlTVREHLMFQahlrMPRRVTKkekrervDEVLQALGLRKCAN----------TRIGVPGRvkGLSGGERKRLAFASELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265182468 488 RNPQFLLLDEATASLDSES-EKLVQESLETVMKERTSLVIAHRLSTVI--NADQIVVIEEGQV--TGSGTH 553
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSELfeLFDKIILMAEGRVayLGSPDQ 253
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
334-559 |
1.74e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 88.31 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 334 SLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYV 413
Cdd:PRK10575 11 TFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 414 QQDSPILAG-TIRENLIYG-------LERH-VTD-EEIEEAAKLAN----AHHFIQSfeaqyetmigerginLSGGQRQR 479
Cdd:PRK10575 91 PQQLPAAEGmTVRELVAIGrypwhgaLGRFgAADrEKVEEAISLVGlkplAHRLVDS---------------LSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 480 IAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIA--HRLSTVIN-ADQIVVIEEGQVTGSGTHKEL 556
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINMAARyCDYLVALRGGEMIAQGTPAEL 235
|
...
gi 1265182468 557 LAS 559
Cdd:PRK10575 236 MRG 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
347-568 |
2.43e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 347 KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYePSSGRIFLDGTDSQNVNLRS---WRHLFSYVQQDsPILAGT 423
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQD-PNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 424 IRENLIyglerhvtdEEIEEAAKLANAHHFIQSFEAQYETMIGERGIN----------LSGGQRQRIAIARALLRNPQFL 493
Cdd:PRK15134 377 PRLNVL---------QIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDpetrhrypaeFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 494 LLDEATASLDseseKLVQESLETVMKertSLVIAHRLSTV-INAD---------QIVVIEEGQVTGSGTHKELLA--SHS 561
Cdd:PRK15134 448 ILDEPTSSLD----KTVQAQILALLK---SLQQKHQLAYLfISHDlhvvralchQVIVLRQGEVVEQGDCERVFAapQQE 520
|
....*..
gi 1265182468 562 FYRRLVE 568
Cdd:PRK15134 521 YTRQLLA 527
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
335-547 |
2.88e-19 |
|
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: 86.57 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNvnlrSWRHLFSYVQ 414
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QDSPI-LAGTIRENLIY-----GLERHVTDEEIEE-AAKLANAHHFIQSFEaqyetmigergiNLSGGQRQRIAIARALL 487
Cdd:cd03269 77 EERGLyPKMKVIDQLVYlaqlkGLKKEEARRRIDEwLERLELSEYANKRVE------------ELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 488 RNPQFLLLDEATASLDSESEKLVQESL-ETVMKERTSLVIAHRLSTVIN-ADQIVVIEEGQV 547
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
335-558 |
3.28e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 88.15 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYE-----DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGT----DSQNVNLRS 405
Cdd:PRK13634 3 ITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 406 WRHLFSYVQQ--DSPILAGTIRENLIYG-LERHVTDEEIEEAAKlanahhfiqsfeaqyeTMIGERGIN----------L 472
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGpMNFGVSEEDAKQKAR----------------EMIELVGLPeellarspfeL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 473 SGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTG 549
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFL 226
|
....*....
gi 1265182468 550 SGTHKELLA 558
Cdd:PRK13634 227 QGTPREIFA 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
334-558 |
3.29e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.96 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 334 SLRFDKVAFQYE-----DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDG----TDSQNVNLR 404
Cdd:PRK13641 2 SIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 405 SWRHLFSYVQQ--DSPILAGTIRENLIYG-LERHVTDEEIEEAAKlanahHFIQSFEAQyETMIGERGINLSGGQRQRIA 481
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGpKNFGFSEDEAKEKAL-----KWLKKVGLS-EDLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265182468 482 IARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKE-RTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLA 558
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFS 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
332-533 |
3.51e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 87.40 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 332 VGSLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSS-----GRI--FLDGTDSQNVNLR 404
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVefFNQNIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 405 SWRHLFSYVQQDSPILAGTIRENLIYGLE------RHVTDEEIEEAAKLANAHHFIQSfeaqyetMIGERGINLSGGQRQ 478
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrpKLEIDDIVESALKDADLWDEIKH-------KIHKSALDLSGGQQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 479 RIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVM--KERTSLVIAHRLSTV 533
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQV 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
350-557 |
3.51e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 89.71 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHL----FSYVQQDSPILAG-TI 424
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 425 RENLIYGLE-RHVTDEEIEEAAKLANAHHFIQSFEAQYETmigergiNLSGGQRQRIAIARALLRNPQFLLLDEATASLD 503
Cdd:PRK10070 124 LDNTAFGMElAGINAEERREKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 504 SESEKLVQESLETVM--KERTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELL 557
Cdd:PRK10070 197 PLIRTEMQDELVKLQakHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
342-558 |
4.12e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.37 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 342 FQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGT--DSQNVNLRSWRHLFSYVQQD--S 417
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDpeQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 418 PILAGTIRENLIYGLER-HVTDEEI----EEAAKLANAHHF----IQSfeaqyetmigerginLSGGQRQRIAIARALLR 488
Cdd:PRK13638 89 QIFYTDIDSDIAFSLRNlGVPEAEItrrvDEALTLVDAQHFrhqpIQC---------------LSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 489 NPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVI-AHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLA 558
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
342-529 |
7.87e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 85.00 E-value: 7.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 342 FQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsQNV--NLRSWRHLFSYVQQDSPI 419
Cdd:PRK13540 9 FDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER---QSIkkDLCTYQKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 420 LAG-TIRENLIYGLERHVTDEEIEEAAKLANAHHFIqsfeaQYETMIgerginLSGGQRQRIAIARALLRNPQFLLLDEA 498
Cdd:PRK13540 86 NPYlTLRENCLYDIHFSPGAVGITELCRLFSLEHLI-----DYPCGL------LSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 1265182468 499 TASLDseseklvQESLETVMkertSLVIAHR 529
Cdd:PRK13540 155 LVALD-------ELSLLTII----TKIQEHR 174
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
346-527 |
1.14e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.54 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 346 DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHlfsYV-QQDS--PILag 422
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH---YLgHRNAmkPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 423 TIRENL-----IYGLErhvtDEEIEEAAKLANAHHfIQSFEAQYetmigerginLSGGQRQRIAIARALLRNPQFLLLDE 497
Cdd:PRK13539 89 TVAENLefwaaFLGGE----ELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190
....*....|....*....|....*....|
gi 1265182468 498 ATASLDSESEKLVQESLETVMkERTSLVIA 527
Cdd:PRK13539 154 PTAALDAAAVALFAELIRAHL-AQGGIVIA 182
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
335-558 |
2.60e-18 |
|
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: 88.32 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERF--YEPSSGRIF----------------LDGT 396
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 397 ---------DSQNVNL--------RSWRHLFSYVQQDSPILAG--TIRENLIYGLER--HVTDEEIEEAAKLANahhfiq 455
Cdd:TIGR03269 81 pcpvcggtlEPEEVDFwnlsdklrRRIRKRIAIMLQRTFALYGddTVLDNVLEALEEigYEGKEAVGRAVDLIE------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 456 sfEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESL-ETVMKERTSLVIAHRLSTVI 534
Cdd:TIGR03269 155 --MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeEAVKASGISMVLTSHWPEVI 232
|
250 260
....*....|....*....|....*.
gi 1265182468 535 N--ADQIVVIEEGQVTGSGTHKELLA 558
Cdd:TIGR03269 233 EdlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
350-557 |
3.74e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.12 E-value: 3.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYePSSGRIFLDGTDSQNVNLRSWRHLFSYV-QQDSPILAGTIRENL 428
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLsQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 429 IYGLERHVTDEEIEEA-AKLANAHHfiqsFEAQYETMIGergiNLSGGQRQRIAIARALLR-----NP--QFLLLDEATA 500
Cdd:COG4138 91 ALHQPAGASSEAVEQLlAQLAEALG----LEDKLSRPLT----QLSGGEWQRVRLAAVLLQvwptiNPegQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 501 SLDsesekLVQES-LETVMKE-----RTSLVIAHRLS-TVINADQIVVIEEGQVTGSGTHKELL 557
Cdd:COG4138 163 SLD-----VAQQAaLDRLLRElcqqgITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
25-284 |
4.06e-18 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 85.21 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIK 104
Cdd:cd18567 8 LLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 105 LPVSFYDQNRSGEMVSRItNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKIH 184
Cdd:cd18567 88 LPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 185 KISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAIVGFG 264
Cdd:cd18567 167 RATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLG 246
|
250 260
....*....|....*....|
gi 1265182468 265 AYRVSEGFITAGELVAFVLY 284
Cdd:cd18567 247 ALLVLDGEFTVGMLFAFLAY 266
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
328-559 |
5.71e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.88 E-value: 5.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 328 VLEQVGSLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWR 407
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 408 HLFSYVQQDSPILAG-TIRENLIYGLERH---VTDEEIEEAAKLANAhhfiqsFEAQYETMIGERGIN-LSGGQRQRIAI 482
Cdd:PRK10253 81 RRIGLLAQNATTPGDiTVQELVARGRYPHqplFTRWRKEDEEAVTKA------MQATGITHLADQSVDtLSGGQRQRAWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 483 ARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLAS 559
Cdd:PRK10253 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTA 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
341-551 |
8.59e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 82.58 E-value: 8.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 341 AFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSqnvnlrswrhlfsyvqqdSPIL 420
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS------------------SLLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 421 AG-------TIREN-----LIYGLerhvTDEEIEEAAklanahHFIQSFeAQYETMIGERGINLSGGQRQRIAIARALLR 488
Cdd:cd03220 91 LGggfnpelTGRENiylngRLLGL----SRKEIDEKI------DEIIEF-SELGDFIDLPVKTYSSGMKARLAFAIATAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 489 NPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIA-HRLSTVIN-ADQIVVIEEGQVTGSG 551
Cdd:cd03220 160 EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
335-530 |
8.67e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 83.29 E-value: 8.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVF-------SLIERFYepSSGRIFLDGTD--SQNVNLRS 405
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFR--VEGKVTFHGKNlyAPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 406 WRHLFSYVQQDSPILAGTIRENLIYGLE----RHVTDEEIEEAAKLAnahhfiqSFEAQYETMIGERGINLSGGQRQRIA 481
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIAYGARingyKGDMDELVERSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLC 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1265182468 482 IARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRL 530
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-559 |
1.36e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.79 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 324 ENGEVLEQVgsLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGT------D 397
Cdd:PRK14246 2 EAGKSAEDV--FNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 398 SQNVNLRSWRHLFSYV-QQDSPILAGTIRENLIYGLERHVTDEEIEEAAKLANAHHFIQSFEAQYETMiGERGINLSGGQ 476
Cdd:PRK14246 80 IFQIDAIKLRKEVGMVfQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRL-NSPASQLSGGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 477 RQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKE 555
Cdd:PRK14246 159 QQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNE 238
|
....
gi 1265182468 556 LLAS 559
Cdd:PRK14246 239 IFTS 242
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
346-567 |
1.86e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.44 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 346 DKPVLQEVSFSAKKGEVTAFVGPSGAGKS----TVFSLIERFYEPSSGRIFLDGTDSQNVNLRSwRHLFSYVQQD----S 417
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRG-RKIATIMQNPrsafN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 418 PI--LAGTIRENLIyGLERHVTDE---EIEEAAKLANAHHFIQSFEAQyetmigerginLSGGQRQRIAIARALLRNPQF 492
Cdd:PRK10418 94 PLhtMHTHARETCL-ALGKPADDAtltAALEAVGLENAARVLKLYPFE-----------MSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 493 LLLDEATASLDSESEKLVQESLETVMKERTS--LVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLAS--HSFYRRLV 567
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNApkHAVTRSLV 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
343-571 |
2.00e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.32 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 343 QYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDG--------TDSQ-----NVNLRSWRHL 409
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdKDGQlkvadKNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 410 FSYVQQDSPILAG-TIRENL------IYGLERHvtdEEIEEAAKLANAHHFIQSFEAQYEtmigergINLSGGQRQRIAI 482
Cdd:PRK10619 94 LTMVFQHFNLWSHmTVLENVmeapiqVLGLSKQ---EARERAVKYLAKVGIDERAQGKYP-------VHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 483 ARALLRNPQFLLLDEATASLDSEsekLVQESLETVMK----ERTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELL 557
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPE---LVGEVLRIMQQlaeeGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
250
....*....|....
gi 1265182468 558 ASHSFYRRlveQQF 571
Cdd:PRK10619 241 GNPQSPRL---QQF 251
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
345-557 |
2.48e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 80.65 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 345 EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERF--YEPSSGRIFLDGTDSQN--VNLRSWRHLFSYVQqdSPIl 420
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDlpPEERARLGIFLAFQ--YPP- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 421 agtirenliyglerhvtdeEIEEaAKLANahhFIqsfeaqyetmigeRGIN--LSGGQRQRIAIARALLRNPQFLLLDEA 498
Cdd:cd03217 88 -------------------EIPG-VKNAD---FL-------------RYVNegFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 499 TASLDSESEKLVQESLETVMKERTS-LVIAH--RLSTVINADQIVVIEEGQVTGSGThKELL 557
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREEGKSvLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELA 192
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
334-552 |
2.52e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.74 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 334 SLRFDKVAFQYEDK-PVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsQNVNLRSWR----- 407
Cdd:PRK11650 3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG---RVVNELEPAdrdia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 408 ----------HLfsyvqqdspilagTIRENLIYGL-----ERHVTDEEIEEAAKLANAHHFIQSFEAQyetmigerginL 472
Cdd:PRK11650 80 mvfqnyalypHM-------------SVRENMAYGLkirgmPKAEIEERVAEAARILELEPLLDRKPRE-----------L 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 473 SGGQRQRIAIARALLRNPQFLLLDEATASLDS--------ESEKLvQESLETvmkerTSLVIAH-RLSTVINADQIVVIE 543
Cdd:PRK11650 136 SGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAklrvqmrlEIQRL-HRRLKT-----TSLYVTHdQVEAMTLADRVVVMN 209
|
....*....
gi 1265182468 544 EGQVTGSGT 552
Cdd:PRK11650 210 GGVAEQIGT 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
349-548 |
3.79e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.02 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 349 VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDG------TDSQNVNLRS--------WRHL---FS 411
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklSSAAKAELRNqklgfiyqFHHLlpdFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 412 YVQQDS-PILAGTIRENliyglERHVTDEEIEEAAKLAN-AHHfiqsfeaqyetmigeRGINLSGGQRQRIAIARALLRN 489
Cdd:PRK11629 104 ALENVAmPLLIGKKKPA-----EINSRALEMLAAVGLEHrANH---------------RPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265182468 490 PQFLLLDEATASLDSESEKLVQESL-ETVMKERTS-LVIAHRLSTVINADQIVVIEEGQVT 548
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLgELNRLQGTAfLVVTHDLQLAKRMSRQLEMRDGRLT 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
335-574 |
7.26e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.83 E-value: 7.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVF----SLIERFYEPSSgRIFLDGTDSQNV-----NLRS 405
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGS-HIELLGRTVQREgrlarDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 406 WRHLFSYV-QQDSPILAGTIRENLIYG----------LERHVTDEEIEEA----AKLANAHhfiqsFEAQyetmigeRGI 470
Cdd:PRK09984 84 SRANTGYIfQQFNLVNRLSVLENVLIGalgstpfwrtCFSWFTREQKQRAlqalTRVGMVH-----FAHQ-------RVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 471 NLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQV 547
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRyCERIVALRQGHV 231
|
250 260 270
....*....|....*....|....*....|.
gi 1265182468 548 --TGSGTHKELLASHSFYRRL--VEQQFQTS 574
Cdd:PRK09984 232 fyDGSSQQFDNERFDHLYRSInrVEENAKAA 262
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
344-570 |
9.70e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 79.74 E-value: 9.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 344 YEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTdsqnVnlrswrhlfsyvqqdSPIL--- 420
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----V---------------SALLelg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 421 AG-----TIREN-----LIYGLERHVTDEEIEEAAKLANAHHFIqsfeaqyETMIGergiNLSGGQRQRIAIARALLRNP 490
Cdd:COG1134 97 AGfhpelTGRENiylngRLLGLSRKEIDEKFDEIVEFAELGDFI-------DQPVK----TYSSGMRARLAFAVATAVDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 491 QFLLLDEATASLDSESEKLVQESLETVMKERTSLVIA-HRLSTVIN-ADQIVVIEEGQVTGSGTHKELLAshsFYRRLVE 568
Cdd:COG1134 166 DILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVsHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIA---AYEALLA 242
|
..
gi 1265182468 569 QQ 570
Cdd:COG1134 243 GR 244
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
335-529 |
1.08e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 77.58 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYED-KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIfldgtdsqnvNLRSWRHLFsYV 413
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------GMPEGEDLL-FL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 414 QQDSPILAGTIRENLIYGLERhvtdeeieeaaklanahhfiqsfeaqyetmigergiNLSGGQRQRIAIARALLRNPQFL 493
Cdd:cd03223 70 PQRPYLPLGTLREQLIYPWDD------------------------------------VLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*..
gi 1265182468 494 LLDEATASLDSESEKLVqesLETVMKERTSLV-IAHR 529
Cdd:cd03223 114 FLDEATSALDEESEDRL---YQLLKELGITVIsVGHR 147
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
27-312 |
1.10e-16 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 80.61 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 27 ISFILALINTGASLSIPLVIKEVMEKIAIGVSPQLIAGLL---VLFAAQMVTSAV---SLYLLAQVGQGVVKELRHKVWN 100
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLlalALFLVSLLQSLLlhqYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 101 KLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTeMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLA 180
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLF-LHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 181 RKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEK-----------KEVDsglqsfqslYLFgvKRAKIEAIItpII 249
Cdd:cd18579 160 KLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKpflkrieelrkKELK---------ALR--KFGYLRALN--SF 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 250 STVMTAVMIAIVGFGAYRVSEGFITAGelVAFV-LYLFQIM-VPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18579 227 LFFSTPVLVSLATFATYVLLGNPLTAA--KVFTaLSLFNLLrFPLLMLPQAISSLIEALVSLKRI 289
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
331-546 |
1.17e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 331 QVGSLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsQNVNLRSWRhlf 410
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG---QEMRFASTT--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 411 syvqqdSPILAG--------------TIRENLIYGlerhvtdeeieeaaKLANAHHFIQSFEAQYETM--IGERGIN--- 471
Cdd:PRK11288 75 ------AALAAGvaiiyqelhlvpemTVAENLYLG--------------QLPHKGGIVNRRLLNYEAReqLEHLGVDidp 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 472 ------LSGGQRQRIAIARALLRNPQFLLLDEATASLDS-ESEKLVQESLETVMKERTSLVIAHRLSTVIN-ADQIVVIE 543
Cdd:PRK11288 135 dtplkyLSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIFAlCDAITVFK 214
|
...
gi 1265182468 544 EGQ 546
Cdd:PRK11288 215 DGR 217
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
353-558 |
2.37e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 80.39 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 353 VSFSAKKGEVTAFVGPSGAGKSTV---FSLIErfyEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQ---QD-----SPilA 421
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLarlLTMIE---TPTGGELYYQGQDLLKADPEAQKLLRQKIQivfQNpygslNP--R 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 422 GTIRENLIYGLERHVTDEEIEEAAKLA--------NAHHFiqsfeAQYETMigerginLSGGQRQRIAIARALLRNPQFL 493
Cdd:PRK11308 109 KKVGQILEEPLLINTSLSAAERREKALammakvglRPEHY-----DRYPHM-------FSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 494 LLDEATASLDSESEKLV-------QESLETvmkerTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLA 558
Cdd:PRK11308 177 VADEPVSALDVSVQAQVlnlmmdlQQELGL-----SYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
349-563 |
4.39e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.51 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 349 VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRI------------FLDGTDSQNV----NLRSWRHLFSY 412
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknNHELITNPYSkkikNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 413 VQQ--DSPILAGTIRENLIYG---LERHVtdeeiEEAAKLAnahhfiqsfeAQYETMIG------ERG-INLSGGQRQRI 480
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIMFGpvaLGVKK-----SEAKKLA----------KFYLNKMGlddsylERSpFGLSGGQKRRV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 481 AIARALLRNPQFLLLDEATASLDSESEK-LVQESLETVMKERTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLA 558
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFT 265
|
....*
gi 1265182468 559 SHSFY 563
Cdd:PRK13631 266 DQHII 270
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
335-564 |
4.65e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.01 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYE-DKP----VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRI----FLDGTDSQNVNLRS 405
Cdd:PRK13643 2 IKFEKVNYTYQpNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 406 WRHLFSYVQQ--DSPILAGTIRENLIYGLERHVTDEEieEAAKLAnahhfiqsfeAQYETMIG-------ERGINLSGGQ 476
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKE--KAEKIA----------AEKLEMVGladefweKSPFELSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 477 RQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKE-RTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHK 554
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPS 229
|
250
....*....|
gi 1265182468 555 ELLASHSFYR 564
Cdd:PRK13643 230 DVFQEVDFLK 239
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
345-555 |
5.82e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.31 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 345 EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVN------LRswRHLFSYVQQDsp 418
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalaqLR--REHFGFIFQR-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 419 ilagtirenliYGLERHVTDEE----------IEEAAKLANAHHFIQSFeaQYETMIGERGINLSGGQRQRIAIARALLR 488
Cdd:PRK10535 95 -----------YHLLSHLTAAQnvevpavyagLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 489 NPQFLLLDEATASLDSESEKLVQESLETvMKER--TSLVIAHRLSTVINADQIVVIEEGQ-VTGSGTHKE 555
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQ-LRDRghTVIIVTHDPQVAAQAERVIEIRDGEiVRNPPAQEK 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
350-575 |
6.98e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.91 E-value: 6.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQ--NVNLRSWRhlFSYVQQDsPILAGTIREN 427
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQR--IRMIFQD-PSTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 428 LIYGLE---RHVTDEEIEEAAKLANAH----HFIQSFEAQYETMigerginLSGGQRQRIAIARALLRNPQFLLLDEATA 500
Cdd:PRK15112 106 ISQILDfplRLNTDLEPEQREKQIIETlrqvGLLPDHASYYPHM-------LAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 501 SLD-SESEKLVQESLETVMKERTSL--VIAHRLSTVINADQIVVIEEGQVTGSGTHKELLAS--HSFYRRLVEQQFQTSL 575
Cdd:PRK15112 179 SLDmSMRSQLINLMLELQEKQGISYiyVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASplHELTKRLIAGHFGEAL 258
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
335-561 |
8.50e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 77.23 E-value: 8.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTD-SQNVNLRSWRHLFSYV 413
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDiTDWQTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 414 QQDSPILAG-TIRENLIYG---LERHVTDEEIEEAAKLanahhfiqsFEAQYETMIgERGINLSGGQRQRIAIARALLRN 489
Cdd:PRK11614 86 PEGRRVFSRmTVEENLAMGgffAERDQFQERIKWVYEL---------FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 490 PQFLLLDEATASLdseSEKLVQESLETVMKERTS-----LVIAHRLSTVINADQIVVIEEGQVTGSGTHKELLASHS 561
Cdd:PRK11614 156 PRLLLLDEPSLGL---APIIIQQIFDTIEQLREQgmtifLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
334-559 |
1.01e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.90 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 334 SLRFDKVAFQYE-----DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDG----TDSQNVNLR 404
Cdd:PRK13646 2 TIRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 405 SWRHLFSYVQQ--DSPILAGTIRENLIYGLERHVTDeeIEEAAklANAHHFIQSFEAQYETMiGERGINLSGGQRQRIAI 482
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN--LDEVK--NYAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 483 ARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKE--RTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLAS 559
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
344-556 |
1.15e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.92 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 344 YEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNV--NLRSWRHLF-SYVQQdsPIL 420
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVppAERGVGMVFqSYALY--PHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 421 agTIRENLIYGL-----ERHVTDEEIEEAAKLANAHHFIQsfeaqyetmigERGINLSGGQRQRIAIARALLRNPQFLLL 495
Cdd:PRK11000 91 --SVAENMSFGLklagaKKEEINQRVNQVAEVLQLAHLLD-----------RKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 496 DEATASLDS--------ESEKLvQESLetvmkERTSLVIAH-RLSTVINADQIVVIEEGQVTGSGTHKEL 556
Cdd:PRK11000 158 DEPLSNLDAalrvqmriEISRL-HKRL-----GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-528 |
1.41e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.80 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 344 YEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSG-------RIFLDGTDSQNVN-LRSWRHLFSYVQQ 415
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEarvegevRLFGRNIYSPDVDpIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 416 DSPILAGTIRENLIYGLE-------RHVTDEEIEEAAKLAnahhfiqSFEAQYETMIGERGINLSGGQRQRIAIARALLR 488
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKlnglvksKKELDERVEWALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1265182468 489 NPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIAH 528
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
324-566 |
2.07e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.44 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 324 ENGEVLEQVGSLrfdKVAFQYEDKPVL-----------QEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIF 392
Cdd:PRK15079 3 EGKKVLLEVADL---KVHFDIKDGKQWfwqppktlkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 393 LDGTDSQNVNLRSWRHLFSYVQ---QDSpiLAG-----TIRENLIYGLER---HVTDEEIEEAAKlanahhfiqsfeaqy 461
Cdd:PRK15079 80 WLGKDLLGMKDDEWRAVRSDIQmifQDP--LASlnprmTIGEIIAEPLRTyhpKLSRQEVKDRVK--------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 462 eTMIGERG-----IN-----LSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKE-RTSLV-IAHR 529
Cdd:PRK15079 143 -AMMLKVGllpnlINrypheFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIfIAHD 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1265182468 530 LSTVIN-ADQIVVIEEGQVTGSGTHKELLA--SHSFYRRL 566
Cdd:PRK15079 222 LAVVKHiSDRVLVMYLGHAVELGTYDEVYHnpLHPYTKAL 261
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
335-569 |
2.67e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.92 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIfldgtdSQNVNLRswrhlFSYVQ 414
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLR-----IGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QD---SPILAGTIRENLIygLERHVTDEEIEEAAKLANAHHFIQsFEAQyetmigergiNLSGGQRQRIAIARALLRNPQ 491
Cdd:PRK09544 74 QKlylDTTLPLTVNRFLR--LRPGTKKEDILPALKRVQAGHLID-APMQ----------KLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 492 FLLLDEATASLDSESEKLVQESLETVMKERTS--LVIAHRLSTVINADQIVVIEEGQVTGSGT------HKELLAshSFY 563
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCavLMVSHDLHLVMAKTDEVLCLNHHICCSGTpevvslHPEFIS--MFG 218
|
....*.
gi 1265182468 564 RRLVEQ 569
Cdd:PRK09544 219 PRGAEQ 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
343-551 |
2.83e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.55 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 343 QYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSY-VQQDSPILA 421
Cdd:PRK15439 20 QYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYlVPQEPLLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 422 G-TIRENLIYGLERHVTDEE-IEEAAKLANAHhfiQSFEAQYETmigerginLSGGQRQRIAIARALLRNPQFLLLDEAT 499
Cdd:PRK15439 100 NlSVKENILFGLPKRQASMQkMKQLLAALGCQ---LDLDSSAGS--------LEVADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 500 ASLD-SESEKLVQEsLETVMKERTSLV-IAHRLSTVIN-ADQIVVIEEGQVTGSG 551
Cdd:PRK15439 169 ASLTpAETERLFSR-IRELLAQGVGIVfISHKLPEIRQlADRISVMRDGTIALSG 222
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
94-312 |
3.50e-15 |
|
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: 76.36 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 94 LRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMF 173
Cdd:cd18589 71 LQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 174 VLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVM 253
Cdd:cd18589 151 LVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSG 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265182468 254 TAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18589 231 LALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
339-568 |
4.07e-15 |
|
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: 78.19 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 339 KVAFQYED--KPVLQEVSFSAKKGEVTAFVGPSGAGKS----TVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHL--- 409
Cdd:COG4172 13 SVAFGQGGgtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 410 -FSYVQQD-----SPILagTIRENLIYGLERH--VTDEEIEEAA-------KLANAHHFIQSFEAQyetmigerginLSG 474
Cdd:COG4172 93 rIAMIFQEpmtslNPLH--TIGKQIAEVLRLHrgLSGAAARARAlellervGIPDPERRLDAYPHQ-----------LSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 475 GQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER-TSLV-IAHRLSTVIN-ADQIVVIEEGQVTGSG 551
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgMALLlITHDLGVVRRfADRVAVMRQGEIVEQG 239
|
250
....*....|....*....
gi 1265182468 552 THKELLAS--HSFYRRLVE 568
Cdd:COG4172 240 PTAELFAApqHPYTRKLLA 258
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-559 |
4.11e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.90 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 344 YEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSG-----RIFLDGTDSQNVN--LRSWRHLFSYVQQD 416
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRdvLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 417 SPiLAGTIRENLIYGLERHVTDEEiEEAAKLANAHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLD 496
Cdd:PRK14271 111 NP-FPMSIMDNVLAGVRAHKLVPR-KEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 497 EATASLDSESEKLVQESLETVMKERTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLAS 559
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
350-551 |
4.67e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.35 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSW-----RHLF----SYVQQDS--- 417
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerRRLLrtewGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 418 ---PILAG-TIRENLIYGLERHVTDeeIEEAAKlanahHFIQSFEAQyETMIGERGINLSGGQRQRIAIARALLRNPQFL 493
Cdd:PRK11701 102 lrmQVSAGgNIGERLMAVGARHYGD--IRATAG-----DWLERVEID-AARIDDLPTTFSGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 494 LLDEATASLDSEseklVQESLETVMKertSLVIAHRLSTVIN----------ADQIVVIEEGQVTGSG 551
Cdd:PRK11701 174 FMDEPTGGLDVS----VQARLLDLLR---GLVRELGLAVVIVthdlavarllAHRLLVMKQGRVVESG 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
347-547 |
5.03e-15 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 73.24 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 347 KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHL-FSYV----QQDSPILA 421
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVpedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 422 GTIRENLIygLERHvtdeeieeaaklanahhfiqsfeaqyetmigerginLSGGQRQRIAIARALLRNPQFLLLDEATAS 501
Cdd:cd03215 93 LSVAENIA--LSSL------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1265182468 502 LDSESeklVQESLETVMKERTS----LVIAHRLSTVIN-ADQIVVIEEGQV 547
Cdd:cd03215 135 VDVGA---KAEIYRLIRELADAgkavLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
316-566 |
5.80e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 77.70 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 316 LAEKEENYENGEVLEQVGSLRFDKVAFQYEDKPV-LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLD 394
Cdd:PRK10522 304 LAPYKAEFPRPQAFPDWQTLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLD 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 395 GTDSQNVNLRSWRHLFSYVQQDspilagtirenliYGLERHVTDEEIEEAAKLAnAHHFIQSFEAQYETMIGE---RGIN 471
Cdd:PRK10522 384 GKPVTAEQPEDYRKLFSAVFTD-------------FHLFDQLLGPEGKPANPAL-VEKWLERLKMAHKLELEDgriSNLK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 472 LSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKE--RTSLVIAHRLSTVINADQIVVIEEGQVTG 549
Cdd:PRK10522 450 LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
250
....*....|....*..
gi 1265182468 550 SGTHKELLASHSFYRRL 566
Cdd:PRK10522 530 LTGEERDAASRDAVART 546
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
343-567 |
6.77e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.89 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 343 QYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsqnvnLRSWRHLFSYVQQ------- 415
Cdd:COG4586 31 EYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-------YVPFKRRKEFARRigvvfgq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 416 ------DSPIlagtiRENL-----IYGLERHVTDEEIEEAAKLANAHHFIQsfeaqyeTMIgeRgiNLSGGQRQRIAIAR 484
Cdd:COG4586 104 rsqlwwDLPA-----IDSFrllkaIYRIPDAEYKKRLDELVELLDLGELLD-------TPV--R--QLSLGQRMRCELAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 485 ALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLASHS 561
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFG 247
|
....*.
gi 1265182468 562 FYRRLV 567
Cdd:COG4586 248 PYKTIV 253
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
349-514 |
1.15e-14 |
|
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: 72.91 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 349 VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTIRENL 428
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 429 IYgLERHVTDEEIEEAAKLANAHHFIQSFEAQyetmigerginLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEK 508
Cdd:cd03231 95 RF-WHADHSDEQVEEALARVGLNGFEDRPVAQ-----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
....*.
gi 1265182468 509 LVQESL 514
Cdd:cd03231 163 RFAEAM 168
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
61-308 |
1.75e-14 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 74.09 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 61 LIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVM----NLLSTe 136
Cdd:cd18783 44 LTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQQIERIRQfltgQLFGT- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 137 MIDFVknilSIIVAIVILFTLDVPMTLILLAVIPVMFVLVM----PLARKIHKISREQQDKmsklTAFLAQMLSEIRLIK 212
Cdd:cd18783 123 LLDAT----SLLVFLPVLFFYSPTLALVVLAFSALIALIILaflpPFRRRLQALYRAEGER----QAFLVETVHGIRTVK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 213 ---VSGSEKKEVDSGLQSFQSLYLfgvKRAKIEAIITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIM 289
Cdd:cd18783 195 slaLEPRQRREWDERVARAIRARF---AVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVA 271
|
250
....*....|....*....
gi 1265182468 290 VPVGSLTRFVTSFQQTKGA 308
Cdd:cd18783 272 GPLVQLAGLVQEYQEARLS 290
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
335-549 |
1.79e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.99 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQY-EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRS---WRHLF 410
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 411 SYVQQDSPILAG-TIREN-----LIYGLE----RHVTDEEIEEAAKLANAHHFiqsfeaqyetmigerGINLSGGQRQRI 480
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNvaiplIIAGASgddiRRRVSAALDKVGLLDKAKNF---------------PIQLSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265182468 481 AIARALLRNPQFLLLDEATASLDSE-SEKLVQESLETVMKERTSLVIAHRLSTVINAD-QIVVIEEGQVTG 549
Cdd:PRK10908 147 GIARAVVNKPAVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHLHG 217
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
91-284 |
2.35e-14 |
|
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: 73.91 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 91 VKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIP 170
Cdd:cd18590 68 NLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 171 VMFvlvmpLARKIH-----KISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAII 245
Cdd:cd18590 148 LTA-----IAQKVYntyhqKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVY 222
|
170 180 190
....*....|....*....|....*....|....*....
gi 1265182468 246 TPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLY 284
Cdd:cd18590 223 LLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILY 261
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
60-507 |
2.61e-14 |
|
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: 75.94 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 60 QLIAGLLVLFAAQMVTSAVSlYLLAQVG----QGVVKELRHKVWNKLIKLPVSFYDqNRSGEMVSRITNDTTIVMNLLST 135
Cdd:TIGR00954 137 ILFKWFLIAPPASFINSAIK-YLLKELKlrfrVRLTRYLYSKYLSGFTFYKVSNLD-SRIQNPDQLLTQDVEKFCDSVVE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 136 EMIDFVKNILSIIVAIVILFT-LDVPMTLILLAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLS---EIRLI 211
Cdd:TIGR00954 215 LYSNLTKPILDVILYSFKLLTaLGSVGPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMnseEIAFY 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 212 KVSGSEKKEVDSglqSFQSLYLFGVKRAK-------IEAIITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLY 284
Cdd:TIGR00954 295 QGNKVEKETVMS---SFYRLVEHLNLIIKfrfsygfLDNIVAKYTWSAVGLVAVSIPIFDKTHPAFLEMSEEELMQEFYN 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 285 LFQIMVPVG-SLTRFVTS---FQQTKGASERIFDIL-------------------AEKEENYENGEVLEQVGSLRFDKVA 341
Cdd:TIGR00954 372 NGRLLLKAAdALGRLMLAgrdMTRLAGFTARVDTLLqvlddvksgnfkrprveeiESGREGGRNSNLVPGRGIVEYQDNG 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 342 FQYEDKPV--------LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIE--------RFYEPSSGRIFldgtdsqnvnlrs 405
Cdd:TIGR00954 452 IKFENIPLvtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLF------------- 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 406 wrhlfsYVQQDSPILAGTIRENLIYG------LERHVTDEEIEEAAKLANAHHFIQ---SFEAQYETMIgergiNLSGGQ 476
Cdd:TIGR00954 519 ------YVPQRPYMTLGTLRDQIIYPdssedmKRRGLSDKDLEQILDNVQLTHILEregGWSAVQDWMD-----VLSGGE 587
|
490 500 510
....*....|....*....|....*....|.
gi 1265182468 477 RQRIAIARALLRNPQFLLLDEATASLDSESE 507
Cdd:TIGR00954 588 KQRIAMARLFYHKPQFAILDECTSAVSVDVE 618
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
66-312 |
3.55e-14 |
|
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: 73.46 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 66 LVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNIL 145
Cdd:cd18558 66 LIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 146 SIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGL 225
Cdd:cd18558 146 TFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 226 QSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQT 305
Cdd:cd18558 226 QNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANA 305
|
....*..
gi 1265182468 306 KGASERI 312
Cdd:cd18558 306 RGAAYHI 312
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
318-506 |
3.70e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 75.92 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 318 EKEENYENGEVLEQVGSLRFDkVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFS-LIERfyepSSGRIFLDGT 396
Cdd:TIGR00956 748 EKDMEKESGEDIFHWRNLTYE-VKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAER----VTTGVITGGD 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 397 dsQNVNLRSWRHLFS----YVQQ-DSPILAGTIRENLIYG----LERHVTDEE----IEEAAKLAnahhfiqSFEAQYET 463
Cdd:TIGR00956 823 --RLVNGRPLDSSFQrsigYVQQqDLHLPTSTVRESLRFSaylrQPKSVSKSEkmeyVEEVIKLL-------EMESYADA 893
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1265182468 464 MIGERGINLSGGQRQRIAIARALLRNPQFLL-LDEATASLDSES 506
Cdd:TIGR00956 894 VVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
347-499 |
3.70e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.05 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 347 KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsQNVNLRS----WRHLFSYV----QQDSP 418
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPVRIRSprdaIRAGIAYVpedrKGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 419 ILAGTIRENLIYG-LERHVTDEEIEEAAKLANAHHFIQSFE---AQYETMIGergiNLSGGQRQRIAIARALLRNPQFLL 494
Cdd:COG1129 342 VLDLSIRENITLAsLDRLSRGGLLDRRRERALAEEYIKRLRiktPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLI 417
|
....*
gi 1265182468 495 LDEAT 499
Cdd:COG1129 418 LDEPT 422
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
340-556 |
4.45e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.49 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 340 VAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsQNVNLRSWRHLFSYVQQDSPI 419
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG---ENIPAMSRSRLYTVRKRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 420 LAG-------TIRENLIYGLERHVTDEEI---------EEAAKLANAHHFIQSfeaqyetmigergiNLSGGQRQRIAIA 483
Cdd:PRK11831 90 FQSgalftdmNVFDNVAYPLREHTQLPAPllhstvmmkLEAVGLRGAAKLMPS--------------ELSGGMARRAALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 484 RALLRNPQFLLLDEATASLDSESE----KLVQEsLETVMKeRTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKEL 556
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMgvlvKLISE-LNSALG-VTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
318-558 |
5.06e-14 |
|
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: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 318 EKEENYENGEVLeqvgsLRFDKVAFQY--EDKPVLQEV---SFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRI- 391
Cdd:TIGR03269 268 EKECEVEVGEPI-----IKVRNVSKRYisVDRGVVKAVdnvSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVn 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 392 ------FLDGTDSQNVNL-RSWRHLFSYVQQDSPILAGTIRENLIYGLERHVTDEeieeAAKLANAHHF-IQSFEAQYET 463
Cdd:TIGR03269 343 vrvgdeWVDMTKPGPDGRgRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDE----LARMKAVITLkMVGFDEEKAE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 464 MIGERGIN-LSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKE--RTSLVIAHRLSTVIN-ADQI 539
Cdd:TIGR03269 419 EILDKYPDeLSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLDvCDRA 498
|
250
....*....|....*....
gi 1265182468 540 VVIEEGQVTGSGTHKELLA 558
Cdd:TIGR03269 499 ALMRDGKIVKIGDPEEIVE 517
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
342-552 |
5.90e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 75.44 E-value: 5.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 342 FQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQnVNLRSWRHLFSYVQQDSPILA 421
Cdd:TIGR01257 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 422 G-TIRENLIYGLE---RHVTDEEIEEAAKLANAH-HFIQSFEAQyetmigergiNLSGGQRQRIAIARALLRNPQFLLLD 496
Cdd:TIGR01257 1017 HlTVAEHILFYAQlkgRSWEEAQLEMEAMLEDTGlHHKRNEEAQ----------DLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 497 EATASLDSESEKLVQESLETVMKERTSLVIAHRLSTV-INADQIVVIEEGQVTGSGT 552
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGT 1143
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
61-312 |
6.93e-14 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 72.58 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 61 LIAGLLVLFAAQMVTSAVSLYLL--------AQVGQGVvkeLRHkvwnkLIKLPVSFYDQNRSGEMVSRItNDTTIVMNL 132
Cdd:cd18779 44 LGLGLAALVLTQLLAGLLRSHLLlrlrtrldTQLTLGF---LEH-----LLRLPYRFFQQRSTGDLLMRL-SSNATIREL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 133 LSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIK 212
Cdd:cd18779 115 LTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLATRRRVRELMARELAAQAEAQSYLVEALSGIETLK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 213 VSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPV 292
Cdd:cd18779 195 ASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPL 274
|
250 260
....*....|....*....|
gi 1265182468 293 GSLTRFVTSFQQTKGASERI 312
Cdd:cd18779 275 ASLVGTAQQLQLLGSHLERL 294
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
348-515 |
9.11e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 70.08 E-value: 9.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 348 PVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTIREN 427
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 428 LIYGLERH-VTDEEIEEAAKLANAHHFIQSFEAQyetmigerginLSGGQRQRIAIARALLRNPQFLLLDEATASLDSES 506
Cdd:TIGR01189 94 LHFWAAIHgGAQRTIEDALAAVGLTGFEDLPAAQ-----------LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
....*....
gi 1265182468 507 EKLVQESLE 515
Cdd:TIGR01189 163 VALLAGLLR 171
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
350-551 |
1.50e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsQNVNLRSWRHLFSYVQQDS------PILAGT 423
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG---QPTRQALQKNLVAYVPQSEevdwsfPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 424 IRENLIYG----LER-HVTDEEIEEAAkLANahhfIQSFEAQYEtMIGErginLSGGQRQRIAIARALLRNPQFLLLDEA 498
Cdd:PRK15056 100 VVMMGRYGhmgwLRRaKKRDRQIVTAA-LAR----VDMVEFRHR-QIGE----LSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 499 TASLDSESEKLVQESLETVMKE-RTSLVIAHRLSTVINADQIVVIEEGQVTGSG 551
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
348-555 |
1.96e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 348 PVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsQNVNLRS----WRHLFSYVQQDSP----I 419
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG---HEVVTRSpqdgLANGIVYISEDRKrdglV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 420 LAGTIRENLIYGLERHVTDE--EIEEAAKLANAHHFIQSFEAQYETM---IGergiNLSGGQRQRIAIARALLRNPQFLL 494
Cdd:PRK10762 343 LGMSVKENMSLTALRYFSRAggSLKHADEQQAVSDFIRLFNIKTPSMeqaIG----LLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 495 LDEATASLDSESEKLVQESLETVMKERTSLV-IAHRLSTVIN-ADQIVVIEEGQVTGSGTHKE 555
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQFKAEGLSIIlVSSEMPEVLGmSDRILVMHEGRISGEFTREQ 481
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
24-312 |
2.57e-13 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 70.55 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 24 KLLISFILAL-INTGASLSIPLVIKEVmekIAIGVSPQ-------LIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELR 95
Cdd:cd18571 2 KLILQLLLGLlLGSLLQLIFPFLTQSI---VDKGINNKdlnfiylILIAQLVLFLGSTSIEFIRSWILLHISSRINISII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 96 HKVWNKLIKLPVSFYDQNRSGEMVSRItNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVL 175
Cdd:cd18571 79 SDFLIKLMRLPISFFDTKMTGDILQRI-NDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIGSVLYILW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 176 VMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTA 255
Cdd:cd18571 158 ILLFLKKRKKLDYKRFDLSSENQSKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLKLDQYQQIGALFINQL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 256 VMIAIVGFGAYRVSEGFITAGELVAfVLY-LFQIMVPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18571 238 KNILITFLAAKLVIDGEITLGMMLA-IQYiIGQLNSPIEQLIGFIQSLQDAKISLERL 294
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
303-536 |
2.61e-13 |
|
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: 72.66 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 303 QQTKGASeRI--FDILAEKEENYENGE------VLEQVGS--LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAG 372
Cdd:TIGR03719 282 RQAKSKA-RLarYEELLSQEFQKRNETaeiyipPGPRLGDkvIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAG 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 373 KSTVFSLIERFYEPSSGRIFLDGTdsqnVNLrswrhlfSYVQQDSPILAG--TIRENLIYGLerhvtdEEIEEAAKLANA 450
Cdd:TIGR03719 361 KSTLFRMITGQEQPDSGTIEIGET----VKL-------AYVDQSRDALDPnkTVWEEISGGL------DIIKLGKREIPS 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 451 HHFIQSFE---AQYETMIGErginLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKerTSLVIA 527
Cdd:TIGR03719 424 RAYVGRFNfkgSDQQKKVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAG--CAVVIS 497
|
250
....*....|....*
gi 1265182468 528 H------RLSTVINA 536
Cdd:TIGR03719 498 HdrwfldRIATHILA 512
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
350-557 |
2.70e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.96 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYePSSGRIFLDGTDSQNVNLRSWRHLFSY-VQQDSPILAGTIRENL 428
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYlSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 429 ---------IYGLERHVtdEEIEEAAKLANAHHfiqsfeaqyeTMIGergiNLSGGQRQRIAIARALLR-----NP--QF 492
Cdd:PRK03695 91 tlhqpdktrTEAVASAL--NEVAEALGLDDKLG----------RSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 493 LLLDEATASLDsesekLVQES-LETVMKE-----RTSLVIAHRLS-TVINADQIVVIEEGQVTGSGTHKELL 557
Cdd:PRK03695 155 LLLDEPMNSLD-----VAQQAaLDRLLSElcqqgIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
358-543 |
2.97e-13 |
|
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: 69.74 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 358 KKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDsqnvnlrswrhlFSYV-QQDSPILAGTIRENLIYGLERHV 436
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT------------VSYKpQYIKADYEGTVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 437 TDEEIE-EAAKlanahhfiqsfEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLE 515
Cdd:cd03237 91 THPYFKtEIAK-----------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
170 180 190
....*....|....*....|....*....|..
gi 1265182468 516 TVM--KERTSLVIAHR--LSTVInADQIVVIE 543
Cdd:cd03237 160 RFAenNEKTAFVVEHDiiMIDYL-ADRLIVFE 190
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
28-295 |
3.28e-13 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 70.22 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 28 SFILALINTGASLSIPLVIKEVMEKIAIGVS--PQLIAGLLVLFAAQMVTSAVSL----YLLAQVGQGVVKELRHKVWNK 101
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALSAPASalLAVPLLLLLAYGLARILSSLFNelrdALFARVSQRAVRRLALRVFRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 102 LIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTL-DVPMTLILLAVIPVMFVLVMPLA 180
Cdd:cd18582 81 LHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLyGWSYALITLVTVALYVAFTIKVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 181 RKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEV-----------DSGLQSFQSLYLFGVkrakIEAIItpiI 249
Cdd:cd18582 161 EWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAerydkalakyeKAAVKSQTSLALLNI----GQALI---I 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1265182468 250 STVMTAVMIaivgFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSL 295
Cdd:cd18582 234 SLGLTAIML----LAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFL 275
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
343-546 |
3.97e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.22 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 343 QYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSS--GRIFLDGTDSQNVNLRSwrhlFSYVQQDS--- 417
Cdd:PLN03211 77 QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKR----TGFVTQDDily 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 418 PILagTIRENLIY----GLERHVTDEEIEEAAKLANAHHFIQSFEaqyETMIGE---RGInlSGGQRQRIAIARALLRNP 490
Cdd:PLN03211 153 PHL--TVRETLVFcsllRLPKSLTKQEKILVAESVISELGLTKCE---NTIIGNsfiRGI--SGGERKRVSIAHEMLINP 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265182468 491 QFLLLDEATASLDSESE-KLVQESLETVMKERTSLVIAHRLSTVINA--DQIVVIEEGQ 546
Cdd:PLN03211 226 SLLILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSRVYQmfDSVLVLSEGR 284
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
350-546 |
1.11e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.20 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSS--GRIFLDGTDSQNVNLR-SWRHLFSYVQQD---SPILagT 423
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRdSEALGIVIIHQElalIPYL--S 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 424 IRENLIYGLERH---VTD--EEIEEAAKLANahhfIQSFEAQYETMIGERGInlsgGQRQRIAIARALLRNPQFLLLDEA 498
Cdd:NF040905 95 IAENIFLGNERAkrgVIDwnETNRRARELLA----KVGLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLILDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 499 TASL-DSESEKLVQESLEtvMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQ 546
Cdd:NF040905 167 TAALnEEDSAALLDLLLE--LKAQgiTSIIISHKLNEIRRvADSITVLRDGR 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
330-567 |
1.31e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.65 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 330 EQVGSLRFDKVAFQYEDKPV--LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDG------------ 395
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvie 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 396 ----TDSQNVNLR-------------SWRHLFSYVQQdspiLAGTIRenLIYGLERhvtDEEIEEAAKLANAHHFIQSfe 458
Cdd:PRK10261 90 lseqSAAQMRHVRgadmamifqepmtSLNPVFTVGEQ----IAESIR--LHQGASR---EEAMVEAKRMLDQVRIPEA-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 459 aqyETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLV--IAHRLSTVIN- 535
Cdd:PRK10261 159 ---QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVAEi 235
|
250 260 270
....*....|....*....|....*....|....
gi 1265182468 536 ADQIVVIEEGQVTGSGTHKELLAS--HSFYRRLV 567
Cdd:PRK10261 236 ADRVLVMYQGEAVETGSVEQIFHApqHPYTRALL 269
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
347-529 |
1.49e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.29 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 347 KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQnvnlrswrhlfsyVQQDSPILagtirE 426
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ-------------FGREASLI-----D 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 427 NLiyGLERHVTDE-EIEEAAKLANAHHFIQSFEaqyetmigergiNLSGGQRQRIAIARALLRNPQFLLLDEATASLDSE 505
Cdd:COG2401 105 AI--GRKGDFKDAvELLNAVGLSDAVLWLRRFK------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*.
gi 1265182468 506 SEKLVQESLETVMKER--TSLVIAHR 529
Cdd:COG2401 171 TAKRVARNLQKLARRAgiTLVVATHH 196
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
350-556 |
1.51e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNlrswrHLFSY-------VQQDSPILAG 422
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-----HKLAAqlgigiiYQELSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 423 TIRENLIYGleRHVTDE-------EIEEAAKLANAHHFIQSFEAQYETMIGergiNLSGGQRQRIAIARALLRNPQFLLL 495
Cdd:PRK09700 96 TVLENLYIG--RHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 496 DEATASL-DSESEKLVQeSLETVMKERTSLV-IAHRLSTVIN-ADQIVVIEEGQVTGSGTHKEL 556
Cdd:PRK09700 170 DEPTSSLtNKEVDYLFL-IMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
340-566 |
1.74e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.73 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 340 VAF--QYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKS-TVFSLIERFYEPS----SGRIFLDGTDSQNVNLRSWRH---- 408
Cdd:PRK15134 13 VAFrqQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGvrgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 409 ---------------LFSYVQQDSPILA---GTIRE----NLIYGLERhvtdEEIEEAAK-LANAHHfiqsfeaqyetmi 465
Cdd:PRK15134 93 kiamifqepmvslnpLHTLEKQLYEVLSlhrGMRREaargEILNCLDR----VGIRQAAKrLTDYPH------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 466 gergiNLSGGQRQRIAIARALLRNPQFLLLDEATASLDSEseklVQESLETVMKERTS------LVIAHRLSTVIN-ADQ 538
Cdd:PRK15134 156 -----QLSGGERQRVMIAMALLTRPELLIADEPTTALDVS----VQAQILQLLRELQQelnmglLFITHNLSIVRKlADR 226
|
250 260 270
....*....|....*....|....*....|
gi 1265182468 539 IVVIEEGQVTGSGTHKELLAS--HSFYRRL 566
Cdd:PRK15134 227 VAVMQNGRCVEQNRAATLFSAptHPYTQKL 256
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
347-556 |
2.22e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 69.29 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 347 KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLI--ERfyEPSSGRIFLDGTDSQNVNLRSWRHL-FSYV----QQDSPI 419
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLgVAYIpedrLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 420 LAGTIRENLIygLERHVTDEE-----IEEAAKLANAHHFIQSFE---AQYETMIGergiNLSGGQRQRIAIARALLRNPQ 491
Cdd:COG3845 349 PDMSVAENLI--LGRYRRPPFsrggfLDRKAIRAFAEELIEEFDvrtPGPDTPAR----SLSGGNQQKVILARELSRDPK 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 492 FLLLDEATASLDSESEKLVQESLetvMKERTS----LVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKEL 556
Cdd:COG3845 423 LLIAAQPTRGLDVGAIEFIHQRL---LELRDAgaavLLISEDLDEILAlSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
347-551 |
2.36e-12 |
|
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: 66.13 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 347 KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVF----SLIERFYEPSsGRIFLDGTDSQNVNLRSWRHLfSYV-QQDSPILA 421
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLkalaNRTEGNVSVE-GDIHYNGIPYKEFAEKYPGEI-IYVsEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 422 GTIRENLiyglerhvtdeeieEAAKLANAHHFIqsfeaqyetmigeRGInlSGGQRQRIAIARALLRNPQFLLLDEATAS 501
Cdd:cd03233 98 LTVRETL--------------DFALRCKGNEFV-------------RGI--SGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 502 LDSESeklvqeSLETVMKERTslvIAH--RLSTVINA-----------DQIVVIEEGQVTGSG 551
Cdd:cd03233 149 LDSST------ALEILKCIRT---MADvlKTTTFVSLyqasdeiydlfDKVLVLYEGRQIYYG 202
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
352-549 |
3.41e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 352 EVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYE-PSSGRIFLDGtdsQNVNLRS----WRHLFSYVQQDS------PIL 420
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDG---KPVKIRNpqqaIAQGIAMVPEDRkrdgivPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 421 AgtIRENL-IYGLERHVTDEEIEEAAKLANAHHFIQSFE---AQYETMIGergiNLSGGQRQRIAIARALLRNPQFLLLD 496
Cdd:PRK13549 357 G--VGKNItLAALDRFTGGSRIDDAAELKTILESIQRLKvktASPELAIA----RLSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 497 EATASLD--SESE------KLVQESLETVMkertslvIAHRLSTVIN-ADQIVVIEEGQVTG 549
Cdd:PRK13549 431 EPTRGIDvgAKYEiyklinQLVQQGVAIIV-------ISSELPEVLGlSDRVLVMHEGKLKG 485
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
349-568 |
3.57e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.16 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 349 VLQEVSFSAKKGEVTAFVGPSGAGKSTVF-SLIERFYEPS-------SGRIFLDGTDSQNVNLRSWRHLFSYV-QQDSPI 419
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLpQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 420 LAGTIRENLIYGLERHVT--------DEEIEEAA-KLANAhhfiqsfeaqyETMIGERGINLSGGQRQRIAIARAL---- 486
Cdd:PRK13547 96 FAFSAREIVLLGRYPHARragalthrDGEIAWQAlALAGA-----------TALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 487 -----LRNPQFLLLDEATASLDSESEKLVQESLETVMKERT--SLVIAHRLSTVI-NADQIVVIEEGQVTGSGTHKELL- 557
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNLAArHADRIAMLADGAIVAHGAPADVLt 244
|
250
....*....|....*.
gi 1265182468 558 -----ASHSFYRRLVE 568
Cdd:PRK13547 245 pahiaRCYGFAVRLVD 260
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
353-555 |
6.88e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.01 E-value: 6.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 353 VSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsQNVNLRSWRHLFSY--------VQQDSPILAGTI 424
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDAIRAgimlcpedRKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 425 RENLIYGLERH------VTDEEIEEaaklANAHHFIQSFEAQyeTMIGERGI-NLSGGQRQRIAIARALLRNPQFLLLDE 497
Cdd:PRK11288 349 ADNINISARRHhlragcLINNRWEA----ENADRFIRSLNIK--TPSREQLImNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 498 ATASLD----SESEKLVQESLEtvmKERTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKE 555
Cdd:PRK11288 423 PTRGIDvgakHEIYNVIYELAA---QGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
349-572 |
7.94e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 66.26 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 349 VLQEVSFSAKKGEVTAFVGPSGAGKSTvfsLIERFYE---PSSGRI---FLDGTDSQNVNLRSW---------------- 406
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTT---FIEHLNAlllPDTGTIewiFKDEKNKKKTKEKEKvleklviqktrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 407 -----RHLFSYVQQ--DSPILAGTIRENLIYGLERHVTDEEieEAAKLAnahhfiqsfeAQYETMIG------ERG-INL 472
Cdd:PRK13651 99 kikeiRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKE--EAKKRA----------AKYIELVGldesylQRSpFEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 473 SGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKE-RTSLVIAHRLSTVIN-ADQIVVIEEGQVTGS 550
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEwTKRTIFFKDGKIIKD 246
|
250 260
....*....|....*....|..
gi 1265182468 551 GTHKELLASHSFyrrLVEQQFQ 572
Cdd:PRK13651 247 GDTYDILSDNKF---LIENNME 265
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
350-546 |
1.61e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYePS---SGRIFLDGTDSQNVNLR-SWRHLFSYVQQDSPILAG-TI 424
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRdTERAGIAIIHQELALVKElSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 425 RENLIYGLE---RHVTD--EEIEEAAKLANahhfiqsfEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEAT 499
Cdd:PRK13549 100 LENIFLGNEitpGGIMDydAMYLRAQKLLA--------QLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1265182468 500 ASLdSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQ 546
Cdd:PRK13549 172 ASL-TESETAVLLDIIRDLKAHgiACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
333-566 |
2.19e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.03 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 333 GSLRFDKVAFQYEDKP-----VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGR-IFLDGTDSQNVN---- 402
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtIVGDYAIPANLKkike 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 403 LRSWRHLFSYVQQ--DSPILAGTIRENLIYGlERHVTDEEIEEAAKLANAHHFIQsfeaQYETMIGERGINLSGGQRQRI 480
Cdd:PRK13645 85 VKRLRKEIGLVFQfpEYQLFQETIEKDIAFG-PVNLGENKQEAYKKVPELLKLVQ----LPEDYVKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 481 AIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVI--AHRLSTVIN-ADQIVVIEEGQVTGSGTHKELL 557
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIImvTHNMDQVLRiADEVIVMHEGKVISIGSPFEIF 239
|
....*....
gi 1265182468 558 ASHSFYRRL 566
Cdd:PRK13645 240 SNQELLTKI 248
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
147-308 |
3.29e-11 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 64.38 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 147 IIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQ 226
Cdd:cd18587 128 VLLFLAVIALIGGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 227 SFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTK 306
Cdd:cd18587 208 AVAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELTMGGLIACVILSGRALAPLGQIAGLLTRYQQAR 287
|
..
gi 1265182468 307 GA 308
Cdd:cd18587 288 TA 289
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
352-556 |
1.58e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.69 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 352 EVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPS-SGRIFLDGtdsQNVNLR----SWRHLFSYVQQDS------PIL 420
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFING---KPVDIRnpaqAIRAGIAMVPEDRkrhgivPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 421 AgtIRENL-IYGLERHVTDEEIEEAAKLANAHHFIQSFE---AQYETMIGergiNLSGGQRQRIAIARALLRNPQFLLLD 496
Cdd:TIGR02633 355 G--VGKNItLSVLKSFCFKMRIDAAAELQIIGSAIQRLKvktASPFLPIG----RLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 497 EATASLDSESEKLVQESLETVMKERTSL-VIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKEL 556
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQEGVAIiVVSSELAEVLGlSDRVLVIGEGKLKGDFVNHAL 490
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
356-543 |
2.04e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.26 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 356 SAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDS---QnvnlrswrhlfsYVQQDSPilaGTIRENLiygl 432
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISykpQ------------YISPDYD---GTVEEFL---- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 433 ERHVTDEeieeaaklanahhFIQSFeaqYETMIGER-GI---------NLSGGQRQRIAIARALLRNPQFLLLDEATASL 502
Cdd:COG1245 423 RSANTDD-------------FGSSY---YKTEIIKPlGLeklldknvkDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1265182468 503 DSESEKLVQESLETVMKER--TSLVIAHRLsTVIN--ADQIVVIE 543
Cdd:COG1245 487 DVEQRLAVAKAIRRFAENRgkTAMVVDHDI-YLIDyiSDRLMVFE 530
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
321-564 |
2.44e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.05 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 321 ENYENGEVLEQVGSLRfdkVAFQYEDKPV--LQEVSFSAKKGEVTAFVGPSGAGKS-TVFSLIERFyePSSGRIflDGTD 397
Cdd:PRK09473 4 LAQQQADALLDVKDLR---VTFSTPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLL--AANGRI--GGSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 398 SQN----VNLRSwRHL-------FSYVQQD-----SPILagTIRENLIYGLERH---VTDEEIEEAAKLANAhhfIQSFE 458
Cdd:PRK09473 77 TFNgreiLNLPE-KELnklraeqISMIFQDpmtslNPYM--RVGEQLMEVLMLHkgmSKAEAFEESVRMLDA---VKMPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 459 AQYE-TMIGERginLSGGQRQRIAIARALLRNPQFLLLDEATASLDSEseklVQESLETVMKE-----RTSLV-IAHRLS 531
Cdd:PRK09473 151 ARKRmKMYPHE---FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVT----VQAQIMTLLNElkrefNTAIImITHDLG 223
|
250 260 270
....*....|....*....|....*....|....
gi 1265182468 532 TVIN-ADQIVVIEEGQVTGSGThkellASHSFYR 564
Cdd:PRK09473 224 VVAGiCDKVLVMYAGRTMEYGN-----ARDVFYQ 252
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
346-506 |
2.85e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.83 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 346 DKPVLQEVSFS----AKKGevtaFVGPSGAGKSTVFSLIERFYEPSSGRIFLdgtdSQNVNLrswrhlfSYVQQDsPIL- 420
Cdd:PRK11819 19 KKQILKDISLSffpgAKIG----VLGLNGAGKSTLLRIMAGVDKEFEGEARP----APGIKV-------GYLPQE-PQLd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 421 -AGTIRENLI-------------------YGLERHVTDEEIEEAAKL------ANAHhfiqSFEAQYE------------ 462
Cdd:PRK11819 83 pEKTVRENVEegvaevkaaldrfneiyaaYAEPDADFDALAAEQGELqeiidaADAW----DLDSQLEiamdalrcppwd 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1265182468 463 TMIGergiNLSGGQRQRIAIARALLRNPQFLLLDEATASLDSES 506
Cdd:PRK11819 159 AKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
344-548 |
5.26e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 344 YEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDgtdsQNVNLrswrhlfSYVQQDSP----- 418
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDLIV-------ARLQQDPPrnveg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 419 ----ILAGTIRE---------NLIYGLERHVTDEEIEEAAKLANA--HHFIQSFEAQYETMIGERGIN-------LSGGQ 476
Cdd:PRK11147 82 tvydFVAEGIEEqaeylkryhDISHLVETDPSEKNLNELAKLQEQldHHNLWQLENRINEVLAQLGLDpdaalssLSGGW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 477 RQRIAIARALLRNPQFLLLDEATASLDSESeklvQESLETVMKE-RTSLV-IAHRLSTVIN-ADQIVVIEEGQVT 548
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTfQGSIIfISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
345-545 |
5.90e-10 |
|
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: 58.79 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 345 EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPS--SGRIFLDGTDsqnvNLRSWRHLFSYV-QQDSPILA 421
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRP----LDKNFQRSTGYVeQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 422 GTIRENLIYglerhvtdeeieeAAKLanahhfiqsfeaqyetmigeRGINLSggQRQRIAIARALLRNPQFLLLDEATAS 501
Cdd:cd03232 94 LTVREALRF-------------SALL--------------------RGLSVE--QRKRLTIGVELAAKPSILFLDEPTSG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1265182468 502 LDSESEKLVQESLE-TVMKERTSLVIAHRLSTVI--NADQIVVIEEG 545
Cdd:cd03232 139 LDSQAAYNIVRFLKkLADSGQAILCTIHQPSASIfeKFDRLLLLKRG 185
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
62-312 |
7.37e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 60.37 E-value: 7.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 62 IAGLLVLFAAQMVTSAVSLYLL----AQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEM 137
Cdd:cd18561 35 IMPPLAGIAGVIVLRAALLWLRervaHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 138 IDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSE 217
Cdd:cd18561 115 PQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGAS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 218 KKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTR 297
Cdd:cd18561 195 KRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGA 274
|
250
....*....|....*
gi 1265182468 298 FVTSFQQTKGASERI 312
Cdd:cd18561 275 YWHAGYQGISAADSI 289
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
346-552 |
9.29e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.27 E-value: 9.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 346 DKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERF--YEPSSGRIFLDGTD--SQNVNLRSWRHLFSYVQQdsPI-L 420
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESilDLEPEERAHLGIFLAFQY--PIeI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 421 AGTIREN---LIYGLER-HVTDEEIE---------EAAKLAN-AHHFIqsfeaqyetmigERGIN--LSGGQRQRIAIAR 484
Cdd:CHL00131 97 PGVSNADflrLAYNSKRkFQGLPELDplefleiinEKLKLVGmDPSFL------------SRNVNegFSGGEKKRNEILQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265182468 485 ALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLV-IAH--RLSTVINADQIVVIEEGQVTGSGT 552
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
350-550 |
1.06e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.99 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSS--GRIFLDGTDSQNVNLR-SWRHLFSYVQQDSPILAG-TIR 425
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRdTERAGIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 426 ENLIYGLERHVTDEEIEEAAKLANAHHFIQsfEAQYETMIGERGI-NLSGGQRQRIAIARALLRNPQFLLLDEATASL-D 503
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYNAMYLRAKNLLR--ELQLDADNVTRPVgDYGGGQQQLVEIAKALNKQARLLILDEPSSSLtE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1265182468 504 SESEKLVQESLETVMKERTSLVIAHRLSTVIN-ADQIVVIEEGQVTGS 550
Cdd:TIGR02633 175 KETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVAT 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
346-506 |
1.24e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 60.72 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 346 DKPVLQEVSFS----AKKGevtaFVGPSGAGKSTVFSLIERFYEPSSGRIFLdgtdSQNVNLrswrhlfSYVQQDsPIL- 420
Cdd:TIGR03719 17 KKEILKDISLSffpgAKIG----VLGLNGAGKSTLLRIMAGVDKDFNGEARP----QPGIKV-------GYLPQE-PQLd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 421 -AGTIRENLIYGLE--RHVTDE--EI---------------EEAAKL------ANAHhfiqSFEAQYETMI-------GE 467
Cdd:TIGR03719 81 pTKTVRENVEEGVAeiKDALDRfnEIsakyaepdadfdklaAEQAELqeiidaADAW----DLDSQLEIAMdalrcppWD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1265182468 468 RGI-NLSGGQRQRIAIARALLRNPQFLLLDEATASLDSES 506
Cdd:TIGR03719 157 ADVtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
357-528 |
1.72e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 357 AKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDS---QnvnlrswrhlfsYVQQDSPilaGTIRENLiygle 433
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISykpQ------------YIKPDYD---GTVEDLL----- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 434 RHVTD--------EEIEEAAKLanahhfiqsfEAQYETMIGErginLSGGQRQRIAIARALLRNPQFLLLDEATASLDSE 505
Cdd:PRK13409 422 RSITDdlgssyykSEIIKPLQL----------ERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180
....*....|....*....|....*
gi 1265182468 506 SEKLVQESLETVMKER--TSLVIAH 528
Cdd:PRK13409 488 QRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
49-223 |
1.81e-09 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 58.96 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 49 VMEKIAIGVSPQLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSritndtti 128
Cdd:cd18584 27 FLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELAT-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 129 vmnlLSTEMIDFVKN---------ILSIIVAIVIL---FTLDVPMTLILLA---VIPVMFVLVMPLARkihKISREQQDK 193
Cdd:cd18584 99 ----LLTEGVDALDGyfarylpqlVLAAIVPLLILvavFPLDWVSALILLVtapLIPLFMILIGKAAQ---AASRRQWAA 171
|
170 180 190
....*....|....*....|....*....|
gi 1265182468 194 MSKLTAFLAQMLSEIRLIKVSGSEKKEVDS 223
Cdd:cd18584 172 LSRLSGHFLDRLRGLPTLKLFGRARAQAAR 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
358-542 |
2.00e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 358 KKGEVTAFVGPSGAGKSTVFSLIE--------RFYEPSSGRIFLD---GTDSQNV--NLRSWR----HLFSYVQQDSPIL 420
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILSgelipnlgDYEEEPSWDEVLKrfrGTELQNYfkKLYNGEikvvHKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 421 AGTIRENLIYGLERHVTDEEIEEAAkLANahhfiqsfeaqyetmIGERGI-NLSGGQRQRIAIARALLRNPQFLLLDEAT 499
Cdd:PRK13409 177 KGKVRELLKKVDERGKLDEVVERLG-LEN---------------ILDRDIsELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1265182468 500 ASLD----SESEKLVQEsletVMKERTSLVIAHRLsTVIN--ADQIVVI 542
Cdd:PRK13409 241 SYLDirqrLNVARLIRE----LAEGKYVLVVEHDL-AVLDylADNVHIA 284
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
333-515 |
2.07e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 333 GSLRFD--KVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLdGTDSQnvnlrswrhlF 410
Cdd:PRK11147 316 GKIVFEmeNVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLE----------V 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 411 SYVQQDSPIL--AGTIRENL--------IYGLERHVTDeeieeaaklanahhFIQSF-----EAqyetMIGERGinLSGG 475
Cdd:PRK11147 385 AYFDQHRAELdpEKTVMDNLaegkqevmVNGRPRHVLG--------------YLQDFlfhpkRA----MTPVKA--LSGG 444
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1265182468 476 QRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLE 515
Cdd:PRK11147 445 ERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLD 484
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
28-297 |
2.81e-09 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 58.39 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 28 SFILALINTGASLSIPLVIKEVMEKIAIG--VSPQLIAGLLVLFAAqMVTSAVSL-----YLLAQVGQGVVKELRHKVWN 100
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLAkvKDLESAVTLILLYAL-LRFSSKLLkelrsLLYRRVQQNAYRELSLKTFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 101 KLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPM----TLILLAVIPVMFVLV 176
Cdd:cd18560 80 HLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWlaliVFLSVLLYGVFTIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 177 MPLARKIHKISREQQDKMSKLtAFLAQMLSEIrlIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIISTVMTAV 256
Cdd:cd18560 160 TEWRTKFRRAANKKDNEAHDI-AVDSLLNFET--VKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1265182468 257 MIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTR 297
Cdd:cd18560 237 LTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGT 277
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
349-506 |
3.58e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.48 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 349 VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVN------LRSwRHLfSYVQQdSPILAG 422
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearakLRA-KHV-GFVFQ-SFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 423 TI--RENL-IYGLERHVTDEEIEEAAKlanahhfiqsfEAQYETMIGER----GINLSGGQRQRIAIARALLRNPQFLLL 495
Cdd:PRK10584 102 TLnaLENVeLPALLRGESSRQSRNGAK-----------ALLEQLGLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170
....*....|.
gi 1265182468 496 DEATASLDSES 506
Cdd:PRK10584 171 DEPTGNLDRQT 181
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
359-521 |
4.20e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.46 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 359 KGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDsqnvnlrswrhlfsyvqqdspilagtirenliyglerhvtd 438
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 439 eeieeaaklanaHHFIQSFEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVM 518
Cdd:smart00382 40 ------------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
...
gi 1265182468 519 KER 521
Cdd:smart00382 108 LLL 110
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
337-555 |
5.53e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 337 FDKVAFQYEDKPVL-QEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFldgtDSQNVNLRswrhLFSyvqq 415
Cdd:PLN03073 511 FSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF----RSAKVRMA----VFS---- 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 416 dspilagtirenliyglERHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGERGIN----------LSGGQRQRIAIARA 485
Cdd:PLN03073 579 -----------------QHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSRVAFAKI 641
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 486 LLRNPQFLLLDEATASLDSES-EKLVQeslETVMKERTSLVIAHRLSTVINA-DQIVVIEEGQVTG-SGTHKE 555
Cdd:PLN03073 642 TFKKPHILLLDEPSNHLDLDAvEALIQ---GLVLFQGGVLMVSHDEHLISGSvDELWVVSEGKVTPfHGTFHD 711
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
358-552 |
6.08e-09 |
|
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: 55.66 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 358 KKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTdsqnvnlrswrhlfsyvqqdspilagTIrenliyglerhvt 437
Cdd:cd03222 23 KEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI--------------------------TP------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 438 deeieeaaklanahhfiqSFEAQYetmigergINLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETV 517
Cdd:cd03222 64 ------------------VYKPQY--------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180 190
....*....|....*....|....*....|....*..
gi 1265182468 518 MKE--RTSLVIAHRLSTVINADQIVVIEEGQVTGSGT 552
Cdd:cd03222 118 SEEgkKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGI 154
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
25-314 |
9.75e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 56.74 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGASLSIPLVIKEVMEKIAIGVSPQLIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIK 104
Cdd:cd18580 5 LLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 105 LPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLdvpmTLILLAVIPVMFVLVMPLARKIH 184
Cdd:cd18580 85 APMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIV----SPYFLIVLPPLLVVYYLLQRYYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 185 KISREQQ--DKMSK--LTAFLAQMLSEIRLIKVSGSEKKEVDSGLQ----SFQSLYLF-GVKRAkieaiitpiISTVM-- 253
Cdd:cd18580 161 RTSRQLRrlESESRspLYSHFSETLSGLSTIRAFGWQERFIEENLRlldaSQRAFYLLlAVQRW---------LGLRLdl 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 254 -TAVMIAIVGFGAYrVSEGFITAGeLVAFVL-YLFQIMVPVGSLTRFVTSFQQTKGASERIFD 314
Cdd:cd18580 232 lGALLALVVALLAV-LLRSSISAG-LVGLALtYALSLTGSLQWLVRQWTELETSMVSVERILE 292
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
350-567 |
1.08e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVN---LRSWRHLFSYVQQDsPILAGTIRE 426
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQD-PYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 427 NLIYglerhvtdeEIEEAAKLanaHHFIQSFEAQYET--MIGERGI----------NLSGGQRQRIAIARALLRNPQFLL 494
Cdd:PRK10261 419 TVGD---------SIMEPLRV---HGLLPGKAAAARVawLLERVGLlpehawryphEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 495 LDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLAS--HSFYRRLV 567
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENpqHPYTRKLM 564
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
348-526 |
1.49e-08 |
|
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: 58.10 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 348 PVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTdSQNVNLRSWRHLFSYVQQDSPI---LAGti 424
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK-SILTNISDVHQNMGYCPQFDAIddlLTG-- 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 425 RENL-IYGLERHVTDEEIEEAAKLAnahhfIQSFEAqyeTMIGER-GINLSGGQRQRIAIARALLRNPQFLLLDEATASL 502
Cdd:TIGR01257 2030 REHLyLYARLRGVPAEEIEKVANWS-----IQSLGL---SLYADRlAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180
....*....|....*....|....
gi 1265182468 503 DSESEKLVQESLETVMKERTSLVI 526
Cdd:TIGR01257 2102 DPQARRMLWNTIVSIIREGRAVVL 2125
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
358-531 |
1.57e-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: 55.84 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 358 KKGEVTAFVGPSGAGKSTVFSLIE--------RFYEPSSGRIFLD---GTDSQNVNLR------SWRHLFSYVQQDSPIL 420
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKllegdvKVIVKPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 421 AGTIRENLIYGLERHVTDEEIEeaaKLANAHhfiqsfeaqyetmIGERGI-NLSGGQRQRIAIARALLRNPQFLLLDEAT 499
Cdd:cd03236 104 KGKVGELLKKKDERGKLDELVD---QLELRH-------------VLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 1265182468 500 ASLDS----ESEKLVQESLEtvmKERTSLVIAHRLS 531
Cdd:cd03236 168 SYLDIkqrlNAARLIRELAE---DDNYVLVVEHDLA 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
358-542 |
1.78e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.10 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 358 KKGEVTAFVGPSGAGKSTVFSLIE--------RFYEPSSGRIFLD---GTDSQN--VNLRSWR----HLFSYVQQDSPIL 420
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSgelkpnlgDYDEEPSWDEVLKrfrGTELQDyfKKLANGEikvaHKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 421 AGTIREnLiygLERhvTDEE--IEEAAKLANAHHFIqsfeaqyetmigERGI-NLSGGQRQRIAIARALLRNPQFLLLDE 497
Cdd:COG1245 177 KGTVRE-L---LEK--VDERgkLDELAEKLGLENIL------------DRDIsELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1265182468 498 ATASLD----SESEKLVQESLEtvmKERTSLVIAHRLSTV-INADQIVVI 542
Cdd:COG1245 239 PSSYLDiyqrLNVARLIRELAE---EGKYVLVVEHDLAILdYLADYVHIL 285
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
347-549 |
1.79e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 347 KPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVN-LRSWRHLFSYVQQD---SPILAG 422
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEErrsTGIYAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 423 -TIREN-LIYGLERHVTDEEIEEAAKL-ANAHHFIQSFEAQ---YETMIGergiNLSGGQRQRIAIARALLRNPQFLLLD 496
Cdd:PRK10982 341 lDIGFNsLISNIRNYKNKVGLLDNSRMkSDTQWVIDSMRVKtpgHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 497 EATASLDSESE-KLVQESLETVMKERTSLVIAHRLSTVIN-ADQIVVIEEGQVTG 549
Cdd:PRK10982 417 EPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLVAG 471
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
64-304 |
1.84e-08 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 56.00 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 64 GLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEmVSRITNDTTIVMNLLSTEMIDFVKN 143
Cdd:cd18583 42 VLLRFLQSGGGLGLLRSWLWIPVEQYSYRALSTAAFNHVMNLSMDFHDSKKSGE-VLKAIEQGSSINDLLEQILFQIVPM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 144 ILSIIVAIVILFTL-DVPMTLILLAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVD 222
Cdd:cd18583 121 IIDLVIAIVYLYYLfDPYMGLIVAVVMVLYVWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 223 ---SGLQSFQS---LYLFGvkrakiEAIITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLT 296
Cdd:cd18583 201 ryrEAVKNYQKaerKYLFS------LNLLNAVQSLILTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFA 274
|
....*...
gi 1265182468 297 RFVTSFQQ 304
Cdd:cd18583 275 TLYRSIQS 282
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
335-515 |
2.09e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.42 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDsqnvnLRSWRHlfSYVQ 414
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP-----IRRQRD--EYHQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 415 QDSPI--LAG-----TIRENLIY--GLERHVTDEEIEEAakLAnahhfiqsfeaqyetMIGERGI------NLSGGQRQR 479
Cdd:PRK13538 75 DLLYLghQPGiktelTALENLRFyqRLHGPGDDEALWEA--LA---------------QVGLAGFedvpvrQLSAGQQRR 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 1265182468 480 IAIARALLRNPQFLLLDEATASLDSESEKLVQESLE 515
Cdd:PRK13538 138 VALARLWLTRAPLWILDEPFTAIDKQGVARLEALLA 173
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
349-552 |
2.18e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.55 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 349 VLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIerfyepsSGRI---FLDG-------TDSQNVNLRswrhLFSYVQQD-- 416
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVL-------AGRKtggYIEGdirisgfPKKQETFAR----ISGYCEQNdi 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 417 -SPILagTIRENLIYG----LERHVTDEE----IEEAAKLAnahhfiqSFEAQYETMIGERGIN-LSGGQRQRIAIARAL 486
Cdd:PLN03140 964 hSPQV--TVRESLIYSaflrLPKEVSKEEkmmfVDEVMELV-------ELDNLKDAIVGLPGVTgLSTEQRKRLTIAVEL 1034
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 487 LRNPQFLLLDEATASLDSESEKLVQESLE-TVMKERTSLVIAHRLSTVI--NADQIVVIEE-GQVTGSGT 552
Cdd:PLN03140 1035 VANPSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQPSIDIfeAFDELLLMKRgGQVIYSGP 1104
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
340-556 |
2.39e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.90 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 340 VAFQYEDKP--VLQEVSFSAKKGEVTAFVGPSGAGKS----TVFSLIERFYEPSSGRIFLDGTDSQNVNLRSWRHL---- 409
Cdd:PRK11022 11 VHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLvgae 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 410 FSYVQQDsPILAgtirENLIYglerhVTDEEIEEAAKLanahHFIQSFEAQYE------TMIG----ERGIN-----LSG 474
Cdd:PRK11022 91 VAMIFQD-PMTS----LNPCY-----TVGFQIMEAIKV----HQGGNKKTRRQraidllNQVGipdpASRLDvyphqLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 475 GQRQRIAIARALLRNPQFLLLDEATASLD-SESEKLVQESLETVMKERTSLV-IAHRLSTVIN-ADQIVVIEEGQVTGSG 551
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLLELQQKENMALVlITHDLALVAEaAHKIIVMYAGQVVETG 236
|
....*
gi 1265182468 552 THKEL 556
Cdd:PRK11022 237 KAHDI 241
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
340-516 |
2.77e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.47 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 340 VAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSQNVNlRSwRHLfSY------V 413
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RS-RFM-AYlghlpgL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 414 QQDSPILagtirENLIYGLERHVTDEEIEEAAKLAnahhfIQSFEAQYETMIGErginLSGGQRQRIAIARALLRNPQFL 493
Cdd:PRK13543 94 KADLSTL-----ENLHFLCGLHGRRAKQMPGSALA-----IVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLW 159
|
170 180
....*....|....*....|...
gi 1265182468 494 LLDEATASLDSESEKLVQESLET 516
Cdd:PRK13543 160 LLDEPYANLDLEGITLVNRMISA 182
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
304-505 |
5.14e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 304 QTKGASeRI--FDILAEKEENYENGE------VLEQVGS--LRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGK 373
Cdd:PRK11819 285 QAKSKA-RLarYEELLSEEYQKRNETneifipPGPRLGDkvIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 374 STVFSLIERFYEPSSGRIFLDGTdsqnVNLrswrhlfSYVQQDSPILAG--TIRENLIYGLER-HVTDEEIeeaaklaNA 450
Cdd:PRK11819 364 STLFKMITGQEQPDSGTIKIGET----VKL-------AYVDQSRDALDPnkTVWEEISGGLDIiKVGNREI-------PS 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 451 HHFIQSFE---AQYETMIGergiNLSGGQRQRIAIARALLRNPQFLLLDEATASLDSE 505
Cdd:PRK11819 426 RAYVGRFNfkgGDQQKKVG----VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
345-570 |
8.40e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.64 E-value: 8.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 345 EDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLI--ERFYEPSSGRIFLDGTDSQNVNL--RSWRHLFSYVQQDSPI- 419
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPedRAGEGIFMAFQYPVEIp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 420 -------LAGTIRENLIY----GLERHVTDEEIEEAAKLANAHHFIQSfeaqyetmigeRGINL--SGGQRQRIAIARAL 486
Cdd:PRK09580 92 gvsnqffLQTALNAVRSYrgqePLDRFDFQDLMEEKIALLKMPEDLLT-----------RSVNVgfSGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 487 LRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLVIA---HRLSTVINADQIVVIEEGQVTGSGTH---KELlaSH 560
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDFtlvKQL--EE 238
|
250
....*....|
gi 1265182468 561 SFYRRLVEQQ 570
Cdd:PRK09580 239 QGYGWLTEQQ 248
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
349-546 |
9.48e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 9.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 349 VLQEVSFSAKKGEVTAFVGPSGAGKST----VFSLIERFYEPSSGRIFLDGTDSQNVnLRSWRHLFSYVQQDS---PILa 421
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETDvhfPHL- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 422 gTIRENLIYGLE------RHVTDEEIEEAAKLANAHHFIQSFEAQYETMIGE---RGInlSGGQRQRIAIARALLRNPQF 492
Cdd:TIGR00956 154 -TVGETLDFAARcktpqnRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 493 LLLDEATASLDSESeklvqeSLETVMKERTSLVIAHRLSTVI------NA----DQIVVIEEGQ 546
Cdd:TIGR00956 231 QCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVAiyqcsqDAyelfDKVIVLYEGY 288
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
350-546 |
1.42e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsQNVNLRSWRHLF----SYVQQD-SPILAGTI 424
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFKSSKEALengiSMVHQElNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 425 RENLIYGleRHVTDEEIEEAAKLANAHHFIQSfEAQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLds 504
Cdd:PRK10982 91 MDNMWLG--RYPTKGMFVDQDKMYRDTKAIFD-ELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL-- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1265182468 505 eSEKLVQESLETVMKERTS----LVIAHRLSTVIN-ADQIVVIEEGQ 546
Cdd:PRK10982 166 -TEKEVNHLFTIIRKLKERgcgiVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
343-549 |
3.46e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.87 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 343 QYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKsTVF--SLIERFY-EPSSGRIFLDGT--DSQNVNlRSWRHLFSYVQQDS 417
Cdd:NF040905 269 LHPERKVVDDVSLNVRRGEIVGIAGLMGAGR-TELamSVFGRSYgRNISGTVFKDGKevDVSTVS-DAIDAGLAYVTEDR 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 418 P----ILAGTIRENL-IYGL----ERHVTDE--EIEEAAKLANAHHfIQSFEAQYETMigergiNLSGGQRQRIAIARAL 486
Cdd:NF040905 347 KgyglNLIDDIKRNItLANLgkvsRRGVIDEneEIKVAEEYRKKMN-IKTPSVFQKVG------NLSGGNQQKVVLSKWL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265182468 487 LRNPQFLLLDEATASLDseseklVQESLE--TVMKE-----RTSLVIAHRLSTVIN-ADQIVVIEEGQVTG 549
Cdd:NF040905 420 FTDPDVLILDEPTRGID------VGAKYEiyTIINElaaegKGVIVISSELPELLGmCDRIYVMNEGRITG 484
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
343-550 |
3.51e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 343 QYEDKPVLQ----------EVSFSAKKGEVTAFVGPSGAGKStvfSLIERFY---EPSSGRIFLDGtdsQNVNLRSWR-- 407
Cdd:PRK15439 262 QAAGAPVLTvedltgegfrNISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNG---KEINALSTAqr 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 408 ------HLFSYVQQDSPILAGTIREN---LIYGLERHVTDEEiEEAAKLANAHHFIQSFEAQYETMIGergiNLSGGQRQ 478
Cdd:PRK15439 336 larglvYLPEDRQSSGLYLDAPLAWNvcaLTHNRRGFWIKPA-RENAVLERYRRALNIKFNHAEQAAR----TLSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 479 RIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTS-LVIAHRLSTVIN-ADQIVVIEEGQVTGS 550
Cdd:PRK15439 411 KVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAvLFISSDLEEIEQmADRVLVMHQGEISGA 484
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
61-312 |
4.44e-07 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 51.84 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 61 LIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPvsfYDQNRSGEMVSRItNDTTIVMNLLSTEMIDF 140
Cdd:cd18586 44 LTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVLELP---LESRPSGYWQQLL-RDLDTLRNFLTGPSLFA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 141 VKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKkE 220
Cdd:cd18586 120 FFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLG-N 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 221 VDSGLQSFQSLYL-FGVKRAKIEAIITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFV 299
Cdd:cd18586 199 LRRRWEARHAETLeLQIRASDLAGAISAIGKTLRMALQSLILGVGAYLVIDGELTIGALIAASILSGRALAPIDQLVGAW 278
|
250
....*....|...
gi 1265182468 300 TSFQQTKGASERI 312
Cdd:cd18586 279 KQLSAARQAYERL 291
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
64-177 |
5.77e-07 |
|
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: 51.32 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 64 GLLVLFA-AQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVk 142
Cdd:cd18606 39 GIYAGLGvLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFL- 117
|
90 100 110
....*....|....*....|....*....|....*
gi 1265182468 143 NILSIIVAIVILFTLDVPmtLILLAVIPVMFVLVM 177
Cdd:cd18606 118 YTLSSIIGTFILIIIYLP--WFAIALPPLLVLYYF 150
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
350-569 |
1.04e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGtdsQNVNLRSWRHL----FSYVQQDSPILAG-TI 424
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagIGIIHQELNLIPQlTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 425 RENLIYGLE------RHVTDEEIEEAAKLanahhfIQSFEAQY--ETMIGErginLSGGQRQRIAIARALLRNPQFLLLD 496
Cdd:PRK10762 97 AENIFLGREfvnrfgRIDWKKMYAEADKL------LARLNLRFssDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 497 EATASL-DSESeklvqESLETVMKE-----RTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKEL----LASHSFYRR 565
Cdd:PRK10762 167 EPTDALtDTET-----ESLFRVIRElksqgRGIVYISHRLKEIFEiCDDVTVFRDGQFIAEREVADLtedsLIEMMVGRK 241
|
....
gi 1265182468 566 LVEQ 569
Cdd:PRK10762 242 LEDQ 245
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
90-313 |
1.08e-06 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 50.56 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 90 VVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVI 169
Cdd:cd18585 66 LLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 170 pVMFVLVMPL--ARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITP 247
Cdd:cd18585 146 -LLAGVVIPLlfYRLGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQA 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 248 IISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMVPVGSLTRFVTSFQQTKGASERIF 313
Cdd:cd18585 225 LMILLSGLTVWLVLWLGAPLVQNGALDGALLAMLVFAVLASFEAVAPLPLAFQYLGETRAAARRLF 290
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
343-538 |
1.18e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 343 QYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLI----------------------ERFYEPS------SGRIFLD 394
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndltlfgrrrgsgETIWDIKkhigyvSSSLHLD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 395 ---GTDSQNVnlrswrhlfsyvqqdspILAG---TIrenliyGLERHVTDEEieeaAKLANahhfiqsfeaQYETMIGER 468
Cdd:PRK10938 349 yrvSTSVRNV-----------------ILSGffdSI------GIYQAVSDRQ----QKLAQ----------QWLDILGID 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 469 GI-------NLSGGQrQRIA-IARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKE-RTSLV------------IA 527
Cdd:PRK10938 392 KRtadapfhSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEgETQLLfvshhaedapacIT 470
|
250
....*....|.
gi 1265182468 528 HRLSTVINADQ 538
Cdd:PRK10938 471 HRLEFVPDGDI 481
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
335-543 |
2.14e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 335 LRFDKVAFQYEDKpVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLdgtdsQNVNLRSWRHLF-SYV 413
Cdd:PRK13541 2 LSLHQLQFNIEQK-NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY-----KNCNINNIAKPYcTYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 414 QQDSPI-LAGTIRENLIYGLERHVTDEEIEEAaklanahhfIQSFEAQYetMIGERGINLSGGQRQRIAIARALLRNPQF 492
Cdd:PRK13541 76 GHNLGLkLEMTVFENLKFWSEIYNSAETLYAA---------IHYFKLHD--LLDEKCYSLSSGMQKIVAIARLIACQSDL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 493 LLLDEATASLDSESEKLVQESLetVMKERTS--LVIAHRLSTVINADQIVVIE 543
Cdd:PRK13541 145 WLLDEVETNLSKENRDLLNNLI--VMKANSGgiVLLSSHLESSIKSAQILQLD 195
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
101-282 |
1.17e-05 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. 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: 350006 [Multi-domain] Cd Length: 289 Bit Score: 47.24 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 101 KLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVMPLA 180
Cdd:cd18562 78 HVITLPLSFHSQRGSGRLLRIMLRGTDALFGLWLGFFREHLAALVSLIVLLPVALWMNWRLALLLVVLAAVYAALNRLVM 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 181 RKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLylfgvkrakiEAIITPIIS-----TVMTA 255
Cdd:cd18562 158 RRTKAGQAAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGITRRL----------LAAQYPVLNwwalaSVLTR 227
|
170 180 190
....*....|....*....|....*....|..
gi 1265182468 256 V-----MIAIVGFGAYRVSEGFITAGELVAFV 282
Cdd:cd18562 228 AastltMVAIFALGAWLVQRGELTVGEIVSFV 259
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
74-191 |
1.37e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 47.21 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 74 VTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVI 153
Cdd:cd18602 65 ILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIV 144
|
90 100 110
....*....|....*....|....*....|....*...
gi 1265182468 154 LFTLdVPMTLILLAVIPVMFVLVMPLARkihKISREQQ 191
Cdd:cd18602 145 NAIV-TPYFLIALIPIIIVYYFLQKFYR---ASSRELQ 178
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
353-503 |
1.68e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.81 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 353 VSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDG--TDSQNVNLRswRHL------FSyvqqdspiLAG-- 422
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIATR--RRVgymsqaFS--------LYGel 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 423 TIRENL-----IYGLERHVTDEEIEEAaklanahhfIQSFE-AQYETMIGERginLSGGQRQRIAIARALLRNPQFLLLD 496
Cdd:NF033858 355 TVRQNLelharLFHLPAAEIAARVAEM---------LERFDlADVADALPDS---LPLGIRQRLSLAVAVIHKPELLILD 422
|
....*..
gi 1265182468 497 EATASLD 503
Cdd:NF033858 423 EPTSGVD 429
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
353-556 |
1.81e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 353 VSFSAKKGEVTAFVGPSGAGKSTvFSLIERFYEPSSGRifldgtdsQNVNLRSW----RHLFSYVQQDSPILAG-----T 423
Cdd:NF000106 32 VDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGR--------RPWRF*TWcanrRALRRTIG*HRPVR*GrresfS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 424 IRENLiYGLERHVtdeEIEEAAKLANAHHFIQSFeaQYETMIGERGINLSGGQRQRIAIARALLRNPQFLLLDEATASLD 503
Cdd:NF000106 103 GRENL-YMIGR*L---DLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 504 SESEKLVQESLETVMKERTSLVIAHRLSTVIN--ADQIVVIEEGQVTGSGTHKEL 556
Cdd:NF000106 177 PRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqlAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
334-558 |
1.85e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 334 SLRFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTvfslierFYEPSSGRIFLDGTDSQNVNLRSWRHLFSYV 413
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSA-------LARALAGELPLLSGERQSQFSHITRLSFEQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 414 QQdspILAGTIREN---LIYGLER---HVTDEEIEEAAKLANAhhfIQSFEAQY--ETMIGERGINLSGGQRQRIAIARA 485
Cdd:PRK10938 76 QK---LVSDEWQRNntdMLSPGEDdtgRTTAEIIQDEVKDPAR---CEQLAQQFgiTALLDRRFKYLSTGETRKTLLCQA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182468 486 LLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLV-IAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLA 558
Cdd:PRK10938 150 LMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ 224
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
129-312 |
2.48e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 46.33 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 129 VMNLLST------EMIDFVKNI----LSIIVAIVILFTLdvpM---TLILLAVIPVMFVLVMPLARKIHKISREQQDKMS 195
Cdd:cd18596 117 INNLMSVdanrisEFAAFLHLLvsapLQIVIAIVFLYRL---LgwsALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARD 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 196 KLTAFLAQMLSEIRLIKVSGSEKK-----------EvdsglqsfqslyLFGVKRAKIEAIITPIISTVMTaVMIAIVGFG 264
Cdd:cd18596 194 ARVQLVTEVLQGIRMIKFFAWERKweerileareeE------------LKWLRKRFLLDLLLSLLWFLIP-ILVTVVTFA 260
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265182468 265 AYRVSEGfitaGEL---VAFV-LYLFQIM-VPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18596 261 TYTLVMG----QELtasVAFTsLALFNMLrGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
436-552 |
2.60e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.07 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 436 VTDEEIEEAAKL----ANAHHFIQSFEA---QYETmIGERGINLSGGQRQRIAIARALLR---NPQFLLLDEATASLDSE 505
Cdd:cd03271 128 VLDMTVEEALEFfeniPKIARKLQTLCDvglGYIK-LGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFH 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 506 S-EKLVQESLETVMKERTSLVIAHRLSTVINADQIVVI------EEGQVTGSGT 552
Cdd:cd03271 207 DvKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLgpeggdGGGQVVASGT 260
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
338-559 |
3.92e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 338 DKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFL-----------DGTD--SQNVNLR 404
Cdd:PRK15064 323 ENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWsenanigyyaqDHAYdfENDLTLF 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 405 SWRHLFSYVQQDSPILAGTIRENLIyglerhvTDEEIEEAAKlanahhfiqsfeaqyetmigergiNLSGGQRQRIAIAR 484
Cdd:PRK15064 403 DWMSQWRQEGDDEQAVRGTLGRLLF-------SQDDIKKSVK------------------------VLSGGEKGRMLFGK 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 485 ALLRNPQFLLLDEATASLDSESEKLVQESLEtvMKERTSLVIAH------RLSTVInadqIVVIEEGQVTGSGTHKELLA 558
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMESIESLNMALE--KYEGTLIFVSHdrefvsSLATRI----IEITPDGVVDFSGTYEEYLR 525
|
.
gi 1265182468 559 S 559
Cdd:PRK15064 526 S 526
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
350-560 |
5.08e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.04 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTDSqnvnlrswrhLFSYVQQDSPILAGTirENL- 428
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAA----------LIAISSGLNGQLTGI--ENIe 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 429 IYGLERHVTDEEIEEAA----KLANAHHFIQSFEAQYetmigerginlSGGQRQRIAIARALLRNPQFLLLDEATASLDS 504
Cdd:PRK13545 108 LKGLMMGLTKEKIKEIIpeiiEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265182468 505 E-SEKLVQESLETVMKERTSLVIAHRLSTVIN-ADQIVVIEEGQVTGSGTHKELLASH 560
Cdd:PRK13545 177 TfTKKCLDKMNEFKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHY 234
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
351-564 |
9.55e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.75 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 351 QEVSFsakKGEVTAFVGPSGAGKSTVFSLIerfyepssgRIFLDGTDSQNVNLRswrhlfsyvqQDSPILAGTIRENLIY 430
Cdd:cd03240 16 SEIEF---FSPLTLIVGQNGAGKTTIIEAL---------KYALTGELPPNSKGG----------AHDPKLIREGEVRAQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 431 GLE-RHVTDEEIEEAAKLANAHHFIqsFEAQYET---MIGERGiNLSGGQRQ------RIAIARALLRNPQFLLLDEATA 500
Cdd:cd03240 74 KLAfENANGKKYTITRSLAILENVI--FCHQGESnwpLLDMRG-RCSGGEKVlasliiRLALAETFGSNCGILALDEPTT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265182468 501 SLDSESeklVQESLETVMKERTSLVIAhrlstvinadQIVVIeegqvtgsgTHKELLASH--SFYR 564
Cdd:cd03240 151 NLDEEN---IEESLAEIIEERKSQKNF----------QLIVI---------THDEELVDAadHIYR 194
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
336-558 |
1.29e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 336 RFDKVAFQYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIF-LDGtdsqnvNLRSWRHLFS--- 411
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGG------DMADARHRRAvcp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 412 ---YVQQD-----SPILagTIRENL-----IYGLERHVTDEEIEE---AAKLAnahhfiqSFEaqyetmigER--GiNLS 473
Cdd:NF033858 77 riaYMPQGlgknlYPTL--SVFENLdffgrLFGQDAAERRRRIDEllrATGLA-------PFA--------DRpaG-KLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 474 GGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKERTSLviahrlsTVINA----------DQIVVIE 543
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGM-------SVLVAtaymeeaerfDWLVAMD 211
|
250
....*....|....*
gi 1265182468 544 EGQVTGSGTHKELLA 558
Cdd:NF033858 212 AGRVLATGTPAELLA 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
360-503 |
1.88e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 360 GEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDGTdsqnvnlrsWRhlFSYVQQDSPILAGTIRENLIYGlerhvtDE 439
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN---------WQ--LAWVNQETPALPQPALEYVIDG------DR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 440 E---IEEAAKLANAH---HFIQSFEAQYETM----IGERGINL------------------SGGQRQRIAIARALLRNPQ 491
Cdd:PRK10636 90 EyrqLEAQLHDANERndgHAIATIHGKLDAIdawtIRSRAASLlhglgfsneqlerpvsdfSGGWRMRLNLAQALICRSD 169
|
170
....*....|..
gi 1265182468 492 FLLLDEATASLD 503
Cdd:PRK10636 170 LLLLDEPTNHLD 181
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
63-189 |
2.19e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 43.46 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 63 AGLLVLFaaqMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVK 142
Cdd:cd18601 66 AGLTAAT---FVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQ 142
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1265182468 143 NILsIIVAIVILFTldVPMTLILLAVIPVMFVLVMpLARKIHKISRE 189
Cdd:cd18601 143 LLL-QVVGVVLLAV--VVNPWVLIPVIPLVILFLF-LRRYYLKTSRE 185
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
473-503 |
2.25e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 2.25e-04
10 20 30
....*....|....*....|....*....|.
gi 1265182468 473 SGGQRQRIAIARALLRNPQFLLLDEATASLD 503
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
98-312 |
2.65e-04 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 43.36 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 98 VWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLlSTEMIDFVKNILSIIVAIVILFTLDVPMTLILLAVIPVMFVLVM 177
Cdd:cd18559 77 LYHKALRSPISFFERTPSGELVNLFSKDLDRVDSM-APQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 178 PLARKIHKISREQQDKMSKLTAFLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLFGVKRAKIEAIITPIisTVMTAVM 257
Cdd:cd18559 156 VYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRL--WCVGPCI 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182468 258 IAIVGFGAY-RVSEGFITAGELVAFVLYLFQIMV-PVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18559 234 VLFASFFAYvSRHSLAGLVALKVFYSLALTTYLNwPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
70-174 |
3.03e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 42.85 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 70 AAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIV 149
Cdd:cd18603 52 LGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVIS 131
|
90 100
....*....|....*....|....*
gi 1265182468 150 AIVILfTLDVPmtLILLAVIPVMFV 174
Cdd:cd18603 132 TLVVI-SISTP--IFLVVIIPLAIL 153
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
25-304 |
3.70e-04 |
|
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group represents the transmembrane (TM) domain of an active lipid-linked oligosaccharides flippase PglK (protein glycosylation K), which is a homodimeric ABC transporter that flips a lipid-linked oligosaccharide that serves as a glycan donor in N-linked protein glycosylation. Pglk mediates the ATP-dependent translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate across the cell membrane; this is an essential step during the N-linked protein glycosylation pathway. This TM subunit exhibits 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. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 349997 Cd Length: 300 Bit Score: 42.92 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 25 LLISFILALINTGAslsiplvIKEVMEKIAIGVSPQLI--------------------------AGLLVLFAAQMVTSAV 78
Cdd:cd18553 1 LLFSIFVSLIETIG-------ISAIMPFISVASNFSLIlsnkyykfiynffgfsspvnfviffgIILIGFYIFRSLYNIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 79 SLYLLAQVGQGVVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTeMIDFVKNILSIIVAIVILFTLD 158
Cdd:cd18553 74 YTYLLNRFSFGRYHSIAYRLFKNYLKLNYQDFTNKNSSDLSKSIINEASNLSQVIQS-FLFILSEIFVILFIYSLLLYVN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 159 VPMTLILLAVIPVM-FVLVMPLARKIHK---ISREQQDKMSKLtafLAQMLSEIRLIKVSGSEKKEVDSGLQSFQSLYLF 234
Cdd:cd18553 153 WKITLVLTLFLGLNvFFITKIVSKKIKKqgkKREESQKKFYKI---LSETFGNFKIIKLKSNEKEILKNFSQASLKFAKA 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 235 GVKRAKIEAIITPIISTVMTAVMIAIVGFGAYRVSEGFITAGELVAFVLYLFQIMvPvgSLTRFVTSFQQ 304
Cdd:cd18553 230 NIINQTLQTVPRLILETIGFSLLILIVLYILYKYSDASAVLPIISMYALALYRLL-P--SVNRILSSYNQ 296
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
435-556 |
5.59e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.08 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 435 HVTDEEIEEAAKLANAHHFIqsfeAQY-ETM---------IGERGINLSGGQRQRIAIARALLR---NPQFLLLDEATAS 501
Cdd:TIGR00630 787 DVLDMTVEEAYEFFEAVPSI----SRKlQTLcdvglgyirLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTG 862
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265182468 502 LDSESEKLVQESLET-VMKERTSLVIAHRLSTVINADQIVVI------EEGQVTGSGTHKEL 556
Cdd:TIGR00630 863 LHFDDIKKLLEVLQRlVDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
343-528 |
7.02e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 343 QYEDKPVLQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLD-----GTDSQNvnlrswrhLFSYVQQ-- 415
Cdd:PRK15064 10 QFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlGKLRQD--------QFAFEEFtv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 416 -DSPILAGT-----IRE-NLIYGLErHVTDEEIEEAAKLanahhfiqsfEAQYETMIG------------ERGI------ 470
Cdd:PRK15064 82 lDTVIMGHTelwevKQErDRIYALP-EMSEEDGMKVADL----------EVKFAEMDGytaearagelllGVGIpeeqhy 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 471 ----NLSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLvqesLETVMKERTS--LVIAH 528
Cdd:PRK15064 151 glmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRW----LEDVLNERNStmIIISH 210
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
115-312 |
7.05e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350039 [Multi-domain] Cd Length: 290 Bit Score: 41.69 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 115 SGEMVSRITNDTTIVMNLLStemidFVKNILS----IIVAIVILF-TLDVPMtlilLAVIPVMFVLV---MPLARKIHKI 186
Cdd:cd18595 94 VGEIVNLMSVDAQRIQDLVP-----YLNMLWSaplqIILALYFLWqTLGPSV----LAGLGVMILLIplnAVLARKIKKL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 187 SREQ---QDKMSKLtafLAQMLSEIRLIKVSGSEKkevdsglqSFQS---------LYLFgvKRAkieAIITPIISTVMT 254
Cdd:cd18595 165 QVKQmklKDERIKL---MNEILNGIKVLKLYAWEE--------SFEKkilkirekeLKLL--KKA---AYLNAVSSFLWT 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265182468 255 A--VMIAIVGFGAYRVSEG--FITAGelVAFV-LYLFQIM-VPVGSLTRFVTSFQQTKGASERI 312
Cdd:cd18595 229 CapFLVSLATFATYVLSDPdnVLDAE--KAFVsLSLFNILrFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
31-183 |
7.82e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). 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: 350054 [Multi-domain] Cd Length: 290 Bit Score: 41.75 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 31 LALI-NTGASLSIPLVIKEVMEKiaiGVSPQLIAGLLVLFAAQMVTSAVSLYLLA----QVGQGVVKELRHKVWNKLIKL 105
Cdd:cd18781 7 ISLLaNIAFVFSIANLLQKLLEG---KLTTASLLIVLGILAIAIIVRFICTRLASrasyRASADVKKTLREKIYDKLLRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 106 PVSFYDQNRSGEMVSritndttivmnlLSTEMID------------FVKNILSIIVAIVILFTLDVPMTLILLA---VIP 170
Cdd:cd18781 84 GPSYQEKVSTAEVVQ------------LSVEGVEqleiyfgrylpqFFYSMLAPLTLFVVLAPINWKAALVLLIcvpLIP 151
|
170
....*....|...
gi 1265182468 171 VMFVLVMPLARKI 183
Cdd:cd18781 152 ISIIAVQKIAKKL 164
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
358-415 |
1.02e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 41.90 E-value: 1.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 358 KKGEVTAFVGPSGAGKSTVFS-LIERFYEPSSGR-IFLDGTDSQNVNLRswRHLFSYVQQ 415
Cdd:PRK12727 348 ERGGVIALVGPTGAGKTTTIAkLAQRFAAQHAPRdVALVTTDTQRVGGR--EQLHSYGRQ 405
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
472-567 |
1.05e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.33 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 472 LSGGQRQRIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKER--TSLVIAHRLSTVIN-ADQIVVIEEGQVT 548
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKINVLYCGQTV 238
|
90 100
....*....|....*....|.
gi 1265182468 549 GSGTHKELLAS--HSFYRRLV 567
Cdd:PRK15093 239 ETAPSKELVTTphHPYTQALI 259
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
90-177 |
1.15e-03 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350044 [Multi-domain] Cd Length: 324 Bit Score: 41.33 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 90 VVKELRHKVWNKLIKLPVSFYDQNRSGEMVSRITNDTTIVMNLLSTEMIDFVKNILSIIVAIVILFTLdvpMTLILLAVI 169
Cdd:cd18600 101 VSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSIL---QPYIFLATV 177
|
....*...
gi 1265182468 170 PVMFVLVM 177
Cdd:cd18600 178 PVIIAFIV 185
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
350-395 |
4.16e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 4.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1265182468 350 LQEVSFSAKKGEVTAFVGPSGAGKSTVFSLIERFYEPSSGRIFLDG 395
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
351-540 |
4.65e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.11 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 351 QEVSFSAkkGEVTAFVGPSGAGKSTVFSLIerfyepssgrIFLDGTDSQNVNLRSWRHLFSYVQQDSPILAGTIrenliy 430
Cdd:cd03227 14 NDVTFGE--GSLTIITGPNGSGKSTILDAI----------GLALGGAQSATRRRSGVKAGCIVAAVSAELIFTR------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 431 glerhvtdeeieeaaklanahhfiqsfeaqyetmigergINLSGGQRQRIAIARAL----LRNPQFLLLDEATASLDSES 506
Cdd:cd03227 76 ---------------------------------------LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRD 116
|
170 180 190
....*....|....*....|....*....|....*
gi 1265182468 507 -EKLVQESLETVMKERTSLVIAHRLSTVINADQIV 540
Cdd:cd03227 117 gQALAEAILEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
441-561 |
6.39e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 441 IEEAAKLanaHHFIQSFEAQYETMI---------GERGINLSGGQRQRIAIARALL---RNPQFLLLDEATASLDSESEK 508
Cdd:PRK00635 1663 IEEVAET---FPFLKKIQKPLQALIdnglgylplGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKS 1739
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 509 LVQESLETVMKERTSLV-IAHRLSTVINADQIVVI------EEGQVTGSGTHKELLASHS 561
Cdd:PRK00635 1740 ALLVQLRTLVSLGHSVIyIDHDPALLKQADYLIEMgpgsgkTGGKILFSGPPKDISASKD 1799
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
359-375 |
8.98e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.76 E-value: 8.98e-03
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
30-218 |
9.29e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 38.30 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 30 ILALINTGASLSIPLVIKEVMEKIAIGVSPQ-----LIAGLLVLFAAQMVTSAVSLYLLAQVGQGVVKELRHKVWNKLIK 104
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEPLsdgylYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKALR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 105 LPVSFYDQNRSGEMVSRITNDTTIVMNLLSTeMIDFVKNILSIIVAIVILFtLDVPMTLIL-LAVIPVMFVLVMPLARKI 183
Cdd:cd18598 84 VRSSSLSKFSTGEIVNLMSTDADRIVNFCPS-FHDLWSLPLQIIVALYLLY-QQVGVAFLAgLVFALVLIPINKWIAKRI 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1265182468 184 HKISRE---QQDKMSKLTaflAQMLSEIRLIKVSGSEK 218
Cdd:cd18598 162 GALSEKmmkHKDARVKLM---TEILSGIRVIKLLAWER 196
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
471-559 |
9.67e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.11 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182468 471 NLSGGQRQ------RIAIARALLRNPQFLLLDEATASLDSESEKLVQESLETVMKErtslviahrlSTVInaDQIVVIEE 544
Cdd:PRK01156 801 SLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKD----------SSDI--PQVIMISH 868
|
90
....*....|....*
gi 1265182468 545 gqvtgsgtHKELLAS 559
Cdd:PRK01156 869 --------HRELLSV 875
|
|
| |
