|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
768-1328 |
6.26e-103 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 339.45 E-value: 6.26e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 768 FKSIWK-VKKLRWFFLLGLLTSLIQGASVPIFAYVISKCLN-LFMQIDPSiGVAFWSSMVLVVAAGSGASYFFSHYIFS- 844
Cdd:COG1132 9 LRRLLRyLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDaLLAGGDLS-ALLLLLLLLLGLALLRALLSYLQRYLLAr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 845 ISAKIWCDHYRLLAVKVLfTQDQAWFDQIENYplVLSKILVNNISDMRNMISSLIEEVFIAFTMAIIGIAWSFATGWRLA 924
Cdd:COG1132 88 LAQRVVADLRRDLFEHLL-RLPLSFFDRRRTG--DLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 925 AVLVAVSPILCLTSRMFSYIYVSTERMCQDVVISTTSILHKTIVNLDTIKGYSVLSFFRENHKNSLRKSWEAFKRRAFWT 1004
Cdd:COG1132 165 LIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1005 SLGFAINNSLLYFVRALLFYCSSIFISKEFYTVEQMVQVLSLATFTLLMASTCIMSLPNVSASRIATSRVLKLSSLKPGN 1084
Cdd:COG1132 245 ALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1085 LHKSGYLKFPLV-GKIEFDGVSFAYPDSERnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYIDG 1161
Cdd:COG1132 325 PDPPGAVPLPPVrGEIEFENVSFSYPGDRP---VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYdPTSgRILIDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1162 YPLTNIDTNWLLKKVAIVDQKPHLLGSTILESLLYGV-DRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQ 1240
Cdd:COG1132 402 VDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1241 IQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS--CTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDEL 1318
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMkgRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
570
....*....|
gi 162312251 1319 MNRHTHFWKL 1328
Cdd:COG1132 562 LARGGLYARL 571
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
103-649 |
2.41e-100 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 332.51 E-value: 2.41e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 103 LIFGTLIFTCLSAALEPLMTWTTGKVFDALSQyatsqitlGKMISLINFNSLLITIFGLASCVFSFGVRFLWQYLSAIAG 182
Cdd:COG1132 22 LLILALLLLLLSALLELLLPLLLGRIIDALLA--------GGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 183 KRARSLCFHVLSSKSSTFYSltESKSG-----LVNSVDRCIQFYekSISLPMFhiAENLAISLSCLIISFRYSWSLTLVV 257
Cdd:COG1132 94 ADLRRDLFEHLLRLPLSFFD--RRRTGdllsrLTNDVDAVEQFL--AHGLPQL--VRSVVTLIGALVVLFVIDWRLALIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 258 LASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSFLDAFQ 337
Cdd:COG1132 168 LLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 338 GGVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTVFGSCLSVASSLQQILPAIPDLIKGKFSSHFIKTLCESHDPIEAA 417
Cdd:COG1132 248 FPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 418 KRSAAKIKsisFERGFRFDNVSFAYPSrDENLFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDD 497
Cdd:COG1132 328 PGAVPLPP---VRGEIEFENVSFSYPG-DRPVLK--DISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 498 FPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKE--ASLSGGQ 575
Cdd:COG1132 402 VDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGErgVNLSGGQ 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 576 QQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQR 649
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
751-1331 |
2.92e-86 |
|
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: 297.13 E-value: 2.92e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 751 TFHLFDDKEHACSLTLIFKSIWKVKK-LRWFFLLGLLTSLIqGASVPIFAYVIskclnlfmqID---PSIGVAFWSSMVL 826
Cdd:COG2274 131 TPEFDKRGEKPFGLRWFLRLLRRYRRlLLQVLLASLLINLL-ALATPLFTQVV---------IDrvlPNQDLSTLWVLAI 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 827 VVAAGSGASYFFSH---YIF---------SISAKIWcdhYRLLAVKVLFTQDQAWFDqienyplvlskiLVNNISDM--- 891
Cdd:COG2274 201 GLLLALLFEGLLRLlrsYLLlrlgqridlRLSSRFF---RHLLRLPLSFFESRSVGD------------LASRFRDVesi 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 892 RNMISSLIEEVFIAFTMAIIGIAWSFATGWRLAAVLVAVSPILCLTSRMFSYIYVSTERMCQDVVISTTSILHKTIVNLD 971
Cdd:COG2274 266 REFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIE 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 972 TIKGYSVLSFFRENHKNSLRKSWEAFKRRAFWTSLGFAINNSLLYFVRALLFYCSSIFISKEFYTVEQMVQVLSLATftL 1051
Cdd:COG2274 346 TIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSG--R 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1052 LMAStcIMSLPNVSAS----RIATSRVLKLSSLKPGNLHKSGYLKFP-LVGKIEFDGVSFAYPDSERNhlALNNVSLSIE 1126
Cdd:COG2274 424 FLAP--VAQLIGLLQRfqdaKIALERLDDILDLPPEREEGRSKLSLPrLKGDIELENVSFRYPGDSPP--VLDNISLTIK 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1127 AREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYIDGYPLTNIDTNWLLKKVAIVDQKPHLLGSTILESLLYG-VDRDIN 1203
Cdd:COG2274 500 PGERVAIVGRSGSGKSTLLKLLLGLYePTSgRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGdPDATDE 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1204 SVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS- 1282
Cdd:COG2274 580 EIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLk 659
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 162312251 1283 -CTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKLIHR 1331
Cdd:COG2274 660 gRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
87-656 |
2.19e-82 |
|
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: 285.96 E-value: 2.19e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 87 SSWSDFFYLF--HFSDIPLIFGTLIFTCLSAALEPLMTwttGKVFDalsqyatsQITLGKMISLINfnsLLITIFGLASc 164
Cdd:COG2274 142 FGLRWFLRLLrrYRRLLLQVLLASLLINLLALATPLFT---QVVID--------RVLPNQDLSTLW---VLAIGLLLAL- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 165 VFSFGVRFLWQYLSAIAGKR-----ARSLCFHVLSSKSSTFysltESKSG-----LVNSVDRCIQFyeksISLPMFHIAE 234
Cdd:COG2274 207 LFEGLLRLLRSYLLLRLGQRidlrlSSRFFRHLLRLPLSFF----ESRSVgdlasRFRDVESIREF----LTGSLLTALL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 235 NLAISLSCLIISFRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYR 314
Cdd:COG2274 279 DLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRR 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 315 YFADACSTSSKSFLRFSFLDAFQGGVSQFFlySVFFQG--LWFGNHLATTKRVNVGQVV-------TVFGSCLSVASSLQ 385
Cdd:COG2274 359 RWENLLAKYLNARFKLRRLSNLLSTLSGLL--QQLATValLWLGAYLVIDGQLTLGQLIafnilsgRFLAPVAQLIGLLQ 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 386 QILPAIPDLIKgkfSSHFIKTlceshdPIEAAkRSAAKIKSISFERGFRFDNVSFAYPSRDENLFSliNVSVFIPFGELV 465
Cdd:COG2274 437 RFQDAKIALER---LDDILDL------PPERE-EGRSKLSLPRLKGDIELENVSFRYPGDSPPVLD--NISLTIKPGERV 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 466 HIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIIMRNENASESDFEEV 545
Cdd:COG2274 505 AIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEA 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 546 CRLALVDEFALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTL 623
Cdd:COG2274 585 ARLAGLHDFIEALPMGYDTVVGEggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVI 664
|
570 580 590
....*....|....*....|....*....|...
gi 162312251 624 VITHDMSQINNDELVLVIDKGHLIQRCARKELV 656
Cdd:COG2274 665 IIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
771-1082 |
7.80e-76 |
|
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: 254.30 E-value: 7.80e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 771 IWKVKKLRWFFLLGLLTSLIQGASVPIFAYVISKCLNLFMQIDPSI---GVAFWSSMVLVVAAGSGASYFFSHYIFSISA 847
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDElrsEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 848 KIWCDHYRLLAVKVLFTQDQAWFDQIENYPLVLSKILVNNISDMRNMISSLIEEVFIAFTMAIIGIAWSFATGWRLAAVL 927
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 928 VAVSPILCLTSRMFSYIYVSTERMCQDVVISTTSILHKTIVNLDTIKGYSVLSFFRENHKNSLRKSWEAFKRRAFWTSLG 1007
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1008 FAINNSLLYFVRALLFYCSSIFISKEFYTVEQMVQVLSLATFTLLMASTCIMSLPNVSASRIATSRVLKLSSLKP 1082
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKP 315
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1099-1322 |
1.08e-70 |
|
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: 248.13 E-value: 1.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTNIDTNWLLKKV 1176
Cdd:COG4988 337 IELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYsgSILINGVDLSDLDPASWRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHLLGSTILESL-LYGVDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPR 1255
Cdd:COG4988 414 AWVPQNPYLFAGTIRENLrLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1256 LLILDECTSALDSKSSLLLEKTIQNLS--CTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRH 1322
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLAkgRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
434-645 |
4.85e-69 |
|
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: 229.19 E-value: 4.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:cd03228 2 EFKNVSFSYPGRPKPVLK--DVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFDMTIRENIimrnenasesdfeevcrlalvdefaltfdqsydtpckeasLSGGQQQRIALARALLRDTEILI 593
Cdd:cd03228 80 YVPQDPFLFSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 162312251 594 LDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGH 645
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
249-1327 |
5.29e-68 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 252.64 E-value: 5.29e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 249 YSWSL------TLVVLASYPIIiLVVGFInsfLSSAYEKDRKSS----EKAASILEKSISAIQTVIFHSMQDTEYRYFAD 318
Cdd:PTZ00265 189 YIWSLfknarlTLCITCVFPLI-YICGVI---CNKKVKINKKTSllynNNTMSIIEEALVGIRTVVSYCGEKTILKKFNL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 319 ACSTSSKSFLRFSFLDAFQGGVSQFFLYSVFFQGLWFGNHLATTKRVNV--------GQVVTVFGSCLSVASSLQQILPA 390
Cdd:PTZ00265 265 SEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQqpnndfhgGSVISILLGVLISMFMLTIILPN 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 391 IPDLIKGKFSSHFIKTLCeSHDPIEAAKRSAAKIKSIsfeRGFRFDNVSFAYPSR-DENLFSLINVSvfIPFGELVHIIG 469
Cdd:PTZ00265 345 ITEYMKSLEATNSLYEII-NRKPLVENNDDGKKLKDI---KKIQFKNVRFHYDTRkDVEIYKDLNFT--LTEGKTYAFVG 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 470 PSGSGKSTFISLLLRYFSPTYGNIYLDD-FPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIIMR--------------N 534
Cdd:PTZ00265 419 ESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyN 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 535 ENAS-------------------------------------------ESDFEEVCRLALVDEFALTFDQSYDT--PCKEA 569
Cdd:PTZ00265 499 EDGNdsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikDSEVVDVSKKVLIHDFVSALPDKYETlvGSNAS 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 570 SLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHR--KGKTTLVITHDMSQINNDELVLVI---DKG 644
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrERG 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 645 HLIQRCARKELVLFEDFENNVSIDEK----------------------------VLKEEADNPFILPNEESLLEKYWINY 696
Cdd:PTZ00265 659 STVDVDIIGEDPTKDNKENNNKNNKDdnnnnnnnnnnkinnagsyiieqgthdaLMKNKNGIYYTMINNQKVSSKKSSNN 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 697 NESFSQLSRESLFTSLESPFT--DIESPTIVSRRKIVEQRKLRMEKESFQETNVDQTF----HLFDDKEHA-CSLTLIFK 769
Cdd:PTZ00265 739 DNDKDSDMKSSAYKDSERGYDpdEMNGNSKHENESASNKKSCKMSDENASENNAGGKLpflrNLFKRKPKApNNLRIVYR 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 770 SIWKVKKlrwFFLLGLLTSLIQGASVPIFAYVISKCLN-LFMQIDPSIGVAFWSSMVLVVAAGSGASYFFSHYIFS-ISA 847
Cdd:PTZ00265 819 EIFSYKK---DVTIIALSILVAGGLYPVFALLYAKYVStLFDFANLEANSNKYSLYILVIAIAMFISETLKNYYNNvIGE 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 848 KIWCDHYRLLAVKVLFtQDQAWFDQIENYPLVLSKI-----------LVNNISDMRNMISSLIEEVFIAFTMAII----- 911
Cdd:PTZ00265 896 KVEKTMKRRLFENILY-QEISFFDQDKHAPGLLSAHinrdvhllktgLVNNIVIFTHFIVLFLVSMVMSFYFCPIvaavl 974
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 912 -GIAWSFATGWRLAAVLVAVSPILCLTSRMFS--YIYVSTERMCQDvvisTTSILHKTIVNLDTIKGYSVLSFFRENHKN 988
Cdd:PTZ00265 975 tGTYFIFMRVFAIRARLTANKDVEKKEINQPGtvFAYNSDDEIFKD----PSFLIQEAFYNMNTVIIYGLEDYFCNLIEK 1050
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 989 SLRKSWEAFKRRAFWTSLGFAINNSLLYFVRALLFYCSSIFISKEFYTVEQMVQVLSLATFTLLMASTcIMSLPNVSA-S 1067
Cdd:PTZ00265 1051 AIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGK-LMSLKGDSEnA 1129
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1068 RIATSRVLKLSSLKPG-NLHKSGYLKFP----LVGKIEFDGVSFAYPdSERNHLALNNVSLSIEAREKVAIVGISGSGKS 1142
Cdd:PTZ00265 1130 KLSFEKYYPLIIRKSNiDVRDNGGIRIKnkndIKGKIEIMDVNFRYI-SRPNVPIYKDLTFSCDSKKTTAIVGETGSGKS 1208
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1143 TLVELLRKTYP--------------------------------------------------------SEDIYIDGYPLTN 1166
Cdd:PTZ00265 1209 TVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICD 1288
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1167 IDTNWLLKKVAIVDQKPHLLGSTILESLLYGV-DRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLA 1245
Cdd:PTZ00265 1289 YNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKeDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIA 1368
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1246 FARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS----CTVLIITHQPSLMKLADRIIVMDS-----GIVKESGSFD 1316
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdkadKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHE 1448
|
1290
....*....|.
gi 162312251 1317 ELMNRHTHFWK 1327
Cdd:PTZ00265 1449 ELLSVQDGVYK 1459
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1099-1332 |
9.07e-68 |
|
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: 228.19 E-value: 9.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPdSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYIDGYPLTNIDTNWLLKKV 1176
Cdd:cd03249 1 IEFKNVSFRYP-SRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYdPTSgEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHLLGSTILESLLYGV-DRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPR 1255
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKpDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1256 LLILDECTSALDSKSSLLLEKTIQNLSC--TVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKLIHRG 1332
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKgrTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
434-656 |
3.77e-67 |
|
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: 226.27 E-value: 3.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFsLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:cd03249 2 EFKNVSFRYPSRPDVPI-LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEI 591
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGErgSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 592 LILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELV 656
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
434-656 |
8.15e-67 |
|
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: 236.58 E-value: 8.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDenlFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:COG4988 338 ELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEI 591
Cdd:COG4988 415 WVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEggRGLSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 592 LILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELV 656
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
434-656 |
1.75e-66 |
|
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: 235.82 E-value: 1.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:COG4987 335 ELEDVSFRYPGAGRPVLD--GLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEI 591
Cdd:COG4987 413 VVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEggRRLSGGERRRLALARALLRDAPI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 592 LILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELV 656
Cdd:COG4987 493 LLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
767-1328 |
8.48e-65 |
|
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: 231.14 E-value: 8.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 767 IFKSIWK-VKKLRWFFLLGLLTSLIQGASVPIFAYVISKCLN-LFMQIDPsiGVAFWSSMVLV-VAAGSGASYFFSHYIF 843
Cdd:TIGR02203 1 TFRRLWSyVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDdGFGGRDR--SVLWWVPLVVIgLAVLRGICSFVSTYLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 844 S-ISAKIWCDHYRLLAVKvLFTQDQAWFDqieNYPlvlSKILVNNISDMRNMISSLIEEVFIAF---TMAIIG-IAWSFA 918
Cdd:TIGR02203 79 SwVSNKVVRDIRVRMFEK-LLGLPVSFFD---RQP---TGTLLSRITFDSEQVASAATDAFIVLvreTLTVIGlFIVLLY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 919 TGWRLAAVLVAVSPILCLTSRMFSYIYVSTERMCQDvvisttSILHKTIVNLDTIKGYSVLSFFrenhknslrkSWEAFK 998
Cdd:TIGR02203 152 YSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQN------SMGQVTTVAEETLQGYRVVKLF----------GGQAYE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 999 RRAFwtslGFAINNSLLYFVR---------ALLFYCSSIFISKEFYTV--EQMVQVLSLATFTLLMASTCIM-----SLP 1062
Cdd:TIGR02203 216 TRRF----DAVSNRNRRLAMKmtsagsissPITQLIASLALAVVLFIAlfQAQAGSLTAGDFTAFITAMIALirplkSLT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1063 NVSASR----IATSRVLKLSSlKPGNLHKSGYLKFPLVGKIEFDGVSFAYPDSERNhlALNNVSLSIEAREKVAIVGISG 1138
Cdd:TIGR02203 292 NVNAPMqrglAAAESLFTLLD-SPPEKDTGTRAIERARGDVEFRNVTFRYPGRDRP--ALDSISLVIEPGETVALVGRSG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1139 SGKSTLVELLRKTY-PSE-DIYIDGYPLTNIDTNWLLKKVAIVDQKPHLLGSTILESLLYGVDRDINS--VMDALDKTYM 1214
Cdd:TIGR02203 369 SGKSTLVNLIPRFYePDSgQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRaeIERALAAAYA 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1215 TEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL--SCTVLIITHQP 1292
Cdd:TIGR02203 449 QDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLmqGRTTLVIAHRL 528
|
570 580 590
....*....|....*....|....*....|....*.
gi 162312251 1293 SLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKL 1328
Cdd:TIGR02203 529 STIEKADRIVVMDDGRIVERGTHNELLARNGLYAQL 564
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1046-1331 |
1.09e-64 |
|
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: 230.81 E-value: 1.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1046 LATFTLL-MAST-CIMSLP----NVSASRIATSRVLKLSSLKPGNLHKSGYLKFPLVGKIEFDGVSFAYPDSERNhlALN 1119
Cdd:COG4987 275 LALLVLAaLALFeALAPLPaaaqHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRP--VLD 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1120 NVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTNIDTNWLLKKVAIVDQKPHLLGSTILESLLYG 1197
Cdd:COG4987 353 GLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQsgSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1198 VDR-DINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEK 1276
Cdd:COG4987 433 RPDaTDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLA 512
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 1277 TIQNLSC--TVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKLIHR 1331
Cdd:COG4987 513 DLLEALAgrTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
243-655 |
4.36e-64 |
|
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: 229.22 E-value: 4.36e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 243 LIISFRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACST 322
Cdd:TIGR02203 146 FIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 323 SSKSFLRFSFLDAFQGGVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTVFGSCLSVASSLQQILPAIPDLIKGKFSSH 402
Cdd:TIGR02203 226 NRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAE 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 403 FIKTLCESHDPIEAAKRSAAKIksisfeRG-FRFDNVSFAYPSRDENLFSliNVSVFIPFGELVHIIGPSGSGKSTFISL 481
Cdd:TIGR02203 306 SLFTLLDSPPEKDTGTRAIERA------RGdVEFRNVTFRYPGRDRPALD--SISLVIEPGETVALVGRSGSGKSTLVNL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 482 LLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIIM-RNENASESDFEEVCRLALVDEFALTFDQ 560
Cdd:TIGR02203 378 IPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYgRTEQADRAEIERALAAAYAQDFVDKLPL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 561 SYDTPCKE--ASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELV 638
Cdd:TIGR02203 458 GLDTPIGEngVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
|
410
....*....|....*..
gi 162312251 639 LVIDKGHLIQRCARKEL 655
Cdd:TIGR02203 538 VVMDDGRIVERGTHNEL 554
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1099-1307 |
5.98e-64 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 214.55 E-value: 5.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDseRNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSED--IYIDGYPLTNIDTNWLLKKV 1176
Cdd:cd03228 1 IEFKNVSFSYPG--RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSgeILIDGVDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHLLGSTILESLLygvdrdinsvmdaldktymteviqnlpngldtpllefsknfSGGQIQRLAFARALLRNPRL 1256
Cdd:cd03228 79 AYVPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 162312251 1257 LILDECTSALDSKSSLLLEKTIQNLSC--TVLIITHQPSLMKLADRIIVMDSG 1307
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKgkTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
103-404 |
9.13e-64 |
|
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: 219.27 E-value: 9.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 103 LIFGTlIFTCLSAALEPLMTWTTGKVFDALSQYATSQITLGKMISLINFNSLLITIFGLASCVFSFGVRFLWQYLSAIAG 182
Cdd:cd18577 1 LIIGL-LAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 183 KRARSLCFHVLSSKSSTFYSLTESkSGLVNSVDRCIQFYEKSISLPMFHIAENLAISLSCLIISFRYSWSLTLVVLASYP 262
Cdd:cd18577 80 RRIRKRYLKALLRQDIAWFDKNGA-GELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 263 IIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSFLDAFQGGVSQ 342
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 343 FFLYSVFFQGLWFGNHLATTKRVNVGQVVTVFGSCLSVASSLQQILPAIPDLIKGKFSSHFI 404
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
235-656 |
9.89e-64 |
|
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: 228.05 E-value: 9.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 235 NLAISLSCLIISFRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYR 314
Cdd:TIGR02204 142 NALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 315 YFADACSTSSKSFLRFSFLDAFQGGVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTVFGSCLSVASSLQQILPAIPDL 394
Cdd:TIGR02204 222 RFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGEL 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 395 IKGKFSSHFIKTLCESHDPIEAAKRSAAKIKSISFErgFRFDNVSFAYPSRDENLfSLINVSVFIPFGELVHIIGPSGSG 474
Cdd:TIGR02204 302 QRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGE--IEFEQVNFAYPARPDQP-ALDGLNLTVRPGETVALVGPSGAG 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 475 KSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEF 554
Cdd:TIGR02204 379 KSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEF 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 555 ALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQI 632
Cdd:TIGR02204 459 ISALPEGYDTYLGErgVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATV 538
|
410 420
....*....|....*....|....
gi 162312251 633 NNDELVLVIDKGHLIQRCARKELV 656
Cdd:TIGR02204 539 LKADRIVVMDQGRIVAQGTHAELI 562
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1099-1328 |
1.32e-62 |
|
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: 213.25 E-value: 1.32e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYIDGYPLTNIDTNWLLKKV 1176
Cdd:cd03251 1 VEFKNVTFRYPGDGPP--VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYdVDSgRILIDGHDVRDYTLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHLLGSTILESLLYGV-DRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPR 1255
Cdd:cd03251 79 GLVSQDVFLFNDTVAENIAYGRpGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1256 LLILDECTSALDSKSSLLLEKTIQNLSC--TVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKL 1328
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKnrTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
99-655 |
1.40e-62 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 228.07 E-value: 1.40e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 99 SDIPLIFGTLIFTCLSAALEPLMTWTTGKVFDALSQYATSQitlgkmiSLINfNSLLITIFGLASCVFSFGVRFLWQYLS 178
Cdd:TIGR00958 158 RDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPP-------ALAS-AIFFMCLLSIASSVSAGLRGGSFNYTM 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 179 AIAGKRARSLCFHVLSSKSSTFYSltESKSGLVNS-VDRCIQFYEKSISLPMFHIAENLAISLSCLIISFRYSWSLTLVV 257
Cdd:TIGR00958 230 ARINLRIREDLFRSLLRQDLGFFD--ENKTGELTSrLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 258 LASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSFLDAFQ 337
Cdd:TIGR00958 308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 338 GGVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTVFGSCLSVASSLQQILPAIPDLIKGKFSSHFI-----KTLCESHD 412
Cdd:TIGR00958 388 LWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVfeyldRKPNIPLT 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 413 PIEAAKRSAAKIKsisfergfrFDNVSFAYPSRDENLFsLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGN 492
Cdd:TIGR00958 468 GTLAPLNLEGLIE---------FQDVSFSYPNRPDVPV-LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQ 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 493 IYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKEAS-- 570
Cdd:TIGR00958 538 VLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGsq 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 571 LSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRahRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRC 650
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMG 695
|
....*
gi 162312251 651 ARKEL 655
Cdd:TIGR00958 696 THKQL 700
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
434-656 |
4.99e-61 |
|
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: 209.01 E-value: 4.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYpsrDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:cd03253 2 EFENVTFAY---DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEI 591
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGErgLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 592 LILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELV 656
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
434-655 |
1.43e-60 |
|
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: 207.08 E-value: 1.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYpsrDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:cd03254 4 EFENVNFSY---DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKEAS--LSGGQQQRIALARALLRDTEI 591
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGgnLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 592 LILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKEL 655
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1097-1322 |
2.26e-60 |
|
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: 206.69 E-value: 2.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1097 GKIEFDGVSFAYpdsERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSED--IYIDGYPLTNIDTNWLLK 1174
Cdd:cd03254 1 GEIEFENVNFSY---DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKgqILIDGIDIRDISRKSLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQKPHLLGSTILESLLYGvdRDINS---VMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALL 1251
Cdd:cd03254 78 MIGVVLQDTFLFSGTIMENIRLG--RPNATdeeVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 1252 RNPRLLILDECTSALDSKSSLLLEKTIQNLSC--TVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRH 1322
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMKgrTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
434-656 |
8.66e-60 |
|
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: 205.16 E-value: 8.66e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLfsLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:cd03251 2 EFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEI 591
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGErgVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 592 LILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELV 656
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
889-1329 |
1.69e-57 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 213.05 E-value: 1.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 889 SDMRNMISSLIEEVFI---AFTMAIIGIAWSFATGWRLAAVLVAVSPILCLTSRMFSYIYVSTERMCQDVVISTTSILHK 965
Cdd:TIGR00958 266 SDTQTMSRSLSLNVNVllrNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 966 TIVNLDTIKgysvlSFFRENH-----KNSLRKSWEAFKRRAFwTSLGFAINNSLL-YFVRALLFYCSSIFISKEFYTVEQ 1039
Cdd:TIGR00958 346 ALSGMRTVR-----SFAAEEGeasrfKEALEETLQLNKRKAL-AYAGYLWTTSVLgMLIQVLVLYYGGQLVLTGKVSSGN 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1040 MVQVL------SLATFTLLMASTCIMSlpNVSASRiatsRVLKLSSLKPGNLHKSGYLKFPLVGKIEFDGVSFAYPdSER 1113
Cdd:TIGR00958 420 LVSFLlyqeqlGEAVRVLSYVYSGMMQ--AVGASE----KVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYP-NRP 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1114 NHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYIDGYPLTNIDTNWLLKKVAIVDQKPHLLGSTIL 1191
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPTGgQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVR 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1192 ESLLYGVDR-DINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKS 1270
Cdd:TIGR00958 573 ENIAYGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1271 SLLLEKTIQNLSCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKLI 1329
Cdd:TIGR00958 653 EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
397-641 |
5.92e-56 |
|
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: 204.06 E-value: 5.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 397 GKFSSHFIKTLCESHDPIEAAKRSAAKIKSISFErgfrFDNVSFAYPSRDEnlfSLINVSVFIPFGELVHIIGPSGSGKS 476
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLE----FSGVSVAYPGRRP---ALRPVSFTVPPGERVALVGPSGAGKS 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 477 TFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFAL 556
Cdd:TIGR02857 363 TLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVA 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 557 TFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINN 634
Cdd:TIGR02857 443 ALPQGLDTPIGEggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAAL 522
|
....*..
gi 162312251 635 DELVLVI 641
Cdd:TIGR02857 523 ADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1097-1309 |
6.91e-56 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 193.57 E-value: 6.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1097 GKIEFDGVSFAYPDSERNhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSED--IYIDGYPLTNIDTNWLLK 1174
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIP--ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSgsVLLDGTDIRQLDPADLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQKPHLLGSTILESLLYGV-DRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRN 1253
Cdd:cd03245 79 NIGYVPQDVTLFYGTLRDNITLGApLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1254 PRLLILDECTSALDSKSSLLLEKTIQNLSC--TVLIITHQPSLMKLADRIIVMDSG-IV 1309
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLDLVDRIIVMDSGrIV 217
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1097-1314 |
2.24e-54 |
|
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: 189.24 E-value: 2.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1097 GKIEFDGVSFAYPDSERnhLALNNVSLSIEAREKVAIVGISGSGKSTLV-ELLRKTYPSE-DIYIDGYPLTNIDTNWLLK 1174
Cdd:cd03244 1 GDIEFKNVSLRYRPNLP--PVLKNISFSIKPGEKVGIVGRTGSGKSSLLlALFRLVELSSgSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQKPHLLGSTILESLlygvdrDINS------VMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFAR 1248
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL------DPFGeysdeeLWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1249 ALLRNPRLLILDECTSALDSKSSLLLEKTIQNL--SCTVLIITHQPSLMKLADRIIVMDSGIVKESGS 1314
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
435-647 |
1.07e-53 |
|
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: 187.03 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 435 FDNVSFAYPSrDENLfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITL 514
Cdd:cd03245 5 FRNVSFSYPN-QEIP-ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 515 VCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEIL 592
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGErgRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 593 ILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLI 647
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1099-1331 |
2.16e-53 |
|
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: 187.05 E-value: 2.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDserNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSED--IYIDGYPLTNIDTNWLLKKV 1176
Cdd:cd03253 1 IEFENVTFAYDP---GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSgsILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHLLGSTILESLLYG-VDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPR 1255
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGrPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1256 LLILDECTSALDSKSSLLLEKTIQNLSC--TVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKLIHR 1331
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1099-1328 |
5.33e-53 |
|
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: 185.77 E-value: 5.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAY-PDSErnhLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSED--IYIDGYPLTNIDTNWLLKK 1175
Cdd:cd03252 1 ITFEHVRFRYkPDGP---VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENgrVLVDGHDLALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1176 VAIVDQKPHLLGSTILESL-LYGVDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNP 1254
Cdd:cd03252 78 VGVVLQENVLFNRSIRDNIaLADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 1255 RLLILDECTSALDSKSSLLLEKTIQNLSC--TVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKL 1328
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
424-1330 |
1.15e-50 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 197.12 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 424 IKSISFERGFrfdnvsFAYPSRDENLfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTygniylddfpleEI 503
Cdd:PLN03232 612 APAISIKNGY------FSWDSKTSKP-TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA------------ET 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 504 DEHVLGSTITLVCQQPVIFDMTIRENIIMrnenasESDFEEVCRLALVDEFALTFD----QSYD-TPCKE--ASLSGGQQ 576
Cdd:PLN03232 673 SSVVIRGSVAYVPQVSWIFNATVRENILF------GSDFESERYWRAIDVTALQHDldllPGRDlTEIGErgVNISGGQK 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 577 QRIALARALLRDTEILILDEPTSALDPITKNLVMDA-IRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKEL 655
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 656 ----VLFEDF-ENNVSIDEKV-LKEEADNpfiLPNEESLLEKYWINYNESFSQLSRE--SLFTSLESPFTDIESPTIVSR 727
Cdd:PLN03232 827 sksgSLFKKLmENAGKMDATQeVNTNDEN---ILKLGPTVTIDVSERNLGSTKQGKRgrSVLVKQEERETGIISWNVLMR 903
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 728 RKiveqrklrmekESFQETNVdqTFHLFddkehACSLTlifKSIWKVKKLRWfflLGLLTSLIQGASVPIFAYVISKCLN 807
Cdd:PLN03232 904 YN-----------KAVGGLWV--VMILL-----VCYLT---TEVLRVSSSTW---LSIWTDQSTPKSYSPGFYIVVYALL 959
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 808 LFMQIDPSIGVAFWssmvLVVAAGSGASYFFSHYIFSIsakiwcdhyrlLAVKVLFTQDQAWFDQIENYPLVLSKIlVNN 887
Cdd:PLN03232 960 GFGQVAVTFTNSFW----LISSSLHAAKRLHDAMLNSI-----------LRAPMLFFHTNPTGRVINRFSKDIGDI-DRN 1023
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 888 ISDMRNMISSLIEEVFIAFtmAIIGIAWSFAtgwrlaavLVAVSPILCLTSRMFSYiYVSTERmcqdvvisttsilhkTI 967
Cdd:PLN03232 1024 VANLMNMFMNQLWQLLSTF--ALIGTVSTIS--------LWAIMPLLILFYAAYLY-YQSTSR---------------EV 1077
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 968 VNLDTIKGYSVLSFFRE--NHKNSLRkSWEAFKRRAFWTslGFAINNSLLYfvrALLFYCSSIFISKEFYTVEQMVQVLS 1045
Cdd:PLN03232 1078 RRLDSVTRSPIYAQFGEalNGLSSIR-AYKAYDRMAKIN--GKSMDNNIRF---TLANTSSNRWLTIRLETLGGVMIWLT 1151
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1046 lATFTLL----------MASTCIMSLPNVSASRIATSRVLKLSSLKPGNLHK----SGYLK-----------------FP 1094
Cdd:PLN03232 1152 -ATFAVLrngnaenqagFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSvervGNYIDlpseataiiennrpvsgWP 1230
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1095 LVGKIEFDGVSFAYpdseRNHL--ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTNIDTN 1170
Cdd:PLN03232 1231 SRGSIKFEDVHLRY----RPGLppVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEkgRIMIDDCDVAKFGLT 1306
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1171 WLLKKVAIVDQKPHLLGSTILESLLYGVDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARAL 1250
Cdd:PLN03232 1307 DLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1251 LRNPRLLILDECTSALDSKSSLLLEKTIQN--LSCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTH-FWK 1327
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIREefKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSaFFR 1466
|
...
gi 162312251 1328 LIH 1330
Cdd:PLN03232 1467 MVH 1469
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1095-1307 |
5.50e-50 |
|
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: 176.89 E-value: 5.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1095 LVGKIEFDGVSFAYPdSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSED--IYIDGYPLTNIDTNWL 1172
Cdd:cd03248 8 LKGIVKFQNVTFAYP-TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGgqVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1173 LKKVAIVDQKPHLLGSTILESLLYGV-DRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALL 1251
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAYGLqSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1252 RNPRLLILDECTSALDSKSSLLLEKTIQ--NLSCTVLIITHQPSLMKLADRIIVMDSG 1307
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYdwPERRTVLVIAHRLSTVERADQILVLDGG 224
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
763-1331 |
7.28e-50 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 189.40 E-value: 7.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 763 SLTLIFKSIWK--VKKLRWFFLLGLLTSLIqGASVP-----IFAYVISKC-LNLFMQIdpsigvafwsSMVLVVAAGSGA 834
Cdd:TIGR03797 122 GLRDLLRFALRgaRRDLLAILAMGLLGTLL-GMLVPiatgiLIGTAIPDAdRSLLVQI----------ALALLAAAVGAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 835 SYFFSHYI----------FSISAKIWcDhyRLLAVKVLFtqdqawFDQIENYPLVLSkilVNNISDMRNMISSLIEEVFI 904
Cdd:TIGR03797 191 AFQLAQSLavlrletrmdASLQAAVW-D--RLLRLPVSF------FRQYSTGDLASR---AMGISQIRRILSGSTLTTLL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 905 AFTMAIIGIAWSFATGWRLAAVLVAVSPILCLTSRMFSYIYVSTERMCQDVVISTTSILHKTIVNLDTIK--GYSVLSFF 982
Cdd:TIGR03797 259 SGIFALLNLGLMFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvaGAENRAFA 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 983 RENHKNSLRKSWEAFKRRafWTSLGFAINNSLLYFVRALLFYCSSIFIskefytveqMVQVLSLATFTLLMA--STCIMS 1060
Cdd:TIGR03797 339 RWAKLFSRQRKLELSAQR--IENLLTVFNAVLPVLTSAALFAAAISLL---------GGAGLSLGSFLAFNTafGSFSGA 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1061 LPNVSASRIATSRVLKL----------------SSLKPGNLHksgylkfplvGKIEFDGVSFAY-PDSErnhLALNNVSL 1123
Cdd:TIGR03797 408 VTQLSNTLISILAVIPLwerakpilealpevdeAKTDPGKLS----------GAIEVDRVTFRYrPDGP---LILDDVSL 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1124 SIEAREKVAIVGISGSGKSTLVELLR--KTYPSEDIYIDGYPLTNIDTNWLLKKVAIVDQKPHLLGSTILESLLYGVDRD 1201
Cdd:TIGR03797 475 QIEPGEFVAIVGPSGSGKSTLLRLLLgfETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLT 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1202 INSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL 1281
Cdd:TIGR03797 555 LDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL 634
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 162312251 1282 SCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKLIHR 1331
Cdd:TIGR03797 635 KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARR 684
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
247-656 |
2.14e-49 |
|
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: 188.03 E-value: 2.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 247 FRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTV----IFHSMQDTEYRYFADACST 322
Cdd:TIGR01846 274 FFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIkataTEPQFQNRWDRQLAAYVAA 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 323 SsksfLRFSFLDAFQGGVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVT-------VFGSCLSVAS---SLQQILPAIP 392
Cdd:TIGR01846 354 S----FRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAfnmlagrVTQPVLRLAQlwqDFQQTGIALE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 393 DLikGKFSSHfiktlceshdPIEAAKRSAAKIKSIsfERGFRFDNVSFAYpsRDENLFSLINVSVFIPFGELVHIIGPSG 472
Cdd:TIGR01846 430 RL--GDILNS----------PTEPRSAGLAALPEL--RGAITFENIRFRY--APDSPEVLSNLNLDIKPGEFIGIVGPSG 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 473 SGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVD 552
Cdd:TIGR01846 494 SGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAH 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 553 EFALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMS 630
Cdd:TIGR01846 574 DFISELPQGYNTEVGEkgANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLS 653
|
410 420
....*....|....*....|....*.
gi 162312251 631 QINNDELVLVIDKGHLIQRCARKELV 656
Cdd:TIGR01846 654 TVRACDRIIVLEKGQIAESGRHEELL 679
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
165-647 |
1.40e-48 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 185.45 E-value: 1.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 165 VFSFGVRFLWQYLSAIAGKRA-----RSLCFHVLSSKsstfyslTESKSGLVNSVDRCIQFYEkSI-----SLPMFHIAE 234
Cdd:TIGR03375 198 VFDFVLKTLRSYFLDVAGKKAdlilsAKLFERVLGLR-------MEARPASVGSFANQLREFE-SVrdfftSATLTALID 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 235 nLAISLSCLIISFRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKD-RKSSEKAASILEkSISAIQTVIFHSMQDTEY 313
Cdd:TIGR03375 270 -LPFALLFLLVIAIIGGPLVWVPLVAIPLILLPGLLLQRPLSRLAEESmRESAQRNAVLVE-SLSGLETIKALNAEGRFQ 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 314 RYFADACSTSSKSFLRFSFLDAFQGGVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTVfgSCLS--VASSLQQIlPAI 391
Cdd:TIGR03375 348 RRWEQTVAALARSGLKSRFLSNLATNFAQFIQQLVSVAIVVVGVYLISDGELTMGGLIAC--VMLSgrALAPLGQL-AGL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 392 pdLIKGKFSSHFIKTLCESHD-PIEAAKrSAAKIKSISFERGFRFDNVSFAYPSRDENlfSLINVSVFIPFGELVHIIGP 470
Cdd:TIGR03375 425 --LTRYQQAKTALQSLDELMQlPVERPE-GTRFLHRPRLQGEIEFRNVSFAYPGQETP--ALDNVSLTIRPGEKVAIIGR 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 471 SGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLAL 550
Cdd:TIGR03375 500 IGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGAPYADDEEILRAAELAG 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 551 VDEFALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHD 628
Cdd:TIGR03375 580 VTEFVRRHPDGLDMQIGErgRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHR 659
|
490
....*....|....*....
gi 162312251 629 MSQINNDELVLVIDKGHLI 647
Cdd:TIGR03375 660 TSLLDLVDRIIVMDNGRIV 678
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
435-656 |
5.95e-48 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 181.76 E-value: 5.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 435 FDNVSFAYPSRDENlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITL 514
Cdd:PRK11176 344 FRNVTFTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 515 VCQQPVIFDMTIRENIIM-RNENASESDFEEVCRLALVDEFALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEI 591
Cdd:PRK11176 422 VSQNVHLFNDTIANNIAYaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGEngVLLSGGQRQRIAIARALLRDSPI 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 592 LILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELV 656
Cdd:PRK11176 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
434-649 |
7.10e-48 |
|
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: 181.94 E-value: 7.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAY-PSRDenlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTI 512
Cdd:COG5265 359 RFENVSFGYdPERP----ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 513 TLVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKEA--SLSGGQQQRIALARALLRDTE 590
Cdd:COG5265 435 GIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERglKLSGGEKQRVAIARTLLKNPP 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 591 ILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQR 649
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVER 573
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
970-1304 |
7.14e-48 |
|
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: 180.18 E-value: 7.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 970 LDTIKGYSVLSFFRENHK--NSLRKSWEAFKRR-------AFWTSLgfainnsLLYFVRALlfycsSIFISKEFYTVEQM 1040
Cdd:TIGR02857 187 LDRLRGLPTLKLFGRAKAqaAAIRRSSEEYRERtmrvlriAFLSSA-------VLELFATL-----SVALVAVYIGFRLL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1041 VQVLSLAT--FTLLMASTCIMSLPNVSAS-------RIATSRVLKLSSLKPGNLHKSGYLKFPLVGKIEFDGVSFAYPDS 1111
Cdd:TIGR02857 255 AGDLDLATglFVLLLAPEFYLPLRQLGAQyharadgVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1112 ERnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDGYPLTNIDTNWLLKKVAIVDQKPHLLGST 1189
Cdd:TIGR02857 335 RP---ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDptEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1190 ILESL-LYGVDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDS 1268
Cdd:TIGR02857 412 IAENIrLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
330 340 350
....*....|....*....|....*....|....*...
gi 162312251 1269 KSSLLLEKTIQNLS--CTVLIITHQPSLMKLADRIIVM 1304
Cdd:TIGR02857 492 ETEAEVLEALRALAqgRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
434-656 |
7.16e-48 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 181.31 E-value: 7.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFsliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:PRK13657 336 EFDDVSFSYDNSRQGVE---DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEI 591
Cdd:PRK13657 413 VVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGErgRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 592 LILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELV 656
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELV 557
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
434-646 |
7.77e-48 |
|
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: 170.73 E-value: 7.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFsLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:cd03248 13 KFQNVTFAYPTRPDTLV-LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEI 591
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEkgSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 592 LILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHL 646
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
451-1328 |
8.96e-48 |
|
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: 187.85 E-value: 8.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 451 SLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRyfsptygniylddfPLEEIDEHV-LGSTITLVCQQPVIFDMTIREN 529
Cdd:TIGR00957 653 TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLA--------------EMDKVEGHVhMKGSVAYVPQQAWIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 530 IIM---RNENASESDFEeVCRLALVDEFALTFDQSyDTPCKEASLSGGQQQRIALARALLRDTEILILDEPTSALDPITK 606
Cdd:TIGR00957 719 ILFgkaLNEKYYQQVLE-ACALLPDLEILPSGDRT-EIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 607 NLVMDAI---RAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELV----LFEDFENNVSIDEKVLKEEADNP 679
Cdd:TIGR00957 797 KHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLqrdgAFAEFLRTYAPDEQQGHLEDSWT 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 680 FIL--PNEESLLEKYWINYNESFS-QLSREslFTSLESPFTDIesptivSRR--KIVEQRKLRMEKESFQETNVDQtfhl 754
Cdd:TIGR00957 877 ALVsgEGKEAKLIENGMLVTDVVGkQLQRQ--LSASSSDSGDQ------SRHhgSSAELQKAEAKEETWKLMEADK---- 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 755 fddkehACSLTLIFKSIWKVKKLRWFFLLGLLTSLIQGASVPIFA--YVISKCLNlfmqiDPSI-GVAFWSSMVLVVAAG 831
Cdd:TIGR00957 945 ------AQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALAsnYWLSLWTD-----DPMVnGTQNNTSLRLSVYGA 1013
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 832 SGASYFFSHYIFSISAKIW------CDHYRLLAVKVlfTQDQAWFDQIEnyplvlSKILVNNISDMRNMISSLIEEVFIA 905
Cdd:TIGR00957 1014 LGILQGFAVFGYSMAVSIGgiqasrVLHQDLLHNKL--RSPMSFFERTP------SGNLVNRFSKELDTVDSMIPPVIKM 1085
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 906 FT---MAIIGIAWSFATGWRLAAVLVavsPILCLTSRMFSYIYVSTERMCQDVVISTTSILHKTIVnlDTIKGYSVLSFF 982
Cdd:TIGR00957 1086 FMgslFNVIGALIVILLATPIAAVII---PPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFN--ETLLGVSVIRAF 1160
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 983 REN----HKNSLR-----KSWEAFKRRAFWTSLGFA-INNSLLYFvrALLFYC---SSIFISKEFYTVEQMVQVLSLATF 1049
Cdd:TIGR00957 1161 EEQerfiHQSDLKvdenqKAYYPSIVANRWLAVRLEcVGNCIVLF--AALFAVisrHSLSAGLVGLSVSYSLQVTFYLNW 1238
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1050 TLLMAStcimslpNVSASRIATSRVLKLSSLK---PGNLHKSGYLK-FPLVGKIEFDGVSFAY-PDSErnhLALNNVSLS 1124
Cdd:TIGR00957 1239 LVRMSS-------EMETNIVAVERLKEYSETEkeaPWQIQETAPPSgWPPRGRVEFRNYCLRYrEDLD---LVLRHINVT 1308
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1125 IEAREKVAIVGISGSGKSTL-VELLRKTYPSE-DIYIDGYPLTNIDTNWLLKKVAIVDQKPHLLGSTILESLLYGVDRDI 1202
Cdd:TIGR00957 1309 IHGGEKVGIVGRTGAGKSSLtLGLFRINESAEgEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSD 1388
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1203 NSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTI--QN 1280
Cdd:TIGR00957 1389 EEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIrtQF 1468
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 162312251 1281 LSCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKL 1328
Cdd:TIGR00957 1469 EDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
433-646 |
3.47e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 168.07 E-value: 3.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRDEnlfsLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTI 512
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 513 TLVCQQPVIFDMTIRENIIMRNENASES-DFEEVCRLALvdefALTFDQSY-DTPCKEasLSGGQQQRIALARALLRDTE 590
Cdd:COG4619 77 AYVPQEPALWGGTVRDNLPFPFQLRERKfDRERALELLE----RLGLPPDIlDKPVER--LSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 591 ILILDEPTSALDPITKNLVMDAIR--AHRKGKTTLVITHDMSQINN-DELVLVIDKGHL 646
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLReyLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
910-1322 |
3.60e-47 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 179.06 E-value: 3.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 910 IIGI-AWSFATGWRLAAVLVAVSPILCLTSRMFSYIYVSTERMCQDVVISTTSILHKTIvnldtiKGYS-VLSF------ 981
Cdd:PRK11176 153 IIGLfIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQML------KGHKeVLIFggqeve 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 982 -FRENH-KNSLRksweafkRRAFWTSLGFAINNSLLYFVrallfycSSIFISKEFY--TVEQMVQVLSLATFTLLMASTC 1057
Cdd:PRK11176 227 tKRFDKvSNRMR-------QQGMKMVSASSISDPIIQLI-------ASLALAFVLYaaSFPSVMDTLTAGTITVVFSSMI 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1058 IM-----SLPNVSAS----RIATSRVLKLSSLKPGNlhKSGYLKFPLV-GKIEFDGVSFAYPdsERNHLALNNVSLSIEA 1127
Cdd:PRK11176 293 ALmrplkSLTNVNAQfqrgMAACQTLFAILDLEQEK--DEGKRVIERAkGDIEFRNVTFTYP--GKEVPALRNINFKIPA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1128 REKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDG-----YPLTNidtnwLLKKVAIVDQKPHLLGSTILESLLYGVDR 1200
Cdd:PRK11176 369 GKTVALVGRSGSGKSTIANLLTRFYDidEGEILLDGhdlrdYTLAS-----LRNQVALVSQNVHLFNDTIANNIAYARTE 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1201 --DINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTI 1278
Cdd:PRK11176 444 qySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAAL 523
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 162312251 1279 QNL--SCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRH 1322
Cdd:PRK11176 524 DELqkNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN 569
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
435-656 |
2.60e-46 |
|
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: 166.51 E-value: 2.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 435 FDNVSFAYpsRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITL 514
Cdd:cd03252 3 FEHVRFRY--KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 515 VCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEIL 592
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEqgAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 593 ILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELV 656
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1097-1321 |
5.10e-46 |
|
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: 176.16 E-value: 5.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1097 GKIEFDGVSFAYpDSERNhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYIDGYPLTNIDTNWLLK 1174
Cdd:COG5265 356 GEVRFENVSFGY-DPERP--ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYdVTSgRILIDGQDIRDVTQASLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQKPHLLGSTILESLLYG-VDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRN 1253
Cdd:COG5265 433 AIGIVPQDTVLFNDTIAYNIAYGrPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1254 PRLLILDECTSALDSKSslllEKTIQ-NL-----SCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNR 1321
Cdd:COG5265 513 PPILIFDEATSALDSRT----ERAIQaALrevarGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ 582
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
375-656 |
2.97e-45 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 173.47 E-value: 2.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 375 GSCLSVASSLQQILPAIPDlikgkfsshfiktlceshdpIEAAKRSAAKIKSISFErgfrFDNVSFAYPSRDENLfsLIN 454
Cdd:PRK11160 305 GQVIASARRINEITEQKPE--------------------VTFPTTSTAAADQVSLT----LNNVSFTYPDQPQPV--LKG 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 455 VSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIIMRN 534
Cdd:PRK11160 359 LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 535 ENASESDFEEVcrLALVD-EFALTFDQSYDTPCKEA--SLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMD 611
Cdd:PRK11160 439 PNASDEALIEV--LQQVGlEKLLEDDKGLNAWLGEGgrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILE 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 162312251 612 AIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELV 656
Cdd:PRK11160 517 LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
253-661 |
9.48e-45 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 174.16 E-value: 9.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 253 LTLVVLASYPIIILVV-GFINSFLSSAYEKDRKSSEKAASILEkSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFS 331
Cdd:TIGR01193 297 LFLLSLLSIPVYAVIIiLFKRTFNKLNHDAMQANAVLNSSIIE-DLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQ 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 332 FLDAFQGGVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTvFGSCLS-VASSLQQILPAIPDLIKGKFSSHFIKT--LC 408
Cdd:TIGR01193 376 KADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLIT-FNALLSyFLTPLENIINLQPKLQAARVANNRLNEvyLV 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 409 ESHDpieaaKRSAAKIKSISFERGFRFDNVSFAYPSRDEnlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSP 488
Cdd:TIGR01193 455 DSEF-----INKKKRTELNNLNGDIVINDVSYSYGYGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQA 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 489 TYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIIM-RNENASESDFEEVCRLALVDEFALTFDQSYDTPCK 567
Cdd:TIGR01193 527 RSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELS 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 568 E--ASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIrAHRKGKTTLVITHDMSQINNDELVLVIDKGH 645
Cdd:TIGR01193 607 EegSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGK 685
|
410
....*....|....*.
gi 162312251 646 LIQRCARKELVLFEDF 661
Cdd:TIGR01193 686 IIEQGSHDELLDRNGF 701
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
434-648 |
4.83e-44 |
|
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: 159.58 E-value: 4.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYpsRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:cd03244 4 EFKNVSLRY--RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFDMTIRENIIMRNEnASESDFEEVCRLALVDEFALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEI 591
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEggENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 592 LILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQ 648
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVE 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1099-1322 |
8.47e-44 |
|
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: 159.03 E-value: 8.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYIDGYPLTNIDTNWLLKKV 1176
Cdd:COG1122 1 IELENLSFSYPGGTP---ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLkPTSgEVLVDGKDITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPH--LLGSTILE----SLL-YGVDRD-INS-VMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLAFA 1247
Cdd:COG1122 78 GLVFQNPDdqLFAPTVEEdvafGPEnLGLPREeIRErVEEALELVGLEHLADRPPHEL-----------SGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1248 RALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSL-MKLADRIIVMDSGIVKESGSFDELMNRH 1322
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNkegKTVIIVTHDLDLvAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
433-683 |
8.66e-44 |
|
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: 159.82 E-value: 8.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRdenlFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTI 512
Cdd:COG1120 2 LEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 513 TLVCQQPVI-FDMTIRENIIM-------RNENASESDFEEVCR-LALVD--EFAltfDQSYDTpckeasLSGGQQQRIAL 581
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALgryphlgLFGRPSAEDREAVEEaLERTGleHLA---DRPVDE------LSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 582 ARALLRDTEILILDEPTSALDPITKNLVMDAIR--AHRKGKTTLVITHDMSQINN--DELVLvIDKGHLIQRCARKELV- 656
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRrlARERGRTVVMVLHDLNLAARyaDRLVL-LKDGRIVAQGPPEEVLt 227
|
250 260 270
....*....|....*....|....*....|
gi 162312251 657 --LFED-FENNVSIDEkvlKEEADNPFILP 683
Cdd:COG1120 228 peLLEEvYGVEARVIE---DPVTGRPLVLP 254
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1099-1311 |
1.03e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 158.67 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELL----RktyPSE-DIYIDGYPLTNID----T 1169
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggldR---PTSgEVLIDGQDISSLSerelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1170 NWLLKKVAIVDQKPHLLGS-TILE----SLLY-GVDR--DINSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQI 1241
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALEnvalPLLLaGVSRkeRRERARELLERVGLGDRLDHRPSQL-----------SGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1242 QRLAFARALLRNPRLLILDECTSALDSKSSL----LLEKTIQNLSCTVLIITHQPSLMKLADRIIVMDSGIVKE 1311
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEevleLLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1115-1333 |
4.49e-43 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 166.94 E-value: 4.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1115 HLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE-DIYIDGYPLTNID-TNWLlKKVAIVDQKPHLLGSTILE 1192
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQgSLKINGIELRELDpESWR-KHLSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1193 SLLYG-VDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSS 1271
Cdd:PRK11174 442 NVLLGnPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1272 LLLEKTIQNLSC--TVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKLI-HRGE 1333
Cdd:PRK11174 522 QLVMQALNAASRrqTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLaHRQE 586
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1095-1332 |
7.81e-43 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 166.29 E-value: 7.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1095 LVGKIEFDGVSFAYPDSERnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSED-IYIDGYPLTNIDTNWL 1172
Cdd:PRK13657 331 VKGAVEFDDVSFSYDNSRQ---GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFdPQSGrILIDGTDIRTVTRASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1173 LKKVAIVDQKPHLLGSTILESLLYG-VDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALL 1251
Cdd:PRK13657 408 RRNIAVVFQDAGLFNRSIEDNIRVGrPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1252 RNPRLLILDECTSALDSKSSLLLEKTIQNLSC--TVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKLI 1329
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKgrTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
...
gi 162312251 1330 HRG 1332
Cdd:PRK13657 568 RAQ 570
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
895-1330 |
3.50e-42 |
|
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: 166.45 E-value: 3.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 895 ISSLIEEVFIAFTM-AIIGIAWSFATGWRLAAVLVAV---SPILCLTSRMFSYIyvSTERMCQDVVISTTSIlhKTIVNL 970
Cdd:TIGR01193 269 LASTILSLFLDMWIlVIVGLFLVRQNMLLFLLSLLSIpvyAVIIILFKRTFNKL--NHDAMQANAVLNSSII--EDLNGI 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 971 DTIKGYSV--LSFFRENHK--NSLRKSWEAFKRRAFWTSLGFAINNSLLYFVrallFYCSSIFISKEFYTVEQMVQVLSL 1046
Cdd:TIGR01193 345 ETIKSLTSeaERYSKIDSEfgDYLNKSFKYQKADQGQQAIKAVTKLILNVVI----LWTGAYLVMRGKLTLGQLITFNAL 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1047 ATFTLLMASTCIMSLPNVSASRIATSRvLKLSSLKPGNLHKSGYL--KFPLVGKIEFDGVSFAYpdsERNHLALNNVSLS 1124
Cdd:TIGR01193 421 LSYFLTPLENIINLQPKLQAARVANNR-LNEVYLVDSEFINKKKRteLNNLNGDIVINDVSYSY---GYGSNILSDISLT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1125 IEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTNIDTNWLLKKVAIVDQKPHLLGSTILESLLYGVDRD- 1201
Cdd:TIGR01193 497 IKMNSKTTIVGMSGSGKSTLAKLLVGFFQARsgEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENv 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1202 -INSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDsksSLLLEKTIQN 1280
Cdd:TIGR01193 577 sQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD---TITEKKIVNN 653
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1281 L----SCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKLIH 1330
Cdd:TIGR01193 654 LlnlqDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
434-645 |
5.50e-42 |
|
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: 153.01 E-value: 5.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFSLINVSvfIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLT--IKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQP--VIFDMTIRENII--MRNENASESDFEEVCRLALvdefALTFDQSY-DTPCKEasLSGGQQQRIALARALLRD 588
Cdd:cd03225 79 LVFQNPddQFFGPTVEEEVAfgLENLGLPEEEIEERVEEAL----ELVGLEGLrDRSPFT--LSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 589 TEILILDEPTSALDPITKNLVMDAIRA-HRKGKTTLVITHDMSQINN--DElVLVIDKGH 645
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElaDR-VIVLEDGK 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
236-628 |
1.72e-41 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 160.99 E-value: 1.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 236 LAISLSCLIISFrYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKS--SEKAASIL-------EKSISAIQTVIFH 306
Cdd:TIGR02868 139 VVGAAAVAAIAV-LSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARlrGELAAQLTdaldgaaELVASGALPAALA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 307 SMQDTEYRYFADACSTSSksflrfsfLDAFQGGVSQFFLYSVFFQGLWFGNHLATTKRVNvGQVVTVFGSC-LSVASSLQ 385
Cdd:TIGR02868 218 QVEEADRELTRAERRAAA--------ATALGAALTLLAAGLAVLGALWAGGPAVADGRLA-PVTLAVLVLLpLAAFEAFA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 386 QILPAIPDLIKGKFSSHFIKTLCESHDPIEAAKRSAAKiKSISFERGFRFDNVSFAYPSRDEnlfSLINVSVFIPFGELV 465
Cdd:TIGR02868 289 ALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAG-AVGLGKPTLELRDLSAGYPGAPP---VLDGVSLDLPPGERV 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 466 HIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIIMRNENASESDFEEV 545
Cdd:TIGR02868 365 AILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 546 CRLALVDEFALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTL 623
Cdd:TIGR02868 445 LERVGLADWLRALPDGLDTVLGEggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVV 524
|
....*
gi 162312251 624 VITHD 628
Cdd:TIGR02868 525 LITHH 529
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
433-647 |
1.80e-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: 150.54 E-value: 1.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRDENLFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIdEHVLGSTI 512
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLK--NLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 513 TLVCQQPVIFDMTIRENIIMRnenasesdfeevcrlalvdefaltfdqsydtpckeasLSGGQQQRIALARALLRDTEIL 592
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNLGRR-------------------------------------FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 593 ILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLI 647
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
434-657 |
2.02e-41 |
|
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: 161.45 E-value: 2.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:COG4618 332 SVENLTVVPPGSKRPILR--GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFDMTIRENIimrnenA--SESDFEEV---CRLALVDEFALTFDQSYDTPCKE--ASLSGGQQQRIALARALL 586
Cdd:COG4618 410 YLPQDVELFDGTIAENI------ArfGDADPEKVvaaAKLAGVHEMILRLPDGYDTRIGEggARLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 587 RDTEILILDEPTSALDPITKNLVMDAIRAHRK-GKTTLVITHDMSQINNDELVLVIDKGHlIQRCARKELVL 657
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGR-VQAFGPRDEVL 554
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1097-1331 |
2.76e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 161.53 E-value: 2.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1097 GKIEFDGVSFAYPDseRNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYIDGYPLTNIDTNWLLK 1174
Cdd:PRK11160 337 VSLTLNNVSFTYPD--QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWdPQQgEILLNGQPIADYSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQKPHLLGSTILESLLYGVDRDINSVM-DALDKTYMTEVIQNlPNGLDTPLLEFSKNFSGGQIQRLAFARALLRN 1253
Cdd:PRK11160 415 AISVVSQRVHLFSATLRDNLLLAAPNASDEALiEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHD 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1254 PRLLILDECTSALDSKS-----SLLLEKTIQNlscTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKL 1328
Cdd:PRK11160 494 APLLLLDEPTEGLDAETerqilELLAEHAQNK---TVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
...
gi 162312251 1329 IHR 1331
Cdd:PRK11160 571 KQR 573
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1100-1307 |
5.07e-41 |
|
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: 150.31 E-value: 5.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1100 EFDGVSFAYPDSERNhlALNNVSLSIEAREKVAIVGISGSGKSTLVELL--RKTYPSEDIYIDGYPLTNIDTNWLLKKVA 1177
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLngLLGPTSGEVLVDGKDLTKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1178 IVDQKPH--LLGSTILESLLYG-----VDRDInsvMDALDKTYMTEViqnlpnGLDTPLLEFSKNFSGGQIQRLAFARAL 1250
Cdd:cd03225 79 LVFQNPDdqFFGPTVEEEVAFGlenlgLPEEE---IEERVEEALELV------GLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 1251 LRNPRLLILDECTSALDSKSSLLLEKTIQNLSC---TVLIITHQPSLMK-LADRIIVMDSG 1307
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLeLADRVIVLEDG 210
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1099-1321 |
5.65e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 152.20 E-value: 5.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERnhLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYIDGYPLTNIDTNWLL-KK 1175
Cdd:TIGR04520 1 IEVENVSFSYPESEK--PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLlPTSgKVTVDGLDTLDEENLWEIrKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1176 VAIVDQKP--HLLGSTI-------LESLlyGVDRD--INSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRL 1244
Cdd:TIGR04520 79 VGMVFQNPdnQFVGATVeddvafgLENL--GVPREemRKRVDEALKLVGMEDFRDREPHLL-----------SGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1245 AFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSC----TVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeegiTVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
.
gi 162312251 1321 R 1321
Cdd:TIGR04520 226 Q 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
434-643 |
6.16e-41 |
|
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: 150.31 E-value: 6.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHvlgstIT 513
Cdd:cd03293 2 EVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFD-MTIRENII----MRNENASESDfEEVcrLALVDEFALT-FDQSYdtPckeASLSGGQQQRIALARALLR 587
Cdd:cd03293 77 YVFQQDALLPwLTVLDNVAlgleLQGVPKAEAR-ERA--EELLELVGLSgFENAY--P---HQLSGGMRQRVALARALAV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 588 DTEILILDEPTSALDPITKNLVMDAIRA--HRKGKTTLVITHDMsqinnDELVLVIDK 643
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDI-----DEAVFLADR 201
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
433-647 |
6.94e-41 |
|
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: 150.56 E-value: 6.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRDEnlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTI 512
Cdd:COG1122 1 IELENLSFSYPGGTP---ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 513 TLVCQQPV--IFDMTIRENII--MRNENASESDFEEVCR--LALVD--EFAltfdqsyDTPCkeASLSGGQQQRIALARA 584
Cdd:COG1122 78 GLVFQNPDdqLFAPTVEEDVAfgPENLGLPREEIRERVEeaLELVGleHLA-------DRPP--HELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 585 LLRDTEILILDEPTSALDPITKNLVMDAIRA-HRKGKTTLVITHDMsqinnDEL------VLVIDKGHLI 647
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDL-----DLVaeladrVIVLDDGRIV 213
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
459-656 |
7.02e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 160.40 E-value: 7.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 459 IPFGELVHIIGPSGSGKSTFISLLLRyFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIIMRNENAS 538
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDAS 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 539 ESDFEEVCRLALVDEFALTFDQSYDTPCKEAS--LSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAH 616
Cdd:PRK11174 452 DEQLQQALENAWVSEFLPLLPQGLDTPIGDQAagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA 531
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 162312251 617 RKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELV 656
Cdd:PRK11174 532 SRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELS 571
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
425-656 |
9.17e-41 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 159.88 E-value: 9.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 425 KSISFERGFRFDNV-SFAYPSRDENlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEI 503
Cdd:PRK10789 305 EPVPEGRGELDVNIrQFTYPQTDHP--ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 504 DEHVLGSTITLVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKE--ASLSGGQQQRIAL 581
Cdd:PRK10789 383 QLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGErgVMLSGGQKQRISI 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 582 ARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELV 656
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1097-1328 |
9.45e-41 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 160.27 E-value: 9.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1097 GKIEFDGVSFAYPDserNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDGYPLTNIDTNWLLK 1174
Cdd:PRK10790 339 GRIDIDNVSFAYRD---DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPltEGEIRLDGRPLSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQKPHLLGSTILESLLYGVDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNP 1254
Cdd:PRK10790 416 GVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 1255 RLLILDECTSALDSKSSLLLEKTIQNL--SCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKL 1328
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1099-1324 |
1.09e-40 |
|
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: 150.72 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTL----VELLRKTypSEDIYIDGYPLTNIDTNWLLK 1174
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLlralAGLERPW--SGEVTFDGRPVTRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQKP-------HLLGSTILESL-LYGVDRDINSVMDALDKTymteviqnlpnGLDTPLLE-FSKNFSGGQIQRLA 1245
Cdd:COG1124 80 RVQMVFQDPyaslhprHTVDRILAEPLrIHGLPDREERIAELLEQV-----------GLPPSFLDrYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1246 FARALLRNPRLLILDECTSALDskSSL------LLEKTIQNLSCTVLIITHQPSLM-KLADRIIVMDSGIVKESGSFDEL 1318
Cdd:COG1124 149 IARALILEPELLLLDEPTSALD--VSVqaeilnLLKDLREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADL 226
|
....*.
gi 162312251 1319 MNRHTH 1324
Cdd:COG1124 227 LAGPKH 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1099-1307 |
1.20e-40 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 149.56 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELL----RKTypSEDIYIDGYPLTNID----TN 1170
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILggldRPT--SGEVRVDGTDISKLSekelAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1171 WLLKKVAIVDQKPHLLGS-TILESLLYGVdrDINSVMDALDKTYMTEVIQNLpnGLDTPLLEFSKNFSGGQIQRLAFARA 1249
Cdd:cd03255 79 FRRRHIGFVFQSFNLLPDlTALENVELPL--LLAGVPKKERRERAEELLERV--GLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 1250 LLRNPRLLILDECTSALDSKSSLLLEKTIQNLS----CTVLIITHQPSLMKLADRIIVMDSG 1307
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNkeagTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
433-632 |
1.86e-40 |
|
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: 149.25 E-value: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRDenlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLL-----LRYFSPTYGNIYLDDFPLEEIDEHV 507
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 508 --LGSTITLVCQQPVIFDMTIRENII-------MRNENASESDFEEVCRLA-LVDEFAltfDQSydtpcKEASLSGGQQQ 577
Cdd:cd03260 77 leLRRRVGMVFQKPNPFPGSIYDNVAyglrlhgIKLKEELDERVEEALRKAaLWDEVK---DRL-----HALGLSGGQQQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 578 RIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQI 632
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQA 203
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1097-1323 |
1.93e-40 |
|
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: 158.76 E-value: 1.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1097 GKIEFDGVSFAYPDSERnhLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDGYPLTNIDTNWLLK 1174
Cdd:COG4618 329 GRLSVENLTVVPPGSKR--PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPptAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQKPHLLGSTILE--SLLYGVDRDinSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLR 1252
Cdd:COG4618 407 HIGYLPQDVELFDGTIAEniARFGDADPE--KVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1253 NPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHT 1323
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKargATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARLA 558
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
437-1329 |
2.81e-40 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 163.37 E-value: 2.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 437 NVSFAYPSRDENLfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYlddfpleeidehVLGSTITLVC 516
Cdd:PLN03130 619 NGYFSWDSKAERP-TLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASV------------VIRGTVAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 517 QQPVIFDMTIRENIIMrnenasESDFEEVCRLALVDEFALTFDQSY-----DTPCKE--ASLSGGQQQRIALARALLRDT 589
Cdd:PLN03130 686 QVSWIFNATVRDNILF------GSPFDPERYERAIDVTALQHDLDLlpggdLTEIGErgVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 590 EILILDEPTSALDPITKNLVMDA-IRAHRKGKTTLVIT---HDMSQInnDELVLVIDkGHLiqrcarKELVLFEDFENNV 665
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTnqlHFLSQV--DRIILVHE-GMI------KEEGTYEELSNNG 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 666 SIDEKvLKEEADNpfilpneesllekywinYNESFSQLSRESLFTSLESPFTDIESPTI---VSRRKIVEQRKLRMEKES 742
Cdd:PLN03130 831 PLFQK-LMENAGK-----------------MEEYVEENGEEEDDQTSSKPVANGNANNLkkdSSSKKKSKEGKSVLIKQE 892
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 743 FQETNVdQTFHLFDDKEHAcsltliFKSIWKVKKLrwfFLLGLLTSLIQGASV----------------PIFAYVISKCL 806
Cdd:PLN03130 893 ERETGV-VSWKVLERYKNA------LGGAWVVMIL---FLCYVLTEVFRVSSStwlsewtdqgtpkthgPLFYNLIYALL 962
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 807 NlFMQIDPSIGVAFWssmvLVVAAGSGASYFFSHYIFSIsakiwcdhyrlLAVKVLFTQDQAWFDQIENYPLVLSKIlVN 886
Cdd:PLN03130 963 S-FGQVLVTLLNSYW----LIMSSLYAAKRLHDAMLGSI-----------LRAPMSFFHTNPLGRIINRFAKDLGDI-DR 1025
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 887 NISDMRNM----ISSLIEevfiafTMAIIGIAWSFAtgwrlaavLVAVSPILCLTSRMFSYiYVSTERmcqdvvisttsi 962
Cdd:PLN03130 1026 NVAVFVNMflgqIFQLLS------TFVLIGIVSTIS--------LWAIMPLLVLFYGAYLY-YQSTAR------------ 1078
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 963 lhkTIVNLDTIKGYSVLSFFRE--NHKNSLRkSWEAFKRRAF-----------WTSLGFAINNSL---LYFVRALLFYCS 1026
Cdd:PLN03130 1079 ---EVKRLDSITRSPVYAQFGEalNGLSTIR-AYKAYDRMAEingrsmdnnirFTLVNMSSNRWLairLETLGGLMIWLT 1154
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1027 SIFI-------SKEFYTVEQMVQVLS-------LATFTLLMASTCIMSLPNVSasRIATsrVLKLSSLKP----GNLHKS 1088
Cdd:PLN03130 1155 ASFAvmqngraENQAAFASTMGLLLSyalnitsLLTAVLRLASLAENSLNAVE--RVGT--YIDLPSEAPlvieNNRPPP 1230
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1089 GYlkfPLVGKIEFDGVSFAYpdseRNHL--ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPL 1164
Cdd:PLN03130 1231 GW---PSSGSIKFEDVVLRY----RPELppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELErgRILIDGCDI 1303
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1165 TNIDTNWLLKKVAIVDQKPHLLGSTI---LESLLYGVDRDInsvMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQI 1241
Cdd:PLN03130 1304 SKFGLMDLRKVLGIIPQAPVLFSGTVrfnLDPFNEHNDADL---WESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQR 1380
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1242 QRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQN--LSCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDEL- 1318
Cdd:PLN03130 1381 QLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREefKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLl 1460
|
970
....*....|.
gi 162312251 1319 MNRHTHFWKLI 1329
Cdd:PLN03130 1461 SNEGSAFSKMV 1471
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
1095-1328 |
3.31e-40 |
|
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: 159.91 E-value: 3.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1095 LVGKIEFDGVSFAY-PDSERnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTNIDTNW 1171
Cdd:TIGR01846 452 LRGAITFENIRFRYaPDSPE---VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQhgQVLVDGVDLAIADPAW 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1172 LLKKVAIVDQKPHLLGSTILESL-LYGVDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARAL 1250
Cdd:TIGR01846 529 LRRQMGVVLQENVLFSRSIRDNIaLCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARAL 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1251 LRNPRLLILDECTSALDSKSSLLLEKTIQNLSC--TVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKL 1328
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYESEALIMRNMREICRgrTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
436-647 |
5.32e-40 |
|
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: 146.43 E-value: 5.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYPSRdenlFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLV 515
Cdd:cd03214 3 ENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 516 CQqpvifdmtireniimrnenasesdfeeVCRLALVDEFAltfDQSYDTpckeasLSGGQQQRIALARALLRDTEILILD 595
Cdd:cd03214 79 PQ---------------------------ALELLGLAHLA---DRPFNE------LSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 596 EPTSALDPITKNLVMDAIR--AHRKGKTTLVITHDMSQINN--DELVLvIDKGHLI 647
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRrlARERGKTVVMVLHDLNLAARyaDRVIL-LKDGRIV 177
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
454-660 |
7.94e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 147.90 E-value: 7.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLgSTITLVCQQPVIF-DMTIRENIIM 532
Cdd:COG1131 18 GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-RRIGYVPQEPALYpDLTVRENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 533 ------RNENASESDFEEVCRLALVDEFAltfdqsyDTPCKeaSLSGGQQQRIALARALLRDTEILILDEPTSALDPITK 606
Cdd:COG1131 97 farlygLPRKEARERIDELLELFGLTDAA-------DRKVG--TLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEAR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 607 NLVMDAIRAHRK-GKTTLVITHDMSQInnDEL---VLVIDKGHLIQRCARKELV--LFED 660
Cdd:COG1131 168 RELWELLRELAAeGKTVLLSTHYLEEA--ERLcdrVAIIDKGRIVADGTPDELKarLLED 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1099-1322 |
8.75e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 147.90 E-value: 8.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYpdseRNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRKTypSEDIYIDGYPLTNiDTNWLLK 1174
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRmllgLLRPT--SGEVRVLGEDVAR-DPAEVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQKPHLLGS-TILESL-----LYGVDRD-----INSVMDALDktymteviqnLPNGLDTPLlefsKNFSGGQIQR 1243
Cdd:COG1131 74 RIGYVPQEPALYPDlTVRENLrffarLYGLPRKearerIDELLELFG----------LTDAADRKV----GTLSGGMKQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1244 LAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSLM-KLADRIIVMDSGIVKESGSFDELM 1319
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAaegKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELK 219
|
...
gi 162312251 1320 NRH 1322
Cdd:COG1131 220 ARL 222
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1044-1292 |
4.35e-39 |
|
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: 154.06 E-value: 4.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1044 LSLATFTLLMA-STCIMSLPnvsASRIATSRVLKLSSLKPGNLHKSGYLKFPLVGK---IEFDGVSFAYPDSERnhlALN 1119
Cdd:TIGR02868 279 LPLAAFEAFAAlPAAAQQLT---RVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGkptLELRDLSAGYPGAPP---VLD 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1120 NVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDGYPLTNIDTNWLLKKVAIVDQKPHLLGSTILESLLYG 1197
Cdd:TIGR02868 353 GVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDplQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1198 V-DRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSL-LLE 1275
Cdd:TIGR02868 433 RpDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADeLLE 512
|
250
....*....|....*...
gi 162312251 1276 KTIQNLS-CTVLIITHQP 1292
Cdd:TIGR02868 513 DLLAALSgRTVVLITHHL 530
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
433-644 |
4.55e-39 |
|
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: 143.51 E-value: 4.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRDENLfsLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTI 512
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 513 TLVCQQPVIFDMTIRENIimrnenasesdfeevcrlalvdefaltfdqsydtpckeasLSGGQQQRIALARALLRDTEIL 592
Cdd:cd03246 79 GYLPQDDELFSGSIAENI----------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 162312251 593 ILDEPTSALDPITKNLVMDAIRAHRK-GKTTLVITHDMSQINNDELVLVIDKG 644
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDG 171
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
434-647 |
4.67e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 145.20 E-value: 4.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPsrdENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHvlgstit 513
Cdd:COG2884 3 RFENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 lvcQQP-------VIF-------DMTIRENII--MRNENASESDFEEVCRLALvDEFALTfDQSYDTPckeASLSGGQQQ 577
Cdd:COG2884 73 ---EIPylrrrigVVFqdfrllpDRTVYENVAlpLRVTGKSRKEIRRRVREVL-DLVGLS-DKAKALP---HELSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 578 RIALARALLRDTEILILDEPTSALDPITKNLVMDAI-RAHRKGKTTLVITHDMSQINN-DELVLVIDKGHLI 647
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLeEINRRGTTVLIATHDLELVDRmPKRVLELEDGRLV 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
433-632 |
1.46e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 141.94 E-value: 1.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRdenlFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGS-- 510
Cdd:cd03229 1 LELKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 511 TITLVCQQPVIF-DMTIRENIIMRnenasesdfeevcrlalvdefaltfdqsydtpckeasLSGGQQQRIALARALLRDT 589
Cdd:cd03229 77 RIGMVFQDFALFpHLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 162312251 590 EILILDEPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDMSQI 632
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEA 164
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
434-645 |
4.47e-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: 140.07 E-value: 4.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRdenlFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQqpvifdmtireniimrnenasesdfeevcrlalvdefaltfdqsydtpckeasLSGGQQQRIALARALLRDTEILI 593
Cdd:cd00267 77 YVPQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 162312251 594 LDEPTSALDPITKNLVMDAIRAH-RKGKTTLVITHDMSQINN-DELVLVIDKGH 645
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
434-630 |
5.39e-38 |
|
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: 141.86 E-value: 5.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTF---ISLLLRyfsPTYGNIYLDDFPLEEIDEHVLGS 510
Cdd:cd03255 2 ELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLlniLGGLDR---PTSGEVRVDGTDISKLSEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 511 ----TITLVCQQP-VIFDMTIRENIIMRNENASESDFEEVCR-LALVDEFALtfDQSYDTPCKEasLSGGQQQRIALARA 584
Cdd:cd03255 79 frrrHIGFVFQSFnLLPDLTALENVELPLLLAGVPKKERRERaEELLERVGL--GDRLNHYPSE--LSGGQQQRVAIARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 162312251 585 LLRDTEILILDEPTSALDPITKNLVMDAIR--AHRKGKTTLVITHDMS 630
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPE 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1099-1313 |
7.38e-38 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 141.87 E-value: 7.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTL----VELLRKTypSEDIYIDGYPLTNIDTNWLL- 1173
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLaraiLGLLKPT--SGSIIFDGKDLLKLSRRLRKi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1174 --KKVAIVDQKPHL-------LGSTILESLLygvdrdINSVMDalDKTYMTEVIQNLPNGLDTPlLEFSKN----FSGGQ 1240
Cdd:cd03257 80 rrKEIQMVFQDPMSslnprmtIGEQIAEPLR------IHGKLS--KKEARKEAVLLLLVGVGLP-EEVLNRypheLSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1241 IQRLAFARALLRNPRLLILDECTSALDSKSS---LLLEKTIQN-LSCTVLIITHQPSLMK-LADRIIVMDSGIVKESG 1313
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQaqiLDLLKKLQEeLGLTLLFITHDLGVVAkIADRVAVMYAGKIVEEG 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1099-1309 |
1.21e-37 |
|
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: 139.27 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERnhLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDGYPLTNIDTNWLLKKV 1176
Cdd:cd03246 1 LEVENVSFRYPGAEP--PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRptSGRVRLDGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHLLGSTILESLLygvdrdinsvmdaldktymteviqnlpngldtpllefsknfSGGQIQRLAFARALLRNPRL 1256
Cdd:cd03246 79 GYLPQDDELFSGSIAENIL-----------------------------------------SGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 1257 LILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSLMKLADRIIVMDSGIV 1309
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
434-648 |
1.26e-37 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 141.67 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDenlFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:cd03295 2 EFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIF-DMTIRENIIM-----------RNENASESdfeevcrLALVDEFALTFDQSYdtpckEASLSGGQQQRIAL 581
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALvpkllkwpkekIRERADEL-------LALVGLDPAEFADRY-----PHELSGGQQQRVGV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 582 ARALLRDTEILILDEPTSALDPITK-NLVMDAIRAHRK-GKTTLVITHDMsqinnDELVL------VIDKGHLIQ 648
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRdQLQEEFKRLQQElGKTIVFVTHDI-----DEAFRladriaIMKNGEIVQ 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1099-1307 |
1.35e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 140.34 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERnhlaLNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDGYPLTNIDTNWLLKKV 1176
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPptSGEIYLDGKPLSAMPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHLLGSTILESLLYGVD-RDinsvmDALDKTYMTEVIQNLpnGLDTPLLEFS-KNFSGGQIQRLAFARALLRNP 1254
Cdd:COG4619 77 AYVPQEPALWGGTVRDNLPFPFQlRE-----RKFDRERALELLERL--GLPPDILDKPvERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1255 RLLILDECTSALDSKSSLLLEKTIQNLSC----TVLIITHQPS-LMKLADRIIVMDSG 1307
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAeegrAVLWVSHDPEqIERVADRVLTLEAG 207
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
436-657 |
1.47e-37 |
|
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: 149.81 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYPSrdENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLV 515
Cdd:TIGR01842 320 ENVTIVPPG--GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 516 CQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKE--ASLSGGQQQRIALARALLRDTEILI 593
Cdd:TIGR01842 398 PQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPggATLSGGQRQRIALARALYGDPKLVV 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 594 LDEPTSALDPITKNLVMDAI-RAHRKGKTTLVITHDMSQINNDELVLVIDKGHlIQRCARKELVL 657
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIkALKARGITVVVITHRPSLLGCVDKILVLQDGR-IARFGERDEVL 541
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1063-1319 |
2.29e-37 |
|
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: 149.04 E-value: 2.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1063 NVSASRIATSRVLKLSSLKPGNlhkSGYLKFPLV-GKIEFDGVSFAYPDSerNHLALNNVSLSIEAREKVAIVGISGSGK 1141
Cdd:TIGR01842 283 QFSGARQAYKRLNELLANYPSR---DPAMPLPEPeGHLSVENVTIVPPGG--KKPTLRGISFSLQAGEALAIIGPSGSGK 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1142 STLVELLRKTYPSE--DIYIDGYPLTNIDTNWLLKKVAIVDQKPHLLGSTILESLL-YGVDRDINSVMDALDKTYMTEVI 1218
Cdd:TIGR01842 358 STLARLIVGIWPPTsgSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIArFGENADPEKIIEAAKLAGVHELI 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1219 QNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSLM 1295
Cdd:TIGR01842 438 LRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITHRPSLL 517
|
250 260
....*....|....*....|....
gi 162312251 1296 KLADRIIVMDSGIVKESGSFDELM 1319
Cdd:TIGR01842 518 GCVDKILVLQDGRIARFGERDEVL 541
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1099-1318 |
1.07e-36 |
|
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: 138.47 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSErnhlALNNVSLSIEAREKVAIVGISGSGKSTL-------VELLRKTYPSEDIYIDGYPLTNIDTN- 1170
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLlrllnrlNDLIPGAPDEGEVLLDGKDIYDLDVDv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1171 -WLLKKVAIVDQKPHLLGSTILESLLYGV-DRDI--NSVMDALDKTYMTEViqNLPNGLDTPLLEFSknFSGGQIQRLAF 1246
Cdd:cd03260 77 lELRRRVGMVFQKPNPFPGSIYDNVAYGLrLHGIklKEELDERVEEALRKA--ALWDEVKDRLHALG--LSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 1247 ARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL--SCTVLIITH---QPSlmKLADRIIVMDSGIVKESGSFDEL 1318
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHnmqQAA--RVADRTAFLLNGRLVEFGPTEQI 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
434-628 |
1.29e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.45 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEidehvLGSTIT 513
Cdd:COG1116 9 ELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFD-MTIRENII--MRNENASESDFEEVCRlALVDEFALT-FDQSYdtPckeASLSGGQQQRIALARALLRDT 589
Cdd:COG1116 84 VVFQEPALLPwLTVLDNVAlgLELRGVPKAERRERAR-ELLELVGLAgFEDAY--P---HQLSGGMRQRVAIARALANDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 162312251 590 EILILDEPTSALDPITKNLVMDAIRA--HRKGKTTLVITHD 628
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHD 198
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
434-647 |
1.33e-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: 138.41 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEH---VLGS 510
Cdd:cd03257 3 EVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 511 TITLVCQQPVI-FD--MTIRENI---IMRNENASESDFEEVCRLALVDEFAL--TFDQSYdtPckeASLSGGQQQRIALA 582
Cdd:cd03257 83 EIQMVFQDPMSsLNprMTIGEQIaepLRIHGKLSKKEARKEAVLLLLVGVGLpeEVLNRY--P---HELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 583 RALLRDTEILILDEPTSALDPITKNLVMDAIR--AHRKGKTTLVITHDMS---QINNDelVLVIDKGHLI 647
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGvvaKIADR--VAVMYAGKIV 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
434-647 |
1.51e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 138.25 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTF---ISLLLRyfsPTYGNIYLDDFPLEEIDEHVL-- 508
Cdd:COG1136 6 ELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLlniLGGLDR---PTSGEVLIDGQDISSLSERELar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 509 --GSTITLVCQQP-VIFDMTIRENIIM----RNENASEsDFEEVcrLALVDEFALTfDQSYDTPckeASLSGGQQQRIAL 581
Cdd:COG1136 83 lrRRHIGFVFQFFnLLPELTALENVALplllAGVSRKE-RRERA--RELLERVGLG-DRLDHRP---SQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 582 ARALLRDTEILILDEPTSALDPITKNLVMDAIR--AHRKGKTTLVITHDMSQINNDELVLVIDKGHLI 647
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRelNRELGTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
434-647 |
2.40e-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: 138.02 E-value: 2.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRdenlFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDD---FPLEEIDEHVLGS 510
Cdd:cd03261 2 ELRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGediSGLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 511 TITLVCQQPVIFD-MTIRENI---IMRNENASESDFEEVCRLALvDEFALTFDQSYdtpcKEASLSGGQQQRIALARALL 586
Cdd:cd03261 78 RMGMLFQSGALFDsLTVFENVafpLREHTRLSEEEIREIVLEKL-EAVGLRGAEDL----YPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 587 RDTEILILDEPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDMSQINN--DElVLVIDKGHLI 647
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAiaDR-IAVLYDGKIV 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1099-1321 |
7.79e-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: 136.17 E-value: 7.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLR--KTYPSEDIYIDGYPLTNIDTNWLLK-- 1174
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINglERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 -KVAIVDQKPHLLGS-TILESLLYGVDrdinsvmdaLDKTYMTEVIQNLpngldTPLLEF----------SKNFSGGQIQ 1242
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVALPLE---------IAGVPKAEIEERV-----LELLELvgledkadayPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1243 RLAFARALLRNPRLLILDECTSALDSKSS----LLLEKTIQNLSCTVLIITHQPSLMK-LADRIIVMDSGIVKESGSFDE 1317
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTqsilALLRDINRELGLTIVLITHEMEVVKrICDRVAVMEKGEVVEEGTVEE 227
|
....
gi 162312251 1318 LMNR 1321
Cdd:cd03258 228 VFAN 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1099-1324 |
8.13e-36 |
|
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: 143.89 E-value: 8.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNHL-ALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRktyPSE-DIYIDGYPLTNI---DT 1169
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVrAVDDVSLTLRRGETLGLVGESGSGKSTLARlllgLLR---PTSgSILFDGKDLTKLsrrSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1170 NWLLKKVAIVDQKP-------HLLGSTILESL-LYGV--DRDINS-VMDALDKTymteviqnlpnGLDTPLLE-FSKNFS 1237
Cdd:COG1123 338 RELRRRVQMVFQDPysslnprMTVGDIIAEPLrLHGLlsRAERRErVAELLERV-----------GLPPDLADrYPHELS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1238 GGQIQRLAFARALLRNPRLLILDECTSALDSKSSL----LLEKTIQNLSCTVLIITHQPSLMK-LADRIIVMDSGIVKES 1312
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALDVSVQAqilnLLRDLQRELGLTYLFISHDLAVVRyIADRVAVMYDGRIVED 486
|
250
....*....|..
gi 162312251 1313 GSFDELMNRHTH 1324
Cdd:COG1123 487 GPTEEVFANPQH 498
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
434-644 |
1.75e-35 |
|
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: 134.58 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRdeNLFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHvlgstIT 513
Cdd:cd03235 1 EVEDLTVSYGGH--PVLE--DVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVI---FDMTIRENIIMRN-------ENASESDFEEVCR-LALVD--EFAltfDQSYDTpckeasLSGGQQQRIA 580
Cdd:cd03235 72 YVPQRRSIdrdFPISVRDVVLMGLyghkglfRRLSKADKAKVDEaLERVGlsELA---DRQIGE------LSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 581 LARALLRDTEILILDEPTSALDPITKNLVMDAIRA-HRKGKTTLVITHDMSQINN--DElVLVIDKG 644
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyfDR-VLLLNRT 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
436-646 |
4.06e-35 |
|
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: 132.14 E-value: 4.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYPSRdenlFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGStITLV 515
Cdd:cd03230 4 RNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 516 CQQPVIF-DMTIRENIimrnenasesdfeevcrlalvdefaltfdqsydtpckeaSLSGGQQQRIALARALLRDTEILIL 594
Cdd:cd03230 79 PEEPSLYeNLTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 595 DEPTSALDPITKNLVMDAIRAHRK-GKTTLVITHDMSQInnDEL---VLVIDKGHL 646
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEA--ERLcdrVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1099-1307 |
4.56e-35 |
|
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: 131.93 E-value: 4.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRK-TYPSE-DIYIDGYPLTNIDTNWLL--K 1174
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEPDSgSILIDGEDLTDLEDELPPlrR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQKPHLLgstilesllygvdrdinsvmdaldkTYMTeVIQNLPNGLdtpllefsknfSGGQIQRLAFARALLRNP 1254
Cdd:cd03229 77 RIGMVFQDFALF-------------------------PHLT-VLENIALGL-----------SGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1255 RLLILDECTSALDSKS----SLLLEKTIQNLSCTVLIITHQPS-LMKLADRIIVMDSG 1307
Cdd:cd03229 120 DVLLLDEPTSALDPITrrevRALLKSLQAQLGITVVLVTHDLDeAARLADRVVVLRDG 177
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1099-1313 |
5.32e-35 |
|
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: 132.05 E-value: 5.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERnhLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTNIDTNwLLKKV 1176
Cdd:cd03247 1 LSINNVSFSYPEQEQ--QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQqgEITLDGVPVSDLEKA-LSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHLLGSTILESLlygvdrdinsvmdaldktymteviqnlpngldtpllefSKNFSGGQIQRLAFARALLRNPRL 1256
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1257 LILDECTSALDSKSSL-LLEKTIQNL-SCTVLIITHQPSLMKLADRIIVMDSGIVKESG 1313
Cdd:cd03247 120 VLLDEPTVGLDPITERqLLSLIFEVLkDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1098-1313 |
5.92e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 135.14 E-value: 5.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1098 KIEFDGVSFAYPDSERnhLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTnIDTNW-LLK 1174
Cdd:PRK13635 5 IIRVEHISFRYPDAAT--YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEagTITVGGMVLS-EETVWdVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQKP--HLLGSTI-------LESllYGVDRD--INSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQR 1243
Cdd:PRK13635 82 QVGMVFQNPdnQFVGATVqddvafgLEN--IGVPREemVERVDQALRQVGMEDFLNREPHRL-----------SGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1244 LAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL----SCTVLIITHQPSLMKLADRIIVMDSGIVKESG 1313
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkeqkGITVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
433-644 |
9.52e-35 |
|
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: 132.21 E-value: 9.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRD-ENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLddfpleeidehvlGST 511
Cdd:cd03250 1 ISVEDASFTWDSGEqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-------------PGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 512 ITLVCQQPVIFDMTIRENIIMRNEnASESDFEEVCRL-ALVDEFALtFDQSYDTPCKE--ASLSGGQQQRIALARALLRD 588
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP-FDEERYEKVIKAcALEPDLEI-LPDGDLTEIGEkgINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 589 TEILILDEPTSALDPITKNLVMD-AIRAH-RKGKTTLVITHDMSQINNDELVLVIDKG 644
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFEnCILGLlLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1118-1264 |
1.97e-34 |
|
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: 129.30 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELL-RKTYPSED-IYIDGYPLTNIDTNWLLKKVAIVDQKPHLL-GSTILESL 1194
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIaGLLSPTEGtILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 1195 LYGVDrdinsvMDALDKTYMTEVIQ------NLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTS 1264
Cdd:pfam00005 81 RLGLL------LKGLSKREKDARAEealeklGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
434-647 |
2.99e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 133.35 E-value: 2.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAY-PSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISL---LLRyfsPTYGNIYLDDF---PLEEIDEH 506
Cdd:TIGR04521 2 KLKNVSYIYqPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHlngLLK---PTSGTVTIDGRditAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 507 VLGSTITLVCQQP--VIFDMTIRENIIM--RNENASESDFEE-VCR-LALVDefaltFDQSYdtpcKEAS---LSGGQQQ 577
Cdd:TIGR04521 79 DLRKKVGLVFQFPehQLFEETVYKDIAFgpKNLGLSEEEAEErVKEaLELVG-----LDEEY----LERSpfeLSGGQMR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 578 RIALARALLRDTEILILDEPTSALDPITKNLVMDAI-RAHR-KGKTTLVITHDMSQINN--DElVLVIDKGHLI 647
Cdd:TIGR04521 150 RVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFkRLHKeKGLTVILVTHSMEDVAEyaDR-VIVMHKGKIV 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1100-1307 |
5.40e-34 |
|
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: 128.13 E-value: 5.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1100 EFDGVSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKSTLVELL-RKTYPSE-DIYIDGYPLTNIDTNWLLKKVA 1177
Cdd:cd00267 1 EIENLSFRYGG----RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIaGLLKPTSgEILIDGKDIAKLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1178 IVDQkphllgstilesllygvdrdinsvmdaldktymteviqnlpngldtpllefsknFSGGQIQRLAFARALLRNPRLL 1257
Cdd:cd00267 77 YVPQ------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1258 ILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSL-MKLADRIIVMDSG 1307
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAeegRTVIIVTHDPELaELAADRVIVLKDG 156
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
436-656 |
5.53e-34 |
|
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: 131.46 E-value: 5.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLV 515
Cdd:COG1124 5 RNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 516 CQQP-VIFD--MTIRENI-----IMRNENASEsdfeEVCRLAlvDEFALTFDQSYDTPckeASLSGGQQQRIALARALLR 587
Cdd:COG1124 85 FQDPyASLHprHTVDRILaeplrIHGLPDREE----RIAELL--EQVGLPPSFLDRYP---HQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 588 DTEILILDEPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDMSQInnDEL---VLVIDKGHLIQRCARKELV 656
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVV--AHLcdrVAVMQNGRIVEELTVADLL 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
434-646 |
5.63e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.36 E-value: 5.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYpsRDENLFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEidehvLGSTIT 513
Cdd:COG1121 8 ELENLTVSY--GGRPVLE--DVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVI---FDMTIRENIIM-------RNENASESDFEEVCR-LALVD--EFAltfDQSYDTpckeasLSGGQQQRIA 580
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVLMgrygrrgLFRRPSRADREAVDEaLERVGleDLA---DRPIGE------LSGGQQQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 581 LARALLRDTEILILDEPTSALDPITKNLVMDAIRA-HRKGKTTLVITHDMSQINN--DElVLVIDKGHL 646
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyfDR-VLLLNRGLV 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1099-1322 |
5.74e-34 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 138.11 E-value: 5.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNhlALNNVSLSIEAREKVAIVGISGSGKSTL----VELLRKT-YPSEDIYIDGYPLTNIDTNWLL 1173
Cdd:COG1123 5 LEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLalalMGLLPHGgRISGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1174 KKVAIVDQKP--HLLGSTILESL-----LYGVDRDinsVMDALDKTYMTEViqnlpnGLDTPLLEFSKNFSGGQIQRLAF 1246
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIaealeNLGLSRA---EARARVLELLEAV------GLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1247 ARALLRNPRLLILDECTSALDSKSSL----LLEKTIQNLSCTVLIITHQPSLM-KLADRIIVMDSGIVKESGSFDELMNR 1321
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAeildLLRELQRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
.
gi 162312251 1322 H 1322
Cdd:COG1123 234 P 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1099-1320 |
8.12e-34 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 131.32 E-value: 8.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKSTLVELL-RKTYPSE-DIYIDGYPLTNIDTNWLLKKV 1176
Cdd:COG1120 2 LEAENLSVGYGG----RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALaGLLKPSSgEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHL-LGSTILESLLYG-----------VDRDINSVMDALDKTYMTEVIqnlpnglDTPLLEFSknfsGGQIQRL 1244
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGryphlglfgrpSAEDREAVEEALERTGLEHLA-------DRPVDELS----GGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1245 AFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS----CTVLIITHQPSL-MKLADRIIVMDSGIVKESGSFDELM 1319
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArergRTVVMVLHDLNLaARYADRLVLLKDGRIVAQGPPEEVL 226
|
.
gi 162312251 1320 N 1320
Cdd:COG1120 227 T 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1099-1313 |
9.40e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.79 E-value: 9.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDserNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELL-RKTYPSE-DIYIDGYPLTNIDTN---WLL 1173
Cdd:COG2884 2 IRFENVSKRYPG---GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLyGEERPTSgQVLVNGQDLSRLKRReipYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1174 KKVAIVDQKPHLLGS-TILESLLY-----GVDR-DINS-VMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLA 1245
Cdd:COG2884 79 RRIGVVFQDFRLLPDrTVYENVALplrvtGKSRkEIRRrVREVLDLVGLSDKAKALPHEL-----------SGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 1246 FARALLRNPRLLILDECTSALDSKSSL----LLEKtIQNLSCTVLIITHQPSLM-KLADRIIVMDSGIVKESG 1313
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWeimeLLEE-INRRGTTVLIATHDLELVdRMPKRVLELEDGRLVRDE 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
736-1314 |
9.71e-34 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 142.09 E-value: 9.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 736 LRMEKESFQETNVDQTFHLFDD-KEHACSLTLIFKSIwkVKKLRWFFLLGLLTSLIQGASVPIFAYV---ISKCLNLFMQ 811
Cdd:PTZ00265 18 LSIKDEVEKELNKKGTFELYKKiKTQKIPFFLPFKCL--PASHRKLLGVSFVCATISGGTLPFFVSVfgvIMKNMNLGEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 812 IDPSIgvafwSSMVLVVAAGSGASYFFSHYIFSISAKIwCDHYRLLAVKVLFTQDQAWFDqieNYPlvlSKILVNNISDM 891
Cdd:PTZ00265 96 VNDII-----FSLVLIGIFQFILSFISSFCMDVVTTKI-LKTLKLEFLKSVFYQDGQFHD---NNP---GSKLTSDLDFY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 892 RNMISSLIEEVFIA---FTMAIIGI-AWSFATGWRLAavlvavspiLCLTSrMFSYIYVSTERMCQDVVIS--------- 958
Cdd:PTZ00265 164 LEQVNAGIGTKFITiftYASAFLGLyIWSLFKNARLT---------LCITC-VFPLIYICGVICNKKVKINkktsllynn 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 959 -TTSILHKTIVNLDTIKGY----SVLSFFrenhkNSLRKSWEAFKRRA-FWTSLGFAINNSLLYFVRALLF-YCSSIFIS 1031
Cdd:PTZ00265 234 nTMSIIEEALVGIRTVVSYcgekTILKKF-----NLSEKLYSKYILKAnFMESLHIGMINGFILASYAFGFwYGTRIIIS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1032 --------KEFYTVeqmvQVLSLATFTLLMASTCIMSLPNVS---ASRIATSRVLKLSSLKPGNLHKSGYLKFPLVGKIE 1100
Cdd:PTZ00265 309 dlsnqqpnNDFHGG----SVISILLGVLISMFMLTIILPNITeymKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1101 FDGVSFAYpDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYI-DGYPLTNIDTNWLLKKVA 1177
Cdd:PTZ00265 385 FKNVRFHY-DTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPTEgDIIInDSHNLKDINLKWWRSKIG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1178 IVDQKPHLLGSTILESLLYGV----------------------------------DRDINSVMDALDKTYMTEVIQN--- 1220
Cdd:PTZ00265 464 VVSQDPLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcAGDLNDMSNTTDSNELIEMRKNyqt 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1221 ---------------------LPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQ 1279
Cdd:PTZ00265 544 ikdsevvdvskkvlihdfvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN 623
|
650 660 670
....*....|....*....|....*....|....*....
gi 162312251 1280 NLSCT----VLIITHQPSLMKLADRIIVMDSgivKESGS 1314
Cdd:PTZ00265 624 NLKGNenriTIIIAHRLSTIRYANTIFVLSN---RERGS 659
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1099-1320 |
1.16e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 131.27 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDGYPLTNIDTNWLLKKV 1176
Cdd:PRK13632 8 IKVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKpqSGEIKIDGITISKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKP--HLLGSTILESLLYGVD-RDIN-SVMDALDKTYMTEViqnlpnGLDTPLLEFSKNFSGGQIQRLAFARALLR 1252
Cdd:PRK13632 86 GIIFQNPdnQFIGATVEDDIAFGLEnKKVPpKKMKDIIDDLAKKV------GMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 1253 NPRLLILDECTSALDSKSSLLLEKTIQNL----SCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
433-628 |
1.63e-33 |
|
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: 128.75 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYpsRDENLFSliNVSVFIPFGELVHIIGPSGSGKSTfislLLR----YFSPTYGNIYLDDFPLEEIDEHVl 508
Cdd:COG4133 3 LEAENLSCRR--GERLLFS--GLSFTLAAGEALALTGPNGSGKTT----LLRilagLLPPSAGEVLWNGEPIRDAREDY- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 509 GSTITLVCQQPVIF-DMTIRENII----MRNENASESDFEEVCRLALVDEFAltfdqsyDTPCKEasLSGGQQQRIALAR 583
Cdd:COG4133 74 RRRLAYLGHADGLKpELTVRENLRfwaaLYGLRADREAIDEALEAVGLAGLA-------DLPVRQ--LSAGQKRRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 162312251 584 ALLRDTEILILDEPTSALDPITKNLVMDAIRAHR-KGKTTLVITHD 628
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLaRGGAVLLTTHQ 190
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
100-414 |
2.04e-33 |
|
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: 131.81 E-value: 2.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 100 DIPLIFGTLIFTCLSAALEPLMTWTTGKVFDALSQYATSQitlgkMISLINFNSLLITIFGLASCVFSFGVRFLWQYLSA 179
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDE-----LRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 180 IAGKRARSLCFHVLSSKSSTFYSLTESKSG-LVNSVDRCIQFYEKSISLPMFHIAENLAISLSCLIISFRYSWSLTLVVL 258
Cdd:cd18578 82 RLTRRLRKLAFRAILRQDIAWFDDPENSTGaLTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 259 ASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSFLDAFQG 338
Cdd:cd18578 162 ATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGF 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 339 GVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTVFGSCLSVASSLQQILPAIPDLIKGKFSSHFIKTLCESHDPI 414
Cdd:cd18578 242 GLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
434-648 |
2.25e-33 |
|
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: 128.41 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSrdenLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGstIT 513
Cdd:cd03259 2 ELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN--IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFD-MTIRENII--MRNENASESDFEEVCRLALvDEFALTfDQSYDTPckeASLSGGQQQRIALARALLRDTE 590
Cdd:cd03259 76 MVFQDYALFPhLTVAENIAfgLKLRGVPKAEIRARVRELL-ELVGLE-GLLNRYP---HELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 591 ILILDEPTSALDPITKNLVMDAIRA-HRK-GKTTLVITHDMSqinnDEL-----VLVIDKGHLIQ 648
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKElQRElGITTIYVTHDQE----EALaladrIAVMNEGRIVQ 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
436-647 |
2.34e-33 |
|
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: 129.59 E-value: 2.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYPSRdenlFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGStITLV 515
Cdd:COG4555 5 ENLSKKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 516 CQQPVIFD-MTIRENI--------IMRNENasESDFEEVCRLALVDEFAltfDQSYDTpckeasLSGGQQQRIALARALL 586
Cdd:COG4555 80 PDERGLYDrLTVRENIryfaelygLFDEEL--KKRIEELIELLGLEEFL---DRRVGE------LSTGMKKKVALARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 587 RDTEILILDEPTSALDPITKNLVMDAIRAHRK-GKTTLVITHDMSQINN--DElVLVIDKGHLI 647
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlcDR-VVILHKGKVV 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1099-1304 |
2.35e-33 |
|
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: 128.74 E-value: 2.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRktyPSE-DIYIDGYPLTNIDtnwll 1173
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRiiagLER---PTSgEVLVDGEPVTGPG----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1174 KKVAIVDQKPHLLG-STILESLLYGVDRDINSVMDALDKT--YMTEViqnlpnGLDtpllEFSKNF----SGGQIQRLAF 1246
Cdd:cd03293 73 PDRGYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAeeLLELV------GLS----GFENAYphqlSGGMRQRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1247 ARALLRNPRLLILDECTSALDS--KSSL--LLEKTIQNLSCTVLIITHqpSLMK---LADRIIVM 1304
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDAltREQLqeELLDIWRETGKTVLLVTH--DIDEavfLADRVVVL 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
434-655 |
4.56e-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: 135.42 E-value: 4.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDEnlFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPT---YGNIYLDDFPLEEIDEHVLGS 510
Cdd:COG1123 6 EVRDLSVRYPGGDV--PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 511 TITLVCQQP--VIFDMTIRENII--MRNENASESDFEEVCRLALVDEFALTFDQSYdtpckEASLSGGQQQRIALARALL 586
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAeaLENLGLSRAEARARVLELLEAVGLERRLDRY-----PHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 587 RDTEILILDEPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDMSQI-NNDELVLVIDKGHLIQRCARKEL 655
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1093-1314 |
5.17e-33 |
|
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: 127.14 E-value: 5.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1093 FPLVGKIEFDGVSFAY-PDSERnhlALNNVSLSIEAREKVAIVGISGSGKSTLVE-LLRKTYPSE-DIYIDGYPLTNIDT 1169
Cdd:cd03369 1 WPEHGEIEVENLSVRYaPDLPP---VLKNVSFKVKAGEKIGIVGRTGAGKSTLILaLFRFLEAEEgKIEIDGIDISTIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1170 NWLLKKVAIVDQKPHLLGSTIlesllygvdrdiNSVMDALDKTYMTEVIQNLPngldtpLLEFSKNFSGGQIQRLAFARA 1249
Cdd:cd03369 78 EDLRSSLTIIPQDPTLFSGTI------------RSNLDPFDEYSDEEIYGALR------VSEGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 1250 LLRNPRLLILDECTSALDSKSSLLLEKTIQNL--SCTVLIITHQPSLMKLADRIIVMDSGIVKESGS 1314
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREEftNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
435-655 |
6.80e-33 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 136.00 E-value: 6.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 435 FDNVSFAYpsRDENLFsLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITL 514
Cdd:PRK10790 343 IDNVSFAY--RDDNLV-LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 515 VCQQPVIFDMTIRENIIMRNENASESDFE--EVCRLAlvdEFALTFDQSYDTPCKEA--SLSGGQQQRIALARALLRDTE 590
Cdd:PRK10790 420 VQQDPVVLADTFLANVTLGRDISEEQVWQalETVQLA---ELARSLPDGLYTPLGEQgnNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 591 ILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKEL 655
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQL 561
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1099-1313 |
9.53e-33 |
|
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: 126.87 E-value: 9.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRK-TYPSE-DIYIDGYPLTNIDTNwlLKKV 1176
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlERPDSgEILIDGRDVTGVPPE--RRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQK----PHLlgsTILESLLYG-----VDRD--INSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLA 1245
Cdd:cd03259 75 GMVFQDyalfPHL---TVAENIAFGlklrgVPKAeiRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 1246 FARALLRNPRLLILDECTSALDSKSSL----LLEKTIQNLSCTVLIITHQPS-LMKLADRIIVMDSGIVKESG 1313
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREelreELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1098-1307 |
1.85e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 127.51 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1098 KIEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRktyPSE-DIYIDGYPLTNIDTnwl 1172
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRliagLEK---PTSgEVLVDGKPVTGPGP--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1173 lkKVAIVDQKPHLLG-STILESLLYGVD---------RDInsVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQ 1242
Cdd:COG1116 81 --DRGVVFQEPALLPwLTVLDNVALGLElrgvpkaerRER--ARELLELVGLAGFEDAYPHQL-----------SGGMRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 1243 RLAFARALLRNPRLLILDECTSALDS--KSSL--LLEKTIQNLSCTVLIITHqpSLM---KLADRIIVMDSG 1307
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDAltRERLqdELLRLWQETGKTVLFVTH--DVDeavFLADRVVVLSAR 215
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
434-647 |
1.88e-32 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 127.55 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPsrDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDfpLEEIDEHVLG---S 510
Cdd:TIGR04520 2 EVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWeirK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 511 TITLVCQQPvifD-----MTIRENIIMRNENASEsDFEEVCR-----LALVD--EFAltfDQSydtPckeASLSGGQQQR 578
Cdd:TIGR04520 78 KVGMVFQNP---DnqfvgATVEDDVAFGLENLGV-PREEMRKrvdeaLKLVGmeDFR---DRE---P---HLLSGGQKQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 579 IALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDMSQINNDELVLVIDKGHLI 647
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIV 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
452-630 |
2.02e-32 |
|
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: 125.72 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPL--EEIDEHVLGSTITLVCQQPVIF-DMTIRE 528
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFpHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 529 NII---MRNENASESDFEEVCRlALVDEFALTfDQSYDTPckeASLSGGQQQRIALARALLRDTEILILDEPTSALDPIT 605
Cdd:cd03262 96 NITlapIKVKGMSKAEAEERAL-ELLEKVGLA-DKADAYP---AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
170 180
....*....|....*....|....*.
gi 162312251 606 KNLVMDAIR-AHRKGKTTLVITHDMS 630
Cdd:cd03262 171 VGEVLDVMKdLAEEGMTMVVVTHEMG 196
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
452-631 |
2.18e-32 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 127.03 E-value: 2.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRY--FSPTY---GNIYLD--DFPLEEIDEHVLGSTITLVCQQPVIFDM 524
Cdd:TIGR00972 17 LKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMndLVPGVrieGKVLFDgqDIYDKKIDVVELRRRVGMVFQKPNPFPM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 525 TIRENI---IMRNENASESDFEEVCRLALvdEFALTFDQSYDTPCKEA-SLSGGQQQRIALARALLRDTEILILDEPTSA 600
Cdd:TIGR00972 97 SIYDNIaygPRLHGIKDKKELDEIVEESL--KKAALWDEVKDRLHDSAlGLSGGQQQRLCIARALAVEPEVLLLDEPTSA 174
|
170 180 190
....*....|....*....|....*....|.
gi 162312251 601 LDPITKNLVMDAIRAHRKGKTTLVITHDMSQ 631
Cdd:TIGR00972 175 LDPIATGKIEELIQELKKKYTIVIVTHNMQQ 205
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1099-1321 |
2.49e-32 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 126.20 E-value: 2.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSernhLALNNVSLSIEAREKVAIVGISGSGKSTLVELLR--KTYPSEDIYIDGYPLTNIDTNwlLKKV 1176
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAgfETPTSGEILLDGKDITNLPPH--KRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQK----PHLlgsTILESLLYGVDR------DINS-VMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLA 1245
Cdd:cd03300 75 NTVFQNyalfPHL---TVFENIAFGLRLkklpkaEIKErVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1246 FARALLRNPRLLILDECTSALDSK--SSLLLE-KTIQ-NLSCTVLIITH-QPSLMKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKlrKDMQLElKRLQkELGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
.
gi 162312251 1321 R 1321
Cdd:cd03300 221 E 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
434-655 |
2.69e-32 |
|
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: 126.25 E-value: 2.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRdenlfsLI--NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEH---VL 508
Cdd:COG1127 7 EVRNLTKSFGDR------VVldGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 509 GSTITLVCQQPVIFD-MTIRENI---IMRNENASESDFEEVCR--LALV--DEFALTFdqsydtPckeASLSGGQQQRIA 580
Cdd:COG1127 81 RRRIGMLFQGGALFDsLTVFENVafpLREHTDLSEAEIRELVLekLELVglPGAADKM------P---SELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 581 LARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDMsqinnDEL------VLVIDKGHLIQRCAR 652
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDL-----DSAfaiadrVAVLADGKIIAEGTP 226
|
...
gi 162312251 653 KEL 655
Cdd:COG1127 227 EEL 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
452-1325 |
3.54e-32 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 136.83 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDdfpleeidehvlgSTITLVCQQPVIFDMTIRENII 531
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 532 MRNEN--ASESDFEEVCRLAlVDEFALTFDQSYDTPCKEASLSGGQQQRIALARALLRDTEILILDEPTSALDP-ITKNL 608
Cdd:PTZ00243 743 FFDEEdaARLADAVRVSQLE-ADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVGERV 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 609 VMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHliqrcarkelVLF----EDFENNvSIDEKVLKEEADNPfilpn 684
Cdd:PTZ00243 822 VEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGR----------VEFsgssADFMRT-SLYATLAAELKENK----- 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 685 eesllekywiNYNESFSQLSRESLFTSLESPfTDIESPTIVSRRKIVEQRKLRMEKESFQETNVDqtfhlfddkEHACSL 764
Cdd:PTZ00243 886 ----------DSKEGDADAEVAEVDAAPGGA-VDHEPPVAKQEGNAEGGDGAALDAAAGRLMTRE---------EKASGS 945
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 765 TlifksIWKVKKLRWFFLLGLLTSLIQgasvpIFAYVISKCLNlfmqIDPSIGVAFWSS----------------MVLVV 828
Cdd:PTZ00243 946 V-----PWSTYVAYLRFCGGLHAAGFV-----LATFAVTELVT----VSSGVWLSMWSTrsfklsaatylyvylgIVLLG 1011
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 829 AAGSGASYFFSHYIFSI-SAKIWCDHYRLLAVKVLftqdqAWFDQIenyPL--VLSK------ILVNNISDmrNMISsLI 899
Cdd:PTZ00243 1012 TFSVPLRFFLSYEAMRRgSRNMHRDLLRSVSRGTM-----SFFDTT---PLgrILNRfsrdidILDNTLPM--SYLY-LL 1080
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 900 EEVF-IAFTMAIIGIAWSFatgwrlaaVLVAVSPILCLTSRMFSyIYVSTERMCQdvviSTTSILHKTIVNL--DTIKGY 976
Cdd:PTZ00243 1081 QCLFsICSSILVTSASQPF--------VLVALVPCGYLYYRLMQ-FYNSANREIR----RIKSVAKSPVFTLleEALQGS 1147
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 977 SVLSFFRENHKNSLrkswEAFKRRAFWTSLGFAINNSLLYF-VRALLFYCSSIFISKEFYTVEQMVQVLS----LATFTL 1051
Cdd:PTZ00243 1148 ATITAYGKAHLVMQ----EALRRLDVVYSCSYLENVANRWLgVRVEFLSNIVVTVIALIGVIGTMLRATSqeigLVSLSL 1223
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1052 LMASTCIMSL-------PNVSASRIATSRVL------------KLSSL-------------KPGNL-----HKSGYLKFP 1094
Cdd:PTZ00243 1224 TMAMQTTATLnwlvrqvATVEADMNSVERLLyytdevphedmpELDEEvdalerrtgmaadVTGTVviepaSPTSAAPHP 1303
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1095 LV-GKIEFDGVSFAYpdSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLveLLRKTYPSE----DIYIDGYPLTNIDT 1169
Cdd:PTZ00243 1304 VQaGSLVFEGVQMRY--REGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTL--LLTFMRMVEvcggEIRVNGREIGAYGL 1379
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1170 NWLLKKVAIVDQKPHLLGSTILESLLYGVDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARA 1249
Cdd:PTZ00243 1380 RELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARA 1459
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1250 LLRNPRLLIL-DECTSALDSKssllLEKTIQNL------SCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDEL-MNR 1321
Cdd:PTZ00243 1460 LLKKGSGFILmDEATANIDPA----LDRQIQATvmsafsAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNR 1535
|
....
gi 162312251 1322 HTHF 1325
Cdd:PTZ00243 1536 QSIF 1539
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1099-1309 |
5.62e-32 |
|
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: 124.56 E-value: 5.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKSTLvelLR-----KTYPSEDIYIDGYPLTNIDTNW-- 1171
Cdd:cd03262 1 IEIKNLHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTL---LRcinllEEPDSGTIIIDGLKLTDDKKNIne 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1172 LLKKVAIVDQK----PHLlgsTILESLLY------GVDRD--INSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGG 1239
Cdd:cd03262 74 LRQKVGMVFQQfnlfPHL---TVLENITLapikvkGMSKAeaEERALELLEKVGLADKADAYPAQL-----------SGG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1240 QIQRLAFARALLRNPRLLILDECTSALDSKssLLLE--KTIQNLS---CTVLIITHQpslM----KLADRIIVMDSGIV 1309
Cdd:cd03262 140 QQQRVAIARALAMNPKVMLFDEPTSALDPE--LVGEvlDVMKDLAeegMTMVVVTHE---MgfarEVADRVIFMDDGRI 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
444-648 |
7.17e-32 |
|
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: 125.14 E-value: 7.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 444 SRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLD-----DFPLEEIDehvlgstITLVCQQ 518
Cdd:cd03299 7 SKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditNLPPEKRD-------ISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 519 PVIF-DMTIRENI----IMRNENASESDFEevcrlalVDEFA--LTFDQSYDTpcKEASLSGGQQQRIALARALLRDTEI 591
Cdd:cd03299 80 YALFpHMTVYKNIayglKKRKVDKKEIERK-------VLEIAemLGIDHLLNR--KPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 592 LILDEPTSALDPITKNLVMDAI-RAHRKGKTTLV-ITHDMSQINN-DELVLVIDKGHLIQ 648
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELkKIRKEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQ 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1099-1323 |
1.21e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.43 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYpdseRNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRktyPSE-DIYIDGYPLTNidtnwLL 1173
Cdd:COG1121 7 IELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKailgLLP---PTSgTVRLFGKPPRR-----AR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1174 KKVAIVDQKPHLLGS---TILESLLYG-------------VDRDInsVMDALDKTYMTEV----IQNLpngldtpllefs 1233
Cdd:COG1121 75 RRIGYVPQRAEVDWDfpiTVRDVVLMGrygrrglfrrpsrADREA--VDEALERVGLEDLadrpIGEL------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1234 knfSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPS-LMKLADRIIVMDSGIV 1309
Cdd:COG1121 141 ---SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRregKTILVVTHDLGaVREYFDRVLLLNRGLV 217
|
250
....*....|....
gi 162312251 1310 KeSGSFDELMNRHT 1323
Cdd:COG1121 218 A-HGPPEEVLTPEN 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1099-1318 |
1.32e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 127.12 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELL----RktyPSE-DIYIDGYPLTNIDTNWLL 1173
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInlleR---PTSgSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1174 ---KKVAIVDQKPHLLGS-TILESLLY-----GVDR-DINS-VMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQ 1242
Cdd:COG1135 79 aarRKIGMIFQHFNLLSSrTVAENVALpleiaGVPKaEIRKrVAELLELVGLSDKADAYPSQL-----------SGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1243 RLAFARALLRNPRLLILDECTSALDSKS-----SLLleKTI-QNLSCTVLIITHQpslM----KLADRIIVMDSGIVKES 1312
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETtrsilDLL--KDInRELGLTIVLITHE---MdvvrRICDRVAVLENGRIVEQ 222
|
....*.
gi 162312251 1313 GSFDEL 1318
Cdd:COG1135 223 GPVLDV 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1099-1320 |
1.56e-31 |
|
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: 123.94 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKSTL----VELLRktyPSE-DIYIDGYPLTNIDT---N 1170
Cdd:COG1127 6 IEVRNLTKSFGD----RVVLDGVSLDVPRGEILAIIGGSGSGKSVLlkliIGLLR---PDSgEILVDGQDITGLSEkelY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1171 WLLKKVAIVDQKPHLLGS-TILESLLYGVD----------RDInsVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGG 1239
Cdd:COG1127 79 ELRRRIGMLFQGGALFDSlTVFENVAFPLRehtdlseaeiREL--VLEKLELVGLPGAADKMPSEL-----------SGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1240 QIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS----CTVLIITHQ-PSLMKLADRIIVMDSGIVKESGS 1314
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRdelgLTSVVVTHDlDSAFAIADRVAVLADGKIIAEGT 225
|
....*.
gi 162312251 1315 FDELMN 1320
Cdd:COG1127 226 PEELLA 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
433-693 |
1.67e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 125.10 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRDENLfsLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPL--EEIDEhvLGS 510
Cdd:PRK13632 8 IKVENVSFSYPNSENNA--LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIskENLKE--IRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 511 TITLVCQQPvifD-----MTIRENIIMRNENASEsDFEEVcrLALVDEFALTFDQSYDTPCKEASLSGGQQQRIALARAL 585
Cdd:PRK13632 84 KIGIIFQNP---DnqfigATVEDDIAFGLENKKV-PPKKM--KDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 586 LRDTEILILDEPTSALDPITKNLV---MDAIRAHRKgKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELVlfedfe 662
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIkkiMVDLRKTRK-KTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL------ 230
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 162312251 663 NNvsiDEKVLKEEADNPFILP------------NEESLLEKYW 693
Cdd:PRK13632 231 NN---KEILEKAKIDSPFIYKlskklkgidptyNEEELIEQIC 270
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
454-647 |
1.76e-31 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 123.95 E-value: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHV--LGSTITLVCQQPVIF-DMTIRENI 530
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInkLRRKVGMVFQQFNLFpHLTVLENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 531 I---MRNENASESDFEEVCR--LALV--DEFAltfdQSYdtPckeASLSGGQQQRIALARALLRDTEILILDEPTSALDP 603
Cdd:COG1126 99 TlapIKVKKMSKAEAEERAMelLERVglADKA----DAY--P---AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 162312251 604 ITKNLVMDAIR--AHRkGKTTLVITHDMSQINN--DElVLVIDKGHLI 647
Cdd:COG1126 170 ELVGEVLDVMRdlAKE-GMTMVVVTHEMGFAREvaDR-VVFMDGGRIV 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1099-1307 |
2.56e-31 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 122.19 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSE-RNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE-LLRKTYPSEDIYidgypltnidtnWLLKKV 1176
Cdd:cd03250 1 ISVEDASFTWDSGEqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKLSGSV------------SVPGSI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHLLGSTILESLLYGVDRDI---NSVMDA--LDKTymtevIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALL 1251
Cdd:cd03250 69 AYVSQEPWIQNGTIRENILFGKPFDEeryEKVIKAcaLEPD-----LEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1252 RNPRLLILDECTSALDSK-SSLLLEKTIQNL---SCTVLIITHQPSLMKLADRIIVMDSG 1307
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHvGRHIFENCILGLllnNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1100-1313 |
3.03e-31 |
|
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: 121.39 E-value: 3.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1100 EFDGVSFAYPdserNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTNIDTNWLLKKVA 1177
Cdd:cd03214 1 EVENLSVGYG----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSsgEILLDGKDLASLSPKELARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1178 IVDQKPHLLGstiLESLLygvDRDINSVmdaldktymteviqnlpngldtpllefsknfSGGQIQRLAFARALLRNPRLL 1257
Cdd:cd03214 77 YVPQALELLG---LAHLA---DRPFNEL-------------------------------SGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 1258 ILDECTSALDSKSSLLLEKTIQNLS----CTVLIITHQPSL-MKLADRIIVMDSGIVKESG 1313
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLArergKTVVMVLHDLNLaARYADRVILLKDGRIVAQG 180
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
434-644 |
3.76e-31 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 121.97 E-value: 3.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSrdeNLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGS--- 510
Cdd:TIGR02673 3 EFHNVSKAYPG---GVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 511 TITLVCQQ-PVIFDMTIRENIIM------RNENASESDFEEVCRLALVDEFALTFDQSydtpckeasLSGGQQQRIALAR 583
Cdd:TIGR02673 80 RIGVVFQDfRLLPDRTVYENVALplevrgKKEREIQRRVGAALRQVGLEHKADAFPEQ---------LSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 584 ALLRDTEILILDEPTSALDPITKNLVMDAI-RAHRKGKTTLVITHDMSQI-NNDELVLVIDKG 644
Cdd:TIGR02673 151 AIVNSPPLLLADEPTGNLDPDLSERILDLLkRLNKRGTTVIVATHDLSLVdRVAHRVIILDDG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
434-655 |
4.38e-31 |
|
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: 129.64 E-value: 4.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFSLI-NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHV---LG 509
Cdd:COG1123 262 EVRNLSKRYPVRGKGGVRAVdDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreLR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 510 STITLVCQQP-VIFD--MTIRENI---IMRNENASESDFEEVCRlALVDEFALTFDQSYDTPckeASLSGGQQQRIALAR 583
Cdd:COG1123 342 RRVQMVFQDPySSLNprMTVGDIIaepLRLHGLLSRAERRERVA-ELLERVGLPPDLADRYP---HELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 584 ALLRDTEILILDEPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDMSQINN--DElVLVIDKGHLIQRCARKEL 655
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiaDR-VAVMYDGRIVEDGPTEEV 492
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
454-599 |
6.77e-31 |
|
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: 119.29 E-value: 6.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIF-DMTIRENIIM 532
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENLRL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 533 RNENASESDFEEVCRLA-LVDEFALTFDqsYDTPCKE--ASLSGGQQQRIALARALLRDTEILILDEPTS 599
Cdd:pfam00005 83 GLLLKGLSKREKDARAEeALEKLGLGDL--ADRPVGErpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
452-648 |
2.53e-30 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 119.44 E-value: 2.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENII 531
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 532 MRNENASESDFEevcrlalvdefALTFDQSYDtpckeaSLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMD 611
Cdd:cd03369 104 PFDEYSDEEIYG-----------ALRVSEGGL------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 162312251 612 AIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQ 648
Cdd:cd03369 167 TIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1099-1324 |
3.54e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 120.10 E-value: 3.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKSTLvelLR-----KTYPSEDIYIDGYPLTNIDTNW-- 1171
Cdd:COG1126 2 IEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTL---LRcinllEEPDSGTITVDGEDLTDSKKDInk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1172 LLKKVAIVDQK----PHLlgsTILESLLY------GVDRD--INSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGG 1239
Cdd:COG1126 75 LRRKVGMVFQQfnlfPHL---TVLENVTLapikvkKMSKAeaEERAMELLERVGLADKADAYPAQL-----------SGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1240 QIQRLAFARALLRNPRLLILDECTSALDSksslllE------KTIQNLSC---TVLIITHQpslM----KLADRIIVMDS 1306
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDP------ElvgevlDVMRDLAKegmTMVVVTHE---MgfarEVADRVVFMDG 211
|
250
....*....|....*...
gi 162312251 1307 GIVKESGSFDELMNRHTH 1324
Cdd:COG1126 212 GRIVEEGPPEEFFENPQH 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1099-1309 |
3.62e-30 |
|
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: 117.88 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSErnhlALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRKTypSEDIYIDGYPLTNiDTNWLLK 1174
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKiilgLLKPD--SGEIKVLGKDIKK-EPEEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQKPHLLGstilesllygvdrdinsvmdaldktYMTeVIQNLpngldtpllefskNFSGGQIQRLAFARALLRNP 1254
Cdd:cd03230 74 RIGYLPEEPSLYE-------------------------NLT-VRENL-------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1255 RLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSLM-KLADRIIVMDSGIV 1309
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1100-1309 |
5.02e-30 |
|
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: 118.79 E-value: 5.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1100 EFDGVSFAYpdseRNHLALNNVSLSIEAREKVAIVGISGSGKSTLV----ELLRKTypSEDIYIDGYPLTNIDtnwllKK 1175
Cdd:cd03235 1 EVEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLkailGLLKPT--SGSIRVFGKPLEKER-----KR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1176 VAIVDQKPHLLGS---TILESLLYG-------------VDRDInsVMDALDKTYMTEV----IQNLpngldtpllefskn 1235
Cdd:cd03235 70 IGYVPQRRSIDRDfpiSVRDVVLMGlyghkglfrrlskADKAK--VDEALERVGLSELadrqIGEL-------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1236 fSGGQIQRLAFARALLRNPRLLILDECTSALDSKS-----SLLleKTIQNLSCTVLIITHQP-SLMKLADRIIVMDSGIV 1309
Cdd:cd03235 134 -SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTqediyELL--RELRREGMTILVVTHDLgLVLEYFDRVLLLNRTVV 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
435-646 |
6.71e-30 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 118.66 E-value: 6.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 435 FDNVSFAYPSrdeNLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEH---VLGST 511
Cdd:cd03292 3 FINVTKTYPN---GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 512 ITLVCQQ-PVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPckeASLSGGQQQRIALARALLRDTE 590
Cdd:cd03292 80 IGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALP---AELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 591 ILILDEPTSALDPITKNLVMDAIRA-HRKGKTTLVITHDMSQINN-DELVLVIDKGHL 646
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDTtRHRVIALERGKL 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1099-1320 |
8.61e-30 |
|
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: 118.76 E-value: 8.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYpdseRNHLALNNVSLSIEAREKVAIVGISGSGKSTL----VELLRKTypSEDIYIDG---YPLTNIDTNW 1171
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLlrliVGLLRPD--SGEVLIDGediSGLSEAELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1172 LLKKVAIVDQKPHLLGS-TILESLLYGV-------DRDINS-VMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQ 1242
Cdd:cd03261 75 LRRRMGMLFQSGALFDSlTVFENVAFPLrehtrlsEEEIREiVLEKLEAVGLRGAEDLYPAEL-----------SGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1243 RLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS----CTVLIITHQ-PSLMKLADRIIVMDSGIVKESGSFDE 1317
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKkelgLTSIMVTHDlDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
...
gi 162312251 1318 LMN 1320
Cdd:cd03261 224 LRA 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1099-1318 |
9.33e-30 |
|
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: 119.21 E-value: 9.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELL-RKTYPSE-DIYIDGYPLTNIDTNWLL--- 1173
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLnGLVEPTSgSVLIDGTDINKLKGKALRqlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1174 KKVAIVDQKPHLLG-STILESLLYGV---------------DRDINSVMDALDKTymteviqnlpnGLDTPLLEFSKNFS 1237
Cdd:cd03256 78 RQIGMIFQQFNLIErLSVLENVLSGRlgrrstwrslfglfpKEEKQRALAALERV-----------GLLDKAYQRADQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1238 GGQIQRLAFARALLRNPRLLILDECTSALDSKSSL----LLEKTIQNLSCTVLIITHQPSL-MKLADRIIVMDSGIVKES 1312
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRqvmdLLKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFD 226
|
....*.
gi 162312251 1313 GSFDEL 1318
Cdd:cd03256 227 GPPAEL 232
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
434-648 |
1.79e-29 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 120.20 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPsrdENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:COG1125 3 EFENVTKRYP---DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIF-DMTIRENIIM------RNENASESDFEEVcrLALV----DEFAltfdQSYdtPckeASLSGGQQQRIALA 582
Cdd:COG1125 80 YVIQQIGLFpHMTVAENIATvprllgWDKERIRARVDEL--LELVgldpEEYR----DRY--P---HELSGGQQQRVGVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 583 RALLRDTEILILDEPTSALDPITKNLVMDAIRA-HRK-GKTTLVITHDMsqinnDE---L---VLVIDKGHLIQ 648
Cdd:COG1125 149 RALAADPPILLMDEPFGALDPITREQLQDELLRlQRElGKTIVFVTHDI-----DEalkLgdrIAVMREGRIVQ 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
433-630 |
5.09e-29 |
|
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: 116.90 E-value: 5.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRDEnlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFP---LEEIDEHVLG 509
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 510 STITLVCQQPVIFD-MTIRENIIM-----RN------ENASESDFEEVcrLALVDEFALTfDQSYdTPCKEasLSGGQQQ 577
Cdd:cd03256 78 RQIGMIFQQFNLIErLSVLENVLSgrlgrRStwrslfGLFPKEEKQRA--LAALERVGLL-DKAY-QRADQ--LSGGQQQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 578 RIALARALLRDTEILILDEPTSALDPITKNLVMDAIR--AHRKGKTTLVITHDMS 630
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVD 206
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
434-630 |
5.19e-29 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 117.01 E-value: 5.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDEnlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGST-- 511
Cdd:TIGR02315 3 EVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 512 -ITLVCQQ-PVIFDMTIRENIIMRNENA-----------SESDFEEVcrLALVDEFALtfDQSYDTPCKEasLSGGQQQR 578
Cdd:TIGR02315 80 rIGMIFQHyNLIERLTVLENVLHGRLGYkptwrsllgrfSEEDKERA--LSALERVGL--ADKAYQRADQ--LSGGQQQR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 162312251 579 IALARALLRDTEILILDEPTSALDPITKNLVMDAIR--AHRKGKTTLVITHDMS 630
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKriNKEDGITVIINLHQVD 207
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
434-647 |
5.22e-29 |
|
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: 116.53 E-value: 5.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVL---GS 510
Cdd:cd03258 3 ELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 511 TITLVCQQPVIFD-MTIRENIIMRNENASESDFEEVCR----LALVDefaLTfDQSYDTPckeASLSGGQQQRIALARAL 585
Cdd:cd03258 83 RIGMIFQHFNLLSsRTVFENVALPLEIAGVPKAEIEERvlelLELVG---LE-DKADAYP---AQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 586 LRDTEILILDEPTSALDPITKNLVMDAIRA-HRK-GKTTLVITHDMS---QINNDelVLVIDKGHLI 647
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDiNRElGLTIVLITHEMEvvkRICDR--VAVMEKGEVV 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1118-1307 |
7.70e-29 |
|
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: 114.96 E-value: 7.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELL--RKTYP--SEDIYIDGYPLtniDTNWLLKKVAIVDQKPHLLGS-TILE 1192
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLgvSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTlTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1193 SLLYGVdrdinsvmdaldktymteviqNLpngldtpllefsKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSL 1272
Cdd:cd03213 102 TLMFAA---------------------KL------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 162312251 1273 LLEKTIQNLS---CTVLIITHQPS--LMKLADRIIVMDSG 1307
Cdd:cd03213 149 QVMSLLRRLAdtgRTIICSIHQPSseIFELFDKLLLLSQG 188
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1099-1321 |
9.77e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 117.14 E-value: 9.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYpDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTnIDTNWLLK-K 1175
Cdd:PRK13650 5 IEVKNLTFKY-KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsgQIIIDGDLLT-EENVWDIRhK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1176 VAIVDQKP--HLLGSTILESLLYGVDRD-------INSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLAF 1246
Cdd:PRK13650 83 IGMVFQNPdnQFVGATVEDDVAFGLENKgipheemKERVNEALELVGMQDFKEREPARL-----------SGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1247 ARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL----SCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNR 1321
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIrddyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1099-1321 |
1.39e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.82 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNhlALNNVSLSIEAREKVAIVGISGSGKSTLVEL-----LRKTYPSEDIYIDGYPLTNiDTNWLL 1173
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTISKLingllLPDDNPNSKITVDGITLTA-KTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1174 K-KVAIVDQKP--HLLGSTILESLLYG-----VDRD--INSVMDALDKTYMTEVIQNLPngldtpllefsKNFSGGQIQR 1243
Cdd:PRK13640 83 ReKVGIVFQNPdnQFVGATVGDDVAFGlenraVPRPemIKIVRDVLADVGMLDYIDSEP-----------ANLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1244 LAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL----SCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELM 1319
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF 231
|
..
gi 162312251 1320 NR 1321
Cdd:PRK13640 232 SK 233
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
104-372 |
1.53e-28 |
|
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: 116.59 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 104 IFGTLIFTCLSAALEPLMTWTTGKVFDALSQYATSQItlgkmiSLINFNSLLITIFGLASCVFSFGVRFLWQYLSAIAGK 183
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPET------QALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 184 RARSLCFHVLSSKSSTFYSLTeSKSGLVNSVDRCIQFYEKSISLPMFHIAENLAISLSCLIISFRYSWSLTLVVLASYPI 263
Cdd:pfam00664 75 RLRRKLFKKILRQPMSFFDTN-SVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 264 IILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSFLDAFQGGVSQF 343
Cdd:pfam00664 154 YILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQF 233
|
250 260
....*....|....*....|....*....
gi 162312251 344 FLYSVFFQGLWFGNHLATTKRVNVGQVVT 372
Cdd:pfam00664 234 IGYLSYALALWFGAYLVISGELSVGDLVA 262
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
434-648 |
3.26e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.08 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPsrDENL-FSLInvsvfIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLeeidehvlgsTI 512
Cdd:COG3840 3 RLDDLTYRYG--DFPLrFDLT-----IAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL----------TA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 513 TLVCQQPV--IFD-------MTIRENI---IMRNENASESDFEEVCRLAlvDEFALT-FDQsydtpCKEASLSGGQQQRI 579
Cdd:COG3840 66 LPPAERPVsmLFQennlfphLTVAQNIglgLRPGLKLTAEQRAQVEQAL--ERVGLAgLLD-----RLPGQLSGGQRQRV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 580 ALARALLRDTEILILDEPTSALDPITKNLVMDAIR--AHRKGKTTLVITH---DMSQINNDelVLVIDKGHLIQ 648
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDelCRERGLTVLMVTHdpeDAARIADR--VLLVADGRIAA 210
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
433-629 |
4.42e-28 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 114.38 E-value: 4.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRDEnlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEI---DEHVLG 509
Cdd:COG3638 3 LELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgrALRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 510 STITLVCQQPVIFD-MTIRENII------------MRNeNASESDFEEVcrLALVDEFALTfDQSYDtPCKEasLSGGQQ 576
Cdd:COG3638 80 RRIGMIFQQFNLVPrLSVLTNVLagrlgrtstwrsLLG-LFPPEDRERA--LEALERVGLA-DKAYQ-RADQ--LSGGQQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 577 QRIALARALLRDTEILILDEPTSALDPITKNLVMDAIR--AHRKGKTTLVITHDM 629
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRriAREDGITVVVNLHQV 207
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
433-631 |
5.02e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 114.36 E-value: 5.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRDenlfSLINVSVFIPFGELVHIIGPSGSGKSTFI-SL-----LLRYFSPTyGNIYLDDFPL--EEID 504
Cdd:COG1117 12 IEVRNLNVYYGDKQ----ALKDINLDIPENKVTALIGPSGCGKSTLLrCLnrmndLIPGARVE-GEILLDGEDIydPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 505 EHVLGSTITLVCQQPVIFDMTIRENIIM---RNENASESDFEEVC-----RLALVDEFALTFDQSydtpckeA-SLSGGQ 575
Cdd:COG1117 87 VVELRRRVGMVFQKPNPFPKSIYDNVAYglrLHGIKSKSELDEIVeeslrKAALWDEVKDRLKKS-------AlGLSGGQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 576 QQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKgKTTLVI-THDMSQ 631
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvTHNMQQ 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1099-1321 |
5.99e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 116.74 E-value: 5.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKSTLvelLRK----TYPSE-DIYIDGYPLTNIDTNwll 1173
Cdd:COG3842 6 LELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTL---LRMiagfETPDSgRILLDGRDVTGLPPE--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1174 kK--VAIVDQK----PHLlgsTILESLLYG-----VDR-DINS-VMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQ 1240
Cdd:COG3842 76 -KrnVGMVFQDyalfPHL---TVAENVAFGlrmrgVPKaEIRArVAELLELVGLEGLADRYPHQL-----------SGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1241 IQRLAFARALLRNPRLLILDECTSALDSK--SSLLLE-KTIQ-NLSCTVLIITHQPS-LMKLADRIIVMDSGIVKESGSF 1315
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKlrEEMREElRRLQrELGITFIYVTHDQEeALALADRIAVMNDGRIEQVGTP 220
|
....*.
gi 162312251 1316 DELMNR 1321
Cdd:COG3842 221 EEIYER 226
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
781-1069 |
9.46e-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: 114.88 E-value: 9.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 781 FLLGLLTSLIQGASVPIFAYVISKCLNLFMQIDPSI--------GVAFWSSMVLVVAAGSGASYFFSHYIFSISAKIWCD 852
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGEsspdefldDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 853 HYRLLAVKVLFTQDQAWFDQIEnyPLVLSKILVNNISDMRNMISSLIEEVFIAFTMAIIGIAWSFATGWRLAAVLVAVSP 932
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNG--AGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 933 ILCLTSRMFSYIYVSTERMCQDVVISTTSILHKTIVNLDTIKGYSVLSFFRENHKNSLRKSWEAFKRRAFWTSLGFAINN 1012
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 1013 SLLYFVRALLFYCSSIFISKEFYTVEQMVQVLS---LATFTLLMASTCIMSLPN--VSASRI 1069
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFavlIGAFSLGQIAPNLQAFAKarAAAAKI 300
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1099-1314 |
1.11e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 116.05 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELL-RKTYPSE-DIYIDGYPLTNIDTNWLLK-- 1174
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCInLLERPTSgRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 -KVAIVDQKPHLLGS-TI-------LEslLYGVDR-DINS-VmdaldktymteviqnlpngldTPLLE----------FS 1233
Cdd:PRK11153 82 rQIGMIFQHFNLLSSrTVfdnvalpLE--LAGTPKaEIKArV---------------------TELLElvglsdkadrYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1234 KNFSGGQIQRLAFARALLRNPRLLILDECTSALD---SKSSLLLEKTIQ-NLSCTVLIITHQPSLMK-LADRIIVMDSGI 1308
Cdd:PRK11153 139 AQLSGGQKQRVAIARALASNPKVLLCDEATSALDpatTRSILELLKDINrELGLTIVLITHEMDVVKrICDRVAVIDAGR 218
|
....*.
gi 162312251 1309 VKESGS 1314
Cdd:PRK11153 219 LVEQGT 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1120-1313 |
1.14e-27 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 112.00 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1120 NVSLSIEArEKVAIVGISGSGKSTLVELLR--KTYPSEDIYIDGYPL----TNIDTNWLLKKVAIVDQK----PHLlgsT 1189
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAglEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQyalfPHL---N 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1190 ILESLLYGVDRDINSVmdalDKTYMTEVIQNLpnGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALD-- 1267
Cdd:cd03297 92 VRENLAFGLKRKRNRE----DRISVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDra 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 162312251 1268 SKSSLL--LEKTIQNLSCTVLIITHQPS-LMKLADRIIVMDSGIVKESG 1313
Cdd:cd03297 166 LRLQLLpeLKQIKKNLNIPVIFVTHDLSeAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
434-628 |
1.37e-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: 111.58 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPsrdENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDfplEEIDEHVLGSTIT 513
Cdd:cd03226 1 RIENISFSYK---KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQP--VIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALtfdqsydtpcKEA---SLSGGQQQRIALARALLRD 588
Cdd:cd03226 75 YVMQDVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYAL----------KERhplSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 162312251 589 TEILILDEPTSALDPITKNLVMDAIR-AHRKGKTTLVITHD 628
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIReLAAQGKAVIVITHD 185
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
434-648 |
1.43e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 115.58 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRdenlFSLINVSVFIPFGELVHIIGPSGSGKSTfislLLR----YFSPTYGNIYLDdfpleeidehvlG 509
Cdd:COG3842 7 ELENVSKRYGDV----TALDDVSLSIEPGEFVALLGPSGCGKTT----LLRmiagFETPDSGRILLD------------G 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 510 STIT----------LVCQQPVIF-DMTIRENII----MRNENASESDF--EEVcrLALV--DEFALTFdqsydtPckeAS 570
Cdd:COG3842 67 RDVTglppekrnvgMVFQDYALFpHLTVAENVAfglrMRGVPKAEIRArvAEL--LELVglEGLADRY------P---HQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 571 LSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRA-HRK-GKTTLVITHD------MSqinnDELVlVID 642
Cdd:COG3842 136 LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlQRElGITFIYVTHDqeealaLA----DRIA-VMN 210
|
....*.
gi 162312251 643 KGHLIQ 648
Cdd:COG3842 211 DGRIEQ 216
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
454-648 |
2.58e-27 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 115.33 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGST----ITLVCQQPVIF-DMTIRE 528
Cdd:TIGR01186 11 DADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVrrkkIGMVFQQFALFpHMTILQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 529 NIIM-----------RNENASESdfeevcrLALVD--EFAltfDQSYDtpckeaSLSGGQQQRIALARALLRDTEILILD 595
Cdd:TIGR01186 91 NTSLgpellgwpeqeRKEKALEL-------LKLVGleEYE---HRYPD------ELSGGMQQRVGLARALAAEPDILLMD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 596 EPTSALDPITKNLVMDAI-RAHRK-GKTTLVITHDMSQ-INNDELVLVIDKGHLIQ 648
Cdd:TIGR01186 155 EAFSALDPLIRDSMQDELkKLQATlQKTIVFITHDLDEaIRIGDRIVIMKAGEIVQ 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1099-1324 |
2.70e-27 |
|
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: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRKTYPSE-DIYIDGYPLTNIDTNWL- 1172
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARailgLLPPPGITSgEILFDGEDLLKLSEKELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1173 ---LKKVAIVDQKP-------HLLGSTILESLLY--GVDRDinsvmDALDKTY--MTEViqnlpnGLDTP---LLEFSKN 1235
Cdd:COG0444 82 kirGREIQMIFQDPmtslnpvMTVGDQIAEPLRIhgGLSKA-----EARERAIelLERV------GLPDPerrLDRYPHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1236 FSGGQIQRLAFARALLRNPRLLILDECTSALDSksslllekTIQ----NL--------SCTVLIITHQPSLMK-LADRII 1302
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDV--------TIQaqilNLlkdlqrelGLAILFITHDLGVVAeIADRVA 222
|
250 260
....*....|....*....|...
gi 162312251 1303 VMDSG-IVkESGSFDELMNRHTH 1324
Cdd:COG0444 223 VMYAGrIV-EEGPVEELFENPRH 244
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1099-1313 |
3.10e-27 |
|
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: 110.81 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPdserNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDGYPLTNIDTNwlLKKV 1176
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEptSGRIYIGGRDVTDLPPK--DRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQK----PHLlgsTILESLLYG----------VDRDINSVMDALDktyMTEVIQNLPngldtpllefsKNFSGGQIQ 1242
Cdd:cd03301 75 AMVFQNyalyPHM---TVYDNIAFGlklrkvpkdeIDERVREVAELLQ---IEHLLDRKP-----------KQLSGGQRQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 1243 RLAFARALLRNPRLLILDECTSALDSK----SSLLLEKTIQNLSCTVLIITH-QPSLMKLADRIIVMDSGIVKESG 1313
Cdd:cd03301 138 RVALGRAIVREPKVFLMDEPLSNLDAKlrvqMRAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1117-1324 |
3.16e-27 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 117.86 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVE-LLRKTyPSE-DIYIDGYPLTNIDTNWLL---KKVAIVDQKP-------H 1184
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLaLLRLI-PSEgEIRFDGQDLDGLSRRALRplrRRMQVVFQDPfgslsprM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1185 LLGSTILESL------LYGVDRDiNSVMDALDktymtEViqnlpnGLDTPLLE-FSKNFSGGQIQRLAFARALLRNPRLL 1257
Cdd:COG4172 380 TVGQIIAEGLrvhgpgLSAAERR-ARVAEALE-----EV------GLDPAARHrYPHEFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1258 ILDECTSALD---SKSSLLLEKTIQ---NLSCtvLIITHQPSLMK-LADRIIVMDSGIVKESGSFDELMNRHTH 1324
Cdd:COG4172 448 VLDEPTSALDvsvQAQILDLLRDLQrehGLAY--LFISHDLAVVRaLAHRVMVMKDGKVVEQGPTEQVFDAPQH 519
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
108-397 |
4.42e-27 |
|
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: 112.65 E-value: 4.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 108 LIFTCLSAALEPLMTWTTGKVFDalsqyatsQITLGKMISLINFNSLLITIFGLASCVFSFgVRFlwqYLSAIAGKRA-- 185
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLID--------TIIKGGDLDVLNELALILLAIYLLQSVFTF-VRY---YLFNIAGERIva 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 186 --RSLCFHVLSSKSSTFYSltESKSG-LVNSVDRCIQFYEKSISLPMFHIAENLAISLSCLIISFRYSWSLTLVVLASYP 262
Cdd:cd18557 70 rlRRDLFSSLLRQEIAFFD--KHKTGeLTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 263 IIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSFLDAFQGGVSQ 342
Cdd:cd18557 148 LLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITS 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 343 FFLYSVFFQGLWFGNHLATTKRVNVGQVVTVFGSCLSVASSLQQILPAIPDLIKG 397
Cdd:cd18557 228 LLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKA 282
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1099-1307 |
5.55e-27 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 110.60 E-value: 5.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELL----RktyPSE-DIYIDGYPLTNIDTNWLL 1173
Cdd:COG4181 9 IELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLagldR---PTSgTVRLAGQDLFALDEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1174 K----KVAIVDQKPHLLGS-TILES-----LLYGVDRDINSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQR 1243
Cdd:COG4181 86 RlrarHVGFVFQSFQLLPTlTALENvmlplELAGRRDARARARALLERVGLGHRLDHYPAQL-----------SGGEQQR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1244 LAFARALLRNPRLLILDECTSALDSKSS-----LLLEKTiQNLSCTVLIITHQPSLMKLADRIIVMDSG 1307
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGeqiidLLFELN-RERGTTLVLVTHDPALAARCDRVLRLRAG 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
454-628 |
7.02e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.02 E-value: 7.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVI-FDMTIRENIIM 532
Cdd:PRK13548 20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEVVAM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 533 ------RNENASESDFEEVCRLALVDEFAltfDQSYdtpckeASLSGGQQQRIALARALLRDTE------ILILDEPTSA 600
Cdd:PRK13548 100 graphgLSRAEDDALVAAALAQVDLAHLA---GRDY------PQLSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPTSA 170
|
170 180 190
....*....|....*....|....*....|
gi 162312251 601 LDPITKNLVMDAIR--AHRKGKTTLVITHD 628
Cdd:PRK13548 171 LDLAHQHHVLRLARqlAHERGLAVIVVLHD 200
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
436-652 |
9.05e-27 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 110.22 E-value: 9.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDE----HVLGST 511
Cdd:COG4181 12 RGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdaraRLRARH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 512 ITLVCQQ-PVIFDMTIRENIIMRNENASESDFEEVCRlALVDEFALTfDQSYDTPckeASLSGGQQQRIALARALLRDTE 590
Cdd:COG4181 92 VGFVFQSfQLLPTLTALENVMLPLELAGRRDARARAR-ALLERVGLG-HRLDHYP---AQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 591 ILILDEPTSALDPITKNLVMDAIRA-HRKGKTTLVI-THDMsqinndelvlvidkgHLIQRCAR 652
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFElNRERGTTLVLvTHDP---------------ALAARCDR 215
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
435-656 |
1.30e-26 |
|
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: 118.89 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 435 FDNVSFAYpsRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITL 514
Cdd:TIGR00957 1287 FRNYCLRY--REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 515 VCQQPVIFDMTIRENIimrNENASESDfEEV---CRLALVDEFALTFDQSYDTPCKEA--SLSGGQQQRIALARALLRDT 589
Cdd:TIGR00957 1365 IPQDPVLFSGSLRMNL---DPFSQYSD-EEVwwaLELAHLKTFVSALPDKLDHECAEGgeNLSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 590 EILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELV 656
Cdd:TIGR00957 1441 KILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
454-634 |
1.58e-26 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 109.13 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGStITlVCQQP-VIFD-MTIRENI- 530
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQS-LG-YCPQFdALFDeLTVREHLr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 531 ---IMRNENASESDFEevcRLALVDEFALTfdQSYDTPCKEasLSGGQQQRIALARALLRDTEILILDEPTSALDPITKN 607
Cdd:cd03263 98 fyaRLKGLPKSEIKEE---VELLLRVLGLT--DKANKRART--LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRR 170
|
170 180
....*....|....*....|....*..
gi 162312251 608 LVMDAIRAHRKGKTTLVITHDMSQINN 634
Cdd:cd03263 171 AIWDLILEVRKGRSIILTTHSMDEAEA 197
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1113-1321 |
1.87e-26 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 112.50 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1113 RNHLALNnVSLSIEAREKVAIVGISGSGKSTLVE----LLRktyPSE-DIYIDGYPLTNIDTNWLLK----KVAIVDQK- 1182
Cdd:COG4148 11 RGGFTLD-VDFTLPGRGVTALFGPSGSGKTTLLRaiagLER---PDSgRIRLGGEVLQDSARGIFLPphrrRIGYVFQEa 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1183 ---PHLlgsTILESLLYGVDRdinsVMDALDKTYMTEVIQNLpnGLdTPLLE-FSKNFSGGQIQRLAFARALLRNPRLLI 1258
Cdd:COG4148 87 rlfPHL---SVRGNLLYGRKR----APRAERRISFDEVVELL--GI-GHLLDrRPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1259 LDECTSALD--SKSSLL--LEKTIQNLSCTVLIITHQPS-LMKLADRIIVMDSGIVKESGSFDELMNR 1321
Cdd:COG4148 157 MDEPLAALDlaRKAEILpyLERLRDELDIPILYVSHSLDeVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
434-647 |
2.05e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 112.09 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTF---ISLLLRyfsPTYGNIYLDDFPLEEIDEHVLGS 510
Cdd:COG1135 3 ELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLircINLLER---PTSGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 511 T---ITLVCQQpviFDM----TIRENII--MRNENASESDFEEvcR----LALVDefaLTfDQSYDTPckeASLSGGQQQ 577
Cdd:COG1135 80 ArrkIGMIFQH---FNLlssrTVAENVAlpLEIAGVPKAEIRK--RvaelLELVG---LS-DKADAYP---SQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 578 RIALARALLRDTEILILDEPTSALDPITKNLVMDAI-RAHRK-GKTTLVITHDMS---QINNDelVLVIDKGHLI 647
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLkDINRElGLTIVLITHEMDvvrRICDR--VAVLENGRIV 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1121-1321 |
2.70e-26 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 112.13 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1121 VSLSIEAREKVAIVGISGSGKSTLVEL---LRKTYPSEdIYIDGYPLTN----IDTNWLLKKVAIVDQK----PHLlgsT 1189
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLiagLTRPDEGE-IVLNGRTLFDsrkgIFLPPEKRRIGYVFQEarlfPHL---S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1190 ILESLLYGVDRdinsVMDALDKTYMTEVIQNLpnGLDtPLLE-FSKNFSGGQIQRLAFARALLRNPRLLILDECTSALD- 1267
Cdd:TIGR02142 92 VRGNLRYGMKR----ARPSERRISFERVIELL--GIG-HLLGrLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDd 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1268 -SKSSLL--LEKTIQNLSCTVLIITHQPSLM-KLADRIIVMDSGIVKESGSFDELMNR 1321
Cdd:TIGR02142 165 pRKYEILpyLERLHAEFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
454-647 |
2.71e-26 |
|
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: 108.68 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHV---LGstITLVCQQPVIF-DMTIREN 529
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEiarLG--IGRTFQIPRLFpELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 530 IIMRNENASESDF--------EEVCR---LALVDEFALtfDQSYDTPCkeASLSGGQQQRIALARALLRDTEILILDEPT 598
Cdd:cd03219 96 VMVAAQARTGSGLllararreEREAReraEELLERVGL--ADLADRPA--GELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 162312251 599 SALDPITKNLVMDAIRA-HRKGKTTLVITHDMSQINN--DElVLVIDKGHLI 647
Cdd:cd03219 172 AGLNPEETEELAELIRElRERGITVLLVEHDMDVVMSlaDR-VTVLDQGRVI 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1097-1321 |
2.85e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.09 E-value: 2.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1097 GKIEFDGVSFAYPDSErnhlALNNVSLSIEAREKVAIVGISGSGKSTLvelLR------KtyPSE-DIYIDGYPLTNIDT 1169
Cdd:COG3839 2 ASLELENVSKSYGGVE----ALKDIDLDIEDGEFLVLLGPSGCGKSTL---LRmiagleD--PTSgEILIGGRDVTDLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1170 nwllKK--VAIVDQK----PHLlgsTILESLLYG-----VDRD-INS-VMDALDKTYMTEVIQNLPNGLdtpllefsknf 1236
Cdd:COG3839 73 ----KDrnIAMVFQSyalyPHM---TVYENIAFPlklrkVPKAeIDRrVREAAELLGLEDLLDRKPKQL----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1237 SGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTI----QNLSCTVLIITH-QPSLMKLADRIIVMDSGIVKE 1311
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIkrlhRRLGTTTIYVTHdQVEAMTLADRIAVMNDGRIQQ 214
|
250
....*....|
gi 162312251 1312 SGSFDELMNR 1321
Cdd:COG3839 215 VGTPEELYDR 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1102-1310 |
2.91e-26 |
|
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: 107.73 E-value: 2.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1102 DGVSFAYpdsERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSED--IYIDGYPLTNIDtnwLLKKVAIV 1179
Cdd:cd03226 3 ENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSgsILLNGKPIKAKE---RRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1180 DQKP--HLLGSTILESLLYGVDR------DINSVMDALDKTYMTEViqnLPNGLdtpllefsknfSGGQIQRLAFARALL 1251
Cdd:cd03226 77 MQDVdyQLFTDSVREELLLGLKEldagneQAETVLKDLDLYALKER---HPLSL-----------SGGQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 1252 RNPRLLILDECTSALDSKSSLLLEKTIQNLSC---TVLIITHQPS-LMKLADRIIVMDSGIVK 1310
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEfLAKVCDRVLLLANGAIV 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1099-1324 |
3.19e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 108.69 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYpdserNHLALNnVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTniDTNWLLKKV 1176
Cdd:COG3840 2 LRLDDLTYRY-----GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDsgRILWNGQDLT--ALPPAERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQK----PHLlgsTILESLLYGVD-------RDINSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLA 1245
Cdd:COG3840 74 SMLFQEnnlfPHL---TVAQNIGLGLRpglkltaEQRAQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1246 FARALLRNPRLLILDECTSALDS--KSSL--LLEKTIQNLSCTVLIITHQPS-LMKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPalRQEMldLVDELCRERGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLD 219
|
....
gi 162312251 1321 RHTH 1324
Cdd:COG3840 220 GEPP 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
434-647 |
3.57e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 109.72 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDEnlFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEidEHV--LGST 511
Cdd:PRK13635 7 RVEHISFRYPDAAT--YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE--ETVwdVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 512 ITLVCQQPvifD-----MTIRENIIMRNENASESDFEEVCR----LALV--DEFALtfdqsyDTPckeASLSGGQQQRIA 580
Cdd:PRK13635 83 VGMVFQNP---DnqfvgATVQDDVAFGLENIGVPREEMVERvdqaLRQVgmEDFLN------REP---HRLSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 581 LARALLRDTEILILDEPTSALDPITKNLVMDAIRAHR--KGKTTLVITHDMSQINNDELVLVIDKGHLI 647
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQADRVIVMNKGEIL 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
436-648 |
4.58e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.39 E-value: 4.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYPSRDenlfSLINVSVFIPFGELVHIIGPSGSGKSTfislLLRYF----SPTYGNIYLDDfpleeideHVLGST 511
Cdd:COG1118 6 RNISKRFGSFT----LLDDVSLEIASGELVALLGPSGSGKTT----LLRIIagleTPDSGRIVLNG--------RDLFTN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 512 IT-------LVCQQPVIF-DMTIRENII--MRNENASESDFEEVCR--LALV--DEFAltfdQSYdtPckeASLSGGQQQ 577
Cdd:COG1118 70 LPprerrvgFVFQHYALFpHMTVAENIAfgLRVRPPSKAEIRARVEelLELVqlEGLA----DRY--P---SQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 578 RIALARALLRDTEILILDEPTSALDpiTKnlVMDAIRA-----HRK-GKTTLVITHDMsqinnDEL------VLVIDKGH 645
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALD--AK--VRKELRRwlrrlHDElGGTTVFVTHDQ-----EEAleladrVVVMNQGR 211
|
...
gi 162312251 646 LIQ 648
Cdd:COG1118 212 IEQ 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
450-649 |
7.03e-26 |
|
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: 107.00 E-value: 7.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 450 FSLiNVSVFIPfGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGST----ITLVCQQPVIF-DM 524
Cdd:cd03297 13 FTL-KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPqqrkIGLVFQQYALFpHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 525 TIRENI---IMRNENASESDFEEvcrlALVDEFALT-FDQSYdtpckEASLSGGQQQRIALARALLRDTEILILDEPTSA 600
Cdd:cd03297 91 NVRENLafgLKRKRNREDRISVD----ELLDLLGLDhLLNRY-----PAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 162312251 601 LDPITKNLVMDAIRAHRK--GKTTLVITHDMSQINN-DELVLVIDKGHLIQR 649
Cdd:cd03297 162 LDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYI 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1098-1318 |
7.32e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.20 E-value: 7.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1098 KIEFDGVSFAYpdseRNHLALNNVSLSIEAREKVAIVGISGSGKSTLvelLR------KTYP----SEDIYIDGyplTNI 1167
Cdd:COG1117 11 KIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTL---LRclnrmnDLIPgarvEGEILLDG---EDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1168 -----DTNWLLKKVAIVDQKPHLLGSTILESLLYGVdRdINSVmdaLDKTYMTEVIQ------NLPN----GLDTPLLEF 1232
Cdd:COG1117 81 ydpdvDVVELRRRVGMVFQKPNPFPKSIYDNVAYGL-R-LHGI---KSKSELDEIVEeslrkaALWDevkdRLKKSALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1233 SknfsGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS--CTVLIITH---QPSlmKLADRIIVMDSG 1307
Cdd:COG1117 156 S----GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKkdYTIVIVTHnmqQAA--RVSDYTAFFYLG 229
|
250
....*....|.
gi 162312251 1308 IVKESGSFDEL 1318
Cdd:COG1117 230 ELVEFGPTEQI 240
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1116-1320 |
8.34e-26 |
|
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: 108.50 E-value: 8.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1116 LALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYIDGYPLTNIDTNWLL----KKVAIVDQK----PHL 1185
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIePTSgKVLIDGQDIAAMSRKELRelrrKKISMVFQSfallPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1186 lgsTILESLLY-----GVDRDIN--SVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLAFARALLRNPRLLI 1258
Cdd:cd03294 118 ---TVLENVAFglevqGVPRAEReeRAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 1259 LDECTSALDSksslLLEKTIQN--------LSCTVLIITHQPS-LMKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:cd03294 184 MDEAFSALDP----LIRREMQDellrlqaeLQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1099-1320 |
9.67e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 108.30 E-value: 9.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERnhLALNNVSLSIEAREKVAIVGISGSGKSTLVELLR--KTYPSEDIYIDGYPLTNIDTNWLLKKV 1176
Cdd:PRK13648 8 IVFKNVSFQYQSDAS--FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIgiEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKP--HLLGSTI-------LESLLYGVDRDINSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLAFA 1247
Cdd:PRK13648 86 GIVFQNPdnQFVGSIVkydvafgLENHAVPYDEMHRRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 1248 RALLRNPRLLILDECTSALD--SKSSL--LLEKTIQNLSCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDpdARQNLldLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
432-648 |
1.00e-25 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 107.43 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 432 GFRFDNVSFAYPsrdeNLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDfpLEEIDEHVLGST 511
Cdd:cd03296 2 SIEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG--EDATDVPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 512 ITLVCQQPVIF-DMTIRENIIM------RNENASESDF----EEVCRLALVDEFAltfdQSYdtpckEASLSGGQQQRIA 580
Cdd:cd03296 76 VGFVFQHYALFrHMTVFDNVAFglrvkpRSERPPEAEIrakvHELLKLVQLDWLA----DRY-----PAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 581 LARALLRDTEILILDEPTSALDP-ITKNLVMDAIRAH-RKGKTTLVITHDMSQ-INNDELVLVIDKGHLIQ 648
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAkVRKELRRWLRRLHdELHVTTVFVTHDQEEaLEVADRVVVMNKGRIEQ 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
434-648 |
1.88e-25 |
|
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: 106.17 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYpsrdENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGstIT 513
Cdd:cd03300 2 ELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP--VN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIF-DMTIRENII----MR--NENASESDFEEVCRLALVDEFALTfdqsydtpcKEASLSGGQQQRIALARALL 586
Cdd:cd03300 76 TVFQNYALFpHLTVFENIAfglrLKklPKAEIKERVAEALDLVQLEGYANR---------KPSQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 587 RDTEILILDEPTSALD-PITKNLVMDAIRAHRK-GKTTLVITHD------MSqinnDELVlVIDKGHLIQ 648
Cdd:cd03300 147 NEPKVLLLDEPLGALDlKLRKDMQLELKRLQKElGITFVFVTHDqeealtMS----DRIA-VMNKGKIQQ 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1099-1320 |
1.95e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.83 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAY-PDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRKTypSEDIYIDGYPLT--NIDTNW 1171
Cdd:PRK13637 3 IKIENLTHIYmEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQhlngLLKPT--SGKIIIDGVDITdkKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1172 LLKKVAIVDQKP--HLLGSTILESLLYG------VDRDINSVMdaldKTYMTEViqnlpnGLDTPLLEFSKNF--SGGQI 1241
Cdd:PRK13637 81 IRKKVGLVFQYPeyQLFEETIEKDIAFGpinlglSEEEIENRV----KRAMNIV------GLDYEDYKDKSPFelSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1242 QRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL----SCTVLIITHQ-PSLMKLADRIIVMDSGIVKESGSFD 1316
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhkeyNMTIILVSHSmEDVAKLADRIIVMNKGKCELQGTPR 230
|
....
gi 162312251 1317 ELMN 1320
Cdd:PRK13637 231 EVFK 234
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1117-1324 |
1.98e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 109.05 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTL----VELLRKTypSEDIYIDGYPLTNIDTN---WLLKKVAIVDQKP------ 1183
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLgrllLRLEEPT--SGEILFDGQDITGLSGRelrPLRRRMQMVFQDPyaslnp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1184 -HLLGSTILESLlygvdrDINSVMDA---LDKTY--MTEViqnlpnGLDTPLLE-FSKNFSGGQIQRLAFARALLRNPRL 1256
Cdd:COG4608 111 rMTVGDIIAEPL------RIHGLASKaerRERVAelLELV------GLRPEHADrYPHEFSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1257 LILDECTSALDskSSL------LLEKTIQNLSCTVLIITHQPSLMK-LADRIIVMDSGIVKESGSFDELMNRHTH 1324
Cdd:COG4608 179 IVCDEPVSALD--VSIqaqvlnLLEDLQDELGLTYLFISHDLSVVRhISDRVAVMYLGKIVEIAPRDELYARPLH 251
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
435-667 |
2.17e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.14 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 435 FDNVSFAYPSrDENlFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFP-----LEEIDEHvlg 509
Cdd:PRK13648 10 FKNVSFQYQS-DAS-FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitddnFEKLRKH--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 510 stITLVCQQP--------VIFDMTIReniiMRNENASESDFEEVCRLALVDEFALtfDQSYDTPckeASLSGGQQQRIAL 581
Cdd:PRK13648 85 --IGIVFQNPdnqfvgsiVKYDVAFG----LENHAVPYDEMHRRVSEALKQVDML--ERADYEP---NALSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 582 ARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGK--TTLVITHDMSQINNDELVLVIDKGHLIQRCARKElvLFE 659
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTE--IFD 231
|
....*...
gi 162312251 660 DFENNVSI 667
Cdd:PRK13648 232 HAEELTRI 239
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1099-1301 |
3.03e-25 |
|
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: 104.87 E-value: 3.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKSTL----VELLRktyPSE-DIYIDGYPLTNIDTNWLl 1173
Cdd:COG4133 3 LEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGKTTLlrilAGLLP---PSAgEVLWNGEPIRDAREDYR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1174 KKVAIVDQKPHLLGS-TILESL-----LYGVDRDINSVMDALDKTYMTEViqnlpngLDTPLlefsKNFSGGQIQRLAFA 1247
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLrfwaaLYGLRADREAIDEALEAVGLAGL-------ADLPV----RQLSAGQKRRVALA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 1248 RALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSLMKLADRI 1301
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAARVL 200
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
436-649 |
5.20e-25 |
|
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: 104.20 E-value: 5.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYPSRDenlfSLINVSVFIPFGELVhIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDfplEEIDEHV--LGSTIT 513
Cdd:cd03264 4 ENLTKRYGKKR----ALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDG---QDVLKQPqkLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFD-MTIRENI----IMRNENASESDfEEVCR-LALVDefaLTfdQSYDTPCKeaSLSGGQQQRIALARALLR 587
Cdd:cd03264 76 YLPQEFGVYPnFTVREFLdyiaWLKGIPSKEVK-ARVDEvLELVN---LG--DRAKKKIG--SLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 588 DTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQI-NNDELVLVIDKGHLIQR 649
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFE 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1099-1321 |
6.69e-25 |
|
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: 105.08 E-value: 6.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELL-RKTYPSE-DIYIDGYPLTNIDTNWLLKKV 1176
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInRLIEPTSgEIFIDGEDIREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQK----PHLlgsTILESL-----LYGVDRdinsvmdALDKTYMTEVIQNLpnGLDTPLL--EFSKNFSGGQIQRLA 1245
Cdd:cd03295 78 GYVIQQiglfPHM---TVEENIalvpkLLKWPK-------EKIRERADELLALV--GLDPAEFadRYPHELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1246 FARALLRNPRLLILDECTSALD--SKSSLLLE-KTIQN-LSCTVLIITHQ-PSLMKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDpiTRDQLQEEfKRLQQeLGKTIVFVTHDiDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
.
gi 162312251 1321 R 1321
Cdd:cd03295 226 S 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1099-1305 |
7.97e-25 |
|
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: 102.23 E-value: 7.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDserNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIyidGYPLTNidtnwllkKV 1176
Cdd:cd03223 1 IELENLSLATPD---GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPwgSGRI---GMPEGE--------DL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHLLGSTILESLLYgvdrdinsvmdaldktymteviqnlpngldtPLlefSKNFSGGQIQRLAFARALLRNPRL 1256
Cdd:cd03223 67 LFLPQRPYLPLGTLREQLIY-------------------------------PW---DDVLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 162312251 1257 LILDECTSALDSKSSLLLEKTIQNLSCTVLIITHQPSLMKLADRIIVMD 1305
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLD 161
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1108-1309 |
1.25e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.78 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1108 YPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSED--IYIDGYPLTNIDTNWLLKKVAIVDQKPhL 1185
Cdd:COG1101 12 NPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSgsILIDGKDVTKLPEYKRAKYIGRVFQDP-M 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1186 LGS----TILESLL--------YGVDRDINSVMDALDKTYMTEVIQNLPNGLDTP--LLefsknfSGGQIQRLAFARALL 1251
Cdd:COG1101 91 MGTapsmTIEENLAlayrrgkrRGLRRGLTKKRRELFRELLATLGLGLENRLDTKvgLL------SGGQRQALSLLMATL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 1252 RNPRLLILDECTSALDSKSS-LLLEKT---IQNLSCTVLIITHQpslMKLA----DRIIVMDSG-IV 1309
Cdd:COG1101 165 TKPKLLLLDEHTAALDPKTAaLVLELTekiVEENNLTTLMVTHN---MEQAldygNRLIMMHEGrII 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1099-1307 |
1.43e-24 |
|
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: 101.35 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPdserNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDGYPLTnidtnwllkkv 1176
Cdd:cd03216 1 LELRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKpdSGEILVDGKEVS----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 aivdqkphllgstilesllygvdrdINSVMDALDK-TYMteVIQnlpngldtpllefsknFSGGQIQRLAFARALLRNPR 1255
Cdd:cd03216 66 -------------------------FASPRDARRAgIAM--VYQ----------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 1256 LLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPS-LMKLADRIIVMDSG 1307
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRaqgVAVIFISHRLDeVFEIADRVTVLRDG 158
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
454-629 |
1.77e-24 |
|
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: 104.65 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVL----GSTITLVCQQPVIF-DMTIRE 528
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 529 NIIM------RNENASESDFEEVcrLALVDefaLT-FDQSYDTpckeaSLSGGQQQRIALARALLRDTEILILDEPTSAL 601
Cdd:cd03294 122 NVAFglevqgVPRAEREERAAEA--LELVG---LEgWEHKYPD-----ELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190
....*....|....*....|....*....|
gi 162312251 602 DP-ITKNLVMDAIRAHRK-GKTTLVITHDM 629
Cdd:cd03294 192 DPlIRREMQDELLRLQAElQKTIVFITHDL 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1099-1314 |
1.84e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.78 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSE--RNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLrktYPSE-DIYIDGYPLTNIDTNW 1171
Cdd:PRK13633 5 IKCKNVSYKYESNEesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnaLL---IPSEgKVYVDGLDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1172 LLKKVA-IVDQKP-HLLGSTILESLL------YGVDRD-INS-VMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQI 1241
Cdd:PRK13633 82 DIRNKAgMVFQNPdNQIVATIVEEDVafgpenLGIPPEeIRErVDESLKKVGMYEYRRHAPHLL-----------SGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 1242 QRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS----CTVLIITHQPSLMKLADRIIVMDSGIVKESGS 1314
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNkkygITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
454-655 |
2.01e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 106.34 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDfplEEI-DEHVLGSTITLVCQQPVIF-DMTIRENI- 530
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVtHRSIQQRDICMVFQSYALFpHMSLGENVg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 531 ---IMRNENASESDFEEVCRLALVD--EFALTF-DQsydtpckeasLSGGQQQRIALARALLRDTEILILDEPTSALDPI 604
Cdd:PRK11432 101 yglKMLGVPKEERKQRVKEALELVDlaGFEDRYvDQ----------ISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 605 TKNLVMDAIR--AHRKGKTTLVITHDMSQ--INNDElVLVIDKGHLIQRCARKEL 655
Cdd:PRK11432 171 LRRSMREKIRelQQQFNITSLYVTHDQSEafAVSDT-VIVMNKGKIMQIGSPQEL 224
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
454-647 |
2.12e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.04 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVI-FDMTIRENIIM 532
Cdd:COG4559 19 DVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLaFPFTVEEVVAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 533 -RNENASE-SDFEEVCR--LALVD--EFAltfDQSYDTpckeasLSGGQQQRIALARAL--LRDTE-----ILILDEPTS 599
Cdd:COG4559 99 gRAPHGSSaAQDRQIVReaLALVGlaHLA---GRSYQT------LSGGEQQRVQLARVLaqLWEPVdggprWLFLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 600 ALDPITKNLVMDAIRAH-RKGKTTLVITHDMsqinN------DELVLvIDKGHLI 647
Cdd:COG4559 170 ALDLAHQHAVLRLARQLaRRGGGVVAVLHDL----NlaaqyaDRILL-LHQGRLV 219
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
455-688 |
2.18e-24 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 105.16 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 455 VSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFP-LEEIDEhvLGSTITLVCQQPVIF-DMTIRENIIM 532
Cdd:TIGR01188 12 VNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDvVREPRK--VRRSIGIVPQYASVDeDLTGRENLEM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 533 R------NENASESDFEEvcrlaLVDEFALTfdQSYDTPCKeaSLSGGQQQRIALARALLRDTEILILDEPTSALDPITK 606
Cdd:TIGR01188 90 MgrlyglPKDEAEERAEE-----LLELFELG--EAADRPVG--TYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 607 NLVMDAIRAHRK-GKTTLVITHDMSQInnDEL---VLVIDKGHLIQRCARKEL--VLFEDFENNVSIDEKVLKEEADNPF 680
Cdd:TIGR01188 161 RAIWDYIRALKEeGVTILLTTHYMEEA--DKLcdrIAIIDHGRIIAEGTPEELkrRLGKDTLESRPRDIQSLKVEVSMLI 238
|
....*...
gi 162312251 681 ILPNEESL 688
Cdd:TIGR01188 239 AELGETGL 246
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1099-1321 |
2.20e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 103.63 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSErnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRK--TYPSEDIYIDGYPLT--NIDTNWLLK 1174
Cdd:PRK09493 2 IEFKNVSKHFGPTQ----VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKleEITSGDLIVDGLKVNdpKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQK----PHLlgsTILESLLYGVDR-------DINSV-MDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQ 1242
Cdd:PRK09493 78 EAGMVFQQfylfPHL---TALENVMFGPLRvrgaskeEAEKQaRELLAKVGLAERAHHYPSEL-----------SGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1243 RLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSLM-KLADRIIVMDSGIVKESGSFDEL 1318
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAeegMTMVIVTHEIGFAeKVASRLIFIDKGRIAEDGDPQVL 223
|
...
gi 162312251 1319 MNR 1321
Cdd:PRK09493 224 IKN 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
452-631 |
2.94e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.63 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVI---FDMTIRE 528
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaPSMTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 529 NIIM---RNE--------NASESDF--EEVCRLALVDEFALtfdqsyDTPCKeaSLSGGQQQRIALARALLRDTEILILD 595
Cdd:COG1101 102 NLALayrRGKrrglrrglTKKRRELfrELLATLGLGLENRL------DTKVG--LLSGGQRQALSLLMATLTKPKLLLLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 162312251 596 EPTSALDPITKNLVMDAIR--AHRKGKTTLVITHDMSQ 631
Cdd:COG1101 174 EHTAALDPKTAALVLELTEkiVEENNLTTLMVTHNMEQ 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
467-686 |
3.52e-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: 105.27 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 467 IIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGstITLVCQQPVIF-DMTIRENII----MRNENASESD 541
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRH--INMVFQSYALFpHMTVEENVAfglkMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 542 --FEEVCRLALVDEFAltfdQSYDTpckeaSLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRA--HR 617
Cdd:TIGR01187 79 prVLEALRLVQLEEFA----DRKPH-----QLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTiqEQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 618 KGKTTLVITHDMSQ-INNDELVLVIDKGHLIQRCARKElvLFED--------FENNVSIDEKVLKEEADNPFILPNEE 686
Cdd:TIGR01187 150 LGITFVFVTHDQEEaMTMSDRIAIMRKGKIAQIGTPEE--IYEEpanlfvarFIGEINVFEATVIERKSEQVVLAGVE 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1117-1320 |
3.85e-24 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 102.52 E-value: 3.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYIDGYPLTNidtnwlLKKVAIVD-------QKPHLLG 1187
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLrPTSgSVLFDGEDITG------LPPHEIARlgigrtfQIPRLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1188 S-TILESLLYGV----------DRDINSVMDALDKTymTEVIQ--NLPNGLDTPllefSKNFSGGQIQRLAFARALLRNP 1254
Cdd:cd03219 89 ElTVLENVMVAAqartgsglllARARREEREARERA--EELLErvGLADLADRP----AGELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1255 RLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITH-QPSLMKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRELRergITVLLVEHdMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
452-1325 |
5.12e-24 |
|
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: 110.39 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIylddfpleeidEHvlGSTITLVCQQPVIFDMTIRENII 531
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------KH--SGRISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 532 MrNENASESDFEEVCRLALVDEFALTFDQSYDTPCKEA--SLSGGQQQRIALARALLRDTEILILDEPTSALDPIT-KNL 608
Cdd:TIGR01271 509 F-GLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGgiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTeKEI 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 609 VMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKEL-VLFEDFENnvsideKVLKEEADNPFILPNEES 687
Cdd:TIGR01271 588 FESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELqAKRPDFSS------LLLGLEAFDNFSAERRNS 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 688 LLekywinyNESFSQLSRESLFTSLESPFTDIES-----PTIVSRRK-------IVEQRKLRMEKESFQETNV------- 748
Cdd:TIGR01271 662 IL-------TETLRRVSIDGDSTVFSGPETIKQSfkqppPEFAEKRKqsiilnpIASARKFSFVQMGPQKAQAttiedav 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 749 ----DQTFHLFDDKEHACSL---TLIFKSIWKVKKLRWFFLLGLLTSLIQG------------------------ASVPI 797
Cdd:TIGR01271 735 repsERKFSLVPEDEQGEESlprGNQYHHGLQHQAQRRQSVLQLMTHSNRGenrreqlqtsfrkkssitqqnelaSELDI 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 798 FAYVISK--CLNLFMQIDPS-IGVAFWSSMVLVVAAGSGASYFfsHYIFS----ISAKIWCdhYRLLAVKVLFTQDQAWF 870
Cdd:TIGR01271 815 YSRRLSKdsVYEISEEINEEdLKECFADERENVFETTTWNTYL--RYITTnrnlVFVLIFC--LVIFLAEVAASLLGLWL 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 871 dqIENYPLVLSKIlVNNISDMRNMISSLieEVFIAFTMA--IIGI---------AWSFATGWRLAAVLVAVSPIL----- 934
Cdd:TIGR01271 891 --ITDNPSAPNYV-DQQHANASSPDVQK--PVIITPTSAyyIFYIyvgtadsvlALGFFRGLPLVHTLLTVSKRLheqml 965
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 935 --CLTSRMFSYIYVST----ERMCQDV-------------VISTTSILHKTIVNLDTIKGYSVLS--------------F 981
Cdd:TIGR01271 966 hsVLQAPMAVLNTMKAgrilNRFTKDMaiiddmlpltlfdFIQLTLIVLGAIFVVSVLQPYIFIAaipvavifimlrayF 1045
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 982 FRENHK-----------------NSLRKSW--EAFKRRAFWTSLGF-AIN----NSLLYF--VRALLFYCSSIFISkeFY 1035
Cdd:TIGR01271 1046 LRTSQQlkqlesearspifshliTSLKGLWtiRAFGRQSYFETLFHkALNlhtaNWFLYLstLRWFQMRIDIIFVF--FF 1123
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1036 TVEQMVQVLS----------LATFTLLMAST---CIMSLPNVSASRIATSRVLKLSSL-----KPGNLHKSGYLKFPLV- 1096
Cdd:TIGR01271 1124 IAVTFIAIGTnqdgegevgiILTLAMNILSTlqwAVNSSIDVDGLMRSVSRVFKFIDLpqeepRPSGGGGKYQLSTVLVi 1203
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1097 ------------GKIEFDGVSFAYPDSERNhlALNNVSLSIEAREKVAIVGISGSGKSTLVE-LLRKTYPSEDIYIDGYP 1163
Cdd:TIGR01271 1204 enphaqkcwpsgGQMDVQGLTAKYTEAGRA--VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSaLLRLLSTEGEIQIDGVS 1281
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1164 LTNIDTNWLLKKVAIVDQKPHLLGSTI---LESLLYGVDRDINSVMDALDktyMTEVIQNLPNGLDTPLLEFSKNFSGGQ 1240
Cdd:TIGR01271 1282 WNSVTLQTWRKAFGVIPQKVFIFSGTFrknLDPYEQWSDEEIWKVAEEVG---LKSVIEQFPDKLDFVLVDGGYVLSNGH 1358
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1241 IQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL--SCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDEL 1318
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSfsNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKL 1438
|
....*..
gi 162312251 1319 MNRHTHF 1325
Cdd:TIGR01271 1439 LNETSLF 1445
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
781-1049 |
5.24e-24 |
|
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: 103.49 E-value: 5.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 781 FLLGLLTSLIQGASVPIFAYVISKCLNLFMQI--DPSIGVAFWSSMVLVVAAGSGASYFFSHYIFSISAKIWCDHYRLLA 858
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDgdPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 859 VKVLFTQDQAWFDQieNYPLVLSKILVNNISDMRNMISSLIEEVFIAFTMAIIGIAWSFATGWRLAAVLVAVSPILCLTS 938
Cdd:pfam00664 81 FKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 939 RMFSYIYVSTERMCQDVVISTTSILHKTIVNLDTIKGYSVLSFFRENHKNSLRKSWEAFKRRAFWTSLGFAINNSLLYFV 1018
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|.
gi 162312251 1019 RALLFYCSSIFISKEFYTVEQMVQVLSLATF 1049
Cdd:pfam00664 239 YALALWFGAYLVISGELSVGDLVAFLSLFAQ 269
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1105-1320 |
6.22e-24 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 108.26 E-value: 6.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1105 SFAYPDSErnHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTNIDTNWLLKKVAIVDQK 1182
Cdd:PRK10789 320 QFTYPQTD--HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSegDIRFHDIPLTKLQLDSWRSRLAVVSQT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1183 PHLLGSTILESLLYGV-DRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDE 1261
Cdd:PRK10789 398 PFLFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1262 CTSALDSKSslllEKTI-QNLSC-----TVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:PRK10789 478 ALSAVDGRT----EHQIlHNLRQwgegrTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
434-648 |
8.51e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 104.38 E-value: 8.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYpsrdENLFSLINVSVFIPFGELVHIIGPSGSGKSTfislLLR----YFSPTYGNIYLD-----DFPLEEID 504
Cdd:COG3839 5 ELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKST----LLRmiagLEDPTSGEILIGgrdvtDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 505 ehvlgstITLVCQQPVIFD-MTIRENII----MRNENASEsdfeevcRLALVDEFA----LT--FDQsydtpcKEASLSG 573
Cdd:COG3839 77 -------IAMVFQSYALYPhMTVYENIAfplkLRKVPKAE-------IDRRVREAAellgLEdlLDR------KPKQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 574 GQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRA-HRKGKTTLVI-THD------MSqinnDELVlVIDKGH 645
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRlHRRLGTTTIYvTHDqveamtLA----DRIA-VMNDGR 211
|
...
gi 162312251 646 LIQ 648
Cdd:COG3839 212 IQQ 214
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1097-1305 |
9.11e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.59 E-value: 9.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1097 GKIEFDGVSFAYPDserNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELL---------RKTYPSEDiyidgypltni 1167
Cdd:COG4178 361 GALALEDLTLRTPD---GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygsgRIARPAGA----------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1168 dtnwllkKVAIVDQKPHLLGSTILESLLY-GVDRDINS--VMDALDKTYMteviQNLPNGLDTPLlEFSKNFSGGQIQRL 1244
Cdd:COG4178 427 -------RVLFLPQRPYLPLGTLREALLYpATAEAFSDaeLREALEAVGL----GHLAERLDEEA-DWDQVLSLGEQQRL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 1245 AFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL--SCTVLIITHQPSLMKLADRIIVMD 1305
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGHRSTLAAFHDRVLELT 557
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
445-629 |
1.44e-23 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 100.00 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 445 RDENLFSLINVSvfIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDD---FPLEEIDEHVL-GSTITLVCQQ-P 519
Cdd:TIGR03608 9 GDKVILDDLNLT--IEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGqetPPLNSKKASKFrREKLGYLFQNfA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 520 VIFDMTIREN--IIMRNENASESDFEEVCRLALvDEFALTFDQSYdtpcKEASLSGGQQQRIALARALLRDTEILILDEP 597
Cdd:TIGR03608 87 LIENETVEENldLGLKYKKLSKKEKREKKKEAL-EKVGLNLKLKQ----KIYELSGGEQQRVALARAILKPPPLILADEP 161
|
170 180 190
....*....|....*....|....*....|...
gi 162312251 598 TSALDPITKNLVMDAIRAHRK-GKTTLVITHDM 629
Cdd:TIGR03608 162 TGSLDPKNRDEVLDLLLELNDeGKTIIIVTHDP 194
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1099-1314 |
2.17e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 103.87 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSErnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLR--KTYPSEDIYIDGYPLTNI-----DTNW 1171
Cdd:PRK09452 15 VELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAgfETPDSGRIMLDGQDITHVpaenrHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1172 LLKKVAIVdqkPHLlgsTILESLLYGV------DRDINS-VMDALDKTYMTEVIQNLPngldtpllefsKNFSGGQIQRL 1244
Cdd:PRK09452 91 VFQSYALF---PHM---TVFENVAFGLrmqktpAAEITPrVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1245 AFARALLRNPRLLILDECTSALDSKssllLEKTIQN--------LSCTVLIITH-QPSLMKLADRIIVMDSGIVKESGS 1314
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYK----LRKQMQNelkalqrkLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
452-656 |
2.29e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 100.55 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLE--EIDEHVLGSTITLVCQQPVIF-DMTIRE 528
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFpHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 529 NII---MRNENASESDFEEVCRlALVDEFALTfDQSYDTPckeASLSGGQQQRIALARALLRDTEILILDEPTSALDPIT 605
Cdd:PRK09493 97 NVMfgpLRVRGASKEEAEKQAR-ELLAKVGLA-ERAHHYP---SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 606 KNLVMDAIRA-HRKGKTTLVITHDMS---QINNDelVLVIDKGHLIQRCARKELV 656
Cdd:PRK09493 172 RHEVLKVMQDlAEEGMTMVIVTHEIGfaeKVASR--LIFIDKGRIAEDGDPQVLI 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
434-706 |
2.40e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.78 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAY----PSRDEnlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPL--EEIDEHV 507
Cdd:PRK13646 4 RFDNVSYTYqkgtPYEHQ---AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthKTKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 508 --LGSTITLVCQQP--VIFDMTIRENIIMRNENASeSDFEEVCRLA--LVDEFALTFDQSYDTPCKeasLSGGQQQRIAL 581
Cdd:PRK13646 81 rpVRKRIGMVFQFPesQLFEDTVEREIIFGPKNFK-MNLDEVKNYAhrLLMDLGFSRDVMSQSPFQ---MSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 582 ARALLRDTEILILDEPTSALDPITKNLVMDAIRAHR--KGKTTLVITHDMSQINN--DElVLVIDKGHLIQRCARKElvL 657
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyaDE-VIVMKEGSIVSQTSPKE--L 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 658 FEDfennvsiDEKVLKEEADNPFILPNEESLLEKYWINY------NESFSQLSRE 706
Cdd:PRK13646 234 FKD-------KKKLADWHIGLPEIVQLQYDFEQKYQTKLkdialtEEEFVSLYKE 281
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1099-1309 |
2.47e-23 |
|
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: 99.79 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDserNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELL--RKTYPSEDIYIDGYPLTNIDTN---WLL 1173
Cdd:cd03292 1 IEFINVTKTYPN---GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIykEELPTSGTIRVNGQDVSDLRGRaipYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1174 KKVAIVDQKPHLLGS-TILESLLYGVD------RDINS-VMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLA 1245
Cdd:cd03292 78 RKIGVVFQDFRLLPDrNVYENVAFALEvtgvppREIRKrVPAALELVGLSHKHRALPAEL-----------SGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1246 FARALLRNPRLLILDECTSALDSKSS---LLLEKTIQNLSCTVLIITHQPSLM-KLADRIIVMDSGIV 1309
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTweiMNLLKKINKAGTTVVVATHAKELVdTTRHRVIALERGKL 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
454-647 |
3.21e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 101.72 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGstitlvcqqpviF---------DM 524
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIG------------YlpeerglypKM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 525 TIRENII----MRNENASESDfEEVcrLALVDEFALTfdQSYDTPCKEasLSGGQQQRIALARALLRDTEILILDEPTSA 600
Cdd:COG4152 87 KVGEQLVylarLKGLSKAEAK-RRA--DEWLERLGLG--DRANKKVEE--LSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 162312251 601 LDPITKNLVMDAIRAHR-KGKTTLVITHDMSQInnDEL---VLVIDKGHLI 647
Cdd:COG4152 160 LDPVNVELLKDVIRELAaKGTTVIFSSHQMELV--EELcdrIVIINKGRKV 208
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
433-647 |
4.55e-23 |
|
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: 98.01 E-value: 4.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRDEN--LFSLINVSVFIPFGELVHIIGPSGSGKSTFISLL--LRYFSPTYGNIYLDDFPLeeiDEHVL 508
Cdd:cd03213 4 LSFRNLTVTVKSSPSKsgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 509 GSTITLVCQQPVIF-DMTIRENIimrnenasesDFEEVCRlalvdefaltfdqsydtpckeaSLSGGQQQRIALARALLR 587
Cdd:cd03213 81 RKIIGYVPQDDILHpTLTVRETL----------MFAAKLR----------------------GLSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 588 DTEILILDEPTSALDPITKNLVMDAIRAHRK-GKTTLVITHDMSQ--INNDELVLVIDKGHLI 647
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVI 191
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
455-644 |
5.12e-23 |
|
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: 98.51 E-value: 5.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 455 VSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGstiTLVCQQPVIFDMTIRENII--- 531
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIG---YLPEERGLYPKMKVIDQLVyla 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 532 -MRNENASESdfeevcrLALVDEFALTFDQSYDTPCKEASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVM 610
Cdd:cd03269 96 qLKGLKKEEA-------RRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLK 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 162312251 611 DAIRA-HRKGKTTLVITHDMSQInnDEL---VLVIDKG 644
Cdd:cd03269 169 DVIRElARAGKTVILSTHQMELV--EELcdrVLLLNKG 204
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
462-655 |
6.10e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.44 E-value: 6.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFpleEIDehvlgSTITLVCQQPVI-------------FDM---- 524
Cdd:PRK11264 29 GEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDI---TID-----TARSLSQQKGLIrqlrqhvgfvfqnFNLfphr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 525 TIRENIIMRNENASESDFEEVCRLA--LVDEFALTfdqsydtpCKEAS----LSGGQQQRIALARALLRDTEILILDEPT 598
Cdd:PRK11264 101 TVLENIIEGPVIVKGEPKEEATARAreLLAKVGLA--------GKETSyprrLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 599 SALDPITKNLVMDAIRAHRKGKTTLVI-THDMSQINN-DELVLVIDKGHLIQRCARKEL 655
Cdd:PRK11264 173 SALDPELVGEVLNTIRQLAQEKRTMVIvTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
454-647 |
6.18e-23 |
|
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: 98.94 E-value: 6.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDF-PLEEIDEHVlgSTITLVCQQ--PVIFDMTIRE-- 528
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKRRKKFL--RRIGVVFGQktQLWWDLPVIDsf 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 529 NIIMRNENASESDFEEvcRLA-LVDefALTFDQSYDTPCKEASLsgGQQQRIALARALLRDTEILILDEPTSALDPITKN 607
Cdd:cd03267 117 YLLAAIYDLPPARFKK--RLDeLSE--LLDLEELLDTPVRQLSL--GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 162312251 608 LVMDAIRAHRK--GKTTLVITHDMSQINN-DELVLVIDKGHLI 647
Cdd:cd03267 191 NIRNFLKEYNRerGTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1118-1321 |
7.51e-23 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 98.95 E-value: 7.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTNIDTNwlLKKVAIVDQK----PHLlgsTIL 1191
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDsgKILLNGKDITNLPPE--KRDISYVPQNyalfPHM---TVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1192 ESLLYGVDrdINSVMDALDKTYMTEVIQNLpnGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALD--SK 1269
Cdd:cd03299 90 KNIAYGLK--KRKVDKKEIERKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDvrTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1270 SSL--LLEKTIQNLSCTVLIITH-QPSLMKLADRIIVMDSGIVKESGSFDELMNR 1321
Cdd:cd03299 166 EKLreELKKIRKEFGVTVLHVTHdFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
451-647 |
7.51e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.12 E-value: 7.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 451 SLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDF-------PLEEIDEHVlgstiTLVCQQP--VI 521
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVditdkkvKLSDIRKKV-----GLVFQYPeyQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 522 FDMTIRENIIM--RNENASESDFEEVCRLALvDEFALTFDQSYDTPCKEasLSGGQQQRIALARALLRDTEILILDEPTS 599
Cdd:PRK13637 97 FEETIEKDIAFgpINLGLSEEEIENRVKRAM-NIVGLDYEDYKDKSPFE--LSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 162312251 600 ALDPITKNLVMDAIRA-HRKGK-TTLVITHDMSQINN-DELVLVIDKGHLI 647
Cdd:PRK13637 174 GLDPKGRDEILNKIKElHKEYNmTIILVSHSMEDVAKlADRIIVMNKGKCE 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1099-1321 |
1.04e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 101.38 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSErnhlALNNVSLSIEAREKVAIVGISGSGKSTLvelLRKTY----PSE-DIYIDGyplTNIDTNwlL 1173
Cdd:COG1118 3 IEVRNISKRFGSFT----LLDDVSLEIASGELVALLGPSGSGKTTL---LRIIAgletPDSgRIVLNG---RDLFTN--L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1174 K----KVAIVDQK----PHLlgsTILESLLYGVD------RDINS-VMDALDKTYMTEVIQNLPNGLdtpllefsknfSG 1238
Cdd:COG1118 71 PprerRVGFVFQHyalfPHM---TVAENIAFGLRvrppskAEIRArVEELLELVQLEGLADRYPSQL-----------SG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1239 GQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEK----TIQNLSCTVLIITHQPSL-MKLADRIIVMDSGIVKESG 1313
Cdd:COG1118 137 GQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRwlrrLHDELGGTTVFVTHDQEEaLELADRVVVMNQGRIEQVG 216
|
....*...
gi 162312251 1314 SFDELMNR 1321
Cdd:COG1118 217 TPDEVYDR 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1116-1313 |
1.08e-22 |
|
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: 98.11 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1116 LALNNVSLSIEAREKVAIVGISGSGKSTLVELL-----RKTYPSEDIYIDGYPLtNIDTnwLLKKVAIVDQK----PHLl 1186
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrveGGGTTSGQILFNGQPR-KPDQ--FQKCVAYVRQDdillPGL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1187 gsTILESLLYGVDRDINSVMDALDKTYMTEVIQnLPNGLDTPLL-EFSKNFSGGQIQRLAFARALLRNPRLLILDECTSA 1265
Cdd:cd03234 97 --TVRETLTYTAILRLPRKSSDAIRKKRVEDVL-LRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 162312251 1266 LDSKSSLLLEKTIQNLS---CTVLIITHQP--SLMKLADRIIVMDSGIVKESG 1313
Cdd:cd03234 174 LDSFTALNLVSTLSQLArrnRIVILTIHQPrsDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
451-631 |
1.41e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 98.69 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 451 SLINVSV-FIPfGELVHIIGPSGSGKSTFISLLLRY--FSPTYG----------NIYLddfplEEIDEHVLGSTITLVCQ 517
Cdd:PRK14239 20 ALNSVSLdFYP-NEITALIGPSGSGKSTLLRSINRMndLNPEVTitgsivynghNIYS-----PRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 518 QPVIFDMTIRENIIMRNENASESD---FEEVCRLALVDefALTFDQSYDTPCKEA-SLSGGQQQRIALARALLRDTEILI 593
Cdd:PRK14239 94 QPNPFPMSIYENVVYGLRLKGIKDkqvLDEAVEKSLKG--ASIWDEVKDRLHDSAlGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 162312251 594 LDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQ 631
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQ 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
433-632 |
1.67e-22 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 98.23 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRdeNLFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGN-IYLDDFPL--EEIDEhvLG 509
Cdd:COG1119 4 LELRNVTVRRGGK--TILD--DISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRggEDVWE--LR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 510 STITLVC---QQPVIFDMTIRE-------NIIMRNENASESDFEEVCR-LALVDEFALTfDQSYDTpckeasLSGGQQQR 578
Cdd:COG1119 78 KRIGLVSpalQLRFPRDETVLDvvlsgffDSIGLYREPTDEQRERARElLELLGLAHLA-DRPFGT------LSQGEQRR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 579 IALARALLRDTEILILDEPTSALDPITKNLVMDAIRA-HRKGKTTLV-ITHDMSQI 632
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEI 206
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
441-629 |
1.70e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.53 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 441 AYPSRDenlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIylddfpleeidEHVLGSTITLVCQQ-- 518
Cdd:NF040873 1 GYGGRP----VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRse 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 519 -PVIFDMTIRENIIM-------------RNENASESDFEEvcRLALvDEFAltfDQSYDTpckeasLSGGQQQRIALARA 584
Cdd:NF040873 66 vPDSLPLTVRDLVAMgrwarrglwrrltRDDRAAVDDALE--RVGL-ADLA---GRQLGE------LSGGQRQRALLAQG 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 162312251 585 LLRDTEILILDEPTSALDPITKNLVMDAI-RAHRKGKTTLVITHDM 629
Cdd:NF040873 134 LAQEADLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDL 179
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
434-628 |
1.79e-22 |
|
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: 96.94 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRdenlFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLD-----DFPLEEIDehvl 508
Cdd:cd03301 2 ELENVTKRFGNV----TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvtDLPPKDRD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 509 gstITLVCQQPVIF-DMTIRENII----MRNENASESDfEEVCRLALVdefaLTFDQSYDTpcKEASLSGGQQQRIALAR 583
Cdd:cd03301 74 ---IAMVFQNYALYpHMTVYDNIAfglkLRKVPKDEID-ERVREVAEL----LQIEHLLDR--KPKQLSGGQRQRVALGR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 162312251 584 ALLRDTEILILDEPTSALDPitknLVMDAIRA-----HRK-GKTTLVITHD 628
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDA----KLRVQMRAelkrlQQRlGTTTIYVTHD 190
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
452-625 |
2.08e-22 |
|
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: 97.12 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTF---ISLLLRyfsPTYGNIYLDD-----FPLEEIDEhvLGstITLVCQQPVIF- 522
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLlktIMGLLP---PRSGSIRFDGrditgLPPHERAR--AG--IGYVPEGRRIFp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 523 DMTIRENIIM----RNENASESDFEEVCRL--ALvDEFAltfDQsydtpcKEASLSGGQQQRIALARALLRDTEILILDE 596
Cdd:cd03224 89 ELTVEENLLLgayaRRRAKRKARLERVYELfpRL-KERR---KQ------LAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180
....*....|....*....|....*....
gi 162312251 597 PTSALDPITKNLVMDAIRAHRKGKTTLVI 625
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDEGVTILL 187
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
432-648 |
2.50e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 97.39 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 432 GFRFDNVSFAYPSRDenlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLD----DFPlEEIDE-- 505
Cdd:COG4161 2 SIQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAghqfDFS-QKPSEka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 506 -HVLGSTITLVCQQ----PvifDMTIRENII--------MRNENASESDFEEVCRLALvDEFALTFdqsydtPckeASLS 572
Cdd:COG4161 77 iRLLRQKVGMVFQQynlwP---HLTVMENLIeapckvlgLSKEQAREKAMKLLARLRL-TDKADRF------P---LHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 573 GGQQQRIALARALLRDTEILILDEPTSALDP-ITKNLVmDAIRAHRK-GKTTLVITHDM-------SQinndelVLVIDK 643
Cdd:COG4161 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPeITAQVV-EIIRELSQtGITQVIVTHEVefarkvaSQ------VVYMEK 216
|
....*
gi 162312251 644 GHLIQ 648
Cdd:COG4161 217 GRIIE 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
435-628 |
2.75e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.45 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 435 FDNVSFAYPSRDenLFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDfpleeidehvlGSTITL 514
Cdd:COG0488 1 LENLSKSFGGRP--LLD--DVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 515 VCQQPVIFD-MTIRENIIM-------------RNENASESDFEEVCRLA-LVDEFA-----------------LTFDQS- 561
Cdd:COG0488 66 LPQEPPLDDdLTVLDTVLDgdaelraleaeleELEAKLAEPDEDLERLAeLQEEFEalggweaearaeeilsgLGFPEEd 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 562 YDTPCKEasLSGGQQQRIALARALLRDTEILILDEPTSALDpitknlvMDAIR------AHRKGkTTLVITHD 628
Cdd:COG0488 146 LDRPVSE--LSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEwleeflKNYPG-TVLVVSHD 208
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
433-631 |
2.86e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.93 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYpsrdENLFSLINVSVFIPFGELVHIIGPSGSGKSTfislLLRYFS------PTY---GNIYLDDFPL--E 501
Cdd:PRK14243 11 LRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKST----ILRCFNrlndliPGFrveGKVTFHGKNLyaP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 502 EIDEHVLGSTITLVCQQPVIFDMTIRENIIMRNE-NASESDFEEVC-----RLALVDEFALTFDQSydtpckEASLSGGQ 575
Cdd:PRK14243 83 DVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGARiNGYKGDMDELVerslrQAALWDEVKDKLKQS------GLSLSGGQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 576 QQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQ 631
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQ 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1099-1318 |
3.14e-22 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 96.42 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERnhLALNNVSLSIEAREKVAIVGISGSGKSTLVELLR-KTYPSE-DIYIDGYPLTNiDTNWLLKKV 1176
Cdd:cd03263 1 LQIRNLTKTYKKGTK--PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTgELRPTSgTAYINGYSIRT-DRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQK----PHLlgsTILESL-----LYGV-DRDINSVMDALDKTYmteviqNLPNGLDTPllefSKNFSGGQIQRLAF 1246
Cdd:cd03263 78 GYCPQFdalfDEL---TVREHLrfyarLKGLpKSEIKEEVELLLRVL------GLTDKANKR----ARTLSGGMKRKLSL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1247 ARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL--SCTVLIITHQPSLMK-LADRIIVMDSGIVKESGSFDEL 1318
Cdd:cd03263 145 AIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVrkGRSIILTTHSMDEAEaLCDRIAIMSDGKLRCIGSPQEL 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
454-647 |
3.27e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.39 E-value: 3.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVI-FDMTIRE---- 528
Cdd:PRK11231 20 DLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRElvay 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 529 ------NIIMRNENASESDFEEVCRLALVDEFAltfdqsyDTPCkeASLSGGQQQRIALARALLRDTEILILDEPTSALD 602
Cdd:PRK11231 100 grspwlSLWGRLSAEDNARVNQAMEQTRINHLA-------DRRL--TDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 162312251 603 PITKNLVMDAIRAHR-KGKTTLVITHDMSQINN--DELVlVIDKGHLI 647
Cdd:PRK11231 171 INHQVELMRLMRELNtQGKTVVTVLHDLNQASRycDHLV-VLANGHVM 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
456-644 |
4.23e-22 |
|
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: 96.02 E-value: 4.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 456 SVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLD--DFPLEEIDEHvlgsTITLVCQQPVIF-DMTIRENI-I 531
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvDVTAAPPADR----PVSMLFQENNLFaHLTVEQNVgL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 532 MRNENASesdFEEVCRLALVDEFALTFDQSYDTPCKEAsLSGGQQQRIALARALLRDTEILILDEPTSALDPITKN---- 607
Cdd:cd03298 94 GLSPGLK---LTAEDRQAIEVALARVGLAGLEKRLPGE-LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAemld 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 162312251 608 LVMDaIRAHRKgKTTLVITHDMSQINN-DELVLVIDKG 644
Cdd:cd03298 170 LVLD-LHAETK-MTVLMVTHQPEDAKRlAQRVVFLDNG 205
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
432-647 |
4.89e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.89 E-value: 4.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 432 GFRFDNVSFAY----PSRDENLFsliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPL----EEI 503
Cdd:PRK13649 2 GINLQNVSYTYqagtPFEGRALF---DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 504 DEHVLGSTITLVCQQP--VIFDMTIRENIIMRNEN--ASESDFEEVCR--LALVDEFALTFDQSydtpckEASLSGGQQQ 577
Cdd:PRK13649 79 DIKQIRKKVGLVFQFPesQLFEETVLKDVAFGPQNfgVSQEEAEALARekLALVGISESLFEKN------PFELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 578 RIALARALLRDTEILILDEPTSALDPITKNLVMDAIRA-HRKGKTTLVITHDMSQINN-DELVLVIDKGHLI 647
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANyADFVYVLEKGKLV 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1101-1316 |
5.56e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1101 FDGVSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGypltnidtNWllkKVAI 1178
Cdd:COG0488 1 LENLSKSFGG----RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDsgEVSIPK--------GL---RIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1179 VDQKPHLL-GSTILESLLYGvDRDINSVMDALDKTYMT-------------------------------EVIQNLpnGLD 1226
Cdd:COG0488 66 LPQEPPLDdDLTVLDTVLDG-DAELRALEAELEELEAKlaepdedlerlaelqeefealggweaearaeEILSGL--GFP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1227 TPLLEFS-KNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSCTVLIITHQPSLM-KLADRIIVM 1304
Cdd:COG0488 143 EEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLdRVATRILEL 222
|
250
....*....|...
gi 162312251 1305 DSGIVKE-SGSFD 1316
Cdd:COG0488 223 DRGKLTLyPGNYS 235
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1097-1333 |
7.22e-22 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 97.23 E-value: 7.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1097 GKIEFDGVSFAYpdSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE-LLRKTYPSEDIYIDGYPLTNIDTNWLLKK 1175
Cdd:cd03289 1 GQMTVKDLTAKY--TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLNTEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1176 VAIVDQKPHLLGSTILESL-LYGVDRDiNSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNP 1254
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKWSD-EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1255 RLLILDECTSALDSKSSLLLEKTIQN--LSCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKLIHRG 1332
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQafADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPS 237
|
.
gi 162312251 1333 E 1333
Cdd:cd03289 238 D 238
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
432-642 |
7.71e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 95.24 E-value: 7.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 432 GFRFDNVSFAYPSRDenLFSLINVSVfiPFGELVHIIGPSGSGKSTFISLLLRYFSPTY---GNIYLDDFPLEEIDEHVL 508
Cdd:COG4136 1 MLSLENLTITLGGRP--LLAPLSLTV--APGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALPAEQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 509 GstITLVCQQPVIFD-MTIRENI-------IMRNEnasesdfeevcRLALVDEfALT-------FDQsydTPckeASLSG 573
Cdd:COG4136 77 R--IGILFQDDLLFPhLSVGENLafalpptIGRAQ-----------RRARVEQ-ALEeaglagfADR---DP---ATLSG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 574 GQQQRIALARALLRDTEILILDEPTSALDPITKN----LVMDAIRAHrkGKTTLVITHDMSQINNDELVLVID 642
Cdd:COG4136 137 GQRARVALLRALLAEPRALLLDEPFSKLDAALRAqfreFVFEQIRQR--GIPALLVTHDEEDAPAAGRVLDLG 207
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1117-1301 |
8.17e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.38 E-value: 8.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRK--------------TYPSEDIYidgYPLTniDTNWLLKKVAIVDQK 1182
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndlnpevtitgsiVYNGHNIY---SPRT--DTVDLRKEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1183 PHLLGSTILESLLYGVDrdINSVMD--ALDKTYMTEVIQ-NLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLIL 1259
Cdd:PRK14239 95 PNPFPMSIYENVVYGLR--LKGIKDkqVLDEAVEKSLKGaSIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 162312251 1260 DECTSALDSKSSLLLEKTIQNL--SCTVLIITHQpslMKLADRI 1301
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLkdDYTMLLVTRS---MQQASRI 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1114-1313 |
9.04e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 94.98 E-value: 9.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1114 NHLALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRKTypSEDIYIDG-YPLTNIDTnwlLKKV-AIVDQK---PH 1184
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKiilgLIKPD--SGEITFDGkSYQKNIEA---LRRIgALIEAPgfyPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1185 LLGSTILE--SLLYGV-DRDINSVMDALdktymteviqnlpnGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDE 1261
Cdd:cd03268 87 LTARENLRllARLLGIrKKRIDEVLDVV--------------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 1262 CTSALDSKSSLLLEKTIQNLS---CTVLIITHQPS-LMKLADRIIVMDSGIVKESG 1313
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRdqgITVLISSHLLSeIQKVADRIGIINKGKLIEEG 208
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
462-630 |
1.04e-21 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 96.02 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTF---ISLLLRyfsPTYGNIYLDDfplEEID-----------------EHvLGSTITLVCQQpvi 521
Cdd:COG4598 34 GDVISIIGSSGSGKSTFlrcINLLET---PDSGEIRVGG---EEIRlkpdrdgelvpadrrqlQR-IRTRLGMVFQS--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 522 FD----MTIRENII---MRNENASESDFEEVCRlALVDEFALtFDQSYDTPckeASLSGGQQQRIALARALLRDTEILIL 594
Cdd:COG4598 104 FNlwshMTVLENVIeapVHVLGRPKAEAIERAE-ALLAKVGL-ADKRDAYP---AHLSGGQQQRAAIARALAMEPEVMLF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 162312251 595 DEPTSALDPitkNLVMDAIRAHRK----GKTTLVITHDMS 630
Cdd:COG4598 179 DEPTSALDP---ELVGEVLKVMRDlaeeGRTMLVVTHEMG 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
435-647 |
1.22e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.79 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 435 FDNVSFAYPSRDENLFSLINVSvfIPFGELVHIIGPSGSGKSTfISLLLRyfsptyGNIYLDDFPLEEIDehVLGSTITl 514
Cdd:PRK13640 8 FKHVSFTYPDSKKPALNDISFS--IPRGSWTALIGHNGSGKST-ISKLIN------GLLLPDDNPNSKIT--VDGITLT- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 515 vcqQPVIFDMTIRENIIMRN------------------EN--ASESDFEEVCRLALVDEFALTFDQSydtpcKEASLSGG 574
Cdd:PRK13640 76 ---AKTVWDIREKVGIVFQNpdnqfvgatvgddvafglENraVPRPEMIKIVRDVLADVGMLDYIDS-----EPANLSGG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 575 QQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGK--TTLVITHDMSQINNDELVLVIDKGHLI 647
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLL 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
425-630 |
1.25e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.01 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 425 KSISFERGFRFDNVSFAYPSRdenlfSLIN-VSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEI 503
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGR-----TLLHpLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 504 DEHVLGSTITLVCQQ-PVIFDMTIRENIIM----------RNENASESDFEEVCRLALVDEFAltfDQSYDtpckeaSLS 572
Cdd:PRK10575 79 SSKAFARKVAYLPQQlPAAEGMTVRELVAIgrypwhgalgRFGAADREKVEEAISLVGLKPLA---HRLVD------SLS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 573 GGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIR--AHRKGKTTLVITHDMS 630
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHrlSQERGLTVIAVLHDIN 209
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
434-662 |
1.30e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.82 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAY-PSRDENLFSLINVSVFIPFGELVHIIGPSGSGKST----FISLLLryfsPTYGNIylddfplEEIDEHVL 508
Cdd:PRK13641 4 KFENVDYIYsPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTlmqhFNALLK----PSSGTI-------TIAGYHIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 509 GST-----------ITLVCQQP--VIFDMTIRENIIM--RNENASESDFEEVCrLALVDEFALTFDQSYDTPCKeasLSG 573
Cdd:PRK13641 73 PETgnknlkklrkkVSLVFQFPeaQLFENTVLKDVEFgpKNFGFSEDEAKEKA-LKWLKKVGLSEDLISKSPFE---LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 574 GQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRK-GKTTLVITHDM---SQINNDelVLVIDKGHLIQR 649
Cdd:PRK13641 149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMddvAEYADD--VLVLEHGKLIKH 226
|
250
....*....|...
gi 162312251 650 CARKElvLFEDFE 662
Cdd:PRK13641 227 ASPKE--IFSDKE 237
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
455-647 |
1.47e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.59 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 455 VSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEiDEHVLGSTITLVCQqpviFD-----MTIREN 529
Cdd:PRK13536 60 LSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQ----FDnldleFTVREN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 530 IIM--RNENASESDFEEVCRLALvdEFAlTFDQSYDTPCkeASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKN 607
Cdd:PRK13536 135 LLVfgRYFGMSTREIEAVIPSLL--EFA-RLESKADARV--SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 162312251 608 LVMDAIRA-HRKGKTTLVITHDMSQINN--DELVlVIDKGHLI 647
Cdd:PRK13536 210 LIWERLRSlLARGKTILLTTHFMEEAERlcDRLC-VLEAGRKI 251
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
436-655 |
1.48e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 96.31 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYPSRDENLFSLI--NVSVFIPFGELVHIIGPSGSGKST----FISLLLryfsPTYGNIYLDDFPLEEIdEHV-- 507
Cdd:PRK13633 8 KNVSYKYESNEESTEKLAldDVNLEVKKGEFLVILGRNGSGKSTiakhMNALLI----PSEGKVYVDGLDTSDE-ENLwd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 508 LGSTITLVCQQP--VIFDMTIRENIIMRNENASESDFEEVCRlalVDEfALTFDQSYDTPcKEAS--LSGGQQQRIALAR 583
Cdd:PRK13633 83 IRNKAGMVFQNPdnQIVATIVEEDVAFGPENLGIPPEEIRER---VDE-SLKKVGMYEYR-RHAPhlLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 584 ALLRDTEILILDEPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKEL 655
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1099-1322 |
1.48e-21 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 96.03 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDS----ERNHLA-LNNVSLSIEAREKVAIVGISGSGKSTLVELL--RKTYPSEDIYIDGYPLTNID--- 1168
Cdd:TIGR02769 3 LEVRDVTHTYRTGglfgAKQRAPvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLlgLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1169 TNWLLKKVAIVDQ------KPHL-LGSTILESLlygvdRDINSvmdaLDKTYMTEVIQNLPNGLDTP---LLEFSKNFSG 1238
Cdd:TIGR02769 83 RRAFRRDVQLVFQdspsavNPRMtVRQIIGEPL-----RHLTS----LDESEQKARIAELLDMVGLRsedADKLPRQLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1239 GQIQRLAFARALLRNPRLLILDECTSALDSKSSL----LLEKTIQNLSCTVLIITHQPSLM-KLADRIIVMDSG-IVKES 1312
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAvileLLRKLQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGqIVEEC 233
|
250
....*....|
gi 162312251 1313 GSFDELMNRH 1322
Cdd:TIGR02769 234 DVAQLLSFKH 243
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1098-1324 |
1.57e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 95.36 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1098 KIEFDGVSFAYPDSErnhlALNNVSLSIEAREKVAIVGISGSGKST-------LVELLRKTYPSEDIYIDGYPLTNIDTN 1170
Cdd:PRK14247 3 KIEIRDLKVSFGQVE----VLDGVNLEIPDNTITALMGPSGSGKSTllrvfnrLIELYPEARVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1171 WLLKKVAIVDQKPHLLGS-TILESLLYG--VDRDINS-------VMDALDKTYMTEVIQNLpngLDTPllefSKNFSGGQ 1240
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNlSIFENVALGlkLNRLVKSkkelqerVRWALEKAQLWDEVKDR---LDAP----AGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1241 IQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL--SCTVLIITHQPS-LMKLADRIIVMDSGIVKESGSFDE 1317
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELkkDMTIVLVTHFPQqAARISDYVAFLYKGQIVEWGPTRE 231
|
....*..
gi 162312251 1318 LMNRHTH 1324
Cdd:PRK14247 232 VFTNPRH 238
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1117-1324 |
1.87e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 96.96 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELLrkTY---PSE-DIYIDGYPLTNIDT---NWLLKKVAIVDQKPHllGS- 1188
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLL--TMietPTGgELYYQGQDLLKADPeaqKLLRQKIQIVFQNPY--GSl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1189 -------TILESLLygvdrDINSVMDALDKT-----YMTEViqnlpnGLDTpllEFSKN----FSGGQIQRLAFARALLR 1252
Cdd:PRK11308 106 nprkkvgQILEEPL-----LINTSLSAAERRekalaMMAKV------GLRP---EHYDRyphmFSGGQRQRIAIARALML 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1253 NPRLLILDECTSALDskSSL------LLEKTIQNLSCTVLIITHQPSLMK-LADRIIVMDSGIVKESGSFDELMNRHTH 1324
Cdd:PRK11308 172 DPDVVVADEPVSALD--VSVqaqvlnLMMDLQQELGLSYVFISHDLSVVEhIADEVMVMYLGRCVEKGTKEQIFNNPRH 248
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
434-648 |
1.90e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 95.08 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSrDENLFsliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYG--NIYLDDFPLE-EIDEH---V 507
Cdd:PRK11124 4 QLNGINCFYGA-HQALF---DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlNIAGNHFDFSkTPSDKairE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 508 LGSTITLVCQQ----PvifDMTIRENII--------MRNENASESDFEEVCRLALvDEFALTFDQSydtpckeasLSGGQ 575
Cdd:PRK11124 80 LRRNVGMVFQQynlwP---HLTVQQNLIeapcrvlgLSKDQALARAEKLLERLRL-KPYADRFPLH---------LSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 576 QQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRK-GKTTLVITHDMS---QINNDelVLVIDKGHLIQ 648
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEvarKTASR--VVYMENGHIVE 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1099-1320 |
1.93e-21 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 94.71 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSErnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLR--KTYPSEDIYIDGYPLTNIDTNwlLKKV 1176
Cdd:cd03296 3 IEVRNVSKRFGDFV----ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAglERPDSGTILFGGEDATDVPVQ--ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQK----PHLlgsTILESLLYGVDrdINSVMDALDKTYMTEVIQNLPN--GLDTPLLEFSKNFSGGQIQRLAFARAL 1250
Cdd:cd03296 77 GFVFQHyalfRHM---TVFDNVAFGLR--VKPRSERPPEAEIRAKVHELLKlvQLDWLADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1251 LRNPRLLILDECTSALDSKSSLLLEKTIQNL----SCTVLIITH-QPSLMKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLhdelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
961-1329 |
2.22e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 101.59 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 961 SILHKTIVNLDTIKGYSvlsffrenhknslrksWEafkrRAFWTSLGFAINNSLLYFVRALLFYCSSIFIskeFYTVEQM 1040
Cdd:PLN03232 480 GIINEILASMDTVKCYA----------------WE----KSFESRIQGIRNEELSWFRKAQLLSAFNSFI---LNSIPVV 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1041 VQVLSLATFTLL------------MASTCIMSLP--------------NVSASRI-----ATSRVLKLSS-LKPGnlhks 1088
Cdd:PLN03232 537 VTLVSFGVFVLLggdltparaftsLSLFAVLRSPlnmlpnllsqvvnaNVSLQRIeelllSEERILAQNPpLQPG----- 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1089 gylkfplVGKIEFDGVSFAYpDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE-LLRKTYPSEDIYIDgypltni 1167
Cdd:PLN03232 612 -------APAISIKNGYFSW-DSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVV------- 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1168 dtnwLLKKVAIVDQKPHLLGSTILESLLYGVDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFA 1247
Cdd:PLN03232 677 ----IRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMA 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1248 RALLRNPRLLILDECTSALDSKssllLEKTIQNlSC--------TVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELM 1319
Cdd:PLN03232 753 RAVYSNSDIYIFDDPLSALDAH----VAHQVFD-SCmkdelkgkTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
410
....*....|
gi 162312251 1320 NRHTHFWKLI 1329
Cdd:PLN03232 828 KSGSLFKKLM 837
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
434-649 |
2.23e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 97.18 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGST-- 511
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 512 -ITLVCQQpviFDM----TIRENII--MRNENASESDFEEvcR----LALVDefaLTfDQSYDTPckeASLSGGQQQRIA 580
Cdd:PRK11153 83 qIGMIFQH---FNLlssrTVFDNVAlpLELAGTPKAEIKA--RvtelLELVG---LS-DKADRYP---AQLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 581 LARALLRDTEILILDEPTSALDPITKNLVMDAIRA-HRK-GKTTLVITHDMSQINN--DElVLVIDKGHLIQR 649
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDiNRElGLTIVLITHEMDVVKRicDR-VAVIDAGRLVEQ 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1099-1320 |
2.25e-21 |
|
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: 94.04 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSErnhlALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRKTYPSedIYIDGYPLTNIDTNWLLK 1174
Cdd:cd03224 1 LEVENLNAGYGKSQ----ILFGVSLTVPEGEIVALLGRNGAGKTTLLKtimgLLPPRSGS--IRFDGRDITGLPPHERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 K-VAIVDQKPHLLGS-TILESLLYGV-DRDINSVMDALDktymtEVIQNLPNgldtpLLEFSK----NFSGGQIQRLAFA 1247
Cdd:cd03224 75 AgIGYVPEGRRIFPElTVEENLLLGAyARRRAKRKARLE-----RVYELFPR-----LKERRKqlagTLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 1248 RALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSL-MKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRdegVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
437-693 |
2.39e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.57 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 437 NVSFAYPSRDENlFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVC 516
Cdd:PRK13650 9 NLTFKYKEDQEK-YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 517 QQP--VIFDMTIRENIIMRNENASESDFEEVCRlalVDEfALTFDQSYDTPCKE-ASLSGGQQQRIALARALLRDTEILI 593
Cdd:PRK13650 88 QNPdnQFVGATVEDDVAFGLENKGIPHEEMKER---VNE-ALELVGMQDFKEREpARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 594 LDEPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELVLFEDFENNVSIDE-- 669
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLLQLGLDIpf 243
|
250 260 270
....*....|....*....|....*....|
gi 162312251 670 --KVLKEEADNPFILPN----EESLLEKYW 693
Cdd:PRK13650 244 ttSLVQSLRQNGYDLPEgyltEKELEEQLW 273
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1099-1318 |
2.42e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.86 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAY-PDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRKTypSEDIYIDGYPLT----NIDT 1169
Cdd:PRK13634 3 ITFQKVEHRYqYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQhlngLLQPT--SGTVTIGERVITagkkNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1170 NWLLKKVAIVDQKP--HLLGSTILESLLYGvdrDIN---SVMDALDKT-YMTEVIqnlpnGLDTPLLEFSK-NFSGGQIQ 1242
Cdd:PRK13634 81 KPLRKKVGIVFQFPehQLFEETVEKDICFG---PMNfgvSEEDAKQKArEMIELV-----GLPEELLARSPfELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1243 RLAFARALLRNPRLLILDECTSALDSKSSL----LLEKTIQNLSCTVLIITHQpslM----KLADRIIVMDSGIVKESGS 1314
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKemmeMFYKLHKEKGLTTVLVTHS---MedaaRYADQIVVMHKGTVFLQGT 229
|
....
gi 162312251 1315 FDEL 1318
Cdd:PRK13634 230 PREI 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1102-1324 |
2.48e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.78 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1102 DGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKS-TLVELLR------KTYPSEDIYIDGYPLTNIDTNWLLK 1174
Cdd:PRK15134 9 ENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRllpsppVVYPSGDIRFHGESLLHASEQTLRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 ----KVAIVDQKP-------HLLGSTILE--SLLYGVDRDI--NSVMDALDKTYmtevIQNLPNGLDtpllEFSKNFSGG 1239
Cdd:PRK15134 89 vrgnKIAMIFQEPmvslnplHTLEKQLYEvlSLHRGMRREAarGEILNCLDRVG----IRQAAKRLT----DYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1240 QIQRLAFARALLRNPRLLILDECTSALD----SKSSLLLEKTIQNLSCTVLIITHQPSLM-KLADRIIVMDSGIVKESGS 1314
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDvsvqAQILQLLRELQQELNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNR 240
|
250
....*....|
gi 162312251 1315 FDELMNRHTH 1324
Cdd:PRK15134 241 AATLFSAPTH 250
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
434-655 |
2.54e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.86 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRD--ENLfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIylddfpleEIDEHVLGST 511
Cdd:PRK13634 4 TFQKVEHRYQYKTpfERR-ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV--------TIGERVITAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 512 ------------ITLVCQQP--VIFDMTIRENIIM--RNENASESDFEEVCR--LALV--DEFALT---FDqsydtpcke 568
Cdd:PRK13634 75 kknkklkplrkkVGIVFQFPehQLFEETVEKDICFgpMNFGVSEEDAKQKARemIELVglPEELLArspFE--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 569 asLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAI-RAHR-KGKTTLVITHDMSQINN--DELVlVIDKG 644
Cdd:PRK13634 146 --LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFyKLHKeKGLTTVLVTHSMEDAARyaDQIV-VMHKG 222
|
250
....*....|.
gi 162312251 645 HLIQRCARKEL 655
Cdd:PRK13634 223 TVFLQGTPREI 233
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
436-690 |
3.59e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.16 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYpSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLV 515
Cdd:PRK13642 8 ENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 516 CQQP--VIFDMTIRENIIMRNENASESDFEEVCRlalVDEFALTFDQsYDTPCKE-ASLSGGQQQRIALARALLRDTEIL 592
Cdd:PRK13642 87 FQNPdnQFVGATVEDDVAFGMENQGIPREEMIKR---VDEALLAVNM-LDFKTREpARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 593 ILDEPTSALDPITKNLVMDAIRAHRKGK--TTLVITHDMSQINNDELVLVIDKGHLIQRCARKElvLFEDFENNVSI--- 667
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSE--LFATSEDMVEIgld 240
|
250 260 270
....*....|....*....|....*....|
gi 162312251 668 ---DEKVLKEEADNPFILP----NEESLLE 690
Cdd:PRK13642 241 vpfSSNLMKDLRKNGFDLPekylSEDELVE 270
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
454-647 |
3.74e-21 |
|
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: 94.34 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHV---LGSTITLvcQQPVIF-DMTIREN 529
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRiarLGIARTF--QNPRLFpELTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 530 IIM-RNENASESDFEEVCRL---------------ALVDEFALTfDQSyDTPCkeASLSGGQQQRIALARALLRDTEILI 593
Cdd:COG0411 100 VLVaAHARLGRGLLAALLRLprarreereareraeELLERVGLA-DRA-DEPA--GNLSYGQQRRLEIARALATEPKLLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 594 LDEPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDMSQINN--DElVLVIDKGHLI 647
Cdd:COG0411 176 LDEPAAGLNPEETEELAELIRRLRDerGITILLIEHDMDLVMGlaDR-IVVLDFGRVI 232
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
452-658 |
3.79e-21 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 94.87 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEID---EHVLGSTITLVCQQ-PVIFD--MT 525
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDsPSAVNprMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 526 IRENII--MRN-ENASESDFEEVCrLALVDEFALTFDQSYDTPckeASLSGGQQQRIALARALLRDTEILILDEPTSALD 602
Cdd:TIGR02769 107 VRQIIGepLRHlTSLDESEQKARI-AELLDMVGLRSEDADKLP---RQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 603 PITKNLVMDAIRAHRK--GKTTLVITHDMSQINN-DELVLVIDKGHLIQRCARKELVLF 658
Cdd:TIGR02769 183 MVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSF 241
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1117-1320 |
3.82e-21 |
|
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: 94.34 E-value: 3.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYIDGYPLTNidtnwlLKKVAIVD-------QKPHLLG 1187
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYrPTSgRILFDGRDITG------LPPHRIARlgiartfQNPRLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1188 S-TILESLLYGV---------------------DRDINS-VMDALDKTymteviqnlpnGLDTPLLEFSKNFSGGQIQRL 1244
Cdd:COG0411 93 ElTVLENVLVAAharlgrgllaallrlprarreEREARErAEELLERV-----------GLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1245 AFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS----CTVLIITHQPSL-MKLADRIIVMDSGIVKESGSFDELM 1319
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdergITILLIEHDMDLvMGLADRIVVLDFGRVIAEGTPAEVR 241
|
.
gi 162312251 1320 N 1320
Cdd:COG0411 242 A 242
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
452-628 |
4.56e-21 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 97.10 E-value: 4.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVL----GSTITLVCQQpviF----D 523
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELrelrRKKMSMVFQH---FallpH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 524 MTIRENIIM-----------RNENASESdfeevcrLALV--DEFAltfdQSYdtPckeASLSGGQQQRIALARALLRDTE 590
Cdd:COG4175 120 RTVLENVAFgleiqgvpkaeRRERAREA-------LELVglAGWE----DSY--P---DELSGGMQQRVGLARALATDPD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 162312251 591 ILILDEPTSALDPItknlvmdaIRA----------HRKGKTTLVITHD 628
Cdd:COG4175 184 ILLMDEAFSALDPL--------IRRemqdellelqAKLKKTIVFITHD 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
455-657 |
4.72e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.22 E-value: 4.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 455 VSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVI-FDMTIRENIIM- 532
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQVVEMg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 533 ------RNENASESDfEEVCRLAL----VDEFAltfDQSYDtpckeaSLSGGQQQRIALARALLRDTEILILDEPTSALD 602
Cdd:PRK09536 102 rtphrsRFDTWTETD-RAAVERAMertgVAQFA---DRPVT------SLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 603 --------PITKNLVMDairahrkGKTTLVITHD--MSQINNDELVLVIDKGhlIQRCARKELVL 657
Cdd:PRK09536 172 inhqvrtlELVRRLVDD-------GKTAVAAIHDldLAARYCDELVLLADGR--VRAAGPPADVL 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
434-628 |
5.51e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.16 E-value: 5.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIdehvlGSTIT 513
Cdd:COG4525 5 TVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP-----GADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFD-MTIRENI-----------IMRNENASEsdfeevcRLALVDEFALTFDQSYdtpckeaSLSGGQQQRIAL 581
Cdd:COG4525 80 VVFQKDALLPwLNVLDNVafglrlrgvpkAERRARAEE-------LLALVGLADFARRRIW-------QLSGGMRQRVGI 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 162312251 582 ARALLRDTEILILDEPTSALDPITKN----LVMDAirAHRKGKTTLVITHD 628
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREqmqeLLLDV--WQRTGKGVFLITHS 194
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
145-628 |
5.54e-21 |
|
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: 98.72 E-value: 5.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 145 MISLIN--------FNSLLITIFgLASCVFSFGVRFLWQYL------SAIAGKRaRSLCFHVLSS---------KSSTFY 201
Cdd:COG4615 32 LIALINqalnatgaALARLLLLF-AGLLVLLLLSRLASQLLltrlgqHAVARLR-LRLSRRILAAplerlerigAARLLA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 202 SLTESksglVNSVdrciqfyekSISLPMF-HIAENLAISLSCLIISFRYSWSLTLVVLAsypIIILVVGFINSFLSSAYE 280
Cdd:COG4615 110 ALTED----VRTI---------SQAFVRLpELLQSVALVLGCLAYLAWLSPPLFLLTLV---LLGLGVAGYRLLVRRARR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 281 KDRKSSEKaasileksisaiQTVIFHSMQD-TE----------------YRYFADACSTSSKSFLRFSFLDAFQGGVSQF 343
Cdd:COG4615 174 HLRRAREA------------EDRLFKHFRAlLEgfkelklnrrrrraffDEDLQPTAERYRDLRIRADTIFALANNWGNL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 344 FLY----SVFFqglWFGNHLATTKRVnVGQVVTVFgscLSVASSLQQILPAIPDLIKGKFSSHFIKTL------CESHDP 413
Cdd:COG4615 242 LFFaligLILF---LLPALGWADPAV-LSGFVLVL---LFLRGPLSQLVGALPTLSRANVALRKIEELelalaaAEPAAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 414 IEAAKRSAAKIKSIsfergfRFDNVSFAYPSRD-ENLFSL--INVSvfIPFGELVHIIGPSGSGKSTFISLLLRYFSPTY 490
Cdd:COG4615 315 DAAAPPAPADFQTL------ELRGVTYRYPGEDgDEGFTLgpIDLT--IRRGELVFIVGGNGSGKSTLAKLLTGLYRPES 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 491 GNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDmtireNIIMRNENASESDFEEVC-RLALVDEFALTFDQSYDTpckea 569
Cdd:COG4615 387 GEILLDGQPVTADNREAYRQLFSAVFSDFHLFD-----RLLGLDGEADPARARELLeRLELDHKVSVEDGRFSTT----- 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 570 SLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNL----VMDAIRAhrKGKTTLVITHD 628
Cdd:COG4615 457 DLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVfyteLLPELKA--RGKTVIAISHD 517
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
454-715 |
6.41e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 95.26 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLgSTITLVCQ----QPvifDMTIREN 529
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR-QRVGVVPQfdnlDP---DFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 530 IIMRNENASESDFEEVCRLALVDEFAlTFDQSYDTPCKEasLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLV 609
Cdd:PRK13537 101 LLVFGRYFGLSAAAARALVPPLLEFA-KLENKADAKVGE--LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 610 MDAIRA-HRKGKTTLVITHDMSQINN--DELVlVIDKGHLIQRCARKELVlfedfENNVSIDekVLKEEADNPFILPNEE 686
Cdd:PRK13537 178 WERLRSlLARGKTILLTTHFMEEAERlcDRLC-VIEEGRKIAEGAPHALI-----ESEIGCD--VIEIYGPDPVALRDEL 249
|
250 260
....*....|....*....|....*....
gi 162312251 687 SLLEKYwinynesfSQLSRESLFTSLESP 715
Cdd:PRK13537 250 APLAER--------TEISGETLFCYVRDP 270
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
452-633 |
6.53e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.85 E-value: 6.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENII 531
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 532 ----MRNENASESDFeevcrLALVDEFAL---TFDQSYdtpckeASLSGGQQQRIALARALLRDTEILILDEPTSALDPI 604
Cdd:PRK10247 103 fpwqIRNQQPDPAIF-----LDDLERFALpdtILTKNI------AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190
....*....|....*....|....*....|...
gi 162312251 605 TKNLVMDAIraHR----KGKTTLVITHDMSQIN 633
Cdd:PRK10247 172 NKHNVNEII--HRyvreQNIAVLWVTHDKDEIN 202
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
434-647 |
7.06e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.28 E-value: 7.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPsrdENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLD-----DFP-LEEIDEHV 507
Cdd:PRK13644 3 RLENVSYSYP---DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgidtgDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 508 lgstiTLVCQQP--VIFDMTIRENIIMRNENA--SESDFEEVCRLALVdEFALTfDQSYDTPckeASLSGGQQQRIALAR 583
Cdd:PRK13644 80 -----GIVFQNPetQFVGRTVEEDLAFGPENLclPPIEIRKRVDRALA-EIGLE-KYRHRSP---KTLSGGQGQCVALAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 584 ALLRDTEILILDEPTSALDPITKNLVMDAI-RAHRKGKTTLVITHDMSQINNDELVLVIDKGHLI 647
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIkKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
454-649 |
7.17e-21 |
|
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: 92.28 E-value: 7.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDD---FPLEEIDEHVlGSTItlvcQQPVIFD-MTIREN 529
Cdd:cd03268 18 DISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksyQKNIEALRRI-GALI----EAPGFYPnLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 530 ------IIMRNENASESDFEEVcrlalvdefalTFDQSYDTPCKEASLsgGQQQRIALARALLRDTEILILDEPTSALDP 603
Cdd:cd03268 93 lrllarLLGIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSL--GMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 162312251 604 ITKNLVMDAIRAHRK-GKTTLVITHDMSQINN--DELVlVIDKGHLIQR 649
Cdd:cd03268 160 DGIKELRELILSLRDqGITVLISSHLLSEIQKvaDRIG-IINKGKLIEE 207
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
418-667 |
7.82e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.30 E-value: 7.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 418 KRSAAKIKSISFERGFRFDNVSFAYPSRDENLFSLIN-VSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLD 496
Cdd:PRK13631 7 KKKLKVPNPLSDDIILRVKNLYCVFDEKQENELVALNnISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 497 DF-------PLEEIDEHV---------LGSTITLVCQQP--VIFDMTIRENI--------IMRNENASESDFEEVcRLAL 550
Cdd:PRK13631 87 DIyigdkknNHELITNPYskkiknfkeLRRRVSMVFQFPeyQLFKDTIEKDImfgpvalgVKKSEAKKLAKFYLN-KMGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 551 VDEFaltFDQSydtpckEASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIR-AHRKGKTTLVITHDM 629
Cdd:PRK13631 166 DDSY---LERS------PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILdAKANNKTVFVITHTM 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 162312251 630 SQINN--DElVLVIDKGHLIQRCARKELVLFEDFENNVSI 667
Cdd:PRK13631 237 EHVLEvaDE-VIVMDKGKILKTGTPYEIFTDQHIINSTSI 275
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1099-1324 |
8.54e-21 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 97.83 E-value: 8.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKS----TLVELLRKT--YPSEDIYIDGYPLTNIDTNWL 1172
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPaaHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1173 LK----KVAIVDQKP-------HLLGSTILESLL--YGVDRDinsvmDALDKT--YMTEViqnlpnGLDTP---LLEFSK 1234
Cdd:COG4172 87 RRirgnRIAMIFQEPmtslnplHTIGKQIAEVLRlhRGLSGA-----AARARAleLLERV------GIPDPerrLDAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1235 NFSGGQIQRLAFARALLRNPRLLILDECTSALDSksslllekTIQ--------------NLSctVLIITHQPSLM-KLAD 1299
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDV--------TVQaqildllkdlqrelGMA--LLLITHDLGVVrRFAD 225
|
250 260
....*....|....*....|....*
gi 162312251 1300 RIIVMDSGIVKESGSFDELMNRHTH 1324
Cdd:COG4172 226 RVAVMRQGEIVEQGPTAELFAAPQH 250
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
452-643 |
8.58e-21 |
|
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: 92.91 E-value: 8.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDfplEEIDEHvlGSTITLVCQQPVIFD-MTIRENI 530
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG---KQITEP--GPDRMVVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 531 IMR----NENASESDFEEVCR--LALVdefALTFDQSYdtpcKEASLSGGQQQRIALARALLRDTEILILDEPTSALDPI 604
Cdd:TIGR01184 76 ALAvdrvLPDLSKSERRAIVEehIALV---GLTEAADK----RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 162312251 605 TK-NL---VMDAIRAHRkgKTTLVITHDMsqinnDELVLVIDK 643
Cdd:TIGR01184 149 TRgNLqeeLMQIWEEHR--VTVLMVTHDV-----DEALLLSDR 184
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1099-1307 |
8.90e-21 |
|
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: 89.82 E-value: 8.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRktypSEDIYIDGYPLTNIDTnwllkKVAI 1178
Cdd:cd03221 1 IELENLSKTYGG----KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIA----GELEPDEGIVTWGSTV-----KIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1179 VDQkphllgstilesllygvdrdinsvmdaldktymteviqnlpngldtpllefsknFSGGQIQRLAFARALLRNPRLLI 1258
Cdd:cd03221 68 FEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 162312251 1259 LDECTSALDSKSSLLLEKTIQNLSCTVLIITHQPSLM-KLADRIIVMDSG 1307
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLdQVATKIIELEDG 143
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
462-648 |
9.66e-21 |
|
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: 92.23 E-value: 9.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDfpleeidEHVLGST-----ITLVCQQPVIFD-MTIRENI----- 530
Cdd:TIGR01277 24 GEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND-------QSHTGLApyqrpVSMLFQENNLFAhLTVRQNIglglh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 531 --IMRNENASESDFEEVCRLALVDEFALTFDQsydtpckeasLSGGQQQRIALARALLRDTEILILDEPTSALDPITKN- 607
Cdd:TIGR01277 97 pgLKLNAEQQEKVVDAAQQVGIADYLDRLPEQ----------LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREe 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 162312251 608 -LVMDAIRAHRKGKTTLVITHDMSQ-INNDELVLVIDKGHLIQ 648
Cdd:TIGR01277 167 mLALVKQLCSERQRTLLMVTHHLSDaRAIASQIAVVSQGKIKV 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
436-630 |
1.10e-20 |
|
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: 94.73 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSP---TYGNIYLDDFPLEEIDEHVL---- 508
Cdd:COG0444 5 RNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELrkir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 509 GSTITLVCQQ------PVifdMTIRENI---IMRNENASESDFEEVCR--LALV-----DEFAltfdQSYdtPCkeaSLS 572
Cdd:COG0444 85 GREIQMIFQDpmtslnPV---MTVGDQIaepLRIHGGLSKAEARERAIelLERVglpdpERRL----DRY--PH---ELS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 573 GGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDMS 630
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDLG 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1099-1322 |
1.53e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.45 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYP------DSERNHL------------ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIY 1158
Cdd:COG1134 5 IEVENVSKSYRlyhepsRSLKELLlrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILePTSgRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1159 IDGYpltnidTNWLLKKVAIVDqkPHLLGS--TILESLLYGVDR-DINSVMDaldktymtEVIQ--NLPNGLDTPLlefs 1233
Cdd:COG1134 85 VNGR------VSALLELGAGFH--PELTGRenIYLNGRLLGLSRkEIDEKFD--------EIVEfaELGDFIDQPV---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1234 KNFSGGQIQRLAFARALLRNPRLLILDECTSALDS----KSSLLLEKTIQNlSCTVLIITHQPSLMK-LADRIIVMDSGI 1308
Cdd:COG1134 145 KTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLARIRELRES-GRTVIFVSHSMGAVRrLCDRAIWLEKGR 223
|
250
....*....|....
gi 162312251 1309 VKESGSFDELMNRH 1322
Cdd:COG1134 224 LVMDGDPEEVIAAY 237
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
442-628 |
1.56e-20 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 90.95 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 442 YPSRDEnlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLG--STITLVCQQP 519
Cdd:TIGR01166 1 YPGGPE---VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLErrQRVGLVFQDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 520 --VIFDMTIRENIIM--RNENASESDFEEVCRLALVdefALTFDQSYDTPCKeaSLSGGQQQRIALARALLRDTEILILD 595
Cdd:TIGR01166 78 ddQLFAADVDQDVAFgpLNLGLSEAEVERRVREALT---AVGASGLRERPTH--CLSGGEKKRVAIAGAVAMRPDVLLLD 152
|
170 180 190
....*....|....*....|....*....|....
gi 162312251 596 EPTSALDPITKNLVMDAIRAHRKGKTTLVI-THD 628
Cdd:TIGR01166 153 EPTAGLDPAGREQMLAILRRLRAEGMTVVIsTHD 186
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
454-682 |
1.81e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 95.29 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVlgSTITLVCQQPVIF-DMTIRENI-- 530
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMMFQSYALFpHMTVEQNIaf 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 531 ------IMRNENASEsdFEEVCRLALVDEFALTfdqsydtpcKEASLSGGQQQRIALARALLRDTEILILDEPTSALDpi 604
Cdd:PRK11607 115 glkqdkLPKAEIASR--VNEMLGLVHMQEFAKR---------KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD-- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 605 tKNL-------VMDAIraHRKGKTTLVITHDMSQ-INNDELVLVIDKGHLIQRCARKELV------LFEDFENNVSIDEK 670
Cdd:PRK11607 182 -KKLrdrmqleVVDIL--ERVGVTCVMVTHDQEEaMTMAGRIAIMNRGKFVQIGEPEEIYehpttrYSAEFIGSVNVFEG 258
|
250
....*....|..
gi 162312251 671 VLKEEADNPFIL 682
Cdd:PRK11607 259 VLKERQEDGLVI 270
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
452-629 |
2.66e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 91.95 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLD----------DFPLEEIDEH---VLGSTITLVCQQ 518
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvrdkDGQLKVADKNqlrLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 519 PVIFD-MTIRENII---MRNENASESDFEEVCRLALvDEFALTFDQSYDTPckeASLSGGQQQRIALARALLRDTEILIL 594
Cdd:PRK10619 101 FNLWShMTVLENVMeapIQVLGLSKQEARERAVKYL-AKVGIDERAQGKYP---VHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 162312251 595 DEPTSALDPitkNLVMDAIRAHRK----GKTTLVITHDM 629
Cdd:PRK10619 177 DEPTSALDP---ELVGEVLRIMQQlaeeGKTMVVVTHEM 212
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
103-404 |
2.73e-20 |
|
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: 93.50 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 103 LIFGTLIfTCLSAALEPLMTWTTGKVFDALSQYATSQITLGKMISL------------INFNSLLITIFGLASCVFSFGV 170
Cdd:cd18558 1 MVVGILC-AIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSGLNssagpfekleeeMTLYAYYYLIIGAIVLITAYIQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 171 RFLWQYLSAIAGKRARSLCFHVLSSKSSTFYSLTESKSGLVNSVDRCIQFYEkSISLPMFHIAENLAISLSCLIISFRYS 250
Cdd:cd18558 80 GSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINE-GIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 251 WSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRF 330
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 331 SFLDAFQGGVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTVFGSCLSVASSLQQILPAIPDLIKGKFSSHFI 404
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
462-632 |
2.99e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.86 E-value: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GElVH-IIGPSGSGKSTFISLLLRYFSPTYGNIYLDDfpleeiDEHVLGST-------ITLVCQQPVIF-DMTIRENIIM 532
Cdd:COG1129 30 GE-VHaLLGENGAGKSTLMKILSGVYQPDSGEILLDG------EPVRFRSPrdaqaagIAIIHQELNLVpNLSVAENIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 533 RNENASES--DFEEVCRLA--LVDEFALTFDQsyDTPCKEasLSGGQQQRIALARALLRDTEILILDEPTSALDPI-TKN 607
Cdd:COG1129 103 GREPRRGGliDWRAMRRRAreLLARLGLDIDP--DTPVGD--LSVAQQQLVEIARALSRDARVLILDEPTASLTEReVER 178
|
170 180
....*....|....*....|....*..
gi 162312251 608 L--VMDAIRAhrKGKTTLVITHDMSQI 632
Cdd:COG1129 179 LfrIIRRLKA--QGVAIIYISHRLDEV 203
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1099-1321 |
3.74e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.11 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYIDGYPLTNIDTNWLLKKV 1176
Cdd:PRK13647 5 IEVEDLHFRYKDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYlPQRgRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKP--HLLGSTILESLLYG-----VDRD--INSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLAFA 1247
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDDVAFGpvnmgLDKDevERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1248 RALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSL-MKLADRIIVMDSGIVKESGSFDELMNR 1321
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHnqgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
436-629 |
3.74e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.11 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYPSRDEnlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLV 515
Cdd:PRK13647 8 EDLHFRYKDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 516 CQQP--VIFDMTIRENIIM--RNENASESDFEEVCRLAL--VDEFALTFDQSYdtpckeaSLSGGQQQRIALARALLRDT 589
Cdd:PRK13647 85 FQDPddQVFSSTVWDDVAFgpVNMGLDKDEVERRVEEALkaVRMWDFRDKPPY-------HLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 162312251 590 EILILDEPTSALDPITKNLVMDAI-RAHRKGKTTLVITHDM 629
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDV 198
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1118-1311 |
4.15e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 91.67 E-value: 4.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELL----RKTypSEDIYIDGYPLTNIDTNW---LLKKVAIVDQKP------- 1183
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLvgleSPS--QGNVSWRGEPLAKLNRAQrkaFRRDIQMVFQDSisavnpr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1184 HLLGSTILESL--LYGVDRD-----INSVMDALDKTymTEVIQNLPNGLdtpllefsknfSGGQIQRLAFARALLRNPRL 1256
Cdd:PRK10419 106 KTVREIIREPLrhLLSLDKAerlarASEMLRAVDLD--DSVLDKRPPQL-----------SGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 1257 LILDECTSALDSKSSL----LLEKTIQNLSCTVLIITHQPSLM-KLADRIIVMDSG-IVKE 1311
Cdd:PRK10419 173 LILDEAVSNLDLVLQAgvirLLKKLQQQFGTACLFITHDLRLVeRFCQRVMVMDNGqIVET 233
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1100-1320 |
4.72e-20 |
|
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: 90.81 E-value: 4.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1100 EFDGVSFAYPDSErnhlALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRKTypSEDIYIDGYPLTNIDTNWLLKK 1175
Cdd:COG0410 5 EVENLHAGYGGIH----VLHGVSLEVEEGEIVALLGRNGAGKTTLLKaisgLLPPR--SGSIRFDGEDITGLPPHRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1176 -VAIVDQK----PHLlgsTILESLLYG--VDRDINSVMDALDktymtEVIQNLPNgldtpLLEFSKNF----SGGQIQRL 1244
Cdd:COG0410 79 gIGYVPEGrrifPSL---TVEENLLLGayARRDRAEVRADLE-----RVYELFPR-----LKERRRQRagtlSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1245 AFARALLRNPRLLILDECTSALdskSSLLLE------KTIQNLSCTVLIITHQPSL-MKLADRIIVMDSGIVKESGSFDE 1317
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGL---APLIVEeifeiiRRLNREGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAE 222
|
...
gi 162312251 1318 LMN 1320
Cdd:COG0410 223 LLA 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
434-648 |
5.12e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 97.12 E-value: 5.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYpsRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:PLN03130 1239 KFEDVVLRY--RPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFDMTIRENIIMRNENaSESDFEEVCRLALVDEFALTFDQSYDTPCKEA--SLSGGQQQRIALARALLRDTEI 591
Cdd:PLN03130 1317 IIPQAPVLFSGTVRFNLDPFNEH-NDADLWESLERAHLKDVIRRNSLGLDAEVSEAgeNFSVGQRQLLSLARALLRRSKI 1395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 592 LILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQ 648
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVE 1452
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
454-632 |
5.37e-20 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 90.15 E-value: 5.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTItlvcQQPVIF-DMTIRENIIM 532
Cdd:TIGR03740 18 NISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHKIGSLI----ESPPLYeNLTARENLKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 533 R--NENASESDFEEVcrLALVDefaLTfdqsyDTPCKEAS-LSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLV 609
Cdd:TIGR03740 94 HttLLGLPDSRIDEV--LNIVD---LT-----NTGKKKAKqFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQEL 163
|
170 180
....*....|....*....|....
gi 162312251 610 MDAIRAHRKGKTTLVI-THDMSQI 632
Cdd:TIGR03740 164 RELIRSFPEQGITVILsSHILSEV 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1066-1317 |
5.80e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.13 E-value: 5.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1066 ASRI--ATSRVLKLSSLKPGNL-HKSGYLKF-----PLVGK--IEFDGVSFAYPDsernHLALNNVSLSIEAREKVAIVG 1135
Cdd:COG0488 273 ARKAkqAQSRIKALEKLEREEPpRRDKTVEIrfpppERLGKkvLELEGLSKSYGD----KTLLDDLSLRIDRGDRIGLIG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1136 ISGSGKSTLVELLRKTYPsediyidgyPL-------TNIdtnwllkKVAIVDQKPHLL--GSTILESLlygvdrdinsvM 1206
Cdd:COG0488 349 PNGAGKSTLLKLLAGELE---------PDsgtvklgETV-------KIGYFDQHQEELdpDKTVLDEL-----------R 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1207 DALDKTYMTEVIQnlpngldtpLLE---FS--------KNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLE 1275
Cdd:COG0488 402 DGAPGGTEQEVRG---------YLGrflFSgddafkpvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 162312251 1276 KTIQNLSCTVLIITHQPSLM-KLADRIIVMDSGIVKE-SGSFDE 1317
Cdd:COG0488 473 EALDDFPGTVLLVSHDRYFLdRVATRILEFEDGGVREyPGGYDD 516
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1099-1313 |
8.36e-20 |
|
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: 89.47 E-value: 8.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYpdserNHLALNnVSLSIEAREKVAIVGISGSGKSTLVELLR--KTYPSEDIYIDGYPLTNIDTNwlLKKV 1176
Cdd:cd03298 1 VRLDKIRFSY-----GEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAgfETPQSGRVLINGVDVTAAPPA--DRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQK----PHLlgsTILESLlyGVDRDINSVMDALDKTYMTEVIQNLpnGLDTPLLEFSKNFSGGQIQRLAFARALLR 1252
Cdd:cd03298 73 SMLFQEnnlfAHL---TVEQNV--GLGLSPGLKLTAEDRQAIEVALARV--GLAGLEKRLPGELSGGERQRVALARVLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 1253 NPRLLILDECTSALD----SKSSLLLEKTIQNLSCTVLIITHQPS-LMKLADRIIVMDSGIVKESG 1313
Cdd:cd03298 146 DKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1095-1319 |
8.98e-20 |
|
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: 90.35 E-value: 8.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1095 LVGKIEFDGVSFAYPDSERNhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSED--IYIDGYPLTNIDTNWL 1172
Cdd:cd03288 16 LGGEIKIHDLCVRYENNLKP--VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDgkIVIDGIDISKLPLHTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1173 LKKVAIVDQKPHLLGSTILESLLYGVDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLR 1252
Cdd:cd03288 94 RSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1253 NPRLLILDECTSALDSKSSLLLEKTIQNLSC--TVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELM 1319
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFAdrTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
454-648 |
9.36e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 93.09 E-value: 9.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLD-----DFPLEeiDEHVlgstiTLVCQQPVIF-DMTIR 527
Cdd:PRK09452 32 NLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgqditHVPAE--NRHV-----NTVFQSYALFpHMTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 528 ENII--MRNENASESDFEEVCRLAL----VDEFAltfdqsydtPCKEASLSGGQQQRIALARALLRDTEILILDEPTSAL 601
Cdd:PRK09452 105 ENVAfgLRMQKTPAAEITPRVMEALrmvqLEEFA---------QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 602 D-PITKNLVMDAIRAHRK-GKTTLVITHD------MSqinnDELVlVIDKGHLIQ 648
Cdd:PRK09452 176 DyKLRKQMQNELKALQRKlGITFVFVTHDqeealtMS----DRIV-VMRDGRIEQ 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1099-1307 |
1.11e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.04 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAY-PDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRKTypSEDIYIDGYPLT----NIDT 1169
Cdd:PRK13641 3 IKFENVDYIYsPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQhfnaLLKPS--SGTITIAGYHITpetgNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1170 NWLLKKVAIVDQKP--HLLGSTILESLLYGVDRDINSVMDALDKT--YMTEViqnlpnGLDTPLLEFSK-NFSGGQIQRL 1244
Cdd:PRK13641 81 KKLRKKVSLVFQFPeaQLFENTVLKDVEFGPKNFGFSEDEAKEKAlkWLKKV------GLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 1245 AFARALLRNPRLLILDECTSALDSKSS---LLLEKTIQNLSCTVLIITHQ-PSLMKLADRIIVMDSG 1307
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRkemMQLFKDYQKAGHTVILVTHNmDDVAEYADDVLVLEHG 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1099-1314 |
1.15e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.18 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLR-KTYPSEDIY-IDGYPLTNIDTNWL--LK 1174
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGcLDKPTSGTYrVAGQDVATLDADALaqLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 K--VAIVDQKPHLLgstilESLLYGVDRDINSVMDALDKTYMTEVIQNLPN--GLDTPLLEFSKNFSGGQIQRLAFARAL 1250
Cdd:PRK10535 85 RehFGFIFQRYHLL-----SHLTAAQNVEVPAVYAGLERKQRLLRAQELLQrlGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1251 LRNPRLLILDECTSALDSKSS---LLLEKTIQNLSCTVLIITHQPSLMKLADRII-VMDSGIVKESGS 1314
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGeevMAILHQLRDRGHTVIIVTHDPQVAAQAERVIeIRDGEIVRNPPA 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1099-1320 |
1.15e-19 |
|
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: 90.14 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKSTLVELL----RKTYpSEDIYIDGYPLTNIDTNWLLK 1174
Cdd:COG1119 4 LELRNVTVRRGG----KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItgdlPPTY-GNDVRLFGERRGGEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVD---QKPHLLGSTILE---SLLYGV--------DRDINSVMDALDKTYMTEVIqnlpnglDTPLLEFSKnfsgGQ 1240
Cdd:COG1119 79 RIGLVSpalQLRFPRDETVLDvvlSGFFDSiglyreptDEQRERARELLELLGLAHLA-------DRPFGTLSQ----GE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1241 IQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL----SCTVLIITHQ----PSLMklaDRIIVMDSGIVKES 1312
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaegAPTLVLVTHHveeiPPGI---THVLLLKDGRVVAA 224
|
....*...
gi 162312251 1313 GSFDELMN 1320
Cdd:COG1119 225 GPKEEVLT 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1118-1324 |
1.18e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 89.81 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTL---VELLRKtyPSE------DIYIDG-YPLTNIDT--NWLLKKVAIVDQK--- 1182
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLEQ--PEAgtirvgDITIDTaRSLSQQKGliRQLRQHVGFVFQNfnl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1183 -PHllgSTILESLLYG---VDRDINSVMDALDKTYMTEViqnlpnGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLI 1258
Cdd:PRK11264 97 fPH---RTVLENIIEGpviVKGEPKEEATARARELLAKV------GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1259 LDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSLMK-LADRIIVMDSGIVKESGSFDELMNRHTH 1324
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAqekRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1090-1322 |
1.27e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.45 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1090 YLKFPLVGKI--EFDGVSFAYPDSERNHL-ALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRKTYPS---EDIYI 1159
Cdd:PRK13631 11 KVPNPLSDDIilRVKNLYCVFDEKQENELvALNNISYTFEKNKIYFIIGNSGSGKSTLVThfngLIKSKYGTiqvGDIYI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1160 DGYPLTNIDTNW-----------LLKKVAIVDQKP--HLLGSTILESLLYGVDRDINSVMDA--LDKTYMTEViqnlpnG 1224
Cdd:PRK13631 91 GDKKNNHELITNpyskkiknfkeLRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAkkLAKFYLNKM------G 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1225 LDTPLLEFSK-NFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSS-----LLLEKTIQNLscTVLIITHQ-PSLMKL 1297
Cdd:PRK13631 165 LDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEhemmqLILDAKANNK--TVFVITHTmEHVLEV 242
|
250 260
....*....|....*....|....*.
gi 162312251 1298 ADRIIVMDSG-IVKESGSFDELMNRH 1322
Cdd:PRK13631 243 ADEVIVMDKGkILKTGTPYEIFTDQH 268
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
452-660 |
1.40e-19 |
|
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: 89.97 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENII 531
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 532 MRNEnASESDFEEVCRLALVDEFALTFDQSYDTPCKEA--SLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLV 609
Cdd:cd03288 117 PECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGgeNFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENIL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 162312251 610 MDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELVLFED 660
Cdd:cd03288 196 QKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQED 246
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
454-655 |
1.55e-19 |
|
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: 88.97 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFP-LEEIDEhvLGSTITLVCQQPVIFD-MTIRENII 531
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvVREPRE--VRRRIGIVFQDLSVDDeLTGWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 532 M-------RNENASESdFEEVCRLALVDEFAltfdqsyDTPCKeaSLSGGQQQRIALARALLRDTEILILDEPTSALDPI 604
Cdd:cd03265 96 IharlygvPGAERRER-IDELLDFVGLLEAA-------DRLVK--TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 605 TKNLVMDAIRA--HRKGKTTLVITHDMSQInnDEL---VLVIDKGHLIQRCARKEL 655
Cdd:cd03265 166 TRAHVWEYIEKlkEEFGMTILLTTHYMEEA--EQLcdrVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1099-1318 |
1.61e-19 |
|
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: 88.58 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSErnhlALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRKTypSEDIYIDGYPLTNiDTNWLLK 1174
Cdd:cd03265 1 IEVENLVKKYGDFE----AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKmlttLLKPT--SGRATVAGHDVVR-EPREVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQKPHLLGS-TILESL-----LYGVDRDInsvmdaldktyMTEVIQNLPNGLDtpLLEFS----KNFSGGQIQRL 1244
Cdd:cd03265 74 RIGIVFQDLSVDDElTGWENLyiharLYGVPGAE-----------RRERIDELLDFVG--LLEAAdrlvKTYSGGMRRRL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1245 AFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL----SCTVLIITHqpsLM----KLADRIIVMDSGIVKESGSFD 1316
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkeefGMTILLTTH---YMeeaeQLCDRVAIIDHGRIIAEGTPE 217
|
..
gi 162312251 1317 EL 1318
Cdd:cd03265 218 EL 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1099-1314 |
1.87e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.05 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERnhlALNNVSLSIEAREKVAIVGISGSGKSTLV----ELLRktyPSEDIYIdgypLTNIDT----- 1169
Cdd:PRK13644 2 IRLENVSYSYPDGTP---ALENINLVIKKGEYIGIIGKNGSGKSTLAlhlnGLLR---PQKGKVL----VSGIDTgdfsk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1170 -NWLLKKVAIVDQKP--HLLGSTILESLLYGVDR------DINSVMD-ALDKTYMTEVIQNLPngldtpllefsKNFSGG 1239
Cdd:PRK13644 72 lQGIRKLVGIVFQNPetQFVGRTVEEDLAFGPENlclppiEIRKRVDrALAEIGLEKYRHRSP-----------KTLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1240 QIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL---SCTVLIITHQPSLMKLADRIIVMDSGIVKESGS 1314
Cdd:PRK13644 141 QGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhekGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
454-647 |
1.91e-19 |
|
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: 86.71 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLE---EIDEHVLGstITLVCQqpvifdmtireni 530
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfasPRDARRAG--IAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 531 imrnenasesdfeevcrlalvdefaltfdqsydtpckeasLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVM 610
Cdd:cd03216 83 ----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 162312251 611 DAIRA-HRKGKTTLVITHDMSQINN--DElVLVIDKGHLI 647
Cdd:cd03216 123 KVIRRlRAQGVAVIFISHRLDEVFEiaDR-VTVLRDGRVV 161
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
455-649 |
2.35e-19 |
|
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: 88.19 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 455 VSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDF-----PLEeidehvLGSTITLVCQQPVIFD-MTIRE 528
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFdvvkePAE------ARRRLGFVSDSTGLYDrLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 529 NII-------MRNENAsesdfeevcrLALVDEFALTFDQSYDTPCKEASLSGGQQQRIALARALLRDTEILILDEPTSAL 601
Cdd:cd03266 98 NLEyfaglygLKGDEL----------TARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 162312251 602 DPITKNLVMDAIRAHRK-GKTTLVITHDMSQINN--DELVlVIDKGHLIQR 649
Cdd:cd03266 168 DVMATRALREFIRQLRAlGKCILFSTHIMQEVERlcDRVV-VLHRGRVVYE 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1099-1311 |
2.79e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 89.37 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDserNHLALNNVSLSIEAREKVAIVGISGSGKSTLV----ELLRKTypSEDIYIDGYPLtNIDTNWLL- 1173
Cdd:PRK13639 2 LETRDLKYSYPD---GTEALKGINFKAEKGEMVALLGPNGAGKSTLFlhfnGILKPT--SGEVLIKGEPI-KYDKKSLLe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1174 --KKVAIVDQKP--HLLGSTILESLLYG-------VDRDINSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQ 1242
Cdd:PRK13639 76 vrKTVGIVFQNPddQLFAPTVEEDVAFGplnlglsKEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1243 RLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSLMKL-ADRIIVMDSG-IVKE 1311
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNkegITIIISTHDVDLVPVyADKVYVMSDGkIIKE 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
449-627 |
3.07e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.62 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 449 LFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDfplEEIDEHVLGSTITLVCQQ----PVifdM 524
Cdd:PRK13539 17 LFS--GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLGHRnamkPA---L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 525 TIRENIIM--RNENASESDFEE-VCRLALVDEFALTFdqsydtpckeASLSGGQQQRIALARALLRDTEILILDEPTSAL 601
Cdd:PRK13539 89 TVAENLEFwaAFLGGEELDIAAaLEAVGLAPLAHLPF----------GYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*..
gi 162312251 602 DPITKNLVMDAIRAHRKGKTTLVI-TH 627
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGGIVIAaTH 185
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
452-655 |
3.47e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.38 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDD--------FPLEEIDEhvLGSTITLVCQQPVIFD 523
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDvllggrsiFNYRDVLE--FRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 524 MTIRENI---IMRNENASESDFEEVC--RLALVDEFALTFDQSYDTPCKeasLSGGQQQRIALARALLRDTEILILDEPT 598
Cdd:PRK14271 115 MSIMDNVlagVRAHKLVPRKEFRGVAqaRLTEVGLWDAVKDRLSDSPFR---LSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 599 SALDPITKNLVMDAIRAHRKGKTTLVITHDMSQIN--NDELVLVIDkGHLIQRCARKEL 655
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAAriSDRAALFFD-GRLVEEGPTEQL 249
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1116-1320 |
3.82e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 91.63 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1116 LALNNVSLSIEAREKVAIVGISGSGKSTLVELL-RKTYPSE-DIYIDGYPLTNIDTNWLL----KKVAIVDQK----PHL 1185
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLnRLIEPTRgQVLIDGVDIAKISDAELRevrrKKIAMVFQSfalmPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1186 lgsTILESLLYGVDrdINSVMDALDKTYMTEVIQNLpnGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSA 1265
Cdd:PRK10070 122 ---TVLDNTAFGME--LAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1266 LDSKSSLLLEKTIQNLSC----TVLIITHQ-PSLMKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAkhqrTIVFISHDlDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
454-647 |
3.95e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.15 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDF-PLEEIDEHVlgSTITLVC---QQpVIFDMTIREN 529
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvPFKRRKEFA--RRIGVVFgqrSQ-LWWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 530 IIMrneNA-----SESDFEEvcRLalvDEFALTFDQS--YDTPCKEASLsgGQQQRIALARALLRDTEILILDEPTSALD 602
Cdd:COG4586 117 FRL---LKaiyriPDAEYKK--RL---DELVELLDLGelLDTPVRQLSL--GQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 162312251 603 PITKNLVMDAIRA-HRKGKTTLVIT-HDMSQInnDEL---VLVIDKGHLI 647
Cdd:COG4586 187 VVSKEAIREFLKEyNRERGTTILLTsHDMDDI--EALcdrVIVIDHGRII 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1105-1313 |
4.37e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 87.59 E-value: 4.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1105 SFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDGypltniDTNWLLKKVAIVDqk 1182
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpdSGTVTVRG------RVSSLLGLGGGFN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1183 PHLLG--STILESLLYGVDRD-INSVMDaldktymtEVIQ--NLPNGLDTPLlefsKNFSGGQIQRLAFARALLRNPRLL 1257
Cdd:cd03220 97 PELTGreNIYLNGRLLGLSRKeIDEKID--------EIIEfsELGDFIDLPV----KTYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 1258 ILDECTSALDS----KSSLLLEKTIQNLScTVLIITHQPSLMK-LADRIIVMDSGIVKESG 1313
Cdd:cd03220 165 LIDEVLAVGDAafqeKCQRRLRELLKQGK-TVILVSHDPSSIKrLCDRALVLEKGKIRFDG 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
415-660 |
4.87e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 4.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 415 EAAKRSAAKIKsISFERG-------FRFDNVSFAYPsrDENLFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFS 487
Cdd:COG0488 292 EEPPRRDKTVE-IRFPPPerlgkkvLELEGLSKSYG--DKTLLD--DLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 488 PTYGNIylddfpleeidehVLGSTITL--VCQQPVIFD--MTIRENIIMRNENASESDfeevcRLALVDEFALTFDQSYd 563
Cdd:COG0488 367 PDSGTV-------------KLGETVKIgyFDQHQEELDpdKTVLDELRDGAPGGTEQE-----VRGYLGRFLFSGDDAF- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 564 TPCKeaSLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHrKGkTTLVITHDMsqinndelvlvidk 643
Cdd:COG0488 428 KPVG--VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHDR-------------- 489
|
250
....*....|....*..
gi 162312251 644 gHLIQRCARKeLVLFED 660
Cdd:COG0488 490 -YFLDRVATR-ILEFED 504
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
454-625 |
5.10e-19 |
|
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: 87.73 E-value: 5.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTF---ISLLLRyfsPTYGNIYLDDfplEEID----EHVLGSTITLVCQQPVIF-DMT 525
Cdd:COG0410 21 GVSLEVEEGEIVALLGRNGAGKTTLlkaISGLLP---PRSGSIRFDG---EDITglppHRIARLGIGYVPEGRRIFpSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 526 IRENIIM-----RNENASESDFEEVC----RLAlvdEFAltfDQsydtpcKEASLSGGQQQRIALARALLRDTEILILDE 596
Cdd:COG0410 95 VEENLLLgayarRDRAEVRADLERVYelfpRLK---ERR---RQ------RAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190
....*....|....*....|....*....|
gi 162312251 597 PTSALDPITKNLVMDAIRA-HRKGKTTLVI 625
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRlNREGVTILLV 192
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1114-1320 |
5.60e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.08 E-value: 5.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1114 NHLALNNVSLSIEAREKVAIVGISGSGKSTL-VELLRKTYPSEDIYIDGYPLTNIDTNWLL---KKVAIVDQKPHL---- 1185
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLINSQGEIWFDGQPLHNLNRRQLLpvrHRIQVVFQDPNSslnp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1186 ---LGSTILESL------LYGVDRDiNSVMDAldktyMTEViqnlpnGLDTPLLE-FSKNFSGGQIQRLAFARALLRNPR 1255
Cdd:PRK15134 378 rlnVLQIIEEGLrvhqptLSAAQRE-QQVIAV-----MEEV------GLDPETRHrYPAEFSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 1256 LLILDECTSALD---SKSSLLLEKTIQN---LSctVLIITHQPSLMK-LADRIIVMDSGIVKESGSFDELMN 1320
Cdd:PRK15134 446 LIILDEPTSSLDktvQAQILALLKSLQQkhqLA--YLFISHDLHVVRaLCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
414-644 |
6.54e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.18 E-value: 6.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 414 IEAAKRSAAKIKSISFERG--FRFDNVSFAYPSrDENLFSLINVSvfIPFGELVHIIGPSGSGKSTfislLLR------- 484
Cdd:COG4178 342 LEAADALPEAASRIETSEDgaLALEDLTLRTPD-GRPLLEDLSLS--LKPGERLLITGPSGSGKST----LLRaiaglwp 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 485 YFSptyGNIYLDDfpleeiDEHVLgstitLVCQQPVIFDMTIRENII--MRNENASESDFEEVCRLALVDEFALTFDQSY 562
Cdd:COG4178 415 YGS---GRIARPA------GARVL-----FLPQRPYLPLGTLREALLypATAEAFSDAELREALEAVGLGHLAERLDEEA 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 563 DTpckEASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVID 642
Cdd:COG4178 481 DW---DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELT 557
|
..
gi 162312251 643 KG 644
Cdd:COG4178 558 GD 559
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
462-640 |
7.04e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 87.33 E-value: 7.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDfpleeiDEHvlgsTITLVCQQPV--IFD-------MTIRENIIM 532
Cdd:PRK10771 25 GERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG------QDH----TTTPPSRRPVsmLFQennlfshLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 533 RNENASESDFEEVCRL-ALVDEFALTfDQSYDTPckeASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKN---- 607
Cdd:PRK10771 95 GLNPGLKLNAAQREKLhAIARQMGIE-DLLARLP---GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQemlt 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 162312251 608 LVMDAIRahRKGKTTLVITH---DMSQINNDELVLV 640
Cdd:PRK10771 171 LVSQVCQ--ERQLTLLMVSHsleDAARIAPRSLVVA 204
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1095-1299 |
7.47e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 87.78 E-value: 7.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1095 LVGKIEFDGVSFAYpDSERnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE-DIYIDG---------YPl 1164
Cdd:PRK14258 4 LIPAIKVNNLSFYY-DTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsEVRVEGrveffnqniYE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1165 TNIDTNWLLKKVAIVDQKPHLLGSTILESLLYGVD-------RDINSVMDALDKTymTEVIQNLPNGLDTPLLEFSknfs 1237
Cdd:PRK14258 79 RRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrpkLEIDDIVESALKD--ADLWDEIKHKIHKSALDLS---- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 1238 GGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL----SCTVLIITHQ-PSLMKLAD 1299
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHNlHQVSRLSD 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
450-647 |
8.10e-19 |
|
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: 89.77 E-value: 8.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 450 FSLiNVSVFIPFGELVHIIGPSGSGKSTFISL---LLRyfsPTYGNIYLDDFPLEEIDEHV--------LGstitLVCQQ 518
Cdd:COG4148 14 FTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLQDSARGIflpphrrrIG----YVFQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 519 PVIFD-MTIRENII--MRNENASES--DFEEVCRL----ALVDEFAltfdqsydtpckeASLSGGQQQRIALARALLRDT 589
Cdd:COG4148 86 ARLFPhLSVRGNLLygRKRAPRAERriSFDEVVELlgigHLLDRRP-------------ATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 590 EILILDEPTSALDPITKNLVMDAI-RAHRKGKT-TLVITHDMsqinnDEL------VLVIDKGHLI 647
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLeRLRDELDIpILYVSHSL-----DEVarladhVVLLEQGRVV 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1099-1323 |
1.04e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.99 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPdserNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLR--KTYPSEDIYIDGYPL---TNIDTN--- 1170
Cdd:PRK11124 3 IQLNGINCFYG----AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNllEMPRSGTLNIAGNHFdfsKTPSDKair 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1171 WLLKKVAIVDQK----PHLlgsTILESLL------YGVDRD--INSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSG 1238
Cdd:PRK11124 79 ELRRNVGMVFQQynlwPHL---TVQQNLIeapcrvLGLSKDqaLARAEKLLERLRLKPYADRFPLHL-----------SG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1239 GQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSLM-KLADRIIVMDSGIVKESGS 1314
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAetgITQVIVTHEVEVArKTASRVVYMENGHIVEQGD 224
|
....*....
gi 162312251 1315 FDELMNRHT 1323
Cdd:PRK11124 225 ASCFTQPQT 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
970-1329 |
1.08e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 92.88 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 970 LDTIKGYSVLSFFRENHKNsLRK---SWeaFKRRAFWTSLGFAINNSLLYFVRALLFYCSSIF-----ISKEFyTVEQMV 1041
Cdd:PLN03130 489 MDTVKCYAWENSFQSKVQT-VRDdelSW--FRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLggdltPARAF-TSLSLF 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1042 QVLSlatFTLLMASTCIMSL--PNVSASRI-----ATSRVLKLS-SLKPGnlhksgylkfplVGKIEFDGVSFAYpDSER 1113
Cdd:PLN03130 565 AVLR---FPLFMLPNLITQAvnANVSLKRLeelllAEERVLLPNpPLEPG------------LPAISIKNGYFSW-DSKA 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1114 NHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPsediyidgyPLTniDTNWLLK-KVAIVDQKPHLLGSTILE 1192
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELP---------PRS--DASVVIRgTVAYVPQVSWIFNATVRD 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1193 SLLYGVDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSK-SS 1271
Cdd:PLN03130 698 NILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHvGR 777
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1272 LLLEKTIQN--LSCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKLI 1329
Cdd:PLN03130 778 QVFDKCIKDelRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLM 837
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
462-628 |
1.10e-18 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 86.72 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDfPLEEID-------------EHVLG------------STITLVC 516
Cdd:COG4778 37 GECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRH-DGGWVDlaqaspreilalrRRTIGyvsqflrviprvSALDVVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 517 qqpvifdmtirENIIMRNENASESDfEEVCRL--------ALVDEFALTFdqsydtpckeaslSGGQQQRIALARALLRD 588
Cdd:COG4778 116 -----------EPLLERGVDREEAR-ARARELlarlnlpeRLWDLPPATF-------------SGGEQQRVNIARGFIAD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 162312251 589 TEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLV-ITHD 628
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHD 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
452-647 |
1.12e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.22 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNI---YLDDFPLEEIDEhVLGSTITLVCQQPV-------- 520
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKE-KEKVLEKLVIQKTRfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 521 ----------------IFDMTIRENIIM--RNENASESDFEEVCR--LALVDefaltFDQSY--DTPckeASLSGGQQQR 578
Cdd:PRK13651 102 eirrrvgvvfqfaeyqLFEQTIEKDIIFgpVSMGVSKEEAKKRAAkyIELVG-----LDESYlqRSP---FELSGGQKRR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 579 IALARALLRDTEILILDEPTSALDP--------ITKNLvmdairaHRKGKTTLVITHDMSQI-NNDELVLVIDKGHLI 647
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPqgvkeileIFDNL-------NKQGKTIILVTHDLDNVlEWTKRTIFFKDGKII 244
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
452-628 |
1.48e-18 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 88.94 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTfislLLRYFS----PTYGNIYLDdfpleeidehvlGSTIT----------LVCQ 517
Cdd:TIGR03265 20 LKDISLSVKKGEFVCLLGPSGCGKTT----LLRIIAglerQTAGTIYQG------------GRDITrlppqkrdygIVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 518 QPVIF-DMTIRENIIM----RNENASESDFEEVCRLALVDefaLTfDQSYDTPckeASLSGGQQQRIALARALLRDTEIL 592
Cdd:TIGR03265 84 SYALFpNLTVADNIAYglknRGMGRAEVAERVAELLDLVG---LP-GSERKYP---GQLSGGQQQRVALARALATSPGLL 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 162312251 593 ILDEPTSALDPITKNLVMDAIRA--HRKGKTTLVITHD 628
Cdd:TIGR03265 157 LLDEPLSALDARVREHLRTEIRQlqRRLGVTTIMVTHD 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
454-683 |
1.79e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.96 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVI-FDMTIREnIIM 532
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQE-LVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 533 RNENASESDFEevcRLALVDEFALT-----------FDQSYDTpckeasLSGGQQQRIALARALLRDTEILILDEPTSAL 601
Cdd:PRK10253 104 RGRYPHQPLFT---RWRKEDEEAVTkamqatgithlADQSVDT------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 602 DpITKNLVMDAIRAH---RKGKTTLVITHDMSQINNDELVLV-IDKGHLIQRCARKELVLFEDFENNVSIDEKVLKEE-A 676
Cdd:PRK10253 175 D-ISHQIDLLELLSElnrEKGYTLAAVLHDLNQACRYASHLIaLREGKIVAQGAPKEIVTAELIERIYGLRCMIIDDPvA 253
|
....*..
gi 162312251 677 DNPFILP 683
Cdd:PRK10253 254 GTPLVVP 260
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
104-387 |
1.83e-18 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 87.61 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 104 IFGTLIFTCLSAALEPLMTWTTGKVFDalsqyatsQITLGKMISLINFNSLLITIFGLASCVFSFGVRFLWQYLSAIAGK 183
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLID--------DVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 184 RARSLCFHVLSSKSSTFYSltESKSG-----LVNSVDRCIQFyeksISLPMFHIAENLAISLSCLIISFRYSWSLTLVVL 258
Cdd:cd07346 73 DLRRDLFRHLQRLSLSFFD--RNRTGdlmsrLTSDVDAVQNL----VSSGLLQLLSDVLTLIGALVILFYLNWKLTLVAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 259 ASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSFLDAFQG 338
Cdd:cd07346 147 LLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFS 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 162312251 339 GVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTVFGSCLSVASSLQQI 387
Cdd:cd07346 227 PLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRL 275
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1117-1318 |
2.62e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 88.74 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRK-TYPSE-DIYIDGYPLTNI-----DTNWLLKKVAIVdqkPHLlgsT 1189
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPTAgQIMLDGVDLSHVppyqrPINMMFQSYALF---PHM---T 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1190 ILESLLYGVDRD------INS-VMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLAFARALLRNPRLLILDEC 1262
Cdd:PRK11607 108 VEQNIAFGLKQDklpkaeIASrVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 1263 TSALDSK--SSLLLEKT--IQNLSCTVLIITH-QPSLMKLADRIIVMDSGIVKESGSFDEL 1318
Cdd:PRK11607 177 MGALDKKlrDRMQLEVVdiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
452-655 |
2.76e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.12 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLR----YFSP-TYGNIYLDDFPLEEIDEHVLGSTITLVCQQP-VIFDMT 525
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEArVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 526 IRENIIM---RNENA-SESDFEEVCRLALvdEFALTFDQ---SYDTPCkeASLSGGQQQRIALARALLRDTEILILDEPT 598
Cdd:PRK14247 99 IFENVALglkLNRLVkSKKELQERVRWAL--EKAQLWDEvkdRLDAPA--GKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 599 SALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINN-DELVLVIDKGHLIQRCARKEL 655
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1114-1301 |
3.54e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.99 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1114 NHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRK--------------TYPSEDIYIDGypltnIDTNWLLKKVAIV 1179
Cdd:PRK14243 22 SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndlipgfrvegkvTFHGKNLYAPD-----VDPVEVRRRIGMV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1180 DQKPHLLGSTILESLLYGVDrdINSVMDALDKTYMTEVIQN-LPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLI 1258
Cdd:PRK14243 97 FQKPNPFPKSIYDNIAYGAR--INGYKGDMDELVERSLRQAaLWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 162312251 1259 LDECTSALDSKSSLLLEKTIQNL--SCTVLIITHQpslMKLADRI 1301
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELkeQYTIIIVTHN---MQQAARV 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1099-1313 |
4.05e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.30 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYpDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSED--IYIDGYPLTNIDTNWLLKKV 1176
Cdd:PRK13642 5 LEVENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEgkVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKP--HLLGSTILESLLYGVDRD-------INSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLAFA 1247
Cdd:PRK13642 84 GMVFQNPdnQFVGATVEDDVAFGMENQgipreemIKRVDEALLAVNMLDFKTREPARL-----------SGGQKQRVAVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 1248 RALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS----CTVLIITHQPSLMKLADRIIVMDSG-IVKESG 1313
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKekyqLTVLSITHDLDEAASSDRILVMKAGeIIKEAA 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1118-1307 |
4.14e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.50 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELLRK-TYPSEDIYIDGY-PLTNI--DTNWLLKKVAIVDQKphllgstiles 1193
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGlETPSAGELLAGTaPLAEAreDTRLMFQDARLLPWK----------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1194 llygvdRDINSVMDALDKTYMTEVIQNLPN-GLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSL 1272
Cdd:PRK11247 97 ------KVIDNVGLGLKGQWRDAALQALAAvGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 162312251 1273 LLEKTIQNL----SCTVLIITHQPS-LMKLADRIIVMDSG 1307
Cdd:PRK11247 171 EMQDLIESLwqqhGFTVLLVTHDVSeAVAMADRVLLIEEG 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1099-1322 |
6.46e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.93 E-value: 6.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGV--SFAypdserNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE-LLRKTYPSE-DIYIDGYPLTNIDTN---- 1170
Cdd:COG4152 2 LELKGLtkRFG------DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRiILGILAPDSgEVLWDGEPLDPEDRRrigy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1171 -----WLLKKVAIVDQkphllgstilesLLY-----GVDR-DINSVMDA-LDKtymteviQNLPNGLDTPLLEFSKnfsg 1238
Cdd:COG4152 76 lpeerGLYPKMKVGEQ------------LVYlarlkGLSKaEAKRRADEwLER-------LGLGDRANKKVEELSK---- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1239 GQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQ-PSLMKLADRIIVMDSGIVKESGS 1314
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAakgTTVIFSSHQmELVEELCDRIVIINKGRKVLSGS 212
|
....*...
gi 162312251 1315 FDELMNRH 1322
Cdd:COG4152 213 VDEIRRQF 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
427-656 |
7.13e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.83 E-value: 7.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 427 ISFERGFRFDNVSFAYPSRDENLF-SLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFP----LE 501
Cdd:PRK13645 1 FDFSKDIILDNVSYTYAKKTPFEFkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipanLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 502 EIDE-HVLGSTITLVCQQP--VIFDMTIRENIIMRNENASEsDFEEVCRLA--LVDEFALTFDQSYDTPCKeasLSGGQQ 576
Cdd:PRK13645 81 KIKEvKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGE-NKQEAYKKVpeLLKLVQLPEDYVKRSPFE---LSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 577 QRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDMSQINN--DELVL-----VIDKGHLI 647
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRiaDEVIVmhegkVISIGSPF 236
|
....*....
gi 162312251 648 QRCARKELV 656
Cdd:PRK13645 237 EIFSNQELL 245
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
437-647 |
7.43e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.40 E-value: 7.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 437 NVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIY--------LDDFPLEEID-EHV 507
Cdd:PRK10535 9 DIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRvagqdvatLDADALAQLRrEHF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 508 --------LGSTITLV--CQQPVIFDMTIRENiimRNENASESdfeeVCRLALVDEFaltfdqSYdtpcKEASLSGGQQQ 577
Cdd:PRK10535 89 gfifqryhLLSHLTAAqnVEVPAVYAGLERKQ---RLLRAQEL----LQRLGLEDRV------EY----QPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 578 RIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHR-KGKTTLVITHDMSQINNDELVLVIDKGHLI 647
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
452-646 |
8.81e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 84.73 E-value: 8.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHvlgstITLVCQ-------QPVIfdm 524
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED-----TRLMFQdarllpwKKVI--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 525 tirENIIMrnenASESDFEEVCRLALvDEFALTfDQSYDTPckeASLSGGQQQRIALARALLRDTEILILDEPTSALDPI 604
Cdd:PRK11247 100 ---DNVGL----GLKGQWRDAALQAL-AAVGLA-DRANEWP---AALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 162312251 605 TKNLVMDAI----RAHrkGKTTLVITHDMSQ-INNDELVLVIDKGHL 646
Cdd:PRK11247 168 TRIEMQDLIeslwQQH--GFTVLLVTHDVSEaVAMADRVLLIEEGKI 212
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1113-1318 |
9.39e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.95 E-value: 9.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1113 RNHLaLNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP-----SEDIYIDGYPLTNidtnWLLKKV-AIVDQKPHLL 1186
Cdd:TIGR00955 37 RKHL-LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvkgSGSVLLNGMPIDA----KEMRAIsAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1187 GS-TILESLLYG----VDRDINSV--MDALDktymtEVIQ--NLPNGLDTPL--LEFSKNFSGGQIQRLAFARALLRNPR 1255
Cdd:TIGR00955 112 PTlTVREHLMFQahlrMPRRVTKKekRERVD-----EVLQalGLRKCANTRIgvPGRVKGLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1256 LLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPS--LMKLADRIIVMDSGIVKESGSFDEL 1318
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAqkgKTIICTIHQPSseLFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
444-627 |
1.35e-17 |
|
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: 82.41 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 444 SRDEnLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFD 523
Cdd:TIGR01189 9 SRGE-RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 524 MTIRENIIMRNENASESDFEEVCRLALVDEFALTfdqsyDTPCkeASLSGGQQQRIALARALLRDTEILILDEPTSALDP 603
Cdd:TIGR01189 88 LSALENLHFWAAIHGGAQRTIEDALAAVGLTGFE-----DLPA--AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*
gi 162312251 604 ITKNLVMDAIRAH-RKGKTTLVITH 627
Cdd:TIGR01189 161 AGVALLAGLLRAHlARGGIVLLTTH 185
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
454-627 |
1.58e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 83.09 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTF---ISLLLRYFSPTYGNIYLDDfplEEIDEHVLGSTITLVCQQPVIFD-MTIREN 529
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPgLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 530 IIMRNENASESDFEEVCRLALVDEFALTfdQSYDTPCKEA---SLSGGQQQRIALARALLRDTEILILDEPTSALDPITK 606
Cdd:cd03234 102 LTYTAILRLPRKSSDAIRKKRVEDVLLR--DLALTRIGGNlvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180
....*....|....*....|..
gi 162312251 607 NLVMDAIRAH-RKGKTTLVITH 627
Cdd:cd03234 180 LNLVSTLSQLaRRNRIVILTIH 201
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1099-1336 |
1.61e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.55 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSErnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSEDI---------------YID--- 1160
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTsgriiyhvalcekcgYVErps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1161 ---------GYPLTNIDTN-W---------LLKKVAIVDQKPHLLgstilesllYGVDRDINSVMDAL--------DKTY 1213
Cdd:TIGR03269 77 kvgepcpvcGGTLEPEEVDfWnlsdklrrrIRKRIAIMLQRTFAL---------YGDDTVLDNVLEALeeigyegkEAVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1214 MT-EVIQNLpnGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLL----LEKTIQNLSCTVLII 1288
Cdd:TIGR03269 148 RAvDLIEMV--QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLT 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 162312251 1289 THQPSLM-KLADRIIVMDSGIVKESGSFDELMNRHTHFWKLIHRGEWIE 1336
Cdd:TIGR03269 226 SHWPEVIeDLSDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVE 274
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
454-654 |
1.64e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.39 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGElVH-IIGPSGSGKSTFISLLLRYFSPTYGNIYLD----DF--PLEEIDehvLGstITLVCQQPVIFD-MT 525
Cdd:COG3845 23 DVSLTVRPGE-IHaLLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvRIrsPRDAIA---LG--IGMVHQHFMLVPnLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 526 IRENIIMRNENASE--SDFEEVCR--LALVDEFALTFDqsydtP-CKEASLSGGQQQRIALARALLRDTEILILDEPTSA 600
Cdd:COG3845 97 VAENIVLGLEPTKGgrLDRKAARAriRELSERYGLDVD-----PdAKVEDLSVGEQQRVEILKALYRGARILILDEPTAV 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 601 LDPITKNLVMDAIRAHRK-GKTTLVITHDMsqinnDEL------VLVIDKGHLIQRCARKE 654
Cdd:COG3845 172 LTPQEADELFEILRRLAAeGKSIIFITHKL-----REVmaiadrVTVLRRGKVVGTVDTAE 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
454-646 |
1.66e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 81.71 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHV---LGstITLVC----QQPVIFDMTI 526
Cdd:cd03215 18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDairAG--IAYVPedrkREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 527 RENIIMRnenasesdfeevcrlalvdefaltfdqsydtpckeASLSGGQQQRIALARALLRDTEILILDEPTSALDPITK 606
Cdd:cd03215 96 AENIALS-----------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 162312251 607 NLVMDAIRAHR-KGKTTLVITHDMsqinnDEL------VLVIDKGHL 646
Cdd:cd03215 141 AEIYRLIRELAdAGKAVLLISSEL-----DELlglcdrILVMYEGRI 182
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
434-647 |
1.72e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.40 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAY-PSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHV----L 508
Cdd:PRK13643 3 KFEKVNYTYqPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 509 GSTITLVCQQP--VIFDMTIRENIIMRNENASESDfEEVCRLAL--VDEFALTFDQSYDTPCKeasLSGGQQQRIALARA 584
Cdd:PRK13643 83 RKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPK-EKAEKIAAekLEMVGLADEFWEKSPFE---LSGGQMRRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 585 LLRDTEILILDEPTSALDPITKNLVMDAIRA-HRKGKTTLVITHDMSQINN-DELVLVIDKGHLI 647
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADyADYVYLLEKGHII 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1099-1313 |
1.81e-17 |
|
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: 82.63 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPdserNHLALNNVSLSIEArEKVAIVGISGSGKSTLVELLRK-TYPSE-DIYIDGYPLTNiDTNWLLKKV 1176
Cdd:cd03264 1 LQLENLTKRYG----KKRALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATlTPPSSgTIRIDGQDVLK-QPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQK----PHLlgsTILESL-----LYGV-DRDINS-VMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLA 1245
Cdd:cd03264 75 GYLPQEfgvyPNF---TVREFLdyiawLKGIpSKEVKArVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 1246 FARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSCTVLII--THQPS-LMKLADRIIVMDSGIVKESG 1313
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVIlsTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1098-1320 |
1.86e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.45 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1098 KIEFDGVSFAYPD-SERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRKTYPSedIYIDGYPLTNIDTNWL 1172
Cdd:PRK13646 2 TIRFDNVSYTYQKgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQninaLLKPTTGT--VTVDDITITHKTKDKY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1173 L----KKVAIVDQKPhllgstilESLLY--GVDRDI-----NSVMDaLD--KTYMTEVIQNLpnGLDTPLLEFSK-NFSG 1238
Cdd:PRK13646 80 IrpvrKRIGMVFQFP--------ESQLFedTVEREIifgpkNFKMN-LDevKNYAHRLLMDL--GFSRDVMSQSPfQMSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1239 GQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSC----TVLIITHQPS-LMKLADRIIVMDSGIVKESG 1313
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdenkTIILVSHDMNeVARYADEVIVMKEGSIVSQT 228
|
....*..
gi 162312251 1314 SFDELMN 1320
Cdd:PRK13646 229 SPKELFK 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
434-645 |
1.88e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 80.57 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDenLFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIylddfpleeidehVLGSTIT 513
Cdd:cd03221 2 ELENLSKTYGGKL--LLK--DISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-------------TWGSTVK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVcqqpvifdmtireniimrnenasesdfeevcrlalvdefalTFDQsydtpckeasLSGGQQQRIALARALLRDTEILI 593
Cdd:cd03221 65 IG-----------------------------------------YFEQ----------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 594 LDEPTSALDPITKNLVMDAIRAHRkgKTTLVITHD---MSQINNDelVLVIDKGH 645
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYP--GTVILVSHDryfLDQVATK--IIELEDGK 144
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
434-634 |
2.13e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.17 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFSLI-NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYL---DDFpleeIDEHVLG 509
Cdd:TIGR03269 281 KVRNVSKRYISVDRGVVKAVdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgDEW----VDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 510 ST--------ITLVCQQPVIF-DMTIRENIImrnenasesdfeEVCRLALVDEFALT----------FDQSYDTPCKEA- 569
Cdd:TIGR03269 357 PDgrgrakryIGILHQEYDLYpHRTVLDNLT------------EAIGLELPDELARMkavitlkmvgFDEEKAEEILDKy 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 570 --SLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDMSQINN 634
Cdd:TIGR03269 425 pdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLD 493
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1099-1318 |
2.45e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 85.14 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSErnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLR--KTYPSEDIYIDGYPLTNIDTNwlLKKV 1176
Cdd:PRK10851 3 IEIANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAglEHQTSGHIRFHGTDVSRLHAR--DRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHLLGS-TILESLLYGVD---RDINSVMDALDK--TYMTEVIQ--NLPNgldtpllEFSKNFSGGQIQRLAFAR 1248
Cdd:PRK10851 77 GFVFQHYALFRHmTVFDNIAFGLTvlpRRERPNAAAIKAkvTQLLEMVQlaHLAD-------RYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1249 ALLRNPRLLILDECTSALDSKSSLLLEKTIQNL----SCTVLIITH-QPSLMKLADRIIVMDSGIVKESGSFDEL 1318
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLheelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
433-627 |
2.61e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 80.66 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRDenlFSLINVSVFIPFGELVHIIGPSGSGKSTF---ISLLLRYFSptyGNIyldDFPLeeiDEHVLg 509
Cdd:cd03223 1 IELENLSLATPDGR---VLLKDLSFEIKPGDRLLITGPSGTGKSSLfraLAGLWPWGS---GRI---GMPE---GEDLL- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 510 stitLVCQQPVIFDMTIRENIImrnenasesdfeevcrlalvdefaltfdqsYdtPCKEAsLSGGQQQRIALARALLRDT 589
Cdd:cd03223 68 ----FLPQRPYLPLGTLREQLI------------------------------Y--PWDDV-LSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 162312251 590 EILILDEPTSALDPITKNLVMDAIRAHrkgKTTLV-ITH 627
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKEL---GITVIsVGH 146
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1113-1307 |
2.77e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 80.94 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1113 RNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELL---RKTYpSEDIYIDGYPLTnidtnwllkkvaivdqkphllGST 1189
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALfglRPPA-SGEITLDGKPVT---------------------RRS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1190 ILESLLYGV-----DRDINSVMDALDktymteVIQN--LPNGLdtpllefsknfSGGQIQRLAFARALLRNPRLLILDEC 1262
Cdd:cd03215 69 PRDAIRAGIayvpeDRKREGLVLDLS------VAENiaLSSLL-----------SGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 162312251 1263 TSALDSKSSLLLEKTIQNLS---CTVLII-THQPSLMKLADRIIVMDSG 1307
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELAdagKAVLLIsSELDELLGLCDRILVMYEG 180
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1100-1318 |
3.05e-17 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 82.19 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1100 EFDGVSFAYPDSErnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDGYPLTNIDTNWLLKK-V 1176
Cdd:TIGR03410 2 EVSNLNVYYGQSH----ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPvkSGSIRLDGEDITKLPPHERARAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQK----PHLlgsTILESLLYGvdrdinsvMDALDKTYmTEVIQNLPnGLDTPLLEFSK----NFSGGQIQRLAFAR 1248
Cdd:TIGR03410 78 AYVPQGreifPRL---TVEENLLTG--------LAALPRRS-RKIPDEIY-ELFPVLKEMLGrrggDLSGGQQQQLAIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1249 ALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS----CTVLIITHQPSL-MKLADRIIVMDSGIVKESGSFDEL 1318
Cdd:TIGR03410 145 ALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRaeggMAILLVEQYLDFaRELADRYYVMERGRVVASGAGDEL 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
436-649 |
3.81e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 82.96 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYPSRD-----ENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGS 510
Cdd:COG4167 8 RNLSKTFKYRTglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 511 TITLVCQQPV-----------IFDMTIRENIIMrNENASESDFEEVCRL-ALVDEFALTFDQSydtpckeasLSGGQQQR 578
Cdd:COG4167 88 HIRMIFQDPNtslnprlnigqILEEPLRLNTDL-TAEEREERIFATLRLvGLLPEHANFYPHM---------LSSGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 579 IALARALLRDTEILILDEPTSALDPITK----NLVMDAIRahRKGKTTLVITHDMSQINN--DElVLVIDKGHLIQR 649
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDMSVRsqiiNLMLELQE--KLGISYIYVSQHLGIVKHisDK-VLVMHQGEVVEY 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1100-1307 |
3.98e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.14 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1100 EFDGVSfaypdsernhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP----SEDIYIDGYPLT--NI-DTNwl 1172
Cdd:PRK13549 14 TFGGVK-----------ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtyEGEIIFEGEELQasNIrDTE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1173 LKKVAIVDQK----PHLlgsTILESLLYGVDRDINSVMDaLDKTY------MTEViqNLPNGLDTPLlefsKNFSGGQIQ 1242
Cdd:PRK13549 81 RAGIAIIHQElalvKEL---SVLENIFLGNEITPGGIMD-YDAMYlraqklLAQL--KLDINPATPV----GNLGLGQQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1243 RLAFARALLRNPRLLILDECTSAL-DSKSSLLLE--KTIQNLSCTVLIITHQ-PSLMKLADRIIVMDSG 1307
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLtESETAVLLDiiRDLKAHGIACIYISHKlNEVKAISDTICVIRDG 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
450-646 |
4.71e-17 |
|
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: 84.39 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 450 FSLiNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGST----ITLVCQQPVIF-DM 524
Cdd:TIGR02142 12 FSL-DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPekrrIGYVFQEARLFpHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 525 TIRENII--MRNENASESD--FEEVCRLalvdefaLTFDQSYDTPckEASLSGGQQQRIALARALLRDTEILILDEPTSA 600
Cdd:TIGR02142 91 SVRGNLRygMKRARPSERRisFERVIEL-------LGIGHLLGRL--PGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 162312251 601 LDPITKNLVMDAI-RAHRK-GKTTLVITHDMSQINN-DELVLVIDKGHL 646
Cdd:TIGR02142 162 LDDPRKYEILPYLeRLHAEfGIPILYVSHSLQEVLRlADRVVVLEDGRV 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
452-648 |
4.74e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 82.81 E-value: 4.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGS---TITLVCQQP---VIFDMT 525
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrDIQMVFQDSisaVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 526 IREnII---MRN-ENASESDfEEVCRLALVDEFALTFDQSYDTPckeASLSGGQQQRIALARALLRDTEILILDEPTSAL 601
Cdd:PRK10419 108 VRE-IIrepLRHlLSLDKAE-RLARASEMLRAVDLDDSVLDKRP---PQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 162312251 602 DPITKNLVMDAIRA--HRKGKTTLVITHDMSQINN-DELVLVIDKGHLIQ 648
Cdd:PRK10419 183 DLVLQAGVIRLLKKlqQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
438-644 |
5.22e-17 |
|
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: 81.61 E-value: 5.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 438 VSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIY----LDDFPLEEIDEHVLGSTIT 513
Cdd:cd03290 3 VTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFDMTIRENIIMrnenasESDFEEVCRLALVDEFALT-------FDQSYDTPCKEASLSGGQQQRIALARALL 586
Cdd:cd03290 83 YAAQKPWLLNATVEENITF------GSPFNKQRYKAVTDACSLQpdidllpFGDQTEIGERGINLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 587 RDTEILILDEPTSALDPITKNLVMDA--IRAHRKGKTTLV-ITHDMSQINNDELVLVIDKG 644
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVlVTHKLQYLPHADWIIAMKDG 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1115-1323 |
5.32e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 81.55 E-value: 5.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1115 HLALNnVSLSIEAREKVAIVGISGSGKSTLVELLR--KTYPSEDIYIDGYPLTNidTNWLLKKVAIVDQK----PHLlgs 1188
Cdd:PRK10771 13 HLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAgfLTPASGSLTLNGQDHTT--TPPSRRPVSMLFQEnnlfSHL--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1189 TILESLLYGVDRDINsvMDALDKTYMTEVIQNLpnGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDs 1268
Cdd:PRK10771 87 TVAQNIGLGLNPGLK--LNAAQREKLHAIARQM--GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1269 kSSL------LLEKTIQNLSCTVLIITHqpSL---MKLADRIIVMDSGIVKESGSFDELMNRHT 1323
Cdd:PRK10771 162 -PALrqemltLVSQVCQERQLTLLMVSH--SLedaARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
434-633 |
5.72e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.39 E-value: 5.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDenlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRyFSPTYGNIYLD---DFPLEEIDE----- 505
Cdd:PRK14258 9 KVNNLSFYYDTQK----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEgrvEFFNQNIYErrvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 506 HVLGSTITLVCQQPVIFDMTIRENIIMRNENAS---ESDFEEVCRLALVDefALTFDQSYDTPCKEA-SLSGGQQQRIAL 581
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGwrpKLEIDDIVESALKD--ADLWDEIKHKIHKSAlDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 162312251 582 ARALLRDTEILILDEPTSALDPITKNLVMDAIRAHR-KGKTTLVI-THDMSQIN 633
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIvSHNLHQVS 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
454-647 |
7.45e-17 |
|
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: 81.44 E-value: 7.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHV---LGstITLVCQQPVIF-DMTIREN 529
Cdd:cd03218 18 GVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrarLG--IGYLPQEASIFrKLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 530 IIMRNENASESDFEEVCRL-ALVDEFALTfdQSYDTPCkeASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNL 608
Cdd:cd03218 96 ILAVLEIRGLSKKEREEKLeELLEEFHIT--HLRKSKA--SSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 162312251 609 VMDAIRAHRKGKTTLVIT-HdmsqiNNDELVLVIDKGHLI 647
Cdd:cd03218 172 IQKIIKILKDRGIGVLITdH-----NVRETLSITDRAYII 206
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1113-1324 |
7.85e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.14 E-value: 7.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1113 RNHL-ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDGYPLTNIDTNWLLKKVAIVDQKPhllgST 1189
Cdd:PRK15112 23 RQTVeAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEptSGELLIDDHPLHFGDYSYRSQRIRMIFQDP----ST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1190 ILE-----SLLYGVDRDINSVMDALDKTymTEVIQNLPN-GLDTPLLEFSKN-FSGGQIQRLAFARALLRNPRLLILDEC 1262
Cdd:PRK15112 99 SLNprqriSQILDFPLRLNTDLEPEQRE--KQIIETLRQvGLLPDHASYYPHmLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1263 TSALD-SKSS----LLLE-KTIQNLSctVLIITHQPSLMK-LADRIIVMDSGIVKESGSFDELMNRHTH 1324
Cdd:PRK15112 177 LASLDmSMRSqlinLMLElQEKQGIS--YIYVTQHLGMMKhISDQVLVMHQGEVVERGSTADVLASPLH 243
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
436-633 |
8.00e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 81.67 E-value: 8.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYpsrdENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLV 515
Cdd:COG4604 5 KNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 516 CQQPVI-FDMTIREniimrnenasesdfeEVC---------RL-----ALVDEfALTF-------DQSYDTpckeasLSG 573
Cdd:COG4604 81 RQENHInSRLTVRE---------------LVAfgrfpyskgRLtaedrEIIDE-AIAYldledlaDRYLDE------LSG 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 574 GQQQRIALARALLRDTEILILDEPTSALDPitKNLV--MDAIR--AHRKGKTTLVITHDmsqIN 633
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDM--KHSVqmMKLLRrlADELGKTVVIVLHD---IN 197
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1118-1307 |
8.15e-17 |
|
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: 79.98 E-value: 8.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELL--RKT--YPSEDIYIDGYPLTNIdtnwLLKKVAIVDQKP-HLLGSTILE 1192
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLagRKTagVITGEILINGRPLDKN----FQRSTGYVEQQDvHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1193 SLlygvdrdinsvmdaldktymteviqnlpngldtpllEFSKNFSG---GQIQRLAFARALLRNPRLLILDECTSALDSK 1269
Cdd:cd03232 99 AL------------------------------------RFSALLRGlsvEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 162312251 1270 SSLLLEKTIQNLS-------CTVliitHQPS--LMKLADRIIVMDSG 1307
Cdd:cd03232 143 AAYNIVRFLKKLAdsgqailCTI----HQPSasIFEKFDRLLLLKRG 185
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1118-1307 |
8.99e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.74 E-value: 8.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELL---RKTYpSEDIYIDGYPLTNIDTNWLLKKVAIVDQKPHL--------- 1185
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALsgeLSPD-SGEVRLNGRPLADWSPAELARRRAVLPQHSSLsfpftveev 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1186 --LGSTILESLLYGVDRDINSVMDALDktymteviqnlpngldtpLLEFSKNF----SGGQIQRLAFARALLR------N 1253
Cdd:PRK13548 97 vaMGRAPHGLSRAEDDALVAAALAQVD------------------LAHLAGRDypqlSGGEQQRVQLARVLAQlwepdgP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1254 PRLLILDECTSALDSKSSLLLEKTIQNLS----CTVLIITHQPSLMKL-ADRIIVMDSG 1307
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAhergLAVIVVLHDLNLAARyADRIVLLHQG 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1099-1304 |
1.09e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.68 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPdserNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDGYPLTNIDTNWLLKK- 1175
Cdd:COG1129 5 LEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQpdSGEILLDGEPVRFRSPRDAQAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1176 VAIVDQKPHLLGS-TILESLLYGvdRDINSvMDALDKTYM----TEVIQNLpnGLDTPLLEFSKNFSGGQIQRLAFARAL 1250
Cdd:COG1129 81 IAIIHQELNLVPNlSVAENIFLG--REPRR-GGLIDWRAMrrraRELLARL--GLDIDPDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1251 LRNPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQ-PSLMKLADRIIVM 1304
Cdd:COG1129 156 SRDARVLILDEPTASLTEREVERLFRIIRRLKaqgVAIIYISHRlDEVFEIADRVTVL 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
437-662 |
1.11e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 81.66 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 437 NVSFAYPSRDEnlfSLINVSVFIPFGELVHIIGPSGSGKSTfisLLLRY---FSPTYGNIYLDDFPLEEIDEHVLG--ST 511
Cdd:PRK13639 6 DLKYSYPDGTE---ALKGINFKAEKGEMVALLGPNGAGKST---LFLHFngiLKPTSGEVLIKGEPIKYDKKSLLEvrKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 512 ITLVCQQP--VIFDMTIRENIIM--RNENASESDFEEVCRLALVdefALTFDQSYDTPCKEasLSGGQQQRIALARALLR 587
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFgpLNLGLSKEEVEKRVKEALK---AVGMEGFENKPPHH--LSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 588 DTEILILDEPTSALDPITKNLVMDAI-RAHRKGKTTLVITHDMSQIN-NDELVLVIDKGHLIQRCARKElvLFEDFE 662
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKE--VFSDIE 229
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1118-1321 |
1.28e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.88 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELL--RKTYP--SEDIYIDGYPLTNIDTNWLLKK---------VAIvdqkPH 1184
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEvtSGSILLDGEDILELSPDERARAgiflafqypVEI----PG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1185 LLGSTILESLLYGVDRDINSVMDALD--KTYMTEViqnlpnGLDTPLLEFSKN--FSGGQIQRLAFARALLRNPRLLILD 1260
Cdd:COG0396 92 VSVSNFLRTALNARRGEELSAREFLKllKEKMKEL------GLDEDFLDRYVNegFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 1261 ECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSLMKL--ADRIIVMDSG-IVKESGSfdELMNR 1321
Cdd:COG0396 166 ETDSGLDIDALRIVAEGVNKLRspdRGILIITHYQRILDYikPDFVHVLVDGrIVKSGGK--ELALE 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1111-1311 |
1.47e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.31 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1111 SERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELL---RKTyPSEDIYIDGYPLTNIDTNWLLKK-VAIVDQKPH-- 1184
Cdd:COG3845 267 DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALaglRPP-ASGSIRLDGEDITGLSPRERRRLgVAYIPEDRLgr 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1185 --LLGSTILESL-LYGVDRDINSVMDALDKTYMTEVIQNL-------PNGLDTPLlefsKNFSGGQIQRLAFARALLRNP 1254
Cdd:COG3845 346 glVPDMSVAENLiLGRYRRPPFSRGGFLDRKAIRAFAEELieefdvrTPGPDTPA----RSLSGGNQQKVILARELSRDP 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 1255 RLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIIthqpS-----LMKLADRIIVMDSG-IVKE 1311
Cdd:COG3845 422 KLLIAAQPTRGLDVGAIEFIHQRLLELRdagAAVLLI----SedldeILALSDRIAVMYEGrIVGE 483
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
452-628 |
1.68e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 80.65 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTfisLLLRY--FSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQ--PViFDMTIR 527
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMagLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQqsPP-FAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 528 ENIIM-----RNENASESDFEEVC-RLALVDEFALTFDQsydtpckeasLSGGQQQRIALARALLR-------DTEILIL 594
Cdd:COG4138 88 QYLALhqpagASSEAVEQLLAQLAeALGLEDKLSRPLTQ----------LSGGEWQRVRLAAVLLQvwptinpEGQLLLL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 162312251 595 DEPTSALDpITKNLVMDAI--RAHRKGKTTLVITHD 628
Cdd:COG4138 158 DEPMNSLD-VAQQAALDRLlrELCQQGITVVMSSHD 192
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1099-1307 |
1.94e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 79.63 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYpdseRNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE-LLRKTYPSE-DIYIDGYPLTNIDTNW----- 1171
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRmILGIILPDSgEVLFDGKPLDIAARNRigylp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1172 ----LLKKVAIVDQKPHLlgstileSLLYGVDR-DI-NSVMDALDKTYMTEViqnlpngLDTPLLEFSKnfsgGQIQRLA 1245
Cdd:cd03269 77 eergLYPKMKVIDQLVYL-------AQLKGLKKeEArRRIDEWLERLELSEY-------ANKRVEELSK----GNQQKVQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 1246 FARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSLM-KLADRIIVMDSG 1307
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELAragKTVILSTHQMELVeELCDRVLLLNKG 204
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
435-647 |
2.63e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.92 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 435 FDNVSFAYpsrdENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEID-EHVLGSTIT 513
Cdd:PRK11614 8 FDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFD-MTIRENIIMRNENASESDFEEvcRLALVDEFaltFDQSYDTPCKEA-SLSGGQQQRIALARALLRDTEI 591
Cdd:PRK11614 84 IVPEGRRVFSrMTVEENLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERRIQRAgTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 592 LILDEPTSALDPITKNLVMDAIRAHRKGKTTLVIthdMSQINNDELVL-----VIDKGHLI 647
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFL---VEQNANQALKLadrgyVLENGHVV 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1118-1318 |
2.82e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.09 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSED--IYIDGYPLT------NIDTNWLLKKVAIVDQKP----HL 1185
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskIKVDGKVLYfgkdifQIDAIKLRKEVGMVFQQPnpfpHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1186 lgsTILESLLYGVD-------RDINSVMD-ALDKTYMTEVIQNLpngLDTPllefSKNFSGGQIQRLAFARALLRNPRLL 1257
Cdd:PRK14246 106 ---SIYDNIAYPLKshgikekREIKKIVEeCLRKVGLWKEVYDR---LNSP----ASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1258 ILDECTSALDSKSSLLLEKTIQNL--SCTVLIITHQP-SLMKLADRIIVMDSGIVKESGSFDEL 1318
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELknEIAIVIVSHNPqQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1117-1307 |
2.97e-16 |
|
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: 79.40 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSED--IYIDGYPLTNIDTnwlLKKVAIVDQKPHLLG------ 1187
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYlPDSGsiLVRHDGGWVDLAQ---ASPREILALRRRTIGyvsqfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1188 ------STI---LESLL-YGVDRDinsvmDALDK-----TYMteviqNLPNGL-DTPllefSKNFSGGQIQRLAFARALL 1251
Cdd:COG4778 103 rviprvSALdvvAEPLLeRGVDRE-----EARARarellARL-----NLPERLwDLP----PATFSGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 1252 RNPRLLILDECTSALDSKS-----SLLLEKTIQnlSCTVLIITHQPSLMK-LADRIIVMDSG 1307
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANravvvELIEEAKAR--GTAIIGIFHDEEVREaVADRVVDVTPF 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1099-1307 |
3.06e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 80.29 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRK-TYPSE-DIYIDGYPLTNIDTNwllkkV 1176
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGfLAPSSgEITLDGVPVTGPGAD-----R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHLLG-STILESL-----LYGVDRdinSVMDALDKTYMTEViqnlpnGLDtpllEFSKNF----SGGQIQRLAF 1246
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVafglrLRGVPK---AERRARAEELLALV------GLA----DFARRRiwqlSGGMRQRVGI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1247 ARALLRNPRLLILDECTSALDSKS-----SLLLeKTIQNLSCTVLIITH--QPSLMkLADRIIVMDSG 1307
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTreqmqELLL-DVWQRTGKGVFLITHsvEEALF-LATRLVVMSPG 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
444-627 |
3.46e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 78.69 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 444 SRDEN-LFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIF 522
Cdd:cd03231 9 ERDGRaLFS--GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 523 DMTIRENIIMRNENASESDFEEVcrLALVDEFALTfdqsyDTPCkeASLSGGQQQRIALARALLRDTEILILDEPTSALD 602
Cdd:cd03231 87 TLSVLENLRFWHADHSDEQVEEA--LARVGLNGFE-----DRPV--AQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|....*.
gi 162312251 603 PITKNLVMDAIRAH-RKGKTTLVITH 627
Cdd:cd03231 158 KAGVARFAEAMAGHcARGGMVVLTTH 183
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1099-1314 |
3.85e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.17 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAY----PDSERnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYIDGYPLT----NID 1168
Cdd:PRK13649 3 INLQNVSYTYqagtPFEGR---ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvPTQgSVRVDDTLITstskNKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1169 TNWLLKKVAIVDQKP--HLLGSTILESLLYGVDR----DINSVMDALDKTYMTEVIQNLpngldtplleFSKN---FSGG 1239
Cdd:PRK13649 80 IKQIRKKVGLVFQFPesQLFEETVLKDVAFGPQNfgvsQEEAEALAREKLALVGISESL----------FEKNpfeLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1240 QIQRLAFARALLRNPRLLILDECTSALDSKSS---LLLEKTIQNLSCTVLIITHqpsLM----KLADRIIVMDSGIVKES 1312
Cdd:PRK13649 150 QMRRVAIAGILAMEPKILVLDEPTAGLDPKGRkelMTLFKKLHQSGMTIVLVTH---LMddvaNYADFVYVLEKGKLVLS 226
|
..
gi 162312251 1313 GS 1314
Cdd:PRK13649 227 GK 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1117-1313 |
5.07e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.58 E-value: 5.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELL---------RKTYPSED-IYIDGYPLTNIDTNWLLK-KVAIVDQKPH- 1184
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALsarlapdagEVHYRMRDgQLRDLYALSEAERRRLLRtEWGFVHQHPRd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1185 ------LLGSTILESLL------YGVDRDInsvmdALDktYMTEV------IQNLPngldtpllefsKNFSGGQIQRLAF 1246
Cdd:PRK11701 101 glrmqvSAGGNIGERLMavgarhYGDIRAT-----AGD--WLERVeidaarIDDLP-----------TTFSGGMQQRLQI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 1247 ARALLRNPRLLILDECTSALD--SKSSLL--LEKTIQNLSCTVLIITHQPSLMK-LADRIIVMDSGIVKESG 1313
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDvsVQARLLdlLRGLVRELGLAVVIVTHDLAVARlLAHRLLVMKQGRVVESG 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
434-681 |
5.25e-16 |
|
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: 82.93 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYpsrdENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLL--LRYFSPTYGNI-----------YLD---- 496
Cdd:TIGR03269 2 EVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgYVErpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 497 ----------DFPLEEID--------EHVLGSTITLVCQQPVIF--DMTIRENIIMRNENASESDFEEVCR-LALVDEFA 555
Cdd:TIGR03269 78 vgepcpvcggTLEPEEVDfwnlsdklRRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGRaVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 556 LtfdqSYDTPCKEASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIR-AHRKGKTTLVITHDMSQINN 634
Cdd:TIGR03269 158 L----SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeAVKASGISMVLTSHWPEVIE 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 162312251 635 D--ELVLVIDKGHLIQRCARKELVlfEDFENNVSIDEKVLKEEADNPFI 681
Cdd:TIGR03269 234 DlsDKAIWLENGEIKEEGTPDEVV--AVFMEGVSEVEKECEVEVGEPII 280
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1115-1304 |
5.29e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 77.66 E-value: 5.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1115 HLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPsediyidgyPLTNIDTNWLLKKVAIVDQKPHL---LGSTIL 1191
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR---------PTSGTVRRAGGARVAYVPQRSEVpdsLPLTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1192 ESLLYGV-------------DRDInsVMDALDKTYMTEViqnLPNGLDTpllefsknFSGGQIQRLAFARALLRNPRLLI 1258
Cdd:NF040873 76 DLVAMGRwarrglwrrltrdDRAA--VDDALERVGLADL---AGRQLGE--------LSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 162312251 1259 LDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSLMKLADRIIVM 1304
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHargATVVVVTHDLELVRRADPCVLL 191
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1118-1307 |
5.86e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.70 E-value: 5.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELL--RKTYPSEDIYIDGYPLTNIDT-------NwllKKVAIVDQKPHLLGS 1188
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLggLDTPTSGDVIFNGQPMSKLSSaakaelrN---QKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1189 -TILES----LLYGVDRDINSVMDALDktyMTEVIqnlpnGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECT 1263
Cdd:PRK11629 102 fTALENvampLLIGKKKPAEINSRALE---MLAAV-----GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 162312251 1264 SALDSKSS-----LLLEKTIQNlSCTVLIITHQPSLMKLADRIIVMDSG 1307
Cdd:PRK11629 174 GNLDARNAdsifqLLGELNRLQ-GTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
767-1311 |
6.54e-16 |
|
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: 82.54 E-value: 6.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 767 IFKSIWKvkKLRWFFLLGLLTSLIQGASVPIFAYVISKCLNLFMQIDPSIGVAFWSSMVLVVAAGSGASYFFSHYIFSIS 846
Cdd:COG4615 3 LLRLLLR--ESRWLLLLALLLGLLSGLANAGLIALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 847 AKIWCDhyrlLAVKVLFTQdqawFDQIENypLVLSKILVNNISDMRN--MISSLIEEVFIAFTMAIIGIAWSFATGWRLA 924
Cdd:COG4615 81 ARLRLR----LSRRILAAP----LERLER--IGAARLLAALTEDVRTisQAFVRLPELLQSVALVLGCLAYLAWLSPPLF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 925 AVLVAVSPILCLTSRMF---SYIYVSTERMCQDVVI-STTSILH--KTiVNLDTIKGYSvlsfFRENHKNSLRKSWEAFK 998
Cdd:COG4615 151 LLTLVLLGLGVAGYRLLvrrARRHLRRAREAEDRLFkHFRALLEgfKE-LKLNRRRRRA----FFDEDLQPTAERYRDLR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 999 RRAF-WTSLGFAINNSLLYFVRALLFycssiFISKEFYTVEQmvQVLSLATFTLLMAST----CIMSLPNVSASRIATSR 1073
Cdd:COG4615 226 IRADtIFALANNWGNLLFFALIGLIL-----FLLPALGWADP--AVLSGFVLVLLFLRGplsqLVGALPTLSRANVALRK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1074 V----LKLSSLKPGNLHKSGYLKFPLVGKIEFDGVSFAYPDSE-RNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELL 1148
Cdd:COG4615 299 IeeleLALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1149 RKTYPSE--DIYIDGYPLTNIDTNWLLKKVAIVDQKPHLLGStileslLYGVDRDINS--VMDALDKTYMTEVIQnLPNG 1224
Cdd:COG4615 379 TGLYRPEsgEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LLGLDGEADParARELLERLELDHKVS-VEDG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1225 ldtpllEFSK-NFSGGQIQRLAFARALLRNPRLLILDECTSALDSK------SSLLLE-----KtiqnlscTVLIITHQP 1292
Cdd:COG4615 452 ------RFSTtDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvfyTELLPElkargK-------TVIAISHDD 518
|
570
....*....|....*....
gi 162312251 1293 SLMKLADRIIVMDSGIVKE 1311
Cdd:COG4615 519 RYFDLADRVLKMDYGKLVE 537
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
437-633 |
6.56e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 77.68 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 437 NVSFAYpsRDENLfsLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYlddFPLEEIDEHVLGStitlvc 516
Cdd:PRK13540 6 ELDFDY--HDQPL--LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIL---FERQSIKKDLCTY------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 517 QQPVIF---------DMTIRENIIMRNENASES-DFEEVCRLalvdeFALtfDQSYDTPCkeASLSGGQQQRIALARALL 586
Cdd:PRK13540 73 QKQLCFvghrsginpYLTLRENCLYDIHFSPGAvGITELCRL-----FSL--EHLIDYPC--GLLSSGQKRQVALLRLWM 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 162312251 587 RDTEILILDEPTSALDPITKNLVMDAIRAHR-KGKTTLVITHDMSQIN 633
Cdd:PRK13540 144 SKAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLN 191
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
454-604 |
6.71e-16 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 78.86 E-value: 6.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHV---LGstITLVCQQPVIF-DMTIREN 529
Cdd:TIGR04406 19 DVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHErarLG--IGYLPQEASIFrKLTVEEN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 530 IIMRNENASESDFEEVCRL--ALVDEFALTFDQSYdtpcKEASLSGGQQQRIALARALLRDTEILILDEPTSALDPI 604
Cdd:TIGR04406 97 IMAVLEIRKDLDRAEREERleALLEEFQISHLRDN----KAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPI 169
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1098-1321 |
6.84e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 81.04 E-value: 6.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1098 KIEFDGVSFAYPDserNHLALNNVSLSIEAREKVAIVGISGSGKSTLvelLR-----KTYPSEDIYIDGYPLTNI---DT 1169
Cdd:PRK11650 3 GLKLQAVRKSYDG---KTQVIKGIDLDVADGEFIVLVGPSGCGKSTL---LRmvaglERITSGEIWIGGRVVNELepaDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1170 NwllkkVAIVDQK----PHLlgsTILESLLYG----------VDRDINSVMDALdktymteviqnlpnGLDtPLLEFS-K 1234
Cdd:PRK11650 77 D-----IAMVFQNyalyPHM---SVRENMAYGlkirgmpkaeIEERVAEAARIL--------------ELE-PLLDRKpR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1235 NFSGGQIQRLAFARALLRNPRLLILDECTSALDSK--SSLLLE-KTIQ-NLSCTVLIITH-QPSLMKLADRIIVMDSGIV 1309
Cdd:PRK11650 134 ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKlrVQMRLEiQRLHrRLKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
250
....*....|..
gi 162312251 1310 KESGSFDELMNR 1321
Cdd:PRK11650 214 EQIGTPVEVYEK 225
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1118-1324 |
8.21e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.37 E-value: 8.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP-------SEDIYIDGYPLTNI-DTNWLLKKVAIVDQKPHLLGST 1189
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyrySGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1190 ILESLLYGVD-------RDINSVMDAldktYMTEViqNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDEC 1262
Cdd:PRK14271 117 IMDNVLAGVRahklvprKEFRGVAQA----RLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1263 TSALDSKSSLLLEKTIQNLS--CTVLIITHQ-PSLMKLADRIIVMDSGIVKESGSFDELMNRHTH 1324
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLAdrLTVIIVTHNlAQAARISDRAALFFDGRLVEEGPTEQLFSSPKH 255
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
436-631 |
8.79e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.59 E-value: 8.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYPSRDenlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIdehvlGSTITLV 515
Cdd:PRK11248 5 SHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP-----GAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 516 CQQPVIFD-MTIRENIIMRNENA--SESDFEEVCR--LALVDefALTFDQSYDTpckeaSLSGGQQQRIALARALLRDTE 590
Cdd:PRK11248 76 FQNEGLLPwRNVQDNVAFGLQLAgvEKMQRLEIAHqmLKKVG--LEGAEKRYIW-----QLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 162312251 591 ILILDEPTSALDPITKNLVMDAIRA--HRKGKTTLVITHDMSQ 631
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIEE 191
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
434-646 |
9.64e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.99 E-value: 9.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDEnlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYL---DDFPLEEIDEHVLGS 510
Cdd:PRK10908 3 RFEHVSKAYLGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsghDITRLKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 511 TITLVCQ-QPVIFDMTIRENIIMR--NENASESDFEEVCRLALvDEFALtFDQSYDTPCKeasLSGGQQQRIALARALLR 587
Cdd:PRK10908 80 QIGMIFQdHHLLMDRTVYDNVAIPliIAGASGDDIRRRVSAAL-DKVGL-LDKAKNFPIQ---LSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 588 DTEILILDEPTSALDPITKNLVMDAIRA-HRKGKTTLVITHDMSQINNDEL-VLVIDKGHL 646
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEfNRVGVTVLMATHDIGLISRRSYrMLTLSDGHL 215
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
454-630 |
1.03e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 79.78 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVL---GSTITLVCQQPviFD-----MT 525
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDP--YAslnprMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 526 IREnII---MR-NENASESDFEEVCR--LALVD---EFAltfdQSYdtPcKEasLSGGQQQRIALARALLRDTEILILDE 596
Cdd:COG4608 114 VGD-IIaepLRiHGLASKAERRERVAelLELVGlrpEHA----DRY--P-HE--FSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 162312251 597 PTSALD-PITK---NLVMDaIRAhRKGKTTLVITHDMS 630
Cdd:COG4608 184 PVSALDvSIQAqvlNLLED-LQD-ELGLTYLFISHDLS 219
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
452-648 |
1.06e-15 |
|
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: 79.13 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSpTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIi 531
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 532 mrNENASESDfEEVCRLA-------LVDEFALTFD-QSYDTPCkeaSLSGGQQQRIALARALLRDTEILILDEPTSALDP 603
Cdd:cd03289 98 --DPYGKWSD-EEIWKVAeevglksVIEQFPGQLDfVLVDGGC---VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 162312251 604 ITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQ 648
Cdd:cd03289 172 ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1118-1307 |
1.50e-15 |
|
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: 77.37 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLV--------ELLRKTYPSEDIYIDGYPLTNIDTNwlLKKVAIVDQKPHLLGST 1189
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlailgemqTLEGKVHWSNKNESEPSFEATRSRN--RYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1190 ILESLLYGVDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSK 1269
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 162312251 1270 SS--LLLE---KTIQNLSCTVLIITHQPSLMKLADRIIVMDSG 1307
Cdd:cd03290 175 LSdhLMQEgilKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1093-1314 |
1.60e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.90 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1093 FPLVGKIEFDGVSFAYPDSERNHL-ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPL-TNI- 1167
Cdd:PRK13645 1 FDFSKDIILDNVSYTYAKKTPFEFkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISEtgQTIVGDYAIpANLk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1168 ---DTNWLLKKVAIVDQKP--HLLGSTILESLLYGvdrdinSVMDALDKtymTEVIQNLPNGLDTPLL--EFSK----NF 1236
Cdd:PRK13645 81 kikEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFG------PVNLGENK---QEAYKKVPELLKLVQLpeDYVKrspfEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1237 SGGQIQRLAFARALLRNPRLLILDECTSALDSKSSL----LLEKTIQNLSCTVLIITHQ-PSLMKLADRIIVMDSGIVKE 1311
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfinLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKVIS 231
|
...
gi 162312251 1312 SGS 1314
Cdd:PRK13645 232 IGS 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
434-648 |
1.74e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.43 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDENLFSLI------------------NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYL 495
Cdd:COG1134 6 EVENVSKSYRLYHEPSRSLKelllrrrrtrreefwalkDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 496 DD---FPLEeidehvLGstitlvcqqpVIF--DMTIRENIIMrneNA-----SESDFEEvcRLALVDEFA-LtfDQSYDT 564
Cdd:COG1134 86 NGrvsALLE------LG----------AGFhpELTGRENIYL---NGrllglSRKEIDE--KFDEIVEFAeL--GDFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 565 PCKeaSLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRK-GKTTLVITHDMSQINN--DElVLVI 641
Cdd:COG1134 143 PVK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELREsGRTVIFVSHSMGAVRRlcDR-AIWL 219
|
....*..
gi 162312251 642 DKGHLIQ 648
Cdd:COG1134 220 EKGRLVM 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1099-1318 |
1.77e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.35 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDGYPL--TNIDTNWLLK 1174
Cdd:PRK13636 6 LKVEELNYNYSDGTH---ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpsSGRILFDGKPIdySRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQKP--HLLGSTILESLLYGV-------DRDINSVMDALDKTYMtEVIQNLPngldTPLLEFsknfsgGQIQRLA 1245
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGAvnlklpeDEVRKRVDNALKRTGI-EHLKDKP----THCLSF------GQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1246 FARALLRNPRLLILDECTSALD----SKSSLLLEKTIQNLSCTVLIITHQPSLMKL-ADRIIVMDSGIVKESGSFDEL 1318
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1119-1318 |
1.80e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 79.69 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1119 NNVSLSIEAREKVAIVGISGSGKSTLVELLR--KTYPSEDIYIDGYPLTNIDTNwlLKKVAIVDQK----PHLlgsTILE 1192
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAglEDITSGDLFIGEKRMNDVPPA--ERGVGMVFQSyalyPHL---SVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1193 SLLYG----------VDRDINSVmdaldktymTEVIQnlpngLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDEC 1262
Cdd:PRK11000 95 NMSFGlklagakkeeINQRVNQV---------AEVLQ-----LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 1263 TSALDSKSSLLLEKTI----QNLSCTVLIITH-QPSLMKLADRIIVMDSGIVKESGSFDEL 1318
Cdd:PRK11000 161 LSNLDAALRVQMRIEIsrlhKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1120-1317 |
1.91e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.53 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1120 NVSLSIEAREKVAIVGISGSGKSTLVELLRK-TYPSE-DIYIDGYPLTNIDTNWLL----KKVAIVDQK----PHLlgsT 1189
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGlTRPQKgRIVLNGRVLFDAEKGICLppekRRIGYVFQDarlfPHY---K 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1190 ILESLLYGvdrdinsvMDALDKTYMTEVIQNLpnGLDtPLLE-FSKNFSGGQIQRLAFARALLRNPRLLILDECTSALD- 1267
Cdd:PRK11144 93 VRGNLRYG--------MAKSMVAQFDKIVALL--GIE-PLLDrYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDl 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 1268 -SKSSLL--LEKTIQNLSCTVLIITHqpSL---MKLADRIIVMDSGIVKESGSFDE 1317
Cdd:PRK11144 162 pRKRELLpyLERLAREINIPILYVSH--SLdeiLRLADRVVVLEQGKVKAFGPLEE 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
454-630 |
1.92e-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: 80.88 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRyFSPTYGNIYLDDFPLEEIDEHVLgstitlvcqQP------VIF-D--- 523
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSRRAL---------RPlrrrmqVVFqDpfg 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 524 -----MTIREnII---MR--NENASESDFEEVCRLALVD-------------EFaltfdqsydtpckeaslSGGQQQRIA 580
Cdd:COG4172 374 slsprMTVGQ-IIaegLRvhGPGLSAAERRARVAEALEEvgldpaarhryphEF-----------------SGGQRQRIA 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 162312251 581 LARALLRDTEILILDEPTSALDPITKNLVMDAIRA--HRKGKTTLVITHDMS 630
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALDVSVQAQILDLLRDlqREHGLAYLFISHDLA 487
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1114-1318 |
1.92e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 79.38 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1114 NHLALNNVSLSIEAREKVAIVGISGSGKST---LVELLRKtyPSE-DIYIDGYPLTniDTNWLLKKVAIVDQK----PHL 1185
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTvlrLVAGLEK--PTEgQIFIDGEDVT--HRSIQQRDICMVFQSyalfPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1186 lgsTILESLLYGVDrdinsvMDALDKTymtEVIQNLPNGLDTPLLE-----FSKNFSGGQIQRLAFARALLRNPRLLILD 1260
Cdd:PRK11432 94 ---SLGENVGYGLK------MLGVPKE---ERKQRVKEALELVDLAgfedrYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 1261 ECTSALDSKSSLLLEKTI----QNLSCTVLIITH-QPSLMKLADRIIVMDSGIVKESGSFDEL 1318
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIrelqQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1116-1320 |
2.62e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.34 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1116 LALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYIDGYPLTNIDTNWLLKK-VAIVDQKPHLLGS-TIL 1191
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkPTGgTILLRGQHIEGLPGHQIARMgVVRTFQHVRLFREmTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1192 ESLLYGVDRDINS-VMDALDKT-----YMTEVIQNLPNGLDT-PLLEFSK----NFSGGQIQRLAFARALLRNPRLLILD 1260
Cdd:PRK11300 99 ENLLVAQHQQLKTgLFSGLLKTpafrrAESEALDRAATWLERvGLLEHANrqagNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1261 ECTSALDSKSSLLLEKTIQNL----SCTVLIITHQPSL-MKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELrnehNVTVLLIEHDMKLvMGISDRIYVVNQGTPLANGTPEEIRN 243
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
452-628 |
2.79e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 78.97 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYL---DDFPLEEIDEHVlgstiTLVCQQPVIF-DMTIR 527
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtDVSRLHARDRKV-----GFVFQHYALFrHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 528 ENI------IMRNE--NASESDFEEVCRLALV--DEFALTFdqsydtpckEASLSGGQQQRIALARALLRDTEILILDEP 597
Cdd:PRK10851 93 DNIafgltvLPRRErpNAAAIKAKVTQLLEMVqlAHLADRY---------PAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190
....*....|....*....|....*....|...
gi 162312251 598 TSALDP-ITKNLVMDAIRAHRKGKTTLV-ITHD 628
Cdd:PRK10851 164 FGALDAqVRKELRRWLRQLHEELKFTSVfVTHD 196
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1117-1320 |
3.02e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.20 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVE-----LLRKTYPSEDIYIDGYPLTNIDT---------------------N 1170
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnalLLPDTGTIEWIFKDEKNKKKTKEkekvleklviqktrfkkikkiK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1171 WLLKKVAIVDQ--KPHLLGSTILESLL-----YGVDRDinsvmDALD--KTYMTEViqnlpnGLDTPLLEFSK-NFSGGQ 1240
Cdd:PRK13651 102 EIRRRVGVVFQfaEYQLFEQTIEKDIIfgpvsMGVSKE-----EAKKraAKYIELV------GLDESYLQRSPfELSGGQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1241 IQRLAFARALLRNPRLLILDECTSALD---SKSSLLLEKTIQNLSCTVLIITHQ-PSLMKLADRIIVMDSG-IVKESGSF 1315
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHDlDNVLEWTKRTIFFKDGkIIKDGDTY 250
|
....*
gi 162312251 1316 DELMN 1320
Cdd:PRK13651 251 DILSD 255
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1118-1307 |
3.10e-15 |
|
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: 76.74 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELLRK-TYPSE-DIYIDGYPLTNIDTNWLlkkvaIVDQKPHLLG-STILESL 1194
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSgGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1195 LYGVDRdinsVMDALDKTYMTEVIQ------NLPNGLDTPLLEFSknfsGGQIQRLAFARALLRNPRLLILDECTSALD- 1267
Cdd:TIGR01184 76 ALAVDR----VLPDLSKSERRAIVEehialvGLTEAADKRPGQLS----GGMKQRVAIARALSIRPKVLLLDEPFGALDa 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 162312251 1268 -SKSSLL--LEKTIQNLSCTVLIITHQ-PSLMKLADRIIVMDSG 1307
Cdd:TIGR01184 148 lTRGNLQeeLMQIWEEHRVTVLMVTHDvDEALLLSDRVVMLTNG 191
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
462-628 |
3.43e-15 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 76.68 E-value: 3.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTFISLLLRYFSPTYGniylddfpleeiDEHVLGSTITLVCQQPVI-FDMTIRENIIMRNENASES 540
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEG------------DIEIELDTVSYKPQYIKAdYEGTVRDLLSSITKDFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 541 DFEEVcrlalvdEFA--LTFDQSYDTPCKEasLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIR--AH 616
Cdd:cd03237 93 PYFKT-------EIAkpLQIEQILDREVPE--LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRrfAE 163
|
170
....*....|..
gi 162312251 617 RKGKTTLVITHD 628
Cdd:cd03237 164 NNEKTAFVVEHD 175
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
462-627 |
3.57e-15 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 75.91 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDfplEEIDEHVLGSTITL-------VCQQ-PVIFDMTIRENIIM- 532
Cdd:NF038007 31 GDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAG---KEVTNLSYSQKIILrreligyIFQSfNLIPHLSIFDNVALp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 533 ---RNENASEsdfeevcRLALVDEFALTFDQSYDTPCKEASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLV 609
Cdd:NF038007 108 lkyRGVAKKE-------RIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNARAV 180
|
170
....*....|....*....
gi 162312251 610 MDAIRA-HRKGKTTLVITH 627
Cdd:NF038007 181 LQQLKYiNQKGTTIIMVTH 199
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
452-632 |
3.64e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.01 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLE------EIDEHVLGSTITLVCQQPVIF-DM 524
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifQIDAIKLRKEVGMVFQQPNPFpHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 525 TIRENIIMRNENASESDFEEVCRLA--LVDEFALtFDQSYDTPCKEAS-LSGGQQQRIALARALLRDTEILILDEPTSAL 601
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKKIVeeCLRKVGL-WKEVYDRLNSPASqLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190
....*....|....*....|....*....|.
gi 162312251 602 DPITKNLVMDAIRAHRKGKTTLVITHDMSQI 632
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEIAIVIVSHNPQQV 215
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1120-1324 |
4.00e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 76.66 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1120 NVSLSIEAREKVAIVGISGSGKS----TLVELL----RKTypSEDIYIDGYPLTNIDTNWllKKVAIVDQKP-------H 1184
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSltcaAALGILpagvRQT--AGRVLLDGKPVAPCALRG--RKIATIMQNPrsafnplH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1185 LLGSTILESLL-YGVDRDINSVMDALDKTymteviqnlpnGLDTP---LLEFSKNFSGGQIQRLAFARALLRNPRLLILD 1260
Cdd:PRK10418 97 TMHTHARETCLaLGKPADDATLTAALEAV-----------GLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1261 ECTSALDSKSSL----LLEKTIQNLSCTVLIITHQPSLM-KLADRIIVMDSGIVKESGSFDELMNRHTH 1324
Cdd:PRK10418 166 EPTTDLDVVAQArildLLESIVQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNAPKH 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
462-633 |
4.94e-15 |
|
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: 79.83 E-value: 4.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTFISLLLRYFSPTYGniylddfpleEIDEHVlgsTITLVCQQPVI-FDMTIRENIIMRNENASES 540
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEG----------EVDEDL---KISYKPQYISPdYDGTVEEFLRSANTDDFGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 541 DFEEVcrlalvdEFA--LTFDQSYDTPCKEasLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIR--AH 616
Cdd:COG1245 433 SYYKT-------EIIkpLGLEKLLDKNVKD--LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRrfAE 503
|
170
....*....|....*..
gi 162312251 617 RKGKTTLVITHDMSQIN 633
Cdd:COG1245 504 NRGKTAMVVDHDIYLID 520
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1117-1324 |
5.12e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.82 E-value: 5.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSED--IYIDGYPLTNI-DTNWLLKKVAI--VDQKP-------H 1184
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDgeVAWLGKDLLGMkDDEWRAVRSDIqmIFQDPlaslnprM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1185 LLGSTILESL-LYGVDRDINSVMDALdKTYMTEV--IQNLPNgldtpllEFSKNFSGGQIQRLAFARALLRNPRLLILDE 1261
Cdd:PRK15079 116 TIGEIIAEPLrTYHPKLSRQEVKDRV-KAMMLKVglLPNLIN-------RYPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1262 CTSALD----SKSSLLLEKTIQNLSCTVLIITHQPSLMK-LADRIIVMDSGIVKESGSFDELMNRHTH 1324
Cdd:PRK15079 188 PVSALDvsiqAQVVNLLQQLQREMGLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEVYHNPLH 255
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
455-646 |
5.37e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.59 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 455 VSVFIPFGELVHIIGPSGSGKSTfislLLRYFSptyGNIYLDDFPLEEIDehVLGSTIT-----------------LVCQ 517
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKST----LLRHLS---GLITGDKSAGSHIE--LLGRTVQregrlardirksrantgYIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 518 Q-PVIFDMTIRENIIMR---------------NENASESDFEEVCRLALVdEFALTfdqsydtpcKEASLSGGQQQRIAL 581
Cdd:PRK09984 94 QfNLVNRLSVLENVLIGalgstpfwrtcfswfTREQKQRALQALTRVGMV-HFAHQ---------RVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 582 ARALLRDTEILILDEPTSALDPITKNLVMDAIR--AHRKGKTTLVITHDMS-QINNDELVLVIDKGHL 646
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1118-1304 |
5.58e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.52 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRKTypSEDIYIDGYPLTNIDTNWLLKKVAIVDQKPHLLGSTILES 1193
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKivasLISPT--SGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1194 LLY-----GVDRDINSVMDALDKTymteviqnlpnGLDTPLLEFSKN-FSGGQIQRLAFARALLRNPRLLILDECTSALD 1267
Cdd:PRK10247 101 LIFpwqirNQQPDPAIFLDDLERF-----------ALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 162312251 1268 SKSSLLLEKTIQNL----SCTVLIITHQPSLMKLADRIIVM 1304
Cdd:PRK10247 170 ESNKHNVNEIIHRYvreqNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
447-629 |
6.71e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.47 E-value: 6.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 447 ENLFSLINVSVFIPfGELVHIIGPSGSGKSTFISLLLRYFSPTYGNiYLDDFPLEEIDEHVLGST--------------- 511
Cdd:PRK13409 85 VNGFKLYGLPIPKE-GKVTGILGPNGIGKTTAVKILSGELIPNLGD-YEEEPSWDEVLKRFRGTElqnyfkklyngeikv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 512 ---ITLVCQQPVIFDMTIREnIIMRNENASESDfeevcrlALVDEFALT--FDQSYDTpckeasLSGGQQQRIALARALL 586
Cdd:PRK13409 163 vhkPQYVDLIPKVFKGKVRE-LLKKVDERGKLD-------EVVERLGLEniLDRDISE------LSGGELQRVAIAAALL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 162312251 587 RDTEILILDEPTSALDpITKNL-VMDAIRAHRKGKTTLVITHDM 629
Cdd:PRK13409 229 RDADFYFFDEPTSYLD-IRQRLnVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
450-633 |
7.64e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.47 E-value: 7.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 450 FSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIyldDFPLE--------EIDehvlgstitlvcqqpvi 521
Cdd:PRK13409 353 FSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELKisykpqyiKPD----------------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 522 FDMTIRENIIMRNENASESDFEEvcrlalvdEFA--LTFDQSYDTPCKEasLSGGQQQRIALARALLRDTEILILDEPTS 599
Cdd:PRK13409 413 YDGTVEDLLRSITDDLGSSYYKS--------EIIkpLQLERLLDKNVKD--LSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
170 180 190
....*....|....*....|....*....|....*.
gi 162312251 600 ALDPITKNLVMDAIR--AHRKGKTTLVITHDMSQIN 633
Cdd:PRK13409 483 HLDVEQRLAVAKAIRriAEEREATALVVDHDIYMID 518
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
437-672 |
8.35e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 76.38 E-value: 8.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 437 NVSFAYPSrdeNLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVC 516
Cdd:PRK13652 8 DLCYSYSG---SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 517 QQP--VIFDMTIRENI------IMRNENASESDFEEVCRLALVDEFALTFDQSydtpckeasLSGGQQQRIALARALLRD 588
Cdd:PRK13652 85 QNPddQIFSPTVEQDIafgpinLGLDEETVAHRVSSALHMLGLEELRDRVPHH---------LSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 589 TEILILDEPTSALDPITKNLVMDAIRA--HRKGKTTLVITHDMSQINN-DELVLVIDKGHLIQRCARKELVLFEDFENNV 665
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDLLARV 235
|
....*..
gi 162312251 666 SIDEKVL 672
Cdd:PRK13652 236 HLDLPSL 242
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
452-630 |
8.36e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.24 E-value: 8.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLE--------EIDEHVLGstitLVCQ-QPVIF 522
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssaakaELRNQKLG----FIYQfHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 523 DMTIRENIIM-------RNENASESDFEEVCRLALVDefaltfdQSYDTPckeASLSGGQQQRIALARALLRDTEILILD 595
Cdd:PRK11629 101 DFTALENVAMplligkkKPAEINSRALEMLAAVGLEH-------RANHRP---SELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 162312251 596 EPTSALDPITKNLVMDAIRA--HRKGKTTLVITHDMS 630
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
462-629 |
8.82e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.74 E-value: 8.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTfisLLLRY--FSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQ-PVIFDMTIRENIIM-----R 533
Cdd:PRK03695 22 GEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLTLhqpdkT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 534 NENASESDFEEVC-RLALVDEFALTFDQsydtpckeasLSGGQQQRIALARALLR-------DTEILILDEPTSALDpIT 605
Cdd:PRK03695 99 RTEAVASALNEVAeALGLDDKLGRSVNQ----------LSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD-VA 167
|
170 180
....*....|....*....|....*.
gi 162312251 606 KNLVMDAIRAH--RKGKTTLVITHDM 629
Cdd:PRK03695 168 QQAALDRLLSElcQQGIAVVMSSHDL 193
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
454-648 |
9.00e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 78.15 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDE----HVLGSTITLVCQQPVIF-DMTIRE 528
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrEVRRKKIAMVFQSFALMpHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 529 NIIMRNENASESDFEEvcRLALVDEFALTFDQSYDTPCKEaSLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNL 608
Cdd:PRK10070 126 NTAFGMELAGINAEER--REKALDALRQVGLENYAHSYPD-ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 162312251 609 VMDA-IRAHRKGKTTLV-ITHDMSQ-INNDELVLVIDKGHLIQ 648
Cdd:PRK10070 203 MQDElVKLQAKHQRTIVfISHDLDEaMRIGDRIAIMQNGEVVQ 245
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1113-1305 |
1.16e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 74.44 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1113 RNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE-----DIYIDGYPLTNIDTnwLLKKVAIVDQK----P 1183
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsasgEVLLNGRRLTALPA--EQRRIGILFQDdllfP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1184 HLlgsTILESLLYGVDRDIN------SVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLAFARALLRNPRLL 1257
Cdd:COG4136 90 HL---SVGENLAFALPPTIGraqrraRVEQALEEAGLAGFADRDPATL-----------SGGQRARVALLRALLAEPRAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 162312251 1258 ILDECTSALDSK-----SSLLLEKtIQNLSCTVLIITHQPSLMKLADRIIVMD 1305
Cdd:COG4136 156 LLDEPFSKLDAAlraqfREFVFEQ-IRQRGIPALLVTHDEEDAPAAGRVLDLG 207
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1118-1321 |
1.27e-14 |
|
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: 74.10 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELL--RKTY-PSE-DIYIDGYPLTNIDTNWLLKK-VAIVDQKP-HLLGSTIL 1191
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYeVTEgEILFKGEDITDLPPEERARLgIFLAFQYPpEIPGVKNA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1192 ESLlygvdRDINsvmdaldktymteviqnlpngldtpllefsKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSS 1271
Cdd:cd03217 96 DFL-----RYVN------------------------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1272 LLLEKTIQNL---SCTVLIITHQPSLMKL--ADRIIVMDSGIVKESGSFdELMNR 1321
Cdd:cd03217 141 RLVAEVINKLreeGKSVLIITHYQRLLDYikPDRVHVLYDGRIVKSGDK-ELALE 194
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1099-1304 |
1.49e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLrktY----PSE-DIYIDGYPLTnIDTnwll 1173
Cdd:COG3845 6 LELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKIL---YglyqPDSgEILIDGKPVR-IRS---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1174 KKVAI------VDQKPHLLGS-TILESLLYGVDRDINSVMD---------ALDKTYmteviqnlpnGLDTPLLEFSKNFS 1237
Cdd:COG3845 74 PRDAIalgigmVHQHFMLVPNlTVAENIVLGLEPTKGGRLDrkaararirELSERY----------GLDVDPDAKVEDLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1238 GGQIQRLAFARALLRNPRLLILDECTSAL-----DSksslLLEkTIQNLS---CTVLIITHQpsL---MKLADRIIVM 1304
Cdd:COG3845 144 VGEQQRVEILKALYRGARILILDEPTAVLtpqeaDE----LFE-ILRRLAaegKSIIFITHK--LrevMAIADRVTVL 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1099-1322 |
1.69e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.41 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYpdseRNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE-LLRKTYPSE-DIYIDGYPLTNiDTNWLLKKV 1176
Cdd:PRK13536 42 IDLAGVSKSY----GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARmILGMTSPDAgKITVLGVPVPA-RARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHL-LGSTILESLL-YG-----VDRDINSVMDALDKtymtevIQNLPNGLDTPLLEFSknfsGGQIQRLAFARA 1249
Cdd:PRK13536 117 GVVPQFDNLdLEFTVRENLLvFGryfgmSTREIEAVIPSLLE------FARLESKADARVSDLS----GGMKRRLTLARA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1250 LLRNPRLLILDECTSALDSKSSLLLEKTIQNLSC---TVLIITHqpsLM----KLADRIIVMDSGIVKESGSFDELMNRH 1322
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLArgkTILLTTH---FMeeaeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1099-1321 |
1.86e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.22 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERnhlALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRKTypSEDIYIDGYPLTNIDTNWLLK 1174
Cdd:PRK13652 4 IETRDLCYSYSGSKE---ALNNINFIAPRNSRIAVIGPNGAGKSTLFRhfngILKPT--SGSVLIRGEPITKENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQKP--HLLGSTILESLLYGvdrDINSVMD-ALDKTYMTEVIQNLpnGLDTPLLEFSKNFSGGQIQRLAFARALL 1251
Cdd:PRK13652 79 FVGLVFQNPddQIFSPTVEQDIAFG---PINLGLDeETVAHRVSSALHML--GLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1252 RNPRLLILDECTSALDSKSSLLLEKTIQNLS----CTVLIITHQPSLM-KLADRIIVMDSGIVKESGSFDELMNR 1321
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPetygMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1114-1333 |
2.27e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.66 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1114 NHLALNNVSLSIEAREKVAIVGISGSGKSTL-----------------VELLRKTYPSEDIYIDGYPLTNIDTNWLLKKV 1176
Cdd:PRK09984 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLlrhlsglitgdksagshIELLGRTVQREGRLARDIRKSRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKphllgsTILESLLYGVDRDI---NSVMDALDKTYMTEVIQNLPN-GLDTPLLEFSKNFSGGQIQRLAFARALLR 1252
Cdd:PRK09984 96 NLVNRL------SVLENVLIGALGSTpfwRTCFSWFTREQKQRALQALTRvGMVHFAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1253 NPRLLILDECTSALDSKSSLLLEKTI----QNLSCTVLIITHQPSL-MKLADRIIVMDSGIVKESGSFDELMN-RHTHFW 1326
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLrdinQNDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNeRFDHLY 249
|
....*..
gi 162312251 1327 KLIHRGE 1333
Cdd:PRK09984 250 RSINRVE 256
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
439-644 |
2.29e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.84 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 439 SFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLR--YFSPTYGNIYLDDFPLEEidehvlgstitlvc 516
Cdd:COG2401 33 AFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGR-------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 517 qqpvifDMTIRENIimrnenASESDFEEVCRL----ALVDefALTFDQSYDTpckeasLSGGQQQRIALARALLRDTEIL 592
Cdd:COG2401 99 ------EASLIDAI------GRKGDFKDAVELlnavGLSD--AVLWLRRFKE------LSTGQKFRFRLALLLAERPKLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 593 ILDEPTSALDPITKNLVMDAIR--AHRKGKTTLVITHDMSQIN--NDELVLVIDKG 644
Cdd:COG2401 159 VIDEFCSHLDRQTAKRVARNLQklARRAGITLVVATHHYDVIDdlQPDLLIFVGYG 214
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
434-628 |
2.60e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 77.70 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPsrdENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTIT 513
Cdd:PRK10522 324 ELRNVTFAYQ---DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQPVIFDMTIREniimRNENASESDFEE-VCRLALVDEFALTFDQSYDTpckeaSLSGGQQQRIALARALLRDTEIL 592
Cdd:PRK10522 401 AVFTDFHLFDQLLGP----EGKPANPALVEKwLERLKMAHKLELEDGRISNL-----KLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 162312251 593 ILDEPTSALDP----ITKNLVMDAIRAhrKGKTTLVITHD 628
Cdd:PRK10522 472 LLDEWAADQDPhfrrEFYQVLLPLLQE--MGKTIFAISHD 509
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
434-602 |
2.65e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.44 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSR--------DENlFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFsPTYGNIYLDDFPLEEIDE 505
Cdd:PRK15134 277 DVEQLQVAFPIRkgilkrtvDHN-VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 506 HVL---GSTITLVCQQP-------VIFDMTIRENIIMRNENASESDFEEVCRLALvDEFALTFDQSYDTPckeASLSGGQ 575
Cdd:PRK15134 355 RQLlpvRHRIQVVFQDPnsslnprLNVLQIIEEGLRVHQPTLSAAQREQQVIAVM-EEVGLDPETRHRYP---AEFSGGQ 430
|
170 180
....*....|....*....|....*..
gi 162312251 576 QQRIALARALLRDTEILILDEPTSALD 602
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1099-1313 |
3.77e-14 |
|
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: 73.17 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSED--IYIDGYPlTNIDTNWLLKKV 1176
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAgfATVDGFD-VVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHLLGS-TILESL-----LYGVDRD-----INSVMDALDktyMTEViqnlpngLDTPLLEFSKnfsgGQIQRLA 1245
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLeyfagLYGLKGDeltarLEELADRLG---MEEL-------LDRRVGGFST----GMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 1246 FARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL---SCTVLIITHQPS-LMKLADRIIVMDSGIVKESG 1313
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLralGKCILFSTHIMQeVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
444-602 |
5.51e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.14 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 444 SRDEN-LFSliNVSVFIPFGELVHIIGPSGSGKSTfislLLRYFS----PTYGNIYLDDFPLEEIDEHVLGSTITLVCQQ 518
Cdd:PRK13538 10 ERDERiLFS--GLSFTLNAGELVQIEGPNGAGKTS----LLRILAglarPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 519 PVIFDMTIRENIIMRNENASESDfEEVCRLAL----VDEFAltfdqsyDTPCkeASLSGGQQQRIALARALLRDTEILIL 594
Cdd:PRK13538 84 GIKTELTALENLRFYQRLHGPGD-DEALWEALaqvgLAGFE-------DVPV--RQLSAGQQRRVALARLWLTRAPLWIL 153
|
....*...
gi 162312251 595 DEPTSALD 602
Cdd:PRK13538 154 DEPFTAID 161
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
450-632 |
5.66e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.24 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 450 FSLINVSVFIPF----GELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDD---FPLEEIDEHVLGstITLVCQQPVIF 522
Cdd:PRK15439 21 YSGVEVLKGIDFtlhaGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcARLTPAKAHQLG--IYLVPQEPLLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 523 -DMTIRENIIMR--NENASESDFEevcrlALVDEFALTFDQSydtpCKEASLSGGQQQRIALARALLRDTEILILDEPTS 599
Cdd:PRK15439 99 pNLSVKENILFGlpKRQASMQKMK-----QLLAALGCQLDLD----SSAGSLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190
....*....|....*....|....*....|....
gi 162312251 600 ALDPITKNLVMDAIRAHR-KGKTTLVITHDMSQI 632
Cdd:PRK15439 170 SLTPAETERLFSRIRELLaQGVGIVFISHKLPEI 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1118-1318 |
6.29e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.24 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTNIDTNwLLKKVAI--VDQKPHLLGS-TILE 1192
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDsgTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1193 SLLYGVDRDinsvmdALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIqrLAFARALLRNPRLLILDECTSALDSKSSL 1272
Cdd:PRK15439 106 NILFGLPKR------QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQI--VEILRGLMRDSRILILDEPTASLTPAETE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 162312251 1273 LLEKTIQNLSCT---VLIITHQ-PSLMKLADRIIVMDSGIVKESGSFDEL 1318
Cdd:PRK15439 178 RLFSRIRELLAQgvgIVFISHKlPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1115-1320 |
8.23e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.08 E-value: 8.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1115 HLALNNVSLSIEAREKVAIVGISGSGKSTL---VELLRKtyPSE-DIYIDGYPLTNI-DTNWLLKkvaIVDQKPHLLGST 1189
Cdd:PRK10619 18 HEVLKGVSLQANAGDVISIIGSSGSGKSTFlrcINFLEK--PSEgSIVVNGQTINLVrDKDGQLK---VADKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1190 ILESL-----LYGVDRDINSVMDA-------------------LDKTYMTEVIQNlpngldtpllEFSKNFSGGQIQRLA 1245
Cdd:PRK10619 93 RLTMVfqhfnLWSHMTVLENVMEApiqvlglskqeareravkyLAKVGIDERAQG----------KYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1246 FARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSLMK-LADRIIVMDSGIVKESGSFDELMN 1320
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1113-1319 |
8.99e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 73.32 E-value: 8.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1113 RNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE----------DIYIDGYPLTNIDTNWLLKKVAIVDQK 1182
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvtgDVTLNGEPLAAIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1183 ------------------PHLL--GSTILEsllygvDRDINSVMDALdktymteviqnlpNGLDTPLLEFSKNFSGGQIQ 1242
Cdd:PRK13547 92 aqpafafsareivllgryPHARraGALTHR------DGEIAWQALAL-------------AGATALVGRDVTTLSGGELA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1243 RLAFARAL---------LRNPRLLILDECTSALDSKSSLLLEKTIQNLS----CTVLIITHQPSL-MKLADRIIVMDSGI 1308
Cdd:PRK13547 153 RVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwnLGVLAIVHDPNLaARHADRIAMLADGA 232
|
250
....*....|.
gi 162312251 1309 VKESGSFDELM 1319
Cdd:PRK13547 233 IVAHGAPADVL 243
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
443-644 |
9.89e-14 |
|
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: 73.35 E-value: 9.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 443 PSRDENLF----------SLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIylddfpleeidEHvlGSTI 512
Cdd:cd03291 34 SSDDNNLFfsnlclvgapVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------KH--SGRI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 513 TLVCQQPVIFDMTIRENIIMrNENASESDFEEVCRLALVDEFALTFDQSYDTPCKEA--SLSGGQQQRIALARALLRDTE 590
Cdd:cd03291 101 SFSSQFSWIMPGTIKENIIF-GVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGgiTLSGGQRARISLARAVYKDAD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 591 ILILDEPTSALDPITKNLVMDA-IRAHRKGKTTLVITHDMSQINNDELVLVIDKG 644
Cdd:cd03291 180 LYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1102-1323 |
1.19e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.51 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1102 DGVSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKSTLVELL-RKTYPSE-DIYIDGYPLTNIDTNWLLKKVAIV 1179
Cdd:PRK10575 15 RNVSFRVPG----RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLgRHQPPSEgEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1180 DQK-PHLLGSTILEslLYGVDR-------------DINSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLA 1245
Cdd:PRK10575 91 PQQlPAAEGMTVRE--LVAIGRypwhgalgrfgaaDREKVEEAISLVGLKPLAHRLVDSL-----------SGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1246 FARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS----CTVLIITHQPSL-MKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSqergLTVIAVLHDINMaARYCDYLVALRGGEMIAQGTPAELMR 237
|
...
gi 162312251 1321 RHT 1323
Cdd:PRK10575 238 GET 240
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
781-1074 |
1.21e-13 |
|
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: 72.97 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 781 FLLGLLTSLIQGASVPIFAYVISKCLNLFMQIDPSIGVAFWSSMVLVVAAGSGASYFFSHYIFSIsakiwcdhyrlLAVK 860
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAAR-----------LGQR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 861 VLFTQDQAWFDQIENYPLV---------LSKILVNNISDMRNMISSLIEEVFIAFTMAIIGIAWSFATGWRLAAVLVAVS 931
Cdd:cd07346 70 VVFDLRRDLFRHLQRLSLSffdrnrtgdLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 932 PILCLTSRMFS-YIYVSTERMcQDVVISTTSILHKTIVNLDTIKGYSVLSFFRENHKNSLRKSWEAFKRRAFWTSLGFAI 1010
Cdd:cd07346 150 PLYVLILRYFRrRIRKASREV-RESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1011 NNSLLYFVRALLFYCSSIFISKEFYTVEQMVQVLSLatftLLMASTCIMSLPNVsASRIATSRV 1074
Cdd:cd07346 229 IGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAY----LGMLFGPIQRLANL-YNQLQQALA 287
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1102-1290 |
1.23e-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: 75.36 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1102 DGVSFAYPDserNHLALNNVSLSIEAREKVAIVGISGSGKSTLVEL---LRKTYPSEDIYIDGYpltnidtnwllkKVAI 1178
Cdd:TIGR03719 8 NRVSKVVPP---KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRImagVDKDFNGEARPQPGI------------KVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1179 VDQKPHLLGS-TILESLLYGVdRDINSVMDALDKTYMT-------------------EVIQN------------------ 1220
Cdd:TIGR03719 73 LPQEPQLDPTkTVRENVEEGV-AEIKDALDRFNEISAKyaepdadfdklaaeqaelqEIIDAadawdldsqleiamdalr 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1221 LPNGlDTPLlefsKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSCTVLIITH 1290
Cdd:TIGR03719 152 CPPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTH 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1117-1307 |
1.29e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.25 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP----SEDIYIDGYPL--TNI-DTNwlLKKVAIVDQKPHLLGS- 1188
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtwDGEIYWSGSPLkaSNIrDTE--RAGIVIIHQELTLVPEl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1189 TILESLLYGvdRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSK---NFSGGQIQRLAFARALLRNPRLLILDECTSA 1265
Cdd:TIGR02633 94 SVAENIFLG--NEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRpvgDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 162312251 1266 LDSKSSLLLEKTIQNL---SCTVLIITHQPSLMK-LADRIIVMDSG 1307
Cdd:TIGR02633 172 LTEKETEILLDIIRDLkahGVACVYISHKLNEVKaVCDTICVIRDG 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
452-628 |
1.29e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.73 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEH----VLGSTITLVCQQ-PVIFDMTI 526
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEarakLRAKHVGFVFQSfMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 527 RENI----IMRNENASESDFEEVcrlALVDEFALTfDQSYDTPckeASLSGGQQQRIALARALLRDTEILILDEPTSALD 602
Cdd:PRK10584 106 LENVelpaLLRGESSRQSRNGAK---ALLEQLGLG-KRLDHLP---AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180
....*....|....*....|....*...
gi 162312251 603 PITKNLVMDAIRA-HRKGKTTLV-ITHD 628
Cdd:PRK10584 179 RQTGDKIADLLFSlNREHGTTLIlVTHD 206
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1063-1318 |
1.30e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.25 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1063 NVSASRIATSRV-LKLSSLKPGNLHKSGYLKFplvgkiEFDGVSFAYPDSERNHlALNNVSLSIEAREKVAIVGISGSGK 1141
Cdd:TIGR02633 227 TMSEDDIITMMVgREITSLYPHEPHEIGDVIL------EARNLTCWDVINPHRK-RVDDVSFSLRRGEILGVAGLVGAGR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1142 STLVELLRKTYPSE---DIYIDGYPLtNIDT--NWLLKKVAIV--DQKPHLL------GSTILESLLYGVDRdINSVMDA 1208
Cdd:TIGR02633 300 TELVQALFGAYPGKfegNVFINGKPV-DIRNpaQAIRAGIAMVpeDRKRHGIvpilgvGKNITLSVLKSFCF-KMRIDAA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1209 LDKTYMTEVIQNLPNGLDTPLLEFSKnFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS----CT 1284
Cdd:TIGR02633 378 AELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAqegvAI 456
|
250 260 270
....*....|....*....|....*....|....
gi 162312251 1285 VLIITHQPSLMKLADRIIVMDSGIVKESGSFDEL 1318
Cdd:TIGR02633 457 IVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHAL 490
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
454-605 |
1.49e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 71.60 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKST-F--ISLLLRyfsPTYGNIYLDDFPLEEIDEHV---LGstITLVCQQPVIF-DMTI 526
Cdd:COG1137 21 DVSLEVNQGEIVGLLGPNGAGKTTtFymIVGLVK---PDSGRIFLDGEDITHLPMHKrarLG--IGYLPQEASIFrKLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 527 RENII----MRNENASESdfEEvcRL-ALVDEFALTF--DQsydtpcKEASLSGGQQQRIALARALLRDTEILILDEPTS 599
Cdd:COG1137 96 EDNILavleLRKLSKKER--EE--RLeELLEEFGITHlrKS------KAYSLSGGERRRVEIARALATNPKFILLDEPFA 165
|
....*.
gi 162312251 600 ALDPIT 605
Cdd:COG1137 166 GVDPIA 171
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1117-1329 |
1.49e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.20 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELLrkT---YPSE-DIYIDGY-PltnidtnW-----LLKKVAIV-DQKPHL 1185
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKML--TgilVPTSgEVRVLGYvP-------FkrrkeFARRIGVVfGQRSQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1186 ---LgsTILESL-----LYGV-DRDINSVMDaldktYMTEV--IQNLpngLDTPLlefsKNFSGGQIQRLAFARALLRNP 1254
Cdd:COG4586 108 wwdL--PAIDSFrllkaIYRIpDAEYKKRLD-----ELVELldLGEL---LDTPV----RQLSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1255 RLLILDECTSALD--SKSSL--LLEKTIQNLSCTVLIITHQpslM----KLADRIIVMDSGIVKESGSFDELMNRHTHFW 1326
Cdd:COG4586 174 KILFLDEPTIGLDvvSKEAIreFLKEYNRERGTTILLTSHD---MddieALCDRVIVIDHGRIIYDGSLEELKERFGPYK 250
|
...
gi 162312251 1327 KLI 1329
Cdd:COG4586 251 TIV 253
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
781-1071 |
1.93e-13 |
|
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: 72.69 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 781 FLLGLLTSLIQGASVPIFAYVISKCLNLF------------MQIDPSIGV--------AFWSSMVLVVAAGSGASYFFSH 840
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFtnggmtnitgnsSGLNSSAGPfekleeemTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 841 YIFSISAKIWCDHYRLLAVKVLFTQDQAWFDQieNYPLVLSKILVNNISDMRNMISSLIEEVFIAFTMAIIGIAWSFATG 920
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDV--NDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 921 WRLAAVLVAVSPILCLTSRMFSYIYVSTERMCQDVVISTTSILHKTIVNLDTIKGYSVLSFFRENHKNSLRKSWEAFKRR 1000
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 1001 AFWTSLGFAINNSLLYFVRALLF-YCSSIFISKEFYTVEQMVQVLSLatftLLMASTCIMSLPNVSASRIAT 1071
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFwYGTYLVTQQEYSIGEVLTVFFSV----LIGAFSAGQQVPSIEAFANAR 306
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1100-1307 |
2.27e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.18 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1100 EFDGVSFAYPDSernhLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTY-PSE-DIYIDGYPLTNIDT-NWLLKKV 1176
Cdd:PRK11288 6 SFDGIGKTFPGV----KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYqPDAgSILIDGQEMRFASTtAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHLLGS-TILESLLYG--------VDRdinsvmdaldKTYMTEVIQNLPN-GLD----TPLlefsKNFSGGQIQ 1242
Cdd:PRK11288 82 AIIYQELHLVPEmTVAENLYLGqlphkggiVNR----------RLLNYEAREQLEHlGVDidpdTPL----KYLSIGQRQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1243 RLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSC---TVLIITHQ-PSLMKLADRIIVMDSG 1307
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAegrVILYVSHRmEEIFALCDAITVFKDG 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
455-631 |
2.36e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.41 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 455 VSVFIPFGELVHIIGPSGSGKSTfislLLRYFS---------------PTYG-NIYLDDFPLEEIDEHVlgstiTLVCQQ 518
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKST----LLRTFNrllelneearvegevRLFGrNIYSPDVDPIEVRREV-----GMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 519 PVIF-DMTIRENII----MRNENASESDFEEVCRLALV-----DEFAltfDQSYDTPckeASLSGGQQQRIALARALLRD 588
Cdd:PRK14267 94 PNPFpHLTIYDNVAigvkLNGLVKSKKELDERVEWALKkaalwDEVK---DRLNDYP---SNLSGGQRQRLVIARALAMK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 162312251 589 TEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQ 631
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQ 210
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
424-632 |
2.62e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.72 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 424 IKSISFERGfrfdnvsfaypsrDENLFSLINVSVfiPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEI 503
Cdd:PRK11831 10 MRGVSFTRG-------------NRCIFDNISLTV--PRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 504 DEHVLGST---ITLVCQQPVIF-DMTIRENI---IMRNENASESDFEEVCRLALVdefALTFDQSYDTpcKEASLSGGQQ 576
Cdd:PRK11831 75 SRSRLYTVrkrMSMLFQSGALFtDMNVFDNVaypLREHTQLPAPLLHSTVMMKLE---AVGLRGAAKL--MPSELSGGMA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 577 QRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRA--HRKGKTTLVITHDMSQI 632
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISElnSALGVTCVVVSHDVPEV 207
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
454-630 |
3.43e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 71.17 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHV---LGSTITLvcQQPVIF-DMTIREN 529
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarMGVVRTF--QHVRLFrEMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 530 IIMRNENASES----------DFEEVCRLALvdEFALTF-DQSYDTPC--KEAS-LSGGQQQRIALARALLRDTEILILD 595
Cdd:PRK11300 101 LLVAQHQQLKTglfsgllktpAFRRAESEAL--DRAATWlERVGLLEHanRQAGnLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 162312251 596 EPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDMS 630
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMK 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
434-632 |
3.77e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.79 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSrdenLFSLINVSVFIPFGElVH-IIGPSGSGKSTFISLLLRYFSPTYGNIYLDDfpleeiDEHVLGST- 511
Cdd:PRK11288 6 SFDGIGKTFPG----VKALDDISFDCRAGQ-VHaLMGENGAGKSTLLKILSGNYQPDAGSILIDG------QEMRFASTt 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 512 ------ITLVCQQ----PvifDMTIRENIIM-----RNENASESDFEEVCRLALvDEFALTFDQsyDTPCKEasLSGGQQ 576
Cdd:PRK11288 75 aalaagVAIIYQElhlvP---EMTVAENLYLgqlphKGGIVNRRLLNYEAREQL-EHLGVDIDP--DTPLKY--LSIGQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 577 QRIALARALLRDTEILILDEPTSALD-PITKNL--VMDAIRAhrKGKTTLVITHDMSQI 632
Cdd:PRK11288 147 QMVEIAKALARNARVIAFDEPTSSLSaREIEQLfrVIRELRA--EGRVILYVSHRMEEI 203
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
455-646 |
5.00e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 74.28 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 455 VSVFIPFG--------------ELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEeIDEHVLGSTITLVCQQPV 520
Cdd:TIGR01257 935 VKIFEPSGrpavdrlnitfyenQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 521 IFD-MTIRENIIMRNENASESDFEEVCRL-ALVDEFALTFDQSydtpcKEA-SLSGGQQQRIALARALLRDTEILILDEP 597
Cdd:TIGR01257 1014 LFHhLTVAEHILFYAQLKGRSWEEAQLEMeAMLEDTGLHHKRN-----EEAqDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 162312251 598 TSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINN-DELVLVIDKGHL 646
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRL 1138
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
433-647 |
5.49e-13 |
|
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: 69.87 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRDENLFSLI------------------NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIY 494
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKklgilgrkgevgefwalkDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 495 LD---DFPLEeidehvLGSTItlvcqQPvifDMTIRENIIMrneNASESDFEEVCRLALVD---EFAlTFDQSYDTPCKE 568
Cdd:cd03220 81 VRgrvSSLLG------LGGGF-----NP---ELTGRENIYL---NGRLLGLSRKEIDEKIDeiiEFS-ELGDFIDLPVKT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 569 asLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVI-THDMSQI-NNDELVLVIDKGHL 646
Cdd:cd03220 143 --YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILvSHDPSSIkRLCDRALVLEKGKI 220
|
.
gi 162312251 647 I 647
Cdd:cd03220 221 R 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1099-1309 |
6.11e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.45 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSEDIYIdgypltNIDTNWllkKVAI 1178
Cdd:PRK11147 4 ISIHGAWLSFSD----APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI------IYEQDL---IVAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1179 VDQKP------------------------------HLLGSTILESLLYGVDRdINSVMDALD----KTYMTEVIQNLpnG 1224
Cdd:PRK11147 71 LQQDPprnvegtvydfvaegieeqaeylkryhdisHLVETDPSEKNLNELAK-LQEQLDHHNlwqlENRINEVLAQL--G 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1225 L--DTPLLEFSknfsGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSCTVLIITHQPSLM-KLADRI 1301
Cdd:PRK11147 148 LdpDAALSSLS----GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIrNMATRI 223
|
....*...
gi 162312251 1302 IVMDSGIV 1309
Cdd:PRK11147 224 VDLDRGKL 231
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
1118-1321 |
9.01e-13 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 69.60 E-value: 9.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELL--RKTYPSED--IYIDGYPLTNIDTNWLLKK-VAIVDQKP-HLLGSTIL 1191
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSgtILFKGQDLLELEPDERARAgLFLAFQYPeEIPGVSNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1192 ESLlygvdRD-INSV--------MDALD-KTYMTEVIQNLpnGLDTPLLEFSKN--FSGGQIQRLAFARALLRNPRLLIL 1259
Cdd:TIGR01978 96 EFL-----RSaLNARrsargeepLDLLDfEKLLKEKLALL--DMDEEFLNRSVNegFSGGEKKRNEILQMALLEPKLAIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 1260 DECTSALDSKSSLLLEKTIQNL---SCTVLIITHQPSLMKL--ADRIIVMDSGIVKESGSFdELMNR 1321
Cdd:TIGR01978 169 DEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLNYikPDYVHVLLDGRIVKSGDV-ELAKE 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
451-652 |
9.06e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.55 E-value: 9.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 451 SLINVSVFIPFGELVHIIGPSGSGKSTFISLLLR-YFSPTY-GNIYLDDFPLEEidEHVLGST---ITLVCQQ-PVIFDM 524
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvYPHGTWdGEIYWSGSPLKA--SNIRDTEragIVIIHQElTLVPEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 525 TIRENIIMRNE---NASESDFEEVCRLA--LVDEfaLTFDQSYDT-PCKEasLSGGQQQRIALARALLRDTEILILDEPT 598
Cdd:TIGR02633 94 SVAENIFLGNEitlPGGRMAYNAMYLRAknLLRE--LQLDADNVTrPVGD--YGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 599 SALDPITKNLVMDAIR-AHRKGKTTLVITHDMSQIN--NDELVLVIDKGHLIQRCAR 652
Cdd:TIGR02633 170 SSLTEKETEILLDIIRdLKAHGVACVYISHKLNEVKavCDTICVIRDGQHVATKDMS 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1099-1314 |
9.28e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.53 E-value: 9.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAY-PDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVE----LLRKTYPS---EDIYIDGYPLTNiDTN 1170
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQhlngLLQPTEGKvtvGDIVVSSTSKQK-EIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1171 WLLKKVAIVDQKP--HLLGSTILESLLYGVDRDINSVMDAldKTYMTEVIQNLpnGLDTPLLEFSK-NFSGGQIQRLAFA 1247
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKA--EKIAAEKLEMV--GLADEFWEKSPfELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 1248 RALLRNPRLLILDECTSALDSKSSLLLEK---TIQNLSCTVLIITH-QPSLMKLADRIIVMDSGIVKESGS 1314
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQlfeSIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIISCGT 227
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1118-1325 |
9.48e-13 |
|
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: 70.27 E-value: 9.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVEL-LRKTYPSE-DIYIDGypltnidtnwllkKVAIVDQKPHLLGSTILESLL 1195
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLiLGELEPSEgKIKHSG-------------RISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1196 YGVDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDskssLLLE 1275
Cdd:cd03291 120 FGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD----VFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1276 KTIQNlSC--------TVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHF 1325
Cdd:cd03291 196 KEIFE-SCvcklmankTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDF 252
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
462-655 |
1.07e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.97 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDfplEEIDehvLGST-------ITLVC----QQPVIFDMTIRENI 530
Cdd:COG1129 278 GEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPVR---IRSPrdairagIAYVPedrkGEGLVLDLSIRENI 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 531 IMrnenaseSDFEEVCRLALVD---EFALTFDQ---------SYDTPCKeaSLSGGQQQRIALARALLRDTEILILDEPT 598
Cdd:COG1129 352 TL-------ASLDRLSRGGLLDrrrERALAEEYikrlriktpSPEQPVG--NLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 599 SALDPITKNLVMDAIR--AhRKGKTTLVITHDMsqinnDEL------VLVIDKGHLIQRCARKEL 655
Cdd:COG1129 423 RGIDVGAKAEIYRLIRelA-AEGKAVIVISSEL-----PELlglsdrILVMREGRIVGELDREEA 481
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1118-1319 |
1.16e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.66 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELLRK--TYPSEDIYIDGYPLTNIDTNWLLKKVAIVDQkpHLL---GSTILE 1192
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARllTPQSGTVFLGDKPISMLSSRQLARRLALLPQ--HHLtpeGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1193 SLLYG-----------VDRDINSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLAFARALLRNPRLLILDE 1261
Cdd:PRK11231 96 LVAYGrspwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDL-----------SGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1262 CTSALDSKSSLLLEKTIQNLSC---TVLIITH---QPSlmKLADRIIVMDSGIVKESGSFDELM 1319
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTqgkTVVTVLHdlnQAS--RYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1102-1324 |
1.29e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.54 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1102 DGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKS--TLVELLRKTYP----SEDIYIDGYPLTNIDTNWLLK- 1174
Cdd:PRK11022 7 DKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsSLAIMGLIDYPgrvmAEKLEFNGQDLQRISEKERRNl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 ---KVAIVDQKPhllgstiLESL--LYGVDRDInsvMDALD-------KTYMTEVIQNLPN-GLDTP---LLEFSKNFSG 1238
Cdd:PRK11022 87 vgaEVAMIFQDP-------MTSLnpCYTVGFQI---MEAIKvhqggnkKTRRQRAIDLLNQvGIPDPasrLDVYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1239 GQIQRLAFARALLRNPRLLILDECTSALDSK-----SSLLLEktIQNLSCTVLI-ITHQPSLM-KLADRIIVMDSGIVKE 1311
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTiqaqiIELLLE--LQQKENMALVlITHDLALVaEAAHKIIVMYAGQVVE 234
|
250
....*....|...
gi 162312251 1312 SGSFDELMNRHTH 1324
Cdd:PRK11022 235 TGKAHDIFRAPRH 247
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1113-1320 |
1.37e-12 |
|
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: 68.72 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1113 RNHLALNNVSLSIEAREKVAIVGISGSGKSTL----VELLRktyPSE-DIYIDGYPLTNIDtnwllkkvaiVDQKPHL-L 1186
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTfymiVGLVK---PDSgKILLDGQDITKLP----------MHKRARLgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1187 G-----STILESLlyGVDRDINSVMD--ALDKTYMTEVIQNLpngldtpLLEFS-----KNF----SGGQIQRLAFARAL 1250
Cdd:cd03218 78 GylpqeASIFRKL--TVEENILAVLEirGLSKKEREEKLEEL-------LEEFHithlrKSKasslSGGERRRVEIARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1251 LRNPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPS-LMKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKdrgIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1118-1305 |
1.53e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 68.97 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEA-----REKVAIVGISGSGKSTLVELLR-KTYPSEDiyidgypltniDTNWLLKKVAIVDQKPHLLGSTIL 1191
Cdd:cd03237 10 LGEFTLEVEGgsiseSEVIGILGPNGIGKTTFIKMLAgVLKPDEG-----------DIEIELDTVSYKPQYIKADYEGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1192 ESLLYGVDRDINSvmdalDKTYMTEVIQnlPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSS 1271
Cdd:cd03237 79 RDLLSSITKDFYT-----HPYFKTEIAK--PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 162312251 1272 LLLEKTIQ----NLSCTVLIITHQpSLMK--LADRIIVMD 1305
Cdd:cd03237 152 LMASKVIRrfaeNNEKTAFVVEHD-IIMIdyLADRLIVFE 190
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1118-1311 |
1.54e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.45 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE-DIYIDGYPLTNIDTNwllkkvaivdqkphllgSTILESLly 1196
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTpVAGCVDVPDNQFGRE-----------------ASLIDAI-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1197 GVDRDINSVMDALDKTymteviqnlpnGLDTPLLEFSK--NFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLL 1274
Cdd:COG2401 107 GRKGDFKDAVELLNAV-----------GLSDAVLWLRRfkELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 162312251 1275 EKTIQNLS----CTVLIITHQPSLMK-LA-DRIIVMDSGIVKE 1311
Cdd:COG2401 176 ARNLQKLArragITLVVATHHYDVIDdLQpDLLIFVGYGGVPE 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1113-1293 |
1.56e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 69.10 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1113 RNHLaLNNVSLSIEAREKVAIVGISGSGKST-------LVELLRKTYPSEDIYIDGYPLTNIDTNWL--LKKVAIVDQKP 1183
Cdd:PRK14267 16 SNHV-IKGVDLKIPQNGVFALMGPSGCGKSTllrtfnrLLELNEEARVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1184 ----HLlgsTILESLLYGVD--------RDINSVMD-ALDKTYMTEVIQNLPNgldtpllEFSKNFSGGQIQRLAFARAL 1250
Cdd:PRK14267 95 npfpHL---TIYDNVAIGVKlnglvkskKELDERVEwALKKAALWDEVKDRLN-------DYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 162312251 1251 LRNPRLLILDECTSALDSKSSLLLEKTIQNL--SCTVLIITHQPS 1293
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTHSPA 209
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
454-649 |
2.18e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.05 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPV-----------IF 522
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqrisqIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 523 DMTIRENIIMRNEnASESDFEEVCRlalvdEFALTFDQSYDTPckeASLSGGQQQRIALARALLRDTEILILDEPTSALD 602
Cdd:PRK15112 111 DFPLRLNTDLEPE-QREKQIIETLR-----QVGLLPDHASYYP---HMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 162312251 603 PITK----NLVMDAIRAHrkGKTTLVITHD---MSQINNDelVLVIDKGHLIQR 649
Cdd:PRK15112 182 MSMRsqliNLMLELQEKQ--GISYIYVTQHlgmMKHISDQ--VLVMHQGEVVER 231
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1118-1302 |
2.32e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 71.35 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELLRKtypseDIYIDGYPLTnIDTNWLLkkvAIVDQKPHLLGSTILESLLYG 1197
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKN-----EISADGGSYT-FPGNWQL---AWVNQETPALPQPALEYVIDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1198 vDRD----------------------INSVMDALDKTYMTEVIQNLPNGL---DTPLLEFSKNFSGGQIQRLAFARALLR 1252
Cdd:PRK10636 88 -DREyrqleaqlhdanerndghaiatIHGKLDAIDAWTIRSRAASLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQALIC 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 162312251 1253 NPRLLILDECTSALDSKSSLLLEKTIQNLSCTVLIITHQPSLMK-LADRII 1302
Cdd:PRK10636 167 RSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDpIVDKII 217
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1099-1314 |
2.56e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.98 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSErnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELL----RKTYPSedIYIDGYPLTNIDTNWLLK 1174
Cdd:PRK11614 6 LSFDKVSAHYGKIQ----ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLcgdpRATSGR--IVFDGKDITDWQTAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 K-VAIVDQKPHLLGS-TILESLLYG---VDRD-----INSVMDALDKTYMTEViqnlpngldtpllEFSKNFSGGQIQRL 1244
Cdd:PRK11614 80 EaVAIVPEGRRVFSRmTVEENLAMGgffAERDqfqerIKWVYELFPRLHERRI-------------QRAGTMSGGEQQML 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 1245 AFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL---SCTVLIITHQPS-LMKLADRIIVMDSG--IVKESGS 1314
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLreqGMTIFLVEQNANqALKLADRGYVLENGhvVLEDTGD 222
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
430-1307 |
3.53e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.29 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 430 ERGFRFdnvsfAYPSRDENLFSLI-NVSVFIPFGELVHIIGPSGSGKSTFislLLRYFSPTYG-------NIYLDDFPLE 501
Cdd:TIGR00956 59 TRGFRK-----LKKFRDTKTFDILkPMDGLIKPGELTVVLGRPGSGCSTL---LKTIASNTDGfhigvegVITYDGITPE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 502 EIDEHVLGSTItLVCQQPVIF-DMTIRENIIM---------RNENASESDFEEvcRLALVDEFALTFDQSYDTPCKE--- 568
Cdd:TIGR00956 131 EIKKHYRGDVV-YNAETDVHFpHLTVGETLDFaarcktpqnRPDGVSREEYAK--HIADVYMATYGLSHTRNTKVGNdfv 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 569 ASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIR--AHRKGKTTLVITHDMSQiNNDEL---VLVIDK 643
Cdd:TIGR00956 208 RGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKtsANILDTTPLVAIYQCSQ-DAYELfdkVIVLYE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 644 GHLI-QRCARKELVLFE-------------DFENNV-SIDEKVLKEEADNPfiLPNEESLLEKYWINYNEsFSQLSREsl 708
Cdd:TIGR00956 287 GYQIyFGPADKAKQYFEkmgfkcpdrqttaDFLTSLtSPAERQIKPGYEKK--VPRTPQEFETYWRNSPE-YAQLMKE-- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 709 ftsLESPFTDIESPTivsrrkiveqrklrmEKESFQETNV-DQTFHLFDDKEHACSLTLIFKSIWKVKKLRwffllgllt 787
Cdd:TIGR00956 362 ---IDEYLDRCSESD---------------TKEAYRESHVaKQSKRTRPSSPYTVSFSMQVKYCLARNFLR--------- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 788 sLIQGASVPIFayviSKCLNLFMQIDPSiGVAFWSSMVLVVAAGSGASYFFS--HYIFSISAKIwcdhyrllavkvlftq 865
Cdd:TIGR00956 415 -MKGNPSFTLF----MVFGNIIMALILS-SVFYNLPKNTSDFYSRGGALFFAilFNAFSSLLEI---------------- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 866 dqawFDQIENYPLVLSKILVNNISDMRNMISSLIEEVFIAFTMAII-GIAWSFATGWRLAA------VLVAVSPILCLtS 938
Cdd:TIGR00956 473 ----ASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVfNIILYFMVNFRRTAgrfffyLLILFICTLAM-S 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 939 RMFSYIYVSTERMCQDVVISTTSILHKTIVNLDTIKGYSVLSFFR-ENHKNSLRKSWEA-----FKRRAF---------- 1002
Cdd:TIGR00956 548 HLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKwIYYVNPLAYAFESlmvneFHGRRFecsqyvpsgg 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1003 -WTSLGfaINNSLLYFVRALLFycsSIFISKEFYTVEQM-----------------------VQVLSLATFTLLMASTCI 1058
Cdd:TIGR00956 628 gYDNLG--VTNKVCTVVGAEPG---QDYVDGDDYLKLSFqyynshkwrnfgiiigftvffffVYILLTEFNKGAKQKGEI 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1059 MSLPNVSASRIAtsRVLKLSSLKPGNLHKSGYLKFPLVGKiEFDGV---SFAYPDSERN-----------------HLAL 1118
Cdd:TIGR00956 703 LVFRRGSLKRAK--KAGETSASNKNDIEAGEVLGSTDLTD-ESDDVndeKDMEKESGEDifhwrnltyevkikkekRVIL 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1119 NNVSLSIEAREKVAIVGISGSGKSTLVELL--RKT---YPSEDIYIDGYPLtniDTNWLLKKVAIVDQKPHLLGSTILES 1193
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLaeRVTtgvITGGDRLVNGRPL---DSSFQRSIGYVQQQDLHLPTSTVRES 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1194 LLYGV-------------DRDINSVMDALDKTYMTEVIQNLPN-GLDTPllefsknfsggQIQRLAFARALLRNPRLLI- 1258
Cdd:TIGR00956 857 LRFSAylrqpksvsksekMEYVEEVIKLLEMESYADAVVGVPGeGLNVE-----------QRKRLTIGVELVAKPKLLLf 925
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1259 LDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPS--LMKLADRIIVMDSG 1307
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLAdhgQAILCTIHQPSaiLFEEFDRLLLLQKG 979
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
436-647 |
4.17e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.61 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYPSRDenlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDD-----FPLEEIDEHVLGs 510
Cdd:PRK10895 7 KNLAKAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedislLPLHARARRGIG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 511 titLVCQQPVIFD-MTIRENII----MRNENASESdfeevcRLALVDEFALTFDQSYDTPCKEASLSGGQQQRIALARAL 585
Cdd:PRK10895 82 ---YLPQEASIFRrLSVYDNLMavlqIRDDLSAEQ------REDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 586 LRDTEILILDEPTSALDPITKNLVMDAIRAHR-KGKTTLVITHDMSQ-INNDELVLVIDKGHLI 647
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVREtLAVCERAYIVSQGHLI 216
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
437-655 |
4.56e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 68.34 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 437 NVSFAYPSRDENLFSlINVSvfIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHV--LGSTITL 514
Cdd:PRK13636 10 ELNYNYSDGTHALKG-ININ--IKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLmkLRESVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 515 VCQQP--VIFDMTIRENIIM--RNENASESDFEEVCRLALvDEFALTFDQSYDTPCkeasLSGGQQQRIALARALLRDTE 590
Cdd:PRK13636 87 VFQDPdnQLFSASVYQDVSFgaVNLKLPEDEVRKRVDNAL-KRTGIEHLKDKPTHC----LSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 591 ILILDEPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDMSQIN-NDELVLVIDKGHLIQRCARKEL 655
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1103-1324 |
4.77e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1103 GVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKS-TLVELLR------KTYPSEDIYIDGYPLTNIDTNWLLKK 1175
Cdd:PRK10261 17 NLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRlleqagGLVQCDKMLLRRRSRQVIELSEQSAA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1176 ---------VAIVDQKPHL-------LGSTILES--LLYGVDRDinsvmDAL-DKTYMTEVIQnLPNGlDTPLLEFSKNF 1236
Cdd:PRK10261 97 qmrhvrgadMAMIFQEPMTslnpvftVGEQIAESirLHQGASRE-----EAMvEAKRMLDQVR-IPEA-QTILSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1237 SGGQIQRLAFARALLRNPRLLILDECTSALD---SKSSLLLEKTIQ-NLSCTVLIITHQPSLM-KLADRIIVMDSGIVKE 1311
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiQAQILQLIKVLQkEMSMGVIFITHDMGVVaEIADRVLVMYQGEAVE 249
|
250
....*....|...
gi 162312251 1312 SGSFDELMNRHTH 1324
Cdd:PRK10261 250 TGSVEQIFHAPQH 262
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1103-1290 |
5.94e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.15 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1103 GVSFAYPDserNHLALNNVSLSIEAREKVAIVGISGSGKSTLvelLR------KTYPSEDIYIDGYpltnidtnwllkKV 1176
Cdd:PRK11819 11 RVSKVVPP---KKQILKDISLSFFPGAKIGVLGLNGAGKSTL---LRimagvdKEFEGEARPAPGI------------KV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHL-LGSTILESLLYGVdRDINSVMDALDKTYMT-------------------EVIQ-----NLPNGL------ 1225
Cdd:PRK11819 73 GYLPQEPQLdPEKTVRENVEEGV-AEVKAALDRFNEIYAAyaepdadfdalaaeqgelqEIIDaadawDLDSQLeiamda 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 1226 ------DTPLlefsKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSCTVLIITH 1290
Cdd:PRK11819 152 lrcppwDAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTH 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
452-664 |
6.55e-12 |
|
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: 66.01 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLL---RYfSPTYGNIYLDDFPLEE--IDEHV-LGstITLVCQQPVIFDMt 525
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghpKY-EVTEGEILFKGEDITDlpPEERArLG--IFLAFQYPPEIPG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 526 IRENIIMRNenasesdfeevcrlalVDEfaltfdqsydtpckeaSLSGGQQQRIALARALLRDTEILILDEPTSALDPIT 605
Cdd:cd03217 92 VKNADFLRY----------------VNE----------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 606 KNLVMDAIRA-HRKGKTTLVITH--DMSQINNDELVLVIDKGHLIQRcARKELVlfEDFENN 664
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKS-GDKELA--LEIEKK 198
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
103-372 |
6.64e-12 |
|
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: 67.82 E-value: 6.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 103 LIFGtLIFTCLSAALEPLMTWTTGKVFDALSQYATSQITLGKMISLInfnsllitiFGLAscVFSFGVRFLWQYL----S 178
Cdd:cd18541 1 YLLG-ILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLI---------LLLA--LLIGIFRFLWRYLifgaS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 179 AIAGKRARSLCFHVLSSKSSTFYSltESKSG-----LVNSVDRcIQFYeksISLPMFHIAENLAISLSCLIISFRYSWSL 253
Cdd:cd18541 69 RRIEYDLRNDLFAHLLTLSPSFYQ--KNRTGdlmarATNDLNA-VRMA---LGPGILYLVDALFLGVLVLVMMFTISPKL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 254 TLVVLASYPIIILVVGFINSFLSSAYEKDRKS-SEKAASILEkSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSF 332
Cdd:cd18541 143 TLIALLPLPLLALLVYRLGKKIHKRFRKVQEAfSDLSDRVQE-SFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLAR 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 162312251 333 LDAFQGGVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVT 372
Cdd:cd18541 222 VDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVA 261
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1117-1290 |
6.98e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 67.03 E-value: 6.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELLR--KTYPSEDIYIDGYPLTNIDTnwllkKVAIVDQKPHLLG-STILES 1193
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAgfVPYQHGSITLDGKPVEGPGA-----ERGVVFQNEGLLPwRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1194 LLYGVDrdinsvMDALDKTYMTEVIQNLPNGLDtpLLEFSKNF----SGGQIQRLAFARALLRNPRLLILDECTSALDS- 1268
Cdd:PRK11248 91 VAFGLQ------LAGVEKMQRLEIAHQMLKKVG--LEGAEKRYiwqlSGGQRQRVGIARALAANPQLLLLDEPFGALDAf 162
|
170 180
....*....|....*....|....*
gi 162312251 1269 ---KSSLLLEKTIQNLSCTVLIITH 1290
Cdd:PRK11248 163 treQMQTLLLKLWQETGKQVLLITH 187
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1104-1324 |
7.45e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.21 E-value: 7.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1104 VSFAYPDSerNHLALNNVSLSIEAREKVAIVGISGSGKS----TLVELLRKT-YPSEDIYIDGYPLTNIDTNWLLK---- 1174
Cdd:PRK09473 20 VTFSTPDG--DVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANgRIGGSATFNGREILNLPEKELNKlrae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1175 KVAIVDQKPHL-------LGSTILESLL----YGVDRDINSVMDALDKTYMTEVIQNLPngldtpllEFSKNFSGGQIQR 1243
Cdd:PRK09473 98 QISMIFQDPMTslnpymrVGEQLMEVLMlhkgMSKAEAFEESVRMLDAVKMPEARKRMK--------MYPHEFSGGMRQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1244 LAFARALLRNPRLLILDECTSALD----SKSSLLLEKTIQNLSCTVLIITHQPSLMK-LADRIIVMDSGIVKESGSFDEL 1318
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYGNARDV 249
|
....*.
gi 162312251 1319 MNRHTH 1324
Cdd:PRK09473 250 FYQPSH 255
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
452-655 |
8.10e-12 |
|
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: 66.39 E-value: 8.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGST-ITLVCQQPVIF-DMTIREN 529
Cdd:TIGR03410 16 LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVPQGREIFpRLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 530 IIMRNENASESDFEevcrlalVDEFALT-FdqsydtP-CKE------ASLSGGQQQRIALARALLRDTEILILDEPTSAL 601
Cdd:TIGR03410 96 LLTGLAALPRRSRK-------IPDEIYElF------PvLKEmlgrrgGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 602 DP-ITKNL--VMDAIRAhRKGKTTLVITHDMS---QINNDelVLVIDKGHLIQRCARKEL 655
Cdd:TIGR03410 163 QPsIIKDIgrVIRRLRA-EGGMAILLVEQYLDfarELADR--YYVMERGRVVASGAGDEL 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
451-632 |
8.31e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 8.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 451 SLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLgstITLVCQQ-------PVIFd 523
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 524 mtirENIIMRNE--------NASESDFEEV-CRLALVDEFALTFDQSydtpckeASLSGGQQQRIALARALLRDTEILIL 594
Cdd:PRK15056 98 ----EDVVMMGRyghmgwlrRAKKRDRQIVtAALARVDMVEFRHRQI-------GELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 162312251 595 DEPTSALDPITKNLVMDAIRAHR-KGKTTLVITHDMSQI 632
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
455-648 |
8.42e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 68.33 E-value: 8.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 455 VSVFIPFGELVHIIGPSGSGKSTfislLLRYF----SPTYGNIYLDDFPLEEIDEHVLGstITLVCQQPVIF-DMTIREN 529
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKST----LLRMVagleRITSGEIWIGGRVVNELEPADRD--IAMVFQNYALYpHMSVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 530 II--MRNENASESDFEEvcRlalVDEFA--LTFDQSYDTpcKEASLSGGQQQRIALARALLRDTEILILDEPTSALDpiT 605
Cdd:PRK11650 97 MAygLKIRGMPKAEIEE--R---VAEAAriLELEPLLDR--KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD--A 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 162312251 606 KNLV-MDA-IRA-HRKGKTT-LVITHDmsQIN----NDELVlVIDKGHLIQ 648
Cdd:PRK11650 168 KLRVqMRLeIQRlHRRLKTTsLYVTHD--QVEamtlADRVV-VMNGGVAEQ 215
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
452-632 |
9.63e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 9.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLR-YFSPTY-GNIYLDDFPLE--EI-DEHVLGSTI-----TLVCQqpvi 521
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHGTYeGEIIFEGEELQasNIrDTERAGIAIihqelALVKE---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 522 fdMTIRENIIMRNE--NASESDFEEVCRLA--LVDEfaLTFDQSYDTPCKEasLSGGQQQRIALARALLRDTEILILDEP 597
Cdd:PRK13549 97 --LSVLENIFLGNEitPGGIMDYDAMYLRAqkLLAQ--LKLDINPATPVGN--LGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 162312251 598 TSALDPITKNLVMDAIR-AHRKGKTTLVITHDMSQI 632
Cdd:PRK13549 171 TASLTESETAVLLDIIRdLKAHGIACIYISHKLNEV 206
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
447-629 |
9.92e-12 |
|
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: 69.43 E-value: 9.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 447 ENLFSLINVSVFIPfGELVHIIGPSGSGKSTFISLLLRYFSPTYGNiYLDDFPLEEIDEHVLGS------------TITL 514
Cdd:COG1245 85 ENGFRLYGLPVPKK-GKVTGILGPNGIGKSTALKILSGELKPNLGD-YDEEPSWDEVLKRFRGTelqdyfkklangEIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 515 VC--QQ----PVIFDMTIREnIIMRNENASESDfeevcrlALVDEFALtfDQSYDTPCKEasLSGGQQQRIALARALLRD 588
Cdd:COG1245 163 AHkpQYvdliPKVFKGTVRE-LLEKVDERGKLD-------ELAEKLGL--ENILDRDISE--LSGGELQRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 162312251 589 TEILILDEPTSALDpITKNL-VMDAIR-AHRKGKTTLVITHDM 629
Cdd:COG1245 231 ADFYFFDEPSSYLD-IYQRLnVARLIReLAEEGKYVLVVEHDL 272
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1118-1311 |
1.02e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.34 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELLR--KTYPSEDIYIDGYPLTNID----TNWLLKKVAIVDQK----PHL-- 1185
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAglDDGSSGEVSLVGQPLHQMDeearAKLRAKHVGFVFQSfmliPTLna 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1186 LGSTILESLLYGvDRDINSVMDALdktymtEVIQNLpnGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSA 1265
Cdd:PRK10584 106 LENVELPALLRG-ESSRQSRNGAK------ALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 162312251 1266 LDSKS----SLLLEKTIQNLSCTVLIITHQPSLMKLADRIIVMDSGIVKE 1311
Cdd:PRK10584 177 LDRQTgdkiADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1118-1308 |
1.08e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVEL-LRKTYPSEDIYIDGYPLtnidtnwllkKVAIVDQKPHL-----LGSTIL 1191
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVvLGLVAPDEGVIKRNGKL----------RIGYVPQKLYLdttlpLTVNRF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1192 ESLLYGVDRDinSVMDALDKTYMTEViqnlpngLDTPLlefsKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSS 1271
Cdd:PRK09544 90 LRLRPGTKKE--DILPALKRVQAGHL-------IDAPM----QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 162312251 1272 LLLEKTIQN----LSCTVLIITHQPSL-MKLADRIIVMDSGI 1308
Cdd:PRK09544 157 VALYDLIDQlrreLDCAVLMVSHDLHLvMAKTDEVLCLNHHI 198
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
414-634 |
1.16e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.21 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 414 IEAAKRSAakikSISFErgfrFDNVSFAYPsrDENLFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNI 493
Cdd:PRK11147 309 VEEASRSG----KIVFE----MENVNYQID--GKQLVK--DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 494 ---------YLDDFPlEEIDEhvlgstitlvcqqpvifDMTIRENI------IMRNEnasesdfeevcrlalVDEFALTF 558
Cdd:PRK11147 377 hcgtklevaYFDQHR-AELDP-----------------EKTVMDNLaegkqeVMVNG---------------RPRHVLGY 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 559 DQSYDTPCKEA-----SLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIrAHRKGkTTLVITHDMSQIN 633
Cdd:PRK11147 424 LQDFLFHPKRAmtpvkALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELL-DSYQG-TVLLVSHDRQFVD 501
|
.
gi 162312251 634 N 634
Cdd:PRK11147 502 N 502
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
435-657 |
1.45e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.42 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 435 FDNVSFAYpsRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITL 514
Cdd:PTZ00243 1311 FEGVQMRY--REGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSM 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 515 VCQQPVIFDMTIRENIimrnENASESDFEEVCR-LALVD--EFALTFDQSYDTPCKEASL--SGGQQQRIALARALL-RD 588
Cdd:PTZ00243 1389 IPQDPVLFDGTVRQNV----DPFLEASSAEVWAaLELVGlrERVASESEGIDSRVLEGGSnySVGQRQLMCMARALLkKG 1464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 589 TEILILDEPTSALDPI----TKNLVMDAIRAHrkgkTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELVL 657
Cdd:PTZ00243 1465 SGFILMDEATANIDPAldrqIQATVMSAFSAY----TVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVM 1533
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1114-1313 |
1.92e-11 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 64.27 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1114 NHLALNNVSLSIEAREKVAIVGISGSGKSTLV-ELLRKTypSEDIYIDGYPLTNIDtnwllkKVAIVDQkphllgstiLE 1192
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVnEGLYAS--GKARLISFLPKFSRN------KLIFIDQ---------LQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1193 SLLygvdrdinsvmdALDKTYMTeviqnlpngLDTPLlefsKNFSGGQIQRLAFARALLRNPR--LLILDECTSALD-SK 1269
Cdd:cd03238 70 FLI------------DVGLGYLT---------LGQKL----STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHqQD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 162312251 1270 SSLLLE--KTIQNLSCTVLIITHQPSLMKLADRIIVMDSGIVKESG 1313
Cdd:cd03238 125 INQLLEviKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGG 170
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1118-1307 |
2.30e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSEDIyiDGYPLTNID--TNWLLKKVAIVDQK----PHLlgsTIL 1191
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNF--TGTILANNRkpTKQILKRTGFVTQDdilyPHL---TVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1192 ESLLYGVDRDINSVMDALDKTYMTE-VIQNLpnGL---DTPLL--EFSKNFSGGQIQRLAFARALLRNPRLLILDECTSA 1265
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAEsVISEL--GLtkcENTIIgnSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 162312251 1266 LDSKSSLLLEKTIQNLSC---TVLIITHQPS--LMKLADRIIVMDSG 1307
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQkgkTIVTSMHQPSsrVYQMFDSVLVLSEG 283
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
462-655 |
2.93e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.74 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTFISLL--LRyfSPTYGNIYLDDFPLE-----EI----------DEHVLGstitlvcqqpVIFDM 524
Cdd:COG3845 284 GEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITglsprERrrlgvayipeDRLGRG----------LVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 525 TIRENIIMRNenaseSDFEEVCRLALVD-----EFAL----TFD---QSYDTPCKeaSLSGGQQQRIALARALLRDTEIL 592
Cdd:COG3845 352 SVAENLILGR-----YRRPPFSRGGFLDrkairAFAEelieEFDvrtPGPDTPAR--SLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 593 ILDEPTSALDPITKNLVMDAIRAHR-KGKTTLVITHDMsqinnDEL------VLVIDKGHLIQRCARKEL 655
Cdd:COG3845 425 IAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDL-----DEIlalsdrIAVMYEGRIVGEVPAAEA 489
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1117-1307 |
3.07e-11 |
|
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: 65.05 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKT-YPSE-DIYIDGY-PLTNidTNWLLKKVAIV-DQKPHL------L 1186
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLlQPTSgEVRVAGLvPWKR--RKKFLRRIGVVfGQKTQLwwdlpvI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1187 GSTILESLLYGVD-----RDINSVMDALDktymtevIQNLpngLDTPLlefsKNFSGGQIQRLAFARALLRNPRLLILDE 1261
Cdd:cd03267 114 DSFYLLAAIYDLPparfkKRLDELSELLD-------LEEL---LDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 162312251 1262 CTSALDSKSSLLLEKTIQNLS----CTVLIITHQ-PSLMKLADRIIVMDSG 1307
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNrergTTVLLTSHYmKDIEALARRVLVIDKG 230
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1063-1317 |
3.42e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.61 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1063 NVSASRIATSRV-----LKLSSLKPGNlHKSGYLKFPLVGKI-----EFDGVSFAYPDSErnhlALNNVSLSIEAREKVA 1132
Cdd:PRK15064 275 NASKAKQATSRAkqidkIKLEEVKPSS-RQNPFIRFEQDKKLhrnalEVENLTKGFDNGP----LFKNLNLLLEAGERLA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1133 IVGISGSGKSTLVELLRKTYP--------SEDIYIDGYP----------LTNID--TNWllKKVAIVDQkphlLGSTILE 1192
Cdd:PRK15064 350 IIGENGVGKTTLLRTLVGELEpdsgtvkwSENANIGYYAqdhaydfendLTLFDwmSQW--RQEGDDEQ----AVRGTLG 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1193 SLLYGVDrDIN-SVmdaldktymteviqnlpngldtpllefsKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSS 1271
Cdd:PRK15064 424 RLLFSQD-DIKkSV----------------------------KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESI 474
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 162312251 1272 LLLEKTIQNLSCTVLIITHQPSLMK-LADRII-VMDSGIVKESGSFDE 1317
Cdd:PRK15064 475 ESLNMALEKYEGTLIFVSHDREFVSsLATRIIeITPDGVVDFSGTYEE 522
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
437-648 |
3.64e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.59 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 437 NVSFAYpsrDENLFSLiNVSVFIPFGELVHIIGPSGSGKSTfislLLRYFSP----TYGNIYLDDFPLEEIDEHVLGstI 512
Cdd:PRK11000 8 NVTKAY---GDVVISK-DINLDIHEGEFVVFVGPSGCGKST----LLRMIAGlediTSGDLFIGEKRMNDVPPAERG--V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 513 TLVCQQPVIF-DMTIRENII--MRNENASESDFEE-VCRLALVDEFALTFDQsydtpcKEASLSGGQQQRIALARALLRD 588
Cdd:PRK11000 78 GMVFQSYALYpHLSVAENMSfgLKLAGAKKEEINQrVNQVAEVLQLAHLLDR------KPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 589 TEILILDEPTSALDPITK-NLVMDAIRAHRK-GKTTLVITHDmsQIN----NDELVlVIDKGHLIQ 648
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALRvQMRIEISRLHKRlGRTMIYVTHD--QVEamtlADKIV-VLDAGRVAQ 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
426-629 |
4.22e-11 |
|
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: 67.02 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 426 SISFERGFRF----DNVSFAypsrdenlfslinvsvfIPFGELVHIIGPSGSGKS-TFISL--LLRY-FSPTYGNIYLDD 497
Cdd:COG4172 13 SVAFGQGGGTveavKGVSFD-----------------IAAGETLALVGESGSGKSvTALSIlrLLPDpAAHPSGSILFDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 498 FPLEEIDEHVL----GSTITLVCQQPvifdMT-----------IREnIIMRNENASESDFEEVCR--LALV----DEFAL 556
Cdd:COG4172 76 QDLLGLSERELrrirGNRIAMIFQEP----MTslnplhtigkqIAE-VLRLHRGLSGAAARARALelLERVgipdPERRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 557 TfdqSYdtPckeASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRA--HRKGKTTLVITHDM 629
Cdd:COG4172 151 D---AY--P---HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDlqRELGMALLLITHDL 217
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1099-1307 |
4.33e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.13 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSERnhlALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKT-YPSE-DIYIDGYPLT---NIDTNWLL 1173
Cdd:PRK10908 2 IRFEHVSKAYLGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIeRPSAgKIWFSGHDITrlkNREVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1174 KKVAIVDQKPHLL------GSTILESLLYGVD-RDINS-VMDALDKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLA 1245
Cdd:PRK10908 79 RQIGMIFQDHHLLmdrtvyDNVAIPLIIAGASgDDIRRrVSAALDKVGLLDKAKNFPIQL-----------SGGEQQRVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 1246 FARALLRNPRLLILDECTSALD---SKSSLLLEKTIQNLSCTVLIITHQPSLMKLAD-RIIVMDSG 1307
Cdd:PRK10908 148 IARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDG 213
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
454-627 |
4.51e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.70 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLL---RYfSPTYGNIYLDDFPL--EEIDEHV-LGstITLVCQQPV-IFDMTI 526
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghpKY-EVTSGSILLDGEDIleLSPDERArAG--IFLAFQYPVeIPGVSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 527 RE------NIImRNENASESDFEEVCR--LALVDefaltFDQSYDTPCKEASLSGGQQQRIALARALLRDTEILILDEPT 598
Cdd:COG0396 95 SNflrtalNAR-RGEELSAREFLKLLKekMKELG-----LDEDFLDRYVNEGFSGGEKKRNEILQMLLLEPKLAILDETD 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 162312251 599 SALDpitknlvMDAIRA--------HRKGKTTLVITH 627
Cdd:COG0396 169 SGLD-------IDALRIvaegvnklRSPDRGILIITH 198
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
451-632 |
6.81e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 451 SLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDeHVLGST--ITLVCQQ-PVIFDMTIR 527
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQlgIGIIYQElSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 528 ENIIMrnenaSESDFEEVCRLALVD---------EFALTFDQSYDTPCKEASLSGGQQQRIALARALLRDTEILILDEPT 598
Cdd:PRK09700 99 ENLYI-----GRHLTKKVCGVNIIDwremrvraaMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190
....*....|....*....|....*....|....*
gi 162312251 599 SAL-DPITKNLVMDAIRAHRKGKTTLVITHDMSQI 632
Cdd:PRK09700 174 SSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEI 208
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1098-1311 |
7.03e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.53 E-value: 7.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1098 KIEFDGVSFAYPDserNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDGYPLTNIDTNWLLKK 1175
Cdd:PRK10522 322 TLELRNVTFAYQD---NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQpqSGEILLDGKPVTAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1176 VAIVDQKPHLLGSTILESllyGVDRDINSVMDALDKTYMTEVIQnLPNGLDTPLlefskNFSGGQIQRLAFARALLRNPR 1255
Cdd:PRK10522 399 FSAVFTDFHLFDQLLGPE---GKPANPALVEKWLERLKMAHKLE-LEDGRISNL-----KLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1256 LLILDECTSALDSKSS----LLLEKTIQNLSCTVLIITHQPSLMKLADRIIVMDSGIVKE 1311
Cdd:PRK10522 470 ILLLDEWAADQDPHFRrefyQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
452-627 |
7.52e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.61 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTY---GNIYLDDFPLEEidehvlgSTITLVC---QQPVIF--D 523
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPIDA-------KEMRAISayvQQDDLFipT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 524 MTIRENIIMRNENASESDFEEVCRLALVDEF--ALTFDQSYDT----PCKEASLSGGQQQRIALARALLRDTEILILDEP 597
Cdd:TIGR00955 114 LTVREHLMFQAHLRMPRRVTKKEKRERVDEVlqALGLRKCANTrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190
....*....|....*....|....*....|.
gi 162312251 598 TSALDPITKNLVMDAIRA-HRKGKTTLVITH 627
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGlAQKGKTIICTIH 224
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
447-630 |
7.97e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 63.92 E-value: 7.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 447 ENLFSLINVSVFIPfGELVHIIGPSGSGKSTFISLLLRYFSPTYGNI--------YLDDF---PLEEIDEHVLGSTITL- 514
Cdd:cd03236 12 PNSFKLHRLPVPRE-GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDEFrgsELQNYFTKLLEGDVKVi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 515 -----VCQQPVIFDMTIRENIIMRNENASesdFEEVCRlalVDEFALTFDQSYDtpckeaSLSGGQQQRIALARALLRDT 589
Cdd:cd03236 91 vkpqyVDLIPKAVKGKVGELLKKKDERGK---LDELVD---QLELRHVLDRNID------QLSGGELQRVAIAAALARDA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 162312251 590 EILILDEPTSALDpITKNLVMDAI--RAHRKGKTTLVITHDMS 630
Cdd:cd03236 159 DFYFFDEPSSYLD-IKQRLNAARLirELAEDDNYVLVVEHDLA 200
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
784-1061 |
8.25e-11 |
|
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: 64.50 E-value: 8.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 784 GLLTSLIQGASVPIFAYVISKCLNLFMQIDPSIGVAFWSSMVLVVAAGSGASYFFSHYIFSISA-KIWCDhYRLLAVKVL 862
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGeRIVAR-LRRDLFSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 863 FTQDQAWFDQieNYPLVLSKILVNNISDMRNMISSLIEEVFIAFTMAIIGIAWSFATGWRLAAVLVAVSPILCLTSRMFS 942
Cdd:cd18557 80 LRQEIAFFDK--HKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 943 YIYVSTERMCQDVVISTTSILHKTIVNLDTIKGYSVLSFFRENHKNSLRKSWEAFKRRAFWTSLGFAINNSLLYF-VRAL 1021
Cdd:cd18557 158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLsLLLV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 162312251 1022 LFYCSSIFISKEFyTVEQMVQVLsLATFTLLMASTCIMSL 1061
Cdd:cd18557 238 LWYGGYLVLSGQL-TVGELTSFI-LYTIMVASSVGGLSSL 275
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1117-1307 |
1.02e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.97 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP----SEDIYIDGYPLTNIDTNWLLKK-VAIVDQK----PHLlg 1187
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgsyEGEILFDGEVCRFKDIRDSEALgIVIIHQElaliPYL-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1188 sTILESLLYGVDRDINSVMD---ALDKT--YMTEViqnlpnGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDEC 1262
Cdd:NF040905 94 -SIAENIFLGNERAKRGVIDwneTNRRAreLLAKV------GLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 162312251 1263 TSALDSKSS-----LLLEKTIQNLSCtvLIITHQ-PSLMKLADRIIVMDSG 1307
Cdd:NF040905 167 TAALNEEDSaalldLLLELKAQGITS--IIISHKlNEIRRVADSITVLRDG 215
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
467-639 |
1.31e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.22 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 467 IIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEID---EHVLGSTITLVCQQP---------VifdMTIRENIIMRN 534
Cdd:PRK11308 46 VVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNPygslnprkkV---GQILEEPLLIN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 535 ENASESDFEE-----VCRLALVDEFALTFDQSYdtpckeaslSGGQQQRIALARALLRDTEILILDEPTSALDPITK--- 606
Cdd:PRK11308 123 TSLSAAERREkalamMAKVGLRPEHYDRYPHMF---------SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQaqv 193
|
170 180 190
....*....|....*....|....*....|....*..
gi 162312251 607 -NLVMDAIRAHrkGKTTLVITHDMS---QINNDELVL 639
Cdd:PRK11308 194 lNLMMDLQQEL--GLSYVFISHDLSvveHIADEVMVM 228
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
462-643 |
1.47e-10 |
|
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: 60.85 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTFISLLLRYFSPTYGNIylddfpleeidehvlgstitlvcqqpVIFDMtireniimrnenaseSD 541
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDG---------------ED 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 542 FEEVCRLALVDEFALTfdqsydtpcKEASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIR------- 614
Cdd:smart00382 41 ILEEVLDQLLLIIVGG---------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllll 111
|
170 180
....*....|....*....|....*....
gi 162312251 615 AHRKGKTTLVITHDMSQINNDELVLVIDK 643
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
430-642 |
1.48e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 65.54 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 430 ERGFRFDNVSFAYPSRDenlfSLIN-VSVFIPFGELVHIIGPSGSGKSTFISLLLRYFsPTYGniylddfPLEEIDEHvl 508
Cdd:TIGR00954 449 DNGIKFENIPLVTPNGD----VLIEsLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYG-------GRLTKPAK-- 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 509 gSTITLVCQQPVIFDMTIRENII-------MRNENASESDFEEVcrLALVD-EFALTFDQSYDTPC--KEAsLSGGQQQR 578
Cdd:TIGR00954 515 -GKLFYVPQRPYMTLGTLRDQIIypdssedMKRRGLSDKDLEQI--LDNVQlTHILEREGGWSAVQdwMDV-LSGGEKQR 590
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 579 IALARALLRDTEILILDEPTSALDPITKNLVMDAIRahRKGKTTLVITHDMSQINNDELVLVID 642
Cdd:TIGR00954 591 IAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCR--EFGITLFSVSHRKSLWKYHEYLLYMD 652
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
445-645 |
1.54e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 61.57 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 445 RDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLryfsptygniylddfplEEIDEHVLGSTITLVCQQPVIFdm 524
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL-----------------YASGKARLISFLPKFSRNKLIF-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 525 tireniimrnenasesdfeeVCRLALVDEFALTfdqsYDTPCKEAS-LSGGQQQRIALARALLRDTE--ILILDEPTSAL 601
Cdd:cd03238 65 --------------------IDQLQFLIDVGLG----YLTLGQKLStLSGGELQRVKLASELFSEPPgtLFILDEPSTGL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 162312251 602 DPITKNLVMDAIRAHR-KGKTTLVITHDMSQINN-DELvlvIDKGH 645
Cdd:cd03238 121 HQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSaDWI---IDFGP 163
|
|
| urea_trans_UrtD |
TIGR03411 |
urea ABC transporter, ATP-binding protein UrtD; Members of this protein family are ABC ... |
454-629 |
1.71e-10 |
|
urea ABC transporter, ATP-binding protein UrtD; 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: 274568 [Multi-domain] Cd Length: 242 Bit Score: 62.96 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHV---LGstITLVCQQPVIF-DMTIREN 529
Cdd:TIGR03411 20 DLSLYVDPGELRVIIGPNGAGKTTMMDVITGKTRPDEGSVLFGGTDLTGLPEHQiarAG--IGRKFQKPTVFeNLTVFEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 530 IIM--------------RNENASESDFEEVCRL----ALVDEFAltfdqsydtpckeASLSGGQQQRIALARALLRDTEI 591
Cdd:TIGR03411 98 LELalprdksvfaslffRLSAEEKDRIEEVLETiglaDEADRLA-------------GLLSHGQKQWLEIGMLLMQDPKL 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 162312251 592 LILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDM 629
Cdd:TIGR03411 165 LLLDEPVAGMTDEETEKTAELLKSLAGKHSVVVVEHDM 202
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
467-647 |
1.86e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.13 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 467 IIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGST----ITLVCQQPVIF-DMTIRENII--MRNENASE 539
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPekrrIGYVFQDARLFpHYKVRGNLRygMAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 540 sdFEEVCRL----ALVDEFALTfdqsydtpckeasLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAI-R 614
Cdd:PRK11144 109 --FDKIVALlgiePLLDRYPGS-------------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLeR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 162312251 615 AHRKGKT-TLVITHDMsqinnDEL------VLVIDKGHLI 647
Cdd:PRK11144 174 LAREINIpILYVSHSL-----DEIlrladrVVVLEQGKVK 208
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1120-1292 |
2.00e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.81 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1120 NVSLSIEAREKVAIVGISGSGKSTLVELL---------RKTYPSEDIYIDGYPLtniDTNWLLKKVAIvdqKPHLlgsTI 1190
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIagllppaagTIKLDGGDIDDPDVAE---ACHYLGHRNAM---KPAL---TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1191 LESL-----LYGvdRDINSVMDALDKTymteviqNLPNGLDTPllefSKNFSGGQIQRLAFARALLRNPRLLILDECTSA 1265
Cdd:PRK13539 91 AENLefwaaFLG--GEELDIAAALEAV-------GLAPLAHLP----FGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180 190
....*....|....*....|....*....|
gi 162312251 1266 LDSKSSLLLEKTIQ---NLSCTVLIITHQP 1292
Cdd:PRK13539 158 LDAAAVALFAELIRahlAQGGIVIAATHIP 187
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
105-397 |
2.09e-10 |
|
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: 63.33 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 105 FGTLIFTCLSAALEPLMTwttGKVFDALSQyatsqitlGKMISLINFNSLLITIFGLASCVFSfGVR-FLWQYLSAIAGK 183
Cdd:cd18572 2 FVFLVVAALSELAIPHYT---GAVIDAVVA--------DGSREAFYRAVLLLLLLSVLSGLFS-GLRgGCFSYAGTRLVR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 184 RARSLCFHVLSSKSSTFYSLTES---KSGLVNSVDRCIQfyekSISLPMFHIAENLAISLSCLIISFRYSWSLTLVVLAS 260
Cdd:cd18572 70 RLRRDLFRSLLRQDIAFFDATKTgelTSRLTSDCQKVSD----PLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFIT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 261 YPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSFLDAFQGGV 340
Cdd:cd18572 146 VPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAV 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 341 SQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTVFGSCLSVASSLQQILPAIPDLIKG 397
Cdd:cd18572 226 NTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQA 282
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1099-1307 |
2.34e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.29 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKST-LVELLRKTYP-SEDIYIDGYPLTNiDTNWLLKKV 1176
Cdd:PRK13537 8 IDFRNVEKRYGD----KLVVDGLSFHVQRGECFGLLGPNGAGKTTtLRMLLGLTHPdAGSISLCGEPVPS-RARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1177 AIVDQKPHLLGS-TILESLLygvdrdINSVMDALDKTYMTEVIQnlpngldtPLLEFSK----------NFSGGQIQRLA 1245
Cdd:PRK13537 83 GVVPQFDNLDPDfTVRENLL------VFGRYFGLSAAAARALVP--------PLLEFAKlenkadakvgELSGGMKRRLT 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 1246 FARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSC---TVLIITH-QPSLMKLADRIIVMDSG 1307
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLArgkTILLTTHfMEEAERLCDRLCVIEEG 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1119-1310 |
2.41e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1119 NNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP---SEDIYIDGYPLTnIDT--NWLLKKVAIV--DQKPHLL----- 1186
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgrwEGEIFIDGKPVK-IRNpqQAIAQGIAMVpeDRKRDGIvpvmg 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1187 -GSTILESLLygvDR--DINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSkNFSGGQIQRLAFARALLRNPRLLILDECT 1263
Cdd:PRK13549 358 vGKNITLAAL---DRftGGSRIDDAAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 162312251 1264 SALDSKSSLLLEKTIQNLS----CTVLIITHQPSLMKLADRIIVMDSGIVK 1310
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQLVqqgvAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
104-387 |
2.43e-10 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 63.21 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 104 IFGTLIFTCLSAALEPLMTWTTGKVFDalsqyatsQITLGKMISLINFNSLLITIFGLASCVFSFGVRFLWQYLSAIAGK 183
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLD--------DIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 184 RARSLCFHVLSSKSSTFYSlTESKSGLVNSV--DrcIQFYEKSISLPMFHIAENLAISLSCLIISFRYSWSLTLVVLASY 261
Cdd:cd18552 73 DLRNDLFDKLLRLPLSFFD-RNSSGDLISRItnD--VNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 262 PIIILVVGFINSFLssayekdRKSSEKA-------ASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSFLD 334
Cdd:cd18552 150 PLAALPIRRIGKRL-------RKISRRSqesmgdlTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARAR 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 162312251 335 AFQGGVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTVFGSCLSVASSLQQI 387
Cdd:cd18552 223 ALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRL 275
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1117-1310 |
3.11e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.44 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRK-TYPSE--------DIYIDGYPLTNIDTNWLLKKVAIVDQK----P 1183
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGvLEPTSgevnvrvgDEWVDMTKPGPDGRGRAKRYIGILHQEydlyP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1184 HllgSTILESLLYGVDRDIN---SVMDAL--------DKTYMTEVIQNLPNGLdtpllefsknfSGGQIQRLAFARALLR 1252
Cdd:TIGR03269 379 H---RTVLDNLTEAIGLELPdelARMKAVitlkmvgfDEEKAEEILDKYPDEL-----------SEGERHRVALAQVLIK 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1253 NPRLLILDECTSALDSKSSLLLEKTIQN----LSCTVLIITHQPS-LMKLADRIIVMDSG-IVK 1310
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHSILKareeMEQTFIIVSHDMDfVLDVCDRAALMRDGkIVK 508
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1112-1292 |
3.58e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 60.97 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1112 ERNHLAL-NNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTNIDTNWLlKKVAIVDQKPHLLGS 1188
Cdd:cd03231 9 ERDGRALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLagRVLLNGGPLDFQRDSIA-RGLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1189 -TILESL-LYGVDRDINSVMDALDKTYMTEViQNLPNGldtpllefskNFSGGQIQRLAFARALLRNPRLLILDECTSAL 1266
Cdd:cd03231 88 lSVLENLrFWHADHSDEQVEEALARVGLNGF-EDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*....
gi 162312251 1267 DSKS-SLLLEKTIQNLSC--TVLIITHQP 1292
Cdd:cd03231 157 DKAGvARFAEAMAGHCARggMVVLTTHQD 185
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
454-655 |
4.58e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 61.64 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSP----TYGNIYLDDFPLEEIDehVLGSTITLVCQQP-----VIFDM 524
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCA--LRGRKIATIMQNPrsafnPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 525 T--IRENIIMRNENASESDFEEVCRLALVDEfALTFDQSYdtpckEASLSGGQQQRIALARALLRDTEILILDEPTSALD 602
Cdd:PRK10418 99 HthARETCLALGKPADDATLTAALEAVGLEN-AARVLKLY-----PFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 603 PITKNLVMDAIRA--HRKGKTTLVITHDM---SQINNDelVLVIDKGHLIQRCARKEL 655
Cdd:PRK10418 173 VVAQARILDLLESivQKRALGMLLVTHDMgvvARLADD--VAVMSHGRIVEQGDVETL 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
467-647 |
5.84e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.56 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 467 IIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLG--STITLVCQQP--VIFDMTIRENII--MRNENASEs 540
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrQQVATVFQDPeqQIFYTDIDSDIAfsLRNLGVPE- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 541 dfEEVCR-----LALVDefALTFDQSydtPCKeaSLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAI-R 614
Cdd:PRK13638 111 --AEITRrvdeaLTLVD--AQHFRHQ---PIQ--CLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIrR 181
|
170 180 190
....*....|....*....|....*....|....
gi 162312251 615 AHRKGKTTLVITHDMSQINN-DELVLVIDKGHLI 647
Cdd:PRK13638 182 IVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQIL 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1108-1321 |
7.17e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1108 YPDSERNhlaLNNVSLSIEA-----REKVAIVGISGSGKSTLVELLR-KTYPSEdiyidGYPLTNIDtnwllkkvaiVDQ 1181
Cdd:PRK13409 343 YPDLTKK---LGDFSLEVEGgeiyeGEVIGIVGPNGIGKTTFAKLLAgVLKPDE-----GEVDPELK----------ISY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1182 KPHLLGSTI---LESLLYGVDRDINSVMdaldktYMTEVIQNLpnGLDtPLLEFS-KNFSGGQIQRLAFARALLRNPRLL 1257
Cdd:PRK13409 405 KPQYIKPDYdgtVEDLLRSITDDLGSSY------YKSEIIKPL--QLE-RLLDKNvKDLSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1258 ILDECTSALDSKSSLLLEKTIQNL----SCTVLIITHQPSLMK-LADRIIVMD-----SGIVKESGSFDELMNR 1321
Cdd:PRK13409 476 LLDEPSAHLDVEQRLAVAKAIRRIaeerEATALVVDHDIYMIDyISDRLMVFEgepgkHGHASGPMDMREGMNR 549
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1108-1321 |
7.31e-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: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1108 YPDSERNhlaLNNVSLSIEA-----REKVAIVGISGSGKSTLVELLRKtypsediyidgypLTNIDTNWLLKKVAIvDQK 1182
Cdd:COG1245 344 YPDLTKS---YGGFSLEVEGgeireGEVLGIVGPNGIGKTTFAKILAG-------------VLKPDEGEVDEDLKI-SYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1183 PHLLGSTI---LESLLYGVdrdINSVMDalDKTYMTEVIQNLpnGLDtPLLEFS-KNFSGGQIQRLAFARALLRNPRLLI 1258
Cdd:COG1245 407 PQYISPDYdgtVEEFLRSA---NTDDFG--SSYYKTEIIKPL--GLE-KLLDKNvKDLSGGELQRVAIAACLSRDADLYL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 1259 LDECTSALDSKSSLLLEKTIQNL----SCTVLIITHQPSLMKL-ADRIIVMD-----SGIVKESGSFDELMNR 1321
Cdd:COG1245 479 LDEPSAHLDVEQRLAVAKAIRRFaenrGKTAMVVDHDIYLIDYiSDRLMVFEgepgvHGHASGPMDMREGMNR 551
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
436-630 |
8.09e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.19 E-value: 8.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 436 DNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKS-TFISLLLRYFSP----TYGNIYLDDFPLEEIDE----H 506
Cdd:PRK15134 9 ENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEqtlrG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 507 VLGSTITLVCQQPVIFD---MTIRENII--------MRNENA-SE--SDFEEVC------RLAlvdefaltfdqsyDTPC 566
Cdd:PRK15134 89 VRGNKIAMIFQEPMVSLnplHTLEKQLYevlslhrgMRREAArGEilNCLDRVGirqaakRLT-------------DYPH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 567 KeasLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDMS 630
Cdd:PRK15134 156 Q---LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLS 218
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1232-1324 |
1.18e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.36 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1232 FSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSL----LLEKTIQNLSCTVLIITHQPSLM-KLADRIIVMDS 1306
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAqifrLLTRLNQNNNTTILLISHDLQMLsQWADKINVLYC 234
|
90
....*....|....*...
gi 162312251 1307 GIVKESGSFDELMNRHTH 1324
Cdd:PRK15093 235 GQTVETAPSKELVTTPHH 252
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
452-628 |
1.24e-09 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 59.96 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKST--FISLL----LRYFS--PTYGNIYLDDFPLEEIDeHVLGSTITLVCQQPvifd 523
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSlaFDTIYaegqRRYVEslSAYARQFLGQMDKPDVD-SIEGLSPAIAIDQK---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 524 mTIRENIimRNENASESDFEEVCRL--ALVD-----EFALTFDQSYDTPCKEA-SLSGGQQQRIALARALLRD-TEIL-I 593
Cdd:cd03270 86 -TTSRNP--RSTVGTVTEIYDYLRLlfARVGirerlGFLVDVGLGYLTLSRSApTLSGGEAQRIRLATQIGSGlTGVLyV 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 162312251 594 LDEPTSALDPITKNLVMDAIRAHR-KGKTTLVITHD 628
Cdd:cd03270 163 LDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHD 198
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1092-1313 |
1.48e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.57 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1092 KFPLVGKIeFDGVSfaypdseRNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGyplTNIDT 1169
Cdd:PRK10261 322 RFPLRSGL-LNRVT-------REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQggEIIFNG---QRIDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1170 ------NWLLKKVAIVDQKP-------HLLGSTILESLLygVDRDINSVMDALDKTYMTEVIQNLPNGLdtplLEFSKNF 1236
Cdd:PRK10261 391 lspgklQALRRDIQFIFQDPyasldprQTVGDSIMEPLR--VHGLLPGKAAAARVAWLLERVGLLPEHA----WRYPHEF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1237 SGGQIQRLAFARALLRNPRLLILDECTSALDSKS-----SLLLEKTiQNLSCTVLIITHQPSLM-KLADRIIVMDSGIVK 1310
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIrgqiiNLLLDLQ-RDFGIAYLFISHDMAVVeRISHRVAVMYLGQIV 543
|
...
gi 162312251 1311 ESG 1313
Cdd:PRK10261 544 EIG 546
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
452-634 |
1.56e-09 |
|
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: 60.32 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFIS-----LLLRYFspTYGNIYLDDFPLEEIDEHVlgSTITLVCQQPV------ 520
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypALARRL--HLKKEQPGNHDRIEGLEHI--DKVIVIDQSPIgrtprs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 521 -------IFDmTIRENiimrnenasesdFEEVCRLALVDEFAL-------TFDQSYDTPCKEA----------------- 569
Cdd:cd03271 87 npatytgVFD-EIREL------------FCEVCKGKRYNRETLevrykgkSIADVLDMTVEEAleffenipkiarklqtl 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 570 ---------------SLSGGQQQRIALARALL-RDT--EILILDEPTSAL--DPITKNL-VMDAIRAhrKGKTTLVITHD 628
Cdd:cd03271 154 cdvglgyiklgqpatTLSGGEAQRIKLAKELSkRSTgkTLYILDEPTTGLhfHDVKKLLeVLQRLVD--KGNTVVVIEHN 231
|
....*.
gi 162312251 629 MSQINN 634
Cdd:cd03271 232 LDVIKC 237
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
437-648 |
1.56e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.18 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 437 NVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLE-------EIDE---- 505
Cdd:PRK10261 17 NLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrsrqviELSEqsaa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 506 ---HVLGSTITLVCQQPV-----IFDM--TIRENIIMRNENASESDFEEVCRlaLVDEFALTFDQSYDTPCKEaSLSGGQ 575
Cdd:PRK10261 97 qmrHVRGADMAMIFQEPMtslnpVFTVgeQIAESIRLHQGASREEAMVEAKR--MLDQVRIPEAQTILSRYPH-QLSGGM 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 576 QQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLV--ITHDMSQINN-DELVLVIDKGHLIQ 648
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVAEiADRVLVMYQGEAVE 249
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1097-1290 |
1.72e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1097 GKIEFD--GVSFAYPDSErnhlALNNVSLSIEAREKVAIVGISGSGKSTLVEL-LRKTYP-SEDIYIDgyplTNIDtnwl 1172
Cdd:PRK11147 316 GKIVFEmeNVNYQIDGKQ----LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQAdSGRIHCG----TKLE---- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1173 lkkVAIVDQKPHLLG--STILESL--------LYGVDRDINSVM-DAL--DKTYMTEViqnlpngldtpllefsKNFSGG 1239
Cdd:PRK11147 384 ---VAYFDQHRAELDpeKTVMDNLaegkqevmVNGRPRHVLGYLqDFLfhPKRAMTPV----------------KALSGG 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 162312251 1240 QIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSCTVLIITH 1290
Cdd:PRK11147 445 ERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSH 495
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
462-633 |
2.24e-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: 57.97 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDdfpleeidehvlGSTITLVCQQpvifdmtireniimrnenasesd 541
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD------------GITPVYKPQY----------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 542 feevcrlalvdefaltfdqsydtpckeASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIR--AHRKG 619
Cdd:cd03222 70 ---------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRrlSEEGK 122
|
170
....*....|....
gi 162312251 620 KTTLVITHDMSQIN 633
Cdd:cd03222 123 KTALVVEHDLAVLD 136
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
434-629 |
3.16e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.36 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRDenlfSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIylddfpleeidEHVLGSTIT 513
Cdd:PRK09544 6 SLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 514 LVCQQpVIFDMTIR---ENIIMRNENASESDFEEVcrLALVDEFALtfdqsYDTPCKEasLSGGQQQRIALARALLRDTE 590
Cdd:PRK09544 71 YVPQK-LYLDTTLPltvNRFLRLRPGTKKEDILPA--LKRVQAGHL-----IDAPMQK--LSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 162312251 591 ILILDEPTSALDPITKNLVMDAIRAHRK--GKTTLVITHDM 629
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDL 181
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1099-1305 |
3.37e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 61.30 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSErnhLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPsediyIDGYPLTNIDTNwllkKVAI 1178
Cdd:TIGR00954 452 IKFENIPLVTPNGD---VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP-----VYGGRLTKPAKG----KLFY 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1179 VDQKPHLLGSTILESLLY----------GV-DRDINSVMDALDKTYMTEviqnlPNGLDTPLLEFSKNFSGGQIQRLAFA 1247
Cdd:TIGR00954 520 VPQRPYMTLGTLRDQIIYpdssedmkrrGLsDKDLEQILDNVQLTHILE-----REGGWSAVQDWMDVLSGGEKQRIAMA 594
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1248 RALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSCTVLIITHQPSLMKLADRIIVMD 1305
Cdd:TIGR00954 595 RLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMD 652
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
462-629 |
3.59e-09 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 59.07 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDD--------FPLEEIDEHVLGST-ITLVCQQP---VIFDMTIREN 529
Cdd:TIGR02323 29 GEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaelelYQLSEAERRRLMRTeWGFVHQNPrdgLRMRVSAGAN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 530 IIMRNENASESDFEEVcRLALVD---EFALTFDQSYDTPckeASLSGGQQQRIALARALLRDTEILILDEPTSALDPITK 606
Cdd:TIGR02323 109 IGERLMAIGARHYGNI-RATAQDwleEVEIDPTRIDDLP---RAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQ 184
|
170 180
....*....|....*....|....*
gi 162312251 607 NLVMDAIRA--HRKGKTTLVITHDM 629
Cdd:TIGR02323 185 ARLLDLLRGlvRDLGLAVIIVTHDL 209
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1118-1302 |
3.77e-09 |
|
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: 59.17 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLV-ELL----------RKTYPSEDIYIDGypLTNIDtnwllkKVAIVDQKPhlL 1186
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLInDTLypalarrlhlKKEQPGNHDRIEG--LEHID------KVIVIDQSP--I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1187 GST-------------------------------ILESLLYGvdrdiNSVMDALDktyMT-----EVIQNLPN------- 1223
Cdd:cd03271 81 GRTprsnpatytgvfdeirelfcevckgkrynreTLEVRYKG-----KSIADVLD---MTveealEFFENIPKiarklqt 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1224 ----GLD-TPLLEFSKNFSGGQIQRLAFARALLR---NPRLLILDECTSAL---DSKSSLLLEKTIQNLSCTVLIITHQP 1292
Cdd:cd03271 153 lcdvGLGyIKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLhfhDVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
250
....*....|
gi 162312251 1293 SLMKLADRII 1302
Cdd:cd03271 233 DVIKCADWII 242
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1132-1307 |
4.08e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.40 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1132 AIVGISGSGKSTLVELL--RKT--YPSEDIYIDGYPlTNIDTnwLLKKVAIVDQKP-HLLGSTILESLLYG--------V 1198
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLagRKTggYIEGDIRISGFP-KKQET--FARISGYCEQNDiHSPQVTVRESLIYSaflrlpkeV 986
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1199 DRD-----INSVMDALDKTYMTEVIQNLP--NGLDTPllefsknfsggQIQRLAFARALLRNPRLLILDECTSALDSKSS 1271
Cdd:PLN03140 987 SKEekmmfVDEVMELVELDNLKDAIVGLPgvTGLSTE-----------QRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1055
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 162312251 1272 LLLEKTIQN---LSCTVLIITHQPS--LMKLADRIIVMDSG 1307
Cdd:PLN03140 1056 AIVMRTVRNtvdTGRTVVCTIHQPSidIFEAFDELLLMKRG 1096
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1112-1292 |
5.02e-09 |
|
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: 57.75 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1112 ERNHLAL-NNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTNIDTN------WLLKKVAIvdqK 1182
Cdd:TIGR01189 9 SRGERMLfEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDsgEVRWNGTPLAEQRDEphenilYLGHLPGL---K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1183 PHLlgsTILESL------LYGVDRDINsvmDALDKTYMTEvIQNLPNGldtpllefskNFSGGQIQRLAFARALLRNPRL 1256
Cdd:TIGR01189 86 PEL---SALENLhfwaaiHGGAQRTIE---DALAAVGLTG-FEDLPAA----------QLSAGQQRRLALARLWLSRRPL 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 162312251 1257 LILDECTSALDSKSSLLLEKTIQNLSCT---VLIITHQP 1292
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLRAHLARggiVLLTTHQD 187
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
235-387 |
5.12e-09 |
|
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: 59.14 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 235 NLAISLSCLIISFRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYR 314
Cdd:cd18782 125 DVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARW 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 315 YFADACSTSSKSFLRFSFLDAFQGGVSQFF--LYSVFFqgLWFGNHLATTKRVNVGQVVT-------VFGSCLSVASSLQ 385
Cdd:cd18782 205 RWQNRYARSLGEGFKLTVLGTTSGSLSQFLnkLSSLLV--LWVGAYLVLRGELTLGQLIAfrilsgyVTGPILRLSTLWQ 282
|
..
gi 162312251 386 QI 387
Cdd:cd18782 283 QF 284
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1117-1311 |
5.57e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.42 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELL----RKTypSEDIYIDGYPLTnIDTNW--LLKKVAIV--DQKPH--LL 1186
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALfgadPAD--SGEIRLDGKPVR-IRSPRdaIRAGIAYVpeDRKGEglVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1187 GSTILESLLYGVDRDI--NSVMD-ALDKTYMTEVIQNL---PNGLDTPLlefsKNFSGG-QiQRLAFARALLRNPRLLIL 1259
Cdd:COG1129 344 DLSIRENITLASLDRLsrGGLLDrRRERALAEEYIKRLrikTPSPEQPV----GNLSGGnQ-QKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 1260 DECTSALD--SKSSLLleKTIQNLS---CTVLIIThqpS----LMKLADRIIVMDSG-IVKE 1311
Cdd:COG1129 419 DEPTRGIDvgAKAEIY--RLIRELAaegKAVIVIS---SelpeLLGLSDRILVMREGrIVGE 475
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
454-663 |
6.08e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.25 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGS---TITLVCQQPVI-FD--MTIR 527
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrrDIQFIFQDPYAsLDprQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 528 ENII--------MRNENASESDFEEVCRLALVDEFALTFDQSYdtpckeaslSGGQQQRIALARALLRDTEILILDEPTS 599
Cdd:PRK10261 422 DSIMeplrvhglLPGKAAAARVAWLLERVGLLPEHAWRYPHEF---------SGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 600 ALDPITK----NLVMDAIRahRKGKTTLVITHDMSQINN-DELVLVIDKGHLIQRCARKELvlfedFEN 663
Cdd:PRK10261 493 ALDVSIRgqiiNLLLDLQR--DFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAV-----FEN 554
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
527-647 |
6.84e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.36 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 527 RENIIM--RNENASESDFEevcrlALVDEFALTFDQSYDTPCKEASLSGGQQQRIALARALLRDTEILILDEPTSALDPI 604
Cdd:NF000106 104 RENLYMigR*LDLSRKDAR-----ARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 162312251 605 TKNLVMDAIRAH-RKGKTTLVITHDMSQINN--DELVlVIDKGHLI 647
Cdd:NF000106 179 TRNEVWDEVRSMvRDGATVLLTTQYMEEAEQlaHELT-VIDRGRVI 223
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1115-1327 |
6.94e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.90 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1115 HLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRK-TYPSEDiyidgypltNIDTNWLLKKVAIvdqkphllgSTILES 1193
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGvTMPNKG---------TVDIKGSAALIAI---------SSGLNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1194 LLYGVDR-DINSVMDALDKTYMTEVIQNlpngldtpLLEFS----------KNFSGGQIQRLAFARALLRNPRLLILDEC 1262
Cdd:PRK13545 99 QLTGIENiELKGLMMGLTKEKIKEIIPE--------IIEFAdigkfiyqpvKTYSSGMKSRLGFAISVHINPDILVIDEA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1263 TSALD---SKSSLLLEKTIQNLSCTVLIITHQPSLMK-LADRIIVMDSGIVKESGSFDELMNRHTHFWK 1327
Cdd:PRK13545 171 LSVGDqtfTKKCLDKMNEFKEQGKTIFFISHSLSQVKsFCTKALWLHYGQVKEYGDIKEVVDHYDEFLK 239
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1112-1307 |
7.94e-09 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 57.65 E-value: 7.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1112 ERNhlaLNNVSLSIEAREKVAIVGISGSGKSTLV-ELL----RKTY-----PSEDIYIDGYPLTNIDTNWLLKKVAIVDQ 1181
Cdd:cd03270 8 EHN---LKNVDVDIPRNKLVVITGVSGSGKSSLAfDTIyaegQRRYveslsAYARQFLGQMDKPDVDSIEGLSPAIAIDQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1182 K-----PHLLGSTILE-----SLLY---GVDRDINSVMDAldktymteviqnlpnGLDTPLLEFSKN-FSGGQIQRLAFA 1247
Cdd:cd03270 85 KttsrnPRSTVGTVTEiydylRLLFarvGIRERLGFLVDV---------------GLGYLTLSRSAPtLSGGEAQRIRLA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1248 RALLRNPR--LLILDECTSALDSKSSLLLEKTIQNL---SCTVLIITHQPSLMKLADRIIVMDSG 1307
Cdd:cd03270 150 TQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLrdlGNTVLVVEHDEDTIRAADHVIDIGPG 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
454-646 |
8.90e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.45 E-value: 8.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFISLLL-RYFSPTYGNIYLDDFPLE-EIDEHVLGSTITLVCQ----QPVIFDMTIR 527
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFgAYPGKFEGNVFINGKPVDiRNPAQAIRAGIAMVPEdrkrHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 528 ENI----------IMRNENASESDF--EEVCRLALVdefalTFdqSYDTPCkeASLSGGQQQRIALARALLRDTEILILD 595
Cdd:TIGR02633 358 KNItlsvlksfcfKMRIDAAAELQIigSAIQRLKVK-----TA--SPFLPI--GRLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 162312251 596 EPTSALDPITKNLVMDAIRA-HRKGKTTLVITHDMSQI-NNDELVLVIDKGHL 646
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVlGLSDRVLVIGEGKL 481
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1104-1307 |
9.72e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 56.89 E-value: 9.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1104 VSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELL---RKTY--PSEDIYIDGYPltnidtnwllkkVAI 1178
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNvsVEGDIHYNGIP------------YKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1179 VDQKPHllgstilESLLYGVDRDINSvmdaldkTYMTeVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLI 1258
Cdd:cd03233 77 FAEKYP-------GEIIYVSEEDVHF-------PTLT-VRETLDFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1259 LDECTSALDSKSSLLLEKTIQNLS----CTVLIITHQPS--LMKLADRIIVMDSG 1307
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMAdvlkTTTFVSLYQASdeIYDLFDKVLVLYEG 196
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1114-1320 |
1.23e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.25 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1114 NHLALNN----VSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE-DIYIDGYPLTNIDTNWLLKKVAIVDQ--KP--- 1183
Cdd:PRK03695 4 NDVAVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSgSIQFAGQPLEAWSAAELARHRAYLSQqqTPpfa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1184 ----HLLgstileSLLYGVDRDINSVMDALDktymtEVIQNLpnGLDTPLLEFSKNFSGGQIQRLAFARALLR-----NP 1254
Cdd:PRK03695 84 mpvfQYL------TLHQPDKTRTEAVASALN-----EVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1255 --RLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHqpSL---MKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:PRK03695 151 agQLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSH--DLnhtLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1117-1320 |
1.70e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.64 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSEDIYIDgypLTNIDTNWLLKKVA------IVDQKPHLLGS-T 1189
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT---INNINYNKLDHKLAaqlgigIIYQELSVIDElT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1190 ILESLLYG--VDRDINSVmDALDKTYMTEVIQNLPN--GLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSA 1265
Cdd:PRK09700 97 VLENLYIGrhLTKKVCGV-NIIDWREMRVRAAMMLLrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 1266 LDSKSS---LLLEKTIQNLSCTVLIITHQ-PSLMKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:PRK09700 176 LTNKEVdylFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDGSSVCSGMVSDVSN 234
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1118-1314 |
1.80e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.96 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELlrktypsediyIDGYPLTNI-DTNWLLKKVAIVDQKPHL---LGstILES 1193
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKV-----------IAGHPAYKIlEGDILFKGESILDLEPEErahLG--IFLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1194 LLYGVDrdINSV--MDALDKTYMT-EVIQNLPN-----------------GLDTPLLEFSKN--FSGGQIQRLAFARALL 1251
Cdd:CHL00131 90 FQYPIE--IPGVsnADFLRLAYNSkRKFQGLPEldplefleiineklklvGMDPSFLSRNVNegFSGGEKKRNEILQMAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1252 RNPRLLILDECTSALDSKSSLLLEKTIQNLSCT---VLIITHQPSLMK--LADRIIVMDSGIVKESGS 1314
Cdd:CHL00131 168 LDSELAILDETDSGLDIDALKIIAEGINKLMTSensIILITHYQRLLDyiKPDYVHVMQNGKIIKTGD 235
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1099-1313 |
2.20e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.81 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYpdseRN-HLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRK--TYPSEDIYIDGYPltnidTNWLLKK 1175
Cdd:PRK15056 7 IVVNDVTVTW----RNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGfvRLASGKISILGQP-----TRQALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1176 --VAIVDQKPHLLGS--TILESLL----YG--------VDRDINSVMDALDKTYMTEVIQNLPNGLdtpllefsknfSGG 1239
Cdd:PRK15056 78 nlVAYVPQSEEVDWSfpVLVEDVVmmgrYGhmgwlrraKKRDRQIVTAALARVDMVEFRHRQIGEL-----------SGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1240 QIQRLAFARALLRNPRLLILDECTSALDSKS-----SLLLEktIQNLSCTVLIITHQ-PSLMKLADrIIVMDSGIVKESG 1313
Cdd:PRK15056 147 QKKRVFLARAIAQQGQVILLDEPFTGVDVKTeariiSLLRE--LRDEGKTMLVSTHNlGSVTEFCD-YTVMVKGTVLASG 223
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
462-630 |
3.47e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.97 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTFISLLL-RYFSPTY-GNIYLDDfplEEIDEHVLGSTiTLVCQQPVIF-DMTIRENII----MRN 534
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAgRIQGNNFtGTILANN---RKPTKQILKRT-GFVTQDDILYpHLTVRETLVfcslLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 535 ENASESDFEEVCRLALVDEFALTfdqsydtPCKEA--------SLSGGQQQRIALARALLRDTEILILDEPTSALDPITK 606
Cdd:PLN03211 170 PKSLTKQEKILVAESVISELGLT-------KCENTiignsfirGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180
....*....|....*....|....*
gi 162312251 607 -NLVMDAIRAHRKGKTTLVITHDMS 630
Cdd:PLN03211 243 yRLVLTLGSLAQKGKTIVTSMHQPS 267
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
434-629 |
3.83e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 434 RFDNVSFAYPSRdenlFSLINVSVFIPFGELVHIIGPSGSGKSTFISLL-----LRYfsptyGNIylddfpleeideHVL 508
Cdd:NF033858 3 RLEGVSHRYGKT----VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIagarkIQQ-----GRV------------EVL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 509 GSTI------TLVCqqPVIFDM------------TIRENIimrnenasesDFeevcrlalvdeFALTFDQSY-------- 562
Cdd:NF033858 62 GGDMadarhrRAVC--PRIAYMpqglgknlyptlSVFENL----------DF-----------FGRLFGQDAaerrrrid 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 563 ------------DTPCkeASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKN----LVmDAIRAHRKGKTTLVIT 626
Cdd:NF033858 119 ellratglapfaDRPA--GKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRqfweLI-DRIRAERPGMSVLVAT 195
|
...
gi 162312251 627 HDM 629
Cdd:NF033858 196 AYM 198
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
108-384 |
4.40e-08 |
|
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: 56.10 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 108 LIFTCLSAALEPLMTWTTGKVFDALSQYATSQITLGKmiSLINFNSLLITIFGLASCVFSFGVRFLWQYLSAIAGKRARS 187
Cdd:cd18780 2 TIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEAL--RALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 188 LCFHVLSSKSSTFYSLTesKSG-LVNSVDRCIQFYEKSISLPMFHIAENLAISLSCLIISFRYSWSLTLVVLASYPIIIL 266
Cdd:cd18780 80 RLFSAIIAQEIAFFDVT--RTGeLLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 267 VVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSFLDA-FQGGVSQFFL 345
Cdd:cd18780 158 GAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGgFNGFMGAAAQ 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 162312251 346 YSVFFQgLWFGNHLATTKRVNVGQVVTVFGSCLSVASSL 384
Cdd:cd18780 238 LAIVLV-LWYGGRLVIDGELTTGLLTSFLLYTLTVAMSF 275
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1118-1313 |
5.07e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 56.77 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTNIDTNWLLKKVAIVDQKPHL---------- 1185
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTagTVLVAGDDVEALSARAASRRVASVPQDTSLsfefdvrqvv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1186 -LGSTILESLLYGVDR-DINSVMDALDKTYMTEVIqnlpnglDTPLLEfsknFSGGQIQRLAFARALLRNPRLLILDECT 1263
Cdd:PRK09536 99 eMGRTPHRSRFDTWTEtDRAAVERAMERTGVAQFA-------DRPVTS----LSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1264 SALD---SKSSLLLEKTIQNLSCTVLIITHQPSL-MKLADRIIVMDSGIVKESG 1313
Cdd:PRK09536 168 ASLDinhQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELVLLADGRVRAAG 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
455-655 |
5.30e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.25 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 455 VSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNI-YL--DDFPLEEIDEHVLGSTITLVCQQPVIF---DMTIRE 528
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLgkDLLGMKDDEWRAVRSDIQMIFQDPLASlnpRMTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 529 NI-----IMRNENASESDFEEVcrLALVDEFALTFDQSYDTPckeASLSGGQQQRIALARALLRDTEILILDEPTSALDP 603
Cdd:PRK15079 120 IIaeplrTYHPKLSRQEVKDRV--KAMMLKVGLLPNLINRYP---HEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 604 ITKNLVMDAIRAHRK--GKTTLVITHDMSQINN-DELVLVIDKGHLIQRCARKEL 655
Cdd:PRK15079 195 SIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
105-372 |
7.69e-08 |
|
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: 55.52 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 105 FGTLIFTCLSAALEPLMTWttgkvfdaLSQYATSQITLGKMISLINFNSLLITIFGLASCVFSFGVRFLWQYLSAIAGKR 184
Cdd:cd18542 2 LLAILALLLATALNLLIPL--------LIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 185 ARSLCFHVLSSKSSTFYSltESKSG-----LVNSVDRCIQFyeksISLPMFHIAENLAISLSCLIISFRYSWSLTLVVLA 259
Cdd:cd18542 74 LRNDLYDHLQRLSFSFHD--KARTGdlmsrCTSDVDTIRRF----LAFGLVELVRAVLLFIGALIIMFSINWKLTLISLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 260 SYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSFLDAFQGG 339
Cdd:cd18542 148 IIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWP 227
|
250 260 270
....*....|....*....|....*....|...
gi 162312251 340 VSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVT 372
Cdd:cd18542 228 LMDFLSGLQIVLVLWVGGYLVINGEITLGELVA 260
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1118-1316 |
8.20e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 8.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTNIDTNWLLKKvAIV----DQKPH--LLGST 1189
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTsgYVTLDGHEVVTRSPQDGLAN-GIVyiseDRKRDglVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1190 ILESLLYGVDRDINSVMDALDKTYMTEVIQN---LPNgLDTPLLEFS-KNFSGGQIQRLAFARALLRNPRLLILDECTSA 1265
Cdd:PRK10762 347 VKENMSLTALRYFSRAGGSLKHADEQQAVSDfirLFN-IKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1266 LD--SKSSL--LLEKTIQNLSCTVLIITHQPSLMKLADRIIVMDSGivKESGSFD 1316
Cdd:PRK10762 426 VDvgAKKEIyqLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG--RISGEFT 478
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
109-386 |
9.64e-08 |
|
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: 55.01 E-value: 9.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 109 IFTCLSAALEPLMTWTTGKVFDAL------SQYATSQITLGkmisLINFNSLLITifGLASCVFSFGVrflwqylsAIAG 182
Cdd:cd18784 3 FFLLAAAVGEIFIPYYTGQVIDGIvieksqDKFSRAIIIMG----LLAIASSVAA--GIRGGLFTLAM--------ARLN 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 183 KRARSLCFHVLSSKSSTFYSltESKSGLVNS---VDRCIQFYEKSISLPMFhiAENLAISLSCLIISFRYSWSLTLVVLA 259
Cdd:cd18784 69 IRIRNLLFRSIVSQEIGFFD--TVKTGDITSrltSDTTTMSDTVSLNLNIF--LRSLVKAIGVIVFMFKLSWQLSLVTLI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 260 SYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSFLDAFQGG 339
Cdd:cd18784 145 GLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVW 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 340 VSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTVF------GSCL----SVASSLQQ 386
Cdd:cd18784 225 SNELTELALTVSTLYYGGHLVITGQISGGNLISFIlyqlelGSCLesvgSVYTGLMQ 281
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
108-384 |
1.06e-07 |
|
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: 55.18 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 108 LIFTCLSAALEPLMTWTTGKVFDAL----SQYATSQITLgkmislinfnsLLITIFGLAScVFSFGVrflwQYLSAIAGK 183
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQLIDAAlgggDTASLNQIAL-----------LLLGLFLLQA-VFSFFR----IYLFARVGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 184 RA----RSLCFHVLSSKSSTFYSltESKSG-----LVNSVDRcIQFYeKSISLPMFhiAENLAISLSCLIISFRYSWSLT 254
Cdd:cd18576 66 RVvadlRKDLYRHLQRLPLSFFH--ERRVGeltsrLSNDVTQ-IQDT-LTTTLAEF--LRQILTLIGGVVLLFFISWKLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 255 LVVLASYPIIILVVGFINSFLssayekdRKSSEK-------AASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSF 327
Cdd:cd18576 140 LLMLATVPVVVLVAVLFGRRI-------RKLSKKvqdelaeANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLA 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 328 LRFSFLDAFQGGVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTVFGSCLSVASSL 384
Cdd:cd18576 213 LKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSI 269
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
782-1024 |
1.77e-07 |
|
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: 54.44 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 782 LLGLLTSLIQGASVPifaYVISKCLNLFMQIDPSIGVA------FWSSMVLVVAAGSGASyFFSHYIFS-----ISAKIw 850
Cdd:cd18573 2 LALLLVSSAVTMSVP---FAIGKLIDVASKESGDIEIFglslktFALALLGVFVVGAAAN-FGRVYLLRiagerIVARL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 851 cdhyRLLAVKVLFTQDQAWFDQ---------IENYPLVLSKILVNNISD-MRNMIsslieevfiaftMAIIGIAWSFATG 920
Cdd:cd18573 77 ----RKRLFKSILRQDAAFFDKnktgelvsrLSSDTSVVGKSLTQNLSDgLRSLV------------SGVGGIGMMLYIS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 921 WRLAAVLVAVSPILCLTSRMFS-YIYVSTERMcQDVVISTTSILHKTIVNLDTIKgysvlSFFRENH-----KNSLRKSW 994
Cdd:cd18573 141 PKLTLVMLLVVPPIAVGAVFYGrYVRKLSKQV-QDALADATKVAEERLSNIRTVR-----AFAAERKeveryAKKVDEVF 214
|
250 260 270
....*....|....*....|....*....|....*
gi 162312251 995 EAFKRRA-----FWTSLGFAINNSLLyfvrALLFY 1024
Cdd:cd18573 215 DLAKKEAlasglFFGSTGFSGNLSLL----SVLYY 245
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
433-647 |
1.81e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.02 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLL-LRYFSPTY-GNIYLDDFPLEEidehVLGS 510
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGVItGEILINGRPLDK----NFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 511 TITLVCQQPVIFDM-TIREniimrnenasesdfeevcrlalvdefALTFDqsydtpCKEASLSGGQQQRIALARALLRDT 589
Cdd:cd03232 80 STGYVEQQDVHSPNlTVRE--------------------------ALRFS------ALLRGLSVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 590 EILILDEPTSALDPITKNLVMDAIRA-HRKGKTTLVITHDMSQI---NNDELVLVIDKGHLI 647
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSASifeKFDRLLLLKRGGKTV 189
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
452-628 |
2.10e-07 |
|
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: 51.98 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTfislllryfsptygniYLDDfpleeidehvlgstitlvcqqpVIFDMTIRENII 531
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKST----------------ILDA----------------------IGLALGGAQSAT 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 532 MRNENASESDFEevcrlALVD-EFALTFDQsydtpckeasLSGGQQQRIALARAL----LRDTEILILDEPTSALDPITK 606
Cdd:cd03227 53 RRRSGVKAGCIV-----AAVSaELIFTRLQ----------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDG 117
|
170 180
....*....|....*....|...
gi 162312251 607 NLVMDAIRAHRKGKTT-LVITHD 628
Cdd:cd03227 118 QALAEAILEHLVKGAQvIVITHL 140
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
235-398 |
2.26e-07 |
|
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: 54.09 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 235 NLAISLSCLIISFRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYR 314
Cdd:cd18574 126 SVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 315 YFADACSTSSKSFLRFSF-LDAFQGGvSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTVFGSCLSVASSLQQILPAIPD 393
Cdd:cd18574 206 LYEEEVEKAAKLNEKLGLgIGIFQGL-SNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQ 284
|
....*
gi 162312251 394 LIKGK 398
Cdd:cd18574 285 YVKGK 289
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
435-642 |
2.75e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 435 FDNVSFAYPSrDENLFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIY------LDDFPLEEIDEHVL 508
Cdd:PLN03073 511 FSDASFGYPG-GPLLFK--NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrMAVFSQHHVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 509 GSTitlvcqqPVIFDMTIRENIIMRNENASESDFEEVCRLALvdefaltfdQSYDTpckeasLSGGQQQRIALARALLRD 588
Cdd:PLN03073 588 SSN-------PLLYMMRCFPGVPEQKLRAHLGSFGVTGNLAL---------QPMYT------LSGGQKSRVAFAKITFKK 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312251 589 TEILILDEPTSALDpitknlvMDAIRAHRKGKT-----TLVITHDMSQINN--DELVLVID 642
Cdd:PLN03073 646 PHILLLDEPSNHLD-------LDAVEALIQGLVlfqggVLMVSHDEHLISGsvDELWVVSE 699
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
454-602 |
2.83e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKS-TFISLLLRYFSPTYGNIYLDDFPLE-EIDEHVLGSTITLVC----QQPVIFDMTIR 527
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPVKiRNPQQAIAQGIAMVPedrkRDGIVPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 528 ENIIMrnenaseSDFEEVCRLALVDEFA--LTFDQSYD-----TPCKE---ASLSGGQQQRIALARALLRDTEILILDEP 597
Cdd:PRK13549 360 KNITL-------AALDRFTGGSRIDDAAelKTILESIQrlkvkTASPElaiARLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
....*
gi 162312251 598 TSALD 602
Cdd:PRK13549 433 TRGID 437
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
433-647 |
3.03e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.94 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 433 FRFDNVSFAYPSrDENLFSLINVSvFIPfGELVHIIGPSGSGKSTfislLLR-------------YFSPTYGNIYLDDFP 499
Cdd:TIGR03719 5 YTMNRVSKVVPP-KKEILKDISLS-FFP-GAKIGVLGLNGAGKST----LLRimagvdkdfngeaRPQPGIKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 500 leEIDEH--VLGSTITLVCQQPVIFDmtiRENIIMRNENASESDF----EEVCRL-ALVD-----EFALTFDQSYDT--- 564
Cdd:TIGR03719 78 --QLDPTktVRENVEEGVAEIKDALD---RFNEISAKYAEPDADFdklaAEQAELqEIIDaadawDLDSQLEIAMDAlrc 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 565 PCKEAS---LSGGQQQRIALARALLRDTEILILDEPTSALDPIT-----KNLvmdairaHRKGKTTLVITHDMSQINN-D 635
Cdd:TIGR03719 153 PPWDADvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawleRHL-------QEYPGTVVAVTHDRYFLDNvA 225
|
250
....*....|..
gi 162312251 636 ELVLVIDKGHLI 647
Cdd:TIGR03719 226 GWILELDRGRGI 237
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
452-632 |
3.14e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGElVH-IIGPSGSGKSTfislLLRYFSPTY------GNIYLDDFPLEEID----EHvLGstITLVCQQ-P 519
Cdd:NF040905 17 LDDVNLSVREGE-IHaLCGENGAGKST----LMKVLSGVYphgsyeGEILFDGEVCRFKDirdsEA-LG--IVIIHQElA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 520 VIFDMTIRENIIMRNENASES--DFEEVCRLA--LVDEFALtfDQSYDTPCKEasLSGGQQQRIALARALLRDTEILILD 595
Cdd:NF040905 89 LIPYLSIAENIFLGNERAKRGviDWNETNRRAreLLAKVGL--DESPDTLVTD--IGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 162312251 596 EPTSAL-DPITKNLvMDAIRAHR-KGKTTLVITHDMSQI 632
Cdd:NF040905 165 EPTAALnEEDSAAL-LDLLLELKaQGITSIIISHKLNEI 202
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
467-643 |
3.36e-07 |
|
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: 52.22 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 467 IIGPSGSGKSTFISLLLRYFSP-----TYGNIYLDDFPLE-----EID---EHVLGSTITlvcqqpVIFDMTIRENIIMR 533
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYALTGelppnSKGGAHDPKLIREgevraQVKlafENANGKKYT------ITRSLAILENVIFC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 534 NEnasesdfEEVCRLaLVDEfaltfdqsydtpckEASLSGGQQQ------RIALARALLRDTEILILDEPTSALDP--IT 605
Cdd:cd03240 101 HQ-------GESNWP-LLDM--------------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEenIE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 162312251 606 KNLVmDAIRAHRKGKT--TLVITHDmsqinnDELVLVIDK 643
Cdd:cd03240 159 ESLA-EIIEERKSQKNfqLIVITHD------EELVDAADH 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
406-602 |
3.37e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 406 TLCESHDPIEaakrSAAKIKSIsfergfRFDNVSFAYPSRDenlfsLIN-VSVFIPFGELVHIIGPSGSGKSTFisllLR 484
Cdd:PLN03073 161 GVYVNHDGNG----GGPAIKDI------HMENFSISVGGRD-----LIVdASVTLAFGRHYGLVGRNGTGKTTF----LR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 485 YFSPTYgniyLDDFP----LEEIDEHVLGSTIT---------------------LVCQQPVIFDMTIRENIIMRNENASE 539
Cdd:PLN03073 222 YMAMHA----IDGIPkncqILHVEQEVVGDDTTalqcvlntdiertqlleeeaqLVAQQRELEFETETGKGKGANKDGVD 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 540 SD-----FEEVC-RLALVDEFA-----------LTFDQSYDTPcKEASLSGGQQQRIALARALLRDTEILILDEPTSALD 602
Cdd:PLN03073 298 KDavsqrLEEIYkRLELIDAYTaearaasilagLSFTPEMQVK-ATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1235-1321 |
3.45e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.80 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1235 NFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSC----TVLIITHQPSLMK-LADRIIVMDS--- 1306
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegkkTALVVEHDLAVLDyLSDRIHVFEGepg 150
|
90
....*....|....*..
gi 162312251 1307 --GIVKESGSFDELMNR 1321
Cdd:cd03222 151 vyGIASQPKGTREGINR 167
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
414-628 |
4.50e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 414 IEAAKRSAAKIKSISFERG---FR----FDNVSFAYPsrDENLFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYF 486
Cdd:PRK15064 294 LEEVKPSSRQNPFIRFEQDkklHRnaleVENLTKGFD--NGPLFK--NLNLLLEAGERLAIIGENGVGKTTLLRTLVGEL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 487 SPTYGNI----------YLDDfPLEEIDEhvlgstitlvcqqpvifDMTIRENIimrNENASESDFEEVCRLALvdeFAL 556
Cdd:PRK15064 370 EPDSGTVkwsenanigyYAQD-HAYDFEN-----------------DLTLFDWM---SQWRQEGDDEQAVRGTL---GRL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 557 TFDQSyDTPCKEASLSGGQQQRIALARALLRDTEILILDEPTSALDpitknlvMDAIR----AHRKGKTTLV-ITHD 628
Cdd:PRK15064 426 LFSQD-DIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD-------MESIEslnmALEKYEGTLIfVSHD 494
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
435-628 |
4.85e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.17 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 435 FDNVSFAYpsRDENLFSliNVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIylddfpleeidehVLGSTITL 514
Cdd:TIGR03719 325 AENLTKAF--GDKLLID--DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-------------EIGETVKL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 515 --VCQQpvifdmtiRENIimrneNASESDFEEVC------RL--------ALVDEFAltFDQSyDTPCKEASLSGGQQQR 578
Cdd:TIGR03719 388 ayVDQS--------RDAL-----DPNKTVWEEISggldiiKLgkreipsrAYVGRFN--FKGS-DQQKKVGQLSGGERNR 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 162312251 579 IALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHrkGKTTLVITHD 628
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHD 499
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
132-379 |
6.80e-07 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 52.47 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 132 LSQYATSQITLGKMISLINFNSLLITIFGLASCVFSFgvrfLWQYLSAIAGKRA----RSLCFHVLSSKSSTFYSLTESK 207
Cdd:cd18545 22 LIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASR----LRIYLMAKVGQRIlydlRQDLFSHLQKLSFSFFDSRPVG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 208 ---SGLVNSVDRCIQFYEKS-ISLpmfhIAEnlAISLSC-LIISFRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKD 282
Cdd:cd18545 98 kilSRVINDVNSLSDLLSNGlINL----IPD--LLTLVGiVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 283 RKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSFL-DAFQ------GGVSQFFLYsvffqglWF 355
Cdd:cd18545 172 RKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLnALFWplveliSALGTALVY-------WY 244
|
250 260
....*....|....*....|....
gi 162312251 356 GNHLATTKRVNVGqVVTVFGSCLS 379
Cdd:cd18545 245 GGKLVLGGAITVG-VLVAFIGYVG 267
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1120-1292 |
8.26e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.96 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1120 NVSLSIEAREKVAIVGISGSGKSTLVELLRK-TYPSE-DIYIDGYPLT------NIDTNWLLKKVAIvdqKPHLlgsTIL 1191
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGlARPDAgEVLWQGEPIRrqrdeyHQDLLYLGHQPGI---KTEL---TAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1192 ESLLY------GVDRDinSVMDALDKTymteviqNLPNGLDTPLlefsKNFSGGQIQRLAFARALLRNPRLLILDECTSA 1265
Cdd:PRK13538 93 ENLRFyqrlhgPGDDE--ALWEALAQV-------GLAGFEDVPV----RQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190
....*....|....*....|....*....|
gi 162312251 1266 LDSKSSLLLEKTI-QNLS--CTVLIITHQP 1292
Cdd:PRK13538 160 IDKQGVARLEALLaQHAEqgGMVILTTHQD 189
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
437-647 |
8.32e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.11 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 437 NVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFI----SLLLRYFSPTyGNIYLDDFPLEEIDEHVLGSTI 512
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLkalaNRTEGNVSVE-GDIHYNGIPYKEFAEKYPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 513 tLVCQQPVIF-DMTIRENIimrnenasesDFEEVCRlalVDEFAltfdqsydtpckeASLSGGQQQRIALARALLRDTEI 591
Cdd:cd03233 87 -YVSEEDVHFpTLTVRETL----------DFALRCK---GNEFV-------------RGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 592 LILDEPTSALDPITKNLVMDAIR--AHRKGKTTLVIThdmSQINND-----ELVLVIDKGHLI 647
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRtmADVLKTTTFVSL---YQASDEiydlfDKVLVLYEGRQI 199
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
452-642 |
8.35e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTfislLLRYFSPTY------------GNIYLDDFPLEEIDEHVLGSTITLVCQ-- 517
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKST----LLKALAGDLtgggaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 518 QPViFDMTIRENIIM------RNENASESDFEEVCRLALVDEFALTFDQSYDTpckeaSLSGGQQQRIALARAL------ 585
Cdd:PRK13547 93 QPA-FAFSAREIVLLgryphaRRAGALTHRDGEIAWQALALAGATALVGRDVT-----TLSGGELARVQFARVLaqlwpp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 586 ---LRDTEILILDEPTSALDPITKNLVMDAIRA----HRKGktTLVITHD--MSQINNDELVLVID 642
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRlardWNLG--VLAIVHDpnLAARHADRIAMLAD 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
569-676 |
8.69e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 8.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 569 ASLSGGQQQRIALARALLRDTEILILDEPTSALDPIT----KNLVMDAirahrKGkTTLVITHDMSQINNDELVLV-IDK 643
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETiewlEGFLKTF-----QG-SIIFISHDRSFIRNMATRIVdLDR 228
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 162312251 644 GHLIQRCARKELVLFEDFEN-------NVSIDEKVLKEEA 676
Cdd:PRK11147 229 GKLVSYPGNYDQYLLEKEEAlrveelqNAEFDRKLAQEEV 268
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
462-627 |
1.53e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.62 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEhvlGSTITLVCQQPVI-FDMTIRENI----IMRNEN 536
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR---SRFMAYLGHLPGLkADLSTLENLhflcGLHGRR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 537 ASESDFEEVCRLALVDEfaltfdqsYDTPCKEasLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAH 616
Cdd:PRK13543 114 AKQMPGSALAIVGLAGY--------EDTLVRQ--LSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAH 183
|
170
....*....|..
gi 162312251 617 -RKGKTTLVITH 627
Cdd:PRK13543 184 lRGGGAALVTTH 195
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
824-990 |
2.17e-06 |
|
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: 51.10 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 824 MVLVVAAGSGASYFFSHYIFSISAkiwcdhYRLLA--VKVLFT----QDQAWFDQienyplVLSKILVNNISD----MRN 893
Cdd:cd18780 47 ILLGVVLIGSIATFLRSWLFTLAG------ERVVArlRKRLFSaiiaQEIAFFDV------TRTGELLNRLSSdtqvLQN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 894 MISSLIEEVFIAFTMAIIGIAWSFATGWRLAAVLVAVSPILCLTSRMFS-YIYVSTERMcQDVVISTTSILHKTIVNLDT 972
Cdd:cd18780 115 AVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGkYVRKLSKKF-QDALAAASTVAEESISNIRT 193
|
170
....*....|....*...
gi 162312251 973 ikgysVLSFFRENHKNSL 990
Cdd:cd18780 194 -----VRSFAKETKEVSR 206
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1131-1304 |
2.78e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.44 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1131 VAIVGISGSGKSTLVELLRKTY----------PSEDIYID---GYPLTNIDTNWL------LKKVAIVDQKPHLLGSTIL 1191
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLkpnlgkfddpPDWDEILDefrGSELQNYFTKLLegdvkvIVKPQYVDLIPKAVKGKVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1192 ESLLYGVDRD-INSVMDALDktymteviqnLPNGLDTPLlefsKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKS 1270
Cdd:cd03236 109 ELLKKKDERGkLDELVDQLE----------LRHVLDRNI----DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 162312251 1271 SLLLEKTIQNLS---CTVLIITHQPSLMK-LADRIIVM 1304
Cdd:cd03236 175 RLNAARLIRELAeddNYVLVVEHDLAVLDyLSDYIHCL 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
569-629 |
2.80e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 2.80e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 569 ASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKN----LVMDAIRahRKGKTTLVITHDM 629
Cdd:NF033858 396 DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDmfwrLLIELSR--EDGVTIFISTHFM 458
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1117-1307 |
3.78e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYP--SEDIYIDGYPLTNIDTNWLLKK-VAIVDQKPHL-LGSTILE 1192
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQkdSGSILFQGKEIDFKSSKEALENgISMVHQELNLvLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1193 SLLYG--------VD-----RDINSVMDALDktymteviqnlpngLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLIL 1259
Cdd:PRK10982 93 NMWLGryptkgmfVDqdkmyRDTKAIFDELD--------------IDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 162312251 1260 DECTSALDSKSSLLLEKTIQNLS---CTVLIITHQ-PSLMKLADRIIVMDSG 1307
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKergCGIVYISHKmEEIFQLCDEITILRDG 210
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
435-629 |
3.79e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.92 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 435 FDNVSFA-YPsrdenlfslinvsvfipfGELVHIIGPSGSGKSTFISLLLRYFSPTYGNI--------YLDDFPLEEIDE 505
Cdd:PRK11701 22 CRDVSFDlYP------------------GEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqLRDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 506 HVLGST-ITLVCQQPVifD---MTIRE--NIIMRNENASESDFEEVCRLAL--VDEFALTFDQSYDTPckeASLSGGQQQ 577
Cdd:PRK11701 84 RRLLRTeWGFVHQHPR--DglrMQVSAggNIGERLMAVGARHYGDIRATAGdwLERVEIDAARIDDLP---TTFSGGMQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 162312251 578 RIALARALLRDTEILILDEPTSALDPITKNLVMDAIRA--HRKGKTTLVITHDM 629
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlvRELGLAVVIVTHDL 212
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1209-1324 |
5.61e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.98 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1209 LDKTYMTEVIQNLPN-GLD-TPLLEFSKNFSGGQIQRLAFARALL---RNPRLLILDECTSALDSKSSLLLEKTIQNLSC 1283
Cdd:PRK00635 781 LDEPSIHEKIHALCSlGLDyLPLGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTH 860
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 162312251 1284 ---TVLIITHQPSLMKLADRIIVMD------SGIVKESGSFDELMNRHTH 1324
Cdd:PRK00635 861 qghTVVIIEHNMHVVKVADYVLELGpeggnlGGYLLASCSPEELIHLHTP 910
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
454-628 |
6.77e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 454 NVSVfiPFGE-----LvhiIGPSGSGKSTFISLLLRYFSPTYGNIYL-----------DDFPLEE---IDEHVLGSTITL 514
Cdd:PRK15064 19 NISV--KFGGgnrygL---IGANGCGKSTFMKILGGDLEPSAGNVSLdpnerlgklrqDQFAFEEftvLDTVIMGHTELW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 515 VCQQPvifdmtiRENIIMrNENASESDFEEVCRLALvdEFAltfdqSYDTPCKEAS----LSG----------------- 573
Cdd:PRK15064 94 EVKQE-------RDRIYA-LPEMSEEDGMKVADLEV--KFA-----EMDGYTAEARagelLLGvgipeeqhyglmsevap 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 574 GQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAhRKGkTTLVITHD 628
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE-RNS-TMIIISHD 211
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
551-602 |
7.30e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.39 E-value: 7.30e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 551 VDEFALTFDqsYDTPCKEAS---LSGGQQQRIALARALLRDTEILILDEPTSALD 602
Cdd:PRK10762 375 VSDFIRLFN--IKTPSMEQAiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
243-390 |
7.76e-06 |
|
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: 49.35 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 243 LIISFRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACST 322
Cdd:cd18551 128 VVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAER 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 323 SSKSFLRFSFLDAFQGGVSQFFLYSVFFQGLWFGNHLATTKRVNVG----------QVVTVFGSCLSVASSLQQILPA 390
Cdd:cd18551 208 LYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGtlvafllylfQLITPLSQLSSFFTQLQKALGA 285
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
444-638 |
8.16e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 444 SRDENLFSLiNVSvFIPfGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDE-------HVLGstitlvc 516
Cdd:PRK13541 11 IEQKNLFDL-SIT-FLP-SAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpyctyigHNLG------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 517 qqpVIFDMTIRENIIMRNE--NASESDFEEVCRLALVDEFaltfdqsyDTPCkeASLSGGQQQRIALARALLRDTEILIL 594
Cdd:PRK13541 81 ---LKLEMTVFENLKFWSEiyNSAETLYAAIHYFKLHDLL--------DEKC--YSLSSGMQKIVAIARLIACQSDLWLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 162312251 595 DEPTSALDPITKNLVMDAIRAH-RKGKTTLVITHDMSQINNDELV 638
Cdd:PRK13541 148 DEVETNLSKENRDLLNNLIVMKaNSGGIVLLSSHLESSIKSAQIL 192
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1205-1304 |
8.74e-06 |
|
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: 50.17 E-value: 8.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1205 VMDALDKT----YMTEVIQ--NLPNGLDTPLlefsKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTI 1278
Cdd:COG1245 180 VRELLEKVdergKLDELAEklGLENILDRDI----SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLI 255
|
90 100 110
....*....|....*....|....*....|
gi 162312251 1279 QNLS---CTVLIITHQPSLM-KLADRIIVM 1304
Cdd:COG1245 256 RELAeegKYVLVVEHDLAILdYLADYVHIL 285
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1233-1290 |
8.92e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 8.92e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1233 SKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSCTVLIITH 1290
Cdd:PLN03073 342 TKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSH 399
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
570-609 |
9.23e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 9.23e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 162312251 570 SLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLV 609
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLV 440
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
104-371 |
9.59e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 49.07 E-value: 9.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 104 IFGTLIFTCLSAALEPLMTWTTGKVFDALSQYATSQITLGKMISLInfnsllitifgLASCVFSFGVRFLWQYLSAIAGK 183
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLALLL-----------LGAYLLRALLNFLRIYLNHVAEQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 184 RA----RSLCFHVLSSKSSTFYSltESKSG-----LVNSVDRciqfYEKSISlpmfHIAENLAIS----LSCLIISFRYS 250
Cdd:cd18778 70 KVvadlRSDLYDKLQRLSLRYFD--DRQTGdlmsrVINDVAN----VERLIA----DGIPQGITNvltlVGVAIILFSIN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 251 WSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRF 330
Cdd:cd18778 140 PKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRA 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 162312251 331 SFLDAFQGGVSQFF--LYSVFFqgLWFGNHLATTKRVNVGQVV 371
Cdd:cd18778 220 MKLWAIFHPLMEFLtsLGTVLV--LGFGGRLVLAGELTIGDLV 260
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1099-1318 |
9.80e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1099 IEFDGVSFAYPDSErnhLALNNVSLSIEAREKVAIVGISGSGKSTLVELlrktypsediyIDGYPLTNIDTNWLLKKVAI 1178
Cdd:PLN03073 509 ISFSDASFGYPGGP---LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKL-----------ISGELQPSSGTVFRSAKVRM 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1179 VDQKPHLLGstilesllyGVDRDINSVMdaldktYMTEVIQNLPN----------GLDTPL-LEFSKNFSGGQIQRLAFA 1247
Cdd:PLN03073 575 AVFSQHHVD---------GLDLSSNPLL------YMMRCFPGVPEqklrahlgsfGVTGNLaLQPMYTLSGGQKSRVAFA 639
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312251 1248 RALLRNPRLLILDECTSALDSKSsllLEKTIQNLSC---TVLIITHQPSLMkladriivmdsgivkeSGSFDEL 1318
Cdd:PLN03073 640 KITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLfqgGVLMVSHDEHLI----------------SGSVDEL 694
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1117-1322 |
9.82e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREkvaIVGISGS---GKST----LVELLRktyPSE-DIYIDGYPLT--NIDTNwllKKVAIVDQKPHLL 1186
Cdd:NF033858 281 AVDHVSFRIRRGE---IFGFLGSngcGKSTtmkmLTGLLP---ASEgEAWLFGQPVDagDIATR---RRVGYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1187 GS-TILESL-----LYGV-DRDINS-VMDALDKTYMTEVIQNLPNGLdtPLlefsknfsgGQIQRLAFARALLRNPRLLI 1258
Cdd:NF033858 352 GElTVRQNLelharLFHLpAAEIAArVAEMLERFDLADVADALPDSL--PL---------GIRQRLSLAVAVIHKPELLI 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 1259 LDECTS-----ALDSKSSLLLEktiqnLSC----TVLIITHqpsLMKLA---DRIIVMDSGIVKESGSFDELMNRH 1322
Cdd:NF033858 421 LDEPTSgvdpvARDMFWRLLIE-----LSRedgvTIFISTH---FMNEAercDRISLMHAGRVLASDTPAALVAAR 488
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1204-1304 |
1.23e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1204 SVMDALDKT----YMTEVIQ--NLPNGLDTPLlefsKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKT 1277
Cdd:PRK13409 179 KVRELLKKVdergKLDEVVErlGLENILDRDI----SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARL 254
|
90 100 110
....*....|....*....|....*....|
gi 162312251 1278 IQNLSC--TVLIITHQPSLM-KLADRIIVM 1304
Cdd:PRK13409 255 IRELAEgkYVLVVEHDLAVLdYLADNVHIA 284
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
570-632 |
1.25e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 1.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 570 SLSGGQQQRIALARALLRDTEILILDEPTSALDPITK----NLVMDAIrahRKGKTTLVITHDMSQI 632
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfeiyQLIAELA---KKDKGIIIISSEMPEL 454
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
563-647 |
1.34e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 563 DTPCkeASLSGGQQQRIALARALLRDTEILILDEPTSALDPIT-----KNLvmdairaHRKGKTTLVITHDMSQINN-DE 636
Cdd:PRK11819 158 DAKV--TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawleQFL-------HDYPGTVVAVTHDRYFLDNvAG 228
|
90
....*....|.
gi 162312251 637 LVLVIDKGHLI 647
Cdd:PRK11819 229 WILELDRGRGI 239
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1120-1320 |
1.45e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 47.97 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1120 NVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGYPLTNIDTNWLLKK-VAIVDQKPHLLGS-TILESLL 1195
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDagNIIIDDEDISLLPLHARARRgIGYLPQEASIFRRlSVYDNLM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1196 --YGVDRDINSVMDALDKTYMTEV--IQNLPNGLDTPLlefsknfSGGQIQRLAFARALLRNPRLLILDECTSALDSKSS 1271
Cdd:PRK10895 101 avLQIRDDLSAEQREDRANELMEEfhIEHLRDSMGQSL-------SGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 162312251 1272 LLLEKTIQNL---SCTVLIITHQ-PSLMKLADRIIVMDSGIVKESGSFDELMN 1320
Cdd:PRK10895 174 IDIKRIIEHLrdsGLGVLITDHNvRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
570-644 |
1.61e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 49.63 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 570 SLSGGQQQRIALARALL-RDT--EILILDEPTSAL--DPITKnlVMDAIraHR---KGKTTLVITHDMSQINNDElvLVI 641
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSkRSTgrTLYILDEPTTGLhfDDIKK--LLEVL--QRlvdKGNTVVVIEHNLDVIKTAD--YII 902
|
...
gi 162312251 642 DKG 644
Cdd:TIGR00630 903 DLG 905
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
781-977 |
2.73e-05 |
|
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: 47.80 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 781 FLLGLLTSLIQGASVPIFAYVISKCLNLFMQIDPSIGVAFWSSMVLVVAAGSGASYFFSHYIFS-ISAKIWCDhYRLLAV 859
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAyVGQRVVRD-LRNDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 860 KVLFTQDQAWFDQiENYPLVLSKIlVNNISDMRNMISSLIEEVFIAFTMAIIGIAWSFATGWRLAAVLVAVSPILCLTSR 939
Cdd:cd18552 80 DKLLRLPLSFFDR-NSSGDLISRI-TNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIR 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 162312251 940 MFS-YIYVSTERMcQDVVISTTSILHKTIVNLDTIKGYS 977
Cdd:cd18552 158 RIGkRLRKISRRS-QESMGDLTSVLQETLSGIRVVKAFG 195
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
467-628 |
2.76e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.54 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 467 IIGPSGSGKSTF---ISLLLrYFSPTYGNIYLDDFP----------LE-EIDEHVL------GSTITLVCQQP------- 519
Cdd:COG0419 28 IVGPNGAGKSTIleaIRYAL-YGKARSRSKLRSDLInvgseeasveLEfEHGGKRYrierrqGEFAEFLEAKPserkeal 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 520 -VIFDMTIRENIIMR---NENASESDFEEVCRLALVDEFALTFDQSYDTPCkeaSLSGGQQQRIALARALLrdteiLILD 595
Cdd:COG0419 107 kRLLGLEIYEELKERlkeLEEALESALEELAELQKLKQEILAQLSGLDPIE---TLSGGERLRLALADLLS-----LILD 178
|
170 180 190
....*....|....*....|....*....|...
gi 162312251 596 epTSALDPITKNLVMDAIRAHRkgkttlVITHD 628
Cdd:COG0419 179 --FGSLDEERLERLLDALEELA------IITHV 203
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
572-629 |
3.12e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.80 E-value: 3.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 572 SGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTT--LVITHDM 629
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDL 222
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
456-670 |
3.82e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.30 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 456 SVFIPfGELVHIIGPSGSGKSTFISLLLRYFSPTY--GNIYLDDFPleeiDEHVLGSTITLVCQQPVIFD--MTIRENII 531
Cdd:PLN03140 901 GAFRP-GVLTALMGVSGAGKTTLMDVLAGRKTGGYieGDIRISGFP----KKQETFARISGYCEQNDIHSpqVTVRESLI 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 532 MRN--ENASESDFEEvcRLALVDEFA--LTFDQSYDTPCKEA---SLSGGQQQRIALARALLRDTEILILDEPTSALDPI 604
Cdd:PLN03140 976 YSAflRLPKEVSKEE--KMMFVDEVMelVELDNLKDAIVGLPgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 605 TKNLVMDAIRAHRKGKTTLVITHDMSQIN----NDELVLVIDKGHLIQ-----RCARKELVLFEDFENNVSIDEK 670
Cdd:PLN03140 1054 AAAIVMRTVRNTVDTGRTVVCTIHQPSIDifeaFDELLLMKRGGQVIYsgplgRNSHKIIEYFEAIPGVPKIKEK 1128
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
781-1006 |
3.83e-05 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 47.04 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 781 FLLGLLTSLIqGASVPIFayvISKCLNLFMQIDPSIGVAFWssMVLVVAAGSGASYFfSHYIFSISA---------KIWc 851
Cdd:cd18551 5 LLLSLLGTAA-SLAQPLL---VKNLIDALSAGGSSGGLLAL--LVALFLLQAVLSAL-SSYLLGRTGervvldlrrRLW- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 852 dhYRLLAVKVLFtqdqawFDQIEnyPLVLSKILVNNISDMRNMISSLIEEVFIAFTMAIIGIAWSFATGWRLAAVLVAVS 931
Cdd:cd18551 77 --RRLLRLPVSF------FDRRR--SGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312251 932 PILCL-TSRMFSYIYVSTERMcQDVVISTTSILHKTIVNLDTIKGYSVLSFFRENHKNSLRKSWEAFKRRAFWTSL 1006
Cdd:cd18551 147 PLAFLiILPLGRRIRKASKRA-QDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEAL 221
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
225-398 |
4.62e-05 |
|
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: 47.06 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 225 ISLPMfhiaeNLAISLSCLIISFRYSWSLTLVVLASYPI-IILVVGFINSFlssaYEKDRKSSEKAA---SILEKSISAI 300
Cdd:cd18570 120 ISLFL-----DLLMVIISGIILFFYNWKLFLITLLIIPLyILIILLFNKPF----KKKNREVMESNAelnSYLIESLKGI 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 301 QTVIFHSMQDTEYRYFADACSTSSKSFLRFSFLDAFQGGVSQFF--LYSVFFqgLWFGNHLATTKRVNVGQVVTVFGSCL 378
Cdd:cd18570 191 ETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLIslIGSLLI--LWIGSYLVIKGQLSLGQLIAFNALLG 268
|
170 180
....*....|....*....|
gi 162312251 379 SVASSLQQILPAIPDLIKGK 398
Cdd:cd18570 269 YFLGPIENLINLQPKIQEAK 288
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
524-633 |
4.90e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 524 MTIRENIIMRNE-NASESDFEEVC-----RLALVDEFALtfdqSYDTPCKE-ASLSGGQQQRIALARALlrDTEIL---- 592
Cdd:PRK00635 427 MSLQELFIFLSQlPSKSLSIEEVLqglksRLSILIDLGL----PYLTPERAlATLSGGEQERTALAKHL--GAELIgity 500
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 162312251 593 ILDEPTSALDPITKNLVMDAIRAHR-KGKTTLVITHDMSQIN 633
Cdd:PRK00635 501 ILDEPSIGLHPQDTHKLINVIKKLRdQGNTVLLVEHDEQMIS 542
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
571-647 |
5.71e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.66 E-value: 5.71e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 571 LSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMD-AIRAHRKGKTTLV-ITHDmsqinndeLVLVIDKGHLI 647
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIElLLELQQKENMALVlITHD--------LALVAEAAHKI 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1104-1299 |
5.82e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.71 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1104 VSFAYPDsernHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSE--DIYIDGyplTNIDTNWLL--KKVAIV 1179
Cdd:PRK13540 7 LDFDYHD----QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEkgEILFER---QSIKKDLCTyqKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1180 DQK----PHLlgsTILESLLYgvdrDINSVMDALDKTYMTEVIQnLPNGLDTP--LLefsknfSGGQIQRLAFARALLRN 1253
Cdd:PRK13540 80 GHRsginPYL---TLRENCLY----DIHFSPGAVGITELCRLFS-LEHLIDYPcgLL------SSGQKRQVALLRLWMSK 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 162312251 1254 PRLLILDECTSALDSKSSLLLEKTIQNLSC---TVLIITHQPSLMKLAD 1299
Cdd:PRK13540 146 AKLWLLDEPLVALDELSLLTIITKIQEHRAkggAVLLTSHQDLPLNKAD 194
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1237-1304 |
6.14e-05 |
|
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: 44.66 E-value: 6.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 1237 SGGQIQRLAFARAL---LRNPR-LLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQPSLMKLADRIIVM 1304
Cdd:cd03227 79 SGGEKELSALALILalaSLKPRpLYILDEIDRGLDPRDGQALAEAILEHLvkgAQVIVITHLPELAELADKLIHI 153
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
571-646 |
6.15e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.35 E-value: 6.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 571 LSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRA-HRKGKTTLVITHDMSQINN-DELVLVIDKGHL 646
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSiAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1115-1302 |
7.45e-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: 45.29 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1115 HLALNNVsLSIEAREKV-------AIVGISGSGKSTLVELLR-KTYPSEdiyidgyPLTNIDTNWLLKKVAIVDQKphll 1186
Cdd:cd03240 3 KLSIRNI-RSFHERSEIeffspltLIVGQNGAGKTTIIEALKyALTGEL-------PPNSKGGAHDPKLIREGEVR---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1187 GSTILE-SLLYGVDRDINSVMDALDKTYMteviqnLPNG-LDTPLLEFSKNFSGGQ------IQRLAFARALLRNPRLLI 1258
Cdd:cd03240 71 AQVKLAfENANGKKYTITRSLAILENVIF------CHQGeSNWPLLDMRGRCSGGEkvlaslIIRLALAETFGSNCGILA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 162312251 1259 LDECTSALDS---KSSL--LLEKTIQNLSCTVLIITHQPSLMKLADRII 1302
Cdd:cd03240 145 LDEPTTNLDEeniEESLaeIIEERKSQKNFQLIVITHDEELVDAADHIY 193
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
242-371 |
8.24e-05 |
|
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: 46.01 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 242 CLIISFRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYR----YFA 317
Cdd:cd18568 132 YLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWrwenKFA 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 162312251 318 DACSTSSKSFLRFSFLDAFQGGVSQFFLYSVffqgLWFGNHLATTKRVNVGQVV 371
Cdd:cd18568 212 KALNTRFRGQKLSIVLQLISSLINHLGTIAV----LWYGAYLVISGQLTIGQLV 261
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
884-1010 |
1.05e-04 |
|
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: 45.94 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 884 LVNNISDMRNMISSLIEEVFIAFTMAIIGIAWSFATGWRLAAVLVAVSPILCLTSRMFS-YIY-VSTERmcQDVVISTTS 961
Cdd:cd18576 99 LSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGrRIRkLSKKV--QDELAEANT 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 162312251 962 ILHKTIVNLDTIKgysvlSFFRENH-----KNSLRKSWEAFKRRAFWTSLGFAI 1010
Cdd:cd18576 177 IVEETLQGIRVVK-----AFTREDYeieryRKALERVVKLALKRARIRALFSSF 225
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
570-602 |
1.07e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 1.07e-04
10 20 30
....*....|....*....|....*....|...
gi 162312251 570 SLSGGQQQRIALARALLRDTEILILDEPTSALD 602
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
465-632 |
1.27e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 465 VH-IIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLE-EIDEHVLGSTITLVCQQ-PVIFDMTIRENI---------IM 532
Cdd:PRK10982 26 IHaLMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRSVMDNMwlgryptkgMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 533 RNENASESDFEevcrlALVDEFaltfDQSYDTPCKEASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDA 612
Cdd:PRK10982 106 VDQDKMYRDTK-----AIFDEL----DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTI 176
|
170 180
....*....|....*....|.
gi 162312251 613 IRAHR-KGKTTLVITHDMSQI 632
Cdd:PRK10982 177 IRKLKeRGCGIVYISHKMEEI 197
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
462-655 |
1.84e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTFISLLLRYFSPTYGNI-YLDdfplEEID----EHVLGSTITLVCQQ-PVIFDMTIRENIIMRNE 535
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlYLG----KEVTfngpKSSQEAGIGIIHQElNLIPQLTIAENIFLGRE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 536 --NA----------SESDfeevcrlALVDEFALTFdqSYDTPCKEasLSGGQQQRIALARALLRDTEILILDEPTSAL-D 602
Cdd:PRK10762 106 fvNRfgridwkkmyAEAD-------KLLARLNLRF--SSDKLVGE--LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 603 PITKNL--VMDAIRAHRKGktTLVITHDMS---QINNDelVLVIDKGHLIQRCARKEL 655
Cdd:PRK10762 175 TETESLfrVIRELKSQGRG--IVYISHRLKeifEICDD--VTVFRDGQFIAEREVADL 228
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1237-1309 |
2.16e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 2.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 1237 SGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS----CTVLIITHQPSLMKLADRIIVMDSGIV 1309
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkkdkGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1118-1183 |
2.41e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.83 E-value: 2.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLV-ELL----------RKTYPSEDIYIDGypLTNIDtnwllkKVAIVDQKP 1183
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLInETLykalarklngAKKVPGKHKEIEG--LEHLD------KVIDIDQSP 693
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
1188-1305 |
2.69e-04 |
|
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. This entry also includes MRB1590 from Trypanosoma brucei brucei has a central ATPase domain homologous to this domain.
Pssm-ID: 462914 Cd Length: 282 Bit Score: 44.51 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1188 STILESLLYGVDRDI------------NSV-MDALDKTYMTEV-----IQNLPNGLDTPllEFS-KNFSGGQIQRLAFAR 1248
Cdd:pfam09818 93 STLLEALERGVYNHIpgdgrefvvtdpDAVkIRAEDGRSVHGVdispfINNLPPGKDTT--DFStEDASGSTSQAANIME 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 1249 ALLRNPRLLILDECTSA-----LDSKSSLLLEKTIQNLSC---------------TVLIITHQPSLMKLADRIIVMD 1305
Cdd:pfam09818 171 ALEAGASLLLIDEDTSAtnfmiRDERMQALVSKDKEPITPfvdrvrslyddlgvsTILVVGGSGDYLDVADTVILMD 247
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
243-371 |
2.77e-04 |
|
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: 44.41 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 243 LIISFRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACST 322
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLAR 212
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 162312251 323 SSKSFLRFSFLDAFQGGVSQFF--LYSVFFqgLWFGNHLATTKRVNVGQVV 371
Cdd:cd18588 213 YVKASFKTANLSNLASQIVQLIqkLTTLAI--LWFGAYLVMDGELTIGQLI 261
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
571-629 |
3.54e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.02 E-value: 3.54e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 571 LSGGQQQRIALARALL-RDTE--ILILDEPTSAL--DPITKnlVMDAIraHR---KGKTTLVITHDM 629
Cdd:COG0178 827 LSGGEAQRVKLASELSkRSTGktLYILDEPTTGLhfHDIRK--LLEVL--HRlvdKGNTVVVIEHNL 889
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1120-1267 |
3.76e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 43.82 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1120 NVSLSIEAREKVAIVGISGSGKSTLVELL-RKTYPSE-DIYIDGYPLTNIDTNWLLKKVAIVDQKPHLLGSTILESL--- 1194
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLsRLMTPAHgHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELvar 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1195 -------LYGVDR--DINSVMDALDKTYMTEVIQNlpnGLDTpllefsknFSGGQIQRLAFARALLRNPRLLILDECTSA 1265
Cdd:PRK10253 105 gryphqpLFTRWRkeDEEAVTKAMQATGITHLADQ---SVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
..
gi 162312251 1266 LD 1267
Cdd:PRK10253 174 LD 175
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
154-303 |
4.15e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 44.09 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 154 LLITIFGLAScVFSFGVRFLWQYLSAIAGKRARSLCFHVLSSKSSTFYSltESKSG-----LVNSVDRCIQFYEKSISLp 228
Cdd:cd18565 59 LTVAAFLLES-LFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFE--DRQTGdlmsvLNNDVNQLERFLDDGANS- 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 229 mfhIAENLAISLSCLIISFRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTV 303
Cdd:cd18565 135 ---IIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVI 206
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
462-498 |
4.61e-04 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 41.74 E-value: 4.61e-04
10 20 30
....*....|....*....|....*....|....*..
gi 162312251 462 GELVHIIGPSGSGKSTFISlllRYFSPTYgNIYLDDF 498
Cdd:COG4639 2 LSLVVLIGLPGSGKSTFAR---RLFAPTE-VVSSDDI 34
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1237-1320 |
4.73e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.27 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1237 SGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLS---CTVLIITHQ-PSLMKLADRIIVMDSG----- 1307
Cdd:PRK15439 405 SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAaqnVAVLFISSDlEEIEQMADRVLVMHQGeisga 484
|
90
....*....|...
gi 162312251 1308 IVKESGSFDELMN 1320
Cdd:PRK15439 485 LTGAAINVDTIMR 497
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
235-358 |
5.56e-04 |
|
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: 43.63 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 235 NLAISLSCLIISFRYSWSLTLVVLASYPIIILVVGFIN---SFLSsayekdRKSSEK---AASILEKSISAIQTVIFHSM 308
Cdd:cd18575 120 NLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGrrvRRLS------RASQDRladLSAFAEETLSAIKTVQAFTR 193
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 162312251 309 QDTEYRYFADACSTSSKSFLRFSFLDAFQGGVSQFFLYSVFFQGLWFGNH 358
Cdd:cd18575 194 EDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAH 243
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1117-1307 |
6.11e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.84 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1117 ALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSEDIYIdgypltnidtNWLLKKVA-------------IVDQKP 1183
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSI----------LYLGKEVTfngpkssqeagigIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1184 HLLGS-TILESLLYGvdRDINSVMDALDKTYMTEVIQ------NLPNGLDTPLLEFSKnfsgGQIQRLAFARALLRNPRL 1256
Cdd:PRK10762 89 NLIPQlTIAENIFLG--REFVNRFGRIDWKKMYAEADkllarlNLRFSSDKLVGELSI----GEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 1257 LILDECTSALDSKSSLLLEKTIQNL---SCTVLIITHQpslMK----LADRIIVMDSG 1307
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELksqGRGIVYISHR---LKeifeICDDVTVFRDG 217
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1233-1321 |
6.66e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.57 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1233 SKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNL---SCTVLIIT-HQPSLMKLADRIIVMDSGI 1308
Cdd:NF000106 142 AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvrdGATVLLTTqYMEEAEQLAHELTVIDRGR 221
|
90
....*....|...
gi 162312251 1309 VKESGSFDELMNR 1321
Cdd:NF000106 222 VIADGKVDELKTK 234
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
571-629 |
6.94e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.29 E-value: 6.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312251 571 LSGGQQQRIALARALL-RDT--EILILDEPTSAL--DPITKNL-VMDAIRAhrKGKTTLVITHDM 629
Cdd:PRK00349 831 LSGGEAQRVKLAKELSkRSTgkTLYILDEPTTGLhfEDIRKLLeVLHRLVD--KGNTVVVIEHNL 893
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
571-632 |
7.15e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 43.75 E-value: 7.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 571 LSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRA-HRKGKTTLVITHDMSQI 632
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEV 459
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
462-752 |
7.54e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 44.23 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 462 GELVHIIGPSGSGKSTFISLLLRYFSPTYGniylddfpleeiDEHVLGSTITL----------VCQQPVIFD--MTIREN 529
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSG------------DATVAGKSILTnisdvhqnmgYCPQFDAIDdlLTGREH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 530 IIM--RNENASESDFEEVCRLAlVDEFALTFDQSydtpCKEASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKN 607
Cdd:TIGR01257 2033 LYLyaRLRGVPAEEIEKVANWS-IQSLGLSLYAD----RLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 608 LVMDAIRA-HRKGKTTLVITHDMSQINN--DELVLVIdKGHLiqRCARKELVLFEDFENNVSIDEKVLKEEADnpfILPN 684
Cdd:TIGR01257 2108 MLWNTIVSiIREGRAVVLTSHSMEECEAlcTRLAIMV-KGAF--QCLGTIQHLKSKFGDGYIVTMKIKSPKDD---LLPD 2181
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312251 685 EESLLEKYWINYNESfsqLSRESLFTSLESPFTDiESPTIVSRRKIVEQRKLRMEKESFQETNVDQTF 752
Cdd:TIGR01257 2182 LNPVEQFFQGNFPGS---VQRERHYNMLQFQVSS-SSLARIFQLLISHKDSLLIEEYSVTQTTLDQVF 2245
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1069-1313 |
7.78e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1069 IATSRVLKLS-------SLKPGNLHKSGYLKFPLVGKIEFDGVSFAYPDSERNHLALN-------NVSLSIEAREKVAIV 1134
Cdd:PRK00635 1443 IATDRSGSLAehadhliHLGPGSGPQGGYLLSTSALKQSQPDLHNTRSSEETPTLSVSlsihtiqNLNVSAPLHSLVAIS 1522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1135 GISGSGKSTLV---------ELLRKTYP--SEDIYIDGYPL-----TNIDTNWllkkvaivDQKPHL------------- 1185
Cdd:PRK00635 1523 GVSGSGKTSLLlegfykqacALIEKGPSvfSEIIFLDSHPQissqrSDISTYF--------DIAPSLrnfyasltqakal 1594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1186 ---------------------LGSTILESLLYGVDRD-------------INSVM------DALDKTYMTEVIQNLP--- 1222
Cdd:PRK00635 1595 nisasmfstntkqgqcsdcwgLGYQWIDRAFYALEKRpcptcsgfriqplAQEVVyegkhfGQLLQTPIEEVAETFPflk 1674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 1223 -----------NGLD-TPLLEFSKNFSGGQIQRLAFARALL---RNPRLLILDECTSALDS--KSSLL-LEKTIQNLSCT 1284
Cdd:PRK00635 1675 kiqkplqalidNGLGyLPLGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNqqKSALLvQLRTLVSLGHS 1754
|
330 340
....*....|....*....|....*....
gi 162312251 1285 VLIITHQPSLMKLADRIIVMDSGIVKESG 1313
Cdd:PRK00635 1755 VIYIDHDPALLKQADYLIEMGPGSGKTGG 1783
|
|
| PRK07261 |
PRK07261 |
DNA topology modulation protein; |
1130-1171 |
8.67e-04 |
|
DNA topology modulation protein;
Pssm-ID: 180911 [Multi-domain] Cd Length: 171 Bit Score: 41.63 E-value: 8.67e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 162312251 1130 KVAIVGISGSGKSTLVELLRKTYPSEDIYIDGyplTNIDTNW 1171
Cdd:PRK07261 2 KIAIIGYSGSGKSTLARKLSQHYNCPVLHLDT---LHFQPNW 40
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
571-632 |
9.50e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.23 E-value: 9.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312251 571 LSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRA-HRKGKTTLVITHDMSQI 632
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEI 472
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
104-271 |
1.17e-03 |
|
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: 42.39 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 104 IFGTLIFTCLSAALEPLMTWTTGKVFDALSQYATSQITlgkmislINFNSLLITIFGLASC-VFSFGVRFLWQYLSAIAG 182
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGG-------VDFSGLLRILLLLLGLyLLSALFSYLQNRLMARVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 183 KRA----RSLCFHVLSSKSSTFYSlTESK----SGLVNSVDRCIQFYEKSISlpmfhiaeNLAIS----LSCLIISFRYS 250
Cdd:cd18547 74 QRTvydlRKDLFEKLQRLPLSYFD-THSHgdimSRVTNDVDNISQALSQSLT--------QLISSiltiVGTLIMMLYIS 144
|
170 180
....*....|....*....|.
gi 162312251 251 WSLTLVVLASYPIIILVVGFI 271
Cdd:cd18547 145 PLLTLIVLVTVPLSLLVTKFI 165
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
441-628 |
1.18e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.76 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 441 AYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPV 520
Cdd:pfam13304 110 KFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 521 IFDMTIRENIIMRNENASESDFEEVcrlALVDEFALTFDQSYDTPCKEASLSGGQQQRIALARALLRD---TEILILDEP 597
Cdd:pfam13304 190 RGLKLADLNLSDLGEGIEKSLLVDD---RLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLSAlpkGGLLLIDEP 266
|
170 180 190
....*....|....*....|....*....|..
gi 162312251 598 TSALDPITKNLVMDAIRAHRKGKTTLVI-THD 628
Cdd:pfam13304 267 ESGLHPKLLRRLLELLKELSRNGAQLILtTHS 298
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
455-629 |
1.21e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.48 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 455 VSVFIPFGELVHIIGPSGSGKStFISLLLRYFSPTYGNIYLDDFPLEEID---------EHVLGSTITLVCQQP------ 519
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKS-LIAKAICGVTKDNWRVTADRMRFDDIDllrlsprerRKLVGHNVSMIFQEPqscldp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 520 ----------VIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDtpckeasLSGGQQQRIALARALLRDT 589
Cdd:PRK15093 105 servgrqlmqNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYE-------LTEGECQKVMIAIALANQP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 162312251 590 EILILDEPTSALDPITKNLVMDAI-RAHRKGKTT-LVITHDM 629
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLtRLNQNNNTTiLLISHDL 219
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
240-388 |
1.23e-03 |
|
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: 42.50 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 240 LSCLIISFRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTV-IFHSMQDTEYR---Y 315
Cdd:cd18555 130 VIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIkSLGSEKNIYKKwenL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 316 FADACstssKSFLRFSFLDAFQGGVSQF--FLYSVFFqgLWFGNHLATTKRVNVGQVV-------TVFGSCLSVASSLQQ 386
Cdd:cd18555 210 FKKQL----KAFKKKERLSNILNSISSSiqFIAPLLI--LWIGAYLVINGELTLGELIafsslagSFLTPIVSLINSYNQ 283
|
..
gi 162312251 387 IL 388
Cdd:cd18555 284 FI 285
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1237-1302 |
1.30e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.08 E-value: 1.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312251 1237 SGGQIQRLAFARALLR---NPRLLILDECTSALDSKSSLLLEKTIQNL---SCTVLIITHQPSLMKLADRII 1302
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLvdkGNTVVVIEHNLDVIKTADYII 902
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
570-657 |
1.40e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 570 SLSGGQQQRIALARALL---RDTEILILDEPTSALDP-ITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDK-- 643
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHThDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGPeg 888
|
90
....*....|....*...
gi 162312251 644 ----GHLIQRCARKELVL 657
Cdd:PRK00635 889 gnlgGYLLASCSPEELIH 906
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
885-1074 |
1.54e-03 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 42.05 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 885 VNNISDMRNMISSLIEEVFIAFTMAIIGIAWSFATGWRLAAVLVAVSPILCLTSRMFSYIYvstERMCQDVVIS---TTS 961
Cdd:cd18570 105 FNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPF---KKKNREVMESnaeLNS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 962 ILHKTIVNLDTIKGYSVLSFFRENHKNSLRKSWEAFKRRAFWTSLGFAINNSLLYFVRALLFYCSSIFISKEFYTVEQMV 1041
Cdd:cd18570 182 YLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLI 261
|
170 180 190
....*....|....*....|....*....|...
gi 162312251 1042 QVLSLATFTLLMASTCIMSLPNVSASRIATSRV 1074
Cdd:cd18570 262 AFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
104-371 |
1.80e-03 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 42.00 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 104 IFGTLIFTCLSAALEPLMTWTTGKVFDalsqyatsQITLGKMISLINFNSLLITIFGLASCVFSFGVrflwQYLSAIA-- 181
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIID--------EGIANGDLSYILRTGLLMLLLALLGLIAGILA----GYFAAKAsq 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 182 --GKRARSLCFHvlssKSSTFySLTE----SKSGLV----NSVDRCIQFYEKSISL----PMfhiaenlaISLSCLIISF 247
Cdd:cd18548 69 gfGRDLRKDLFE----KIQSF-SFAEidkfGTSSLItrltNDVTQVQNFVMMLLRMlvraPI--------MLIGAIIMAF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 248 RYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADA----CSTS 323
Cdd:cd18548 136 RINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKAnddlTDTS 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 162312251 324 SKSFLRFSFLDAfqggVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVV 371
Cdd:cd18548 216 LKAGRLMALLNP----LMMLIMNLAIVAILWFGGHLINAGSLQVGDLV 259
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1243-1290 |
2.28e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 2.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 162312251 1243 RLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSCTVLIITH 1290
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISH 210
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
452-479 |
2.31e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 2.31e-03
10 20
....*....|....*....|....*...
gi 162312251 452 LINVSVFIPFGELVHIIGPSGSGKSTFI 479
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
230-303 |
2.74e-03 |
|
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: 41.28 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 230 FHIAENLAISLSCLIISF----RYSWSLTLVVLASYPIIILVVGFINSFLSSAYekdRKSSEKAASI---LEKSISAIQT 302
Cdd:cd18549 117 HHGPEDLFISIITIIGSFiillTINVPLTLIVFALLPLMIIFTIYFNKKMKKAF---RRVREKIGEInaqLEDSLSGIRV 193
|
.
gi 162312251 303 V 303
Cdd:cd18549 194 V 194
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
110-319 |
2.78e-03 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 41.17 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 110 FTCLSAAL--EPLMTWTTGKVFDALSQYatsqitlgkmislINFNSLLITIFGLasCVFSFGVRF-------LWQYLSAI 180
Cdd:cd18590 2 FLFLTLAVicETFIPYYTGRVIDILGGE-------------YQHNAFTSAIGLM--CLFSLGSSLsaglrggLFMCTLSR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 181 AGKRARSLCFHVLSSKSSTFYSltESKSGLVNS-VDRCIQFYEKSISLPMFHIAENLAISLSCLIISFRYSWSLTLVVLA 259
Cdd:cd18590 67 LNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSrLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 260 SYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADA 319
Cdd:cd18590 145 EMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEA 204
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
454-477 |
4.73e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 4.73e-03
10 20
....*....|....*....|....
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKST 477
Cdd:COG0178 18 NIDVDIPRNKLVVITGLSGSGKSS 41
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
570-643 |
6.49e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 6.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312251 570 SLSGGQQQRIALARALLRDTEILILDEPTSALDpitknlvMDAI----RAHRKGKTTLV-ITHDmsqinNDELVLVIDK 643
Cdd:PRK10636 149 DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAViwleKWLKSYQGTLIlISHD-----RDFLDPIVDK 215
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1118-1183 |
6.76e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 6.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312251 1118 LNNVSLSIEAREKVAIVGISGSGKSTLVE------LLRKTYPSEDIY-----IDGypLTNIDtnwllkKVAIVDQKP 1183
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNdilypaLARKLNGAKEKPgphdsIEG--LEHID------KVIDIDQSP 689
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
570-643 |
7.48e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 570 SLSGGQQQ------RIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKT----TLVITHDMSQINNDELVL 639
Cdd:PRK01156 801 SLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSdipqVIMISHHRELLSVADVAY 880
|
....
gi 162312251 640 VIDK 643
Cdd:PRK01156 881 EVKK 884
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
243-329 |
8.34e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 39.80 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 243 LIISFRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACST 322
Cdd:cd18564 146 LGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRK 225
|
....*..
gi 162312251 323 SSKSFLR 329
Cdd:cd18564 226 SLRAGLR 232
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
454-479 |
9.16e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 9.16e-03
10 20
....*....|....*....|....*.
gi 162312251 454 NVSVFIPFGELVHIIGPSGSGKSTFI 479
Cdd:COG0178 623 NVDVEIPLGVLTCVTGVSGSGKSTLV 648
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
886-1061 |
9.46e-03 |
|
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: 39.80 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 886 NNISDMRNMISSLIEEVFIAFTMAIIGIAWSFATGWRLAAVLVAVSPILCLTSRMFSYIyvsTERMCQDVVIS---TTSI 962
Cdd:cd18555 106 NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKK---IKKLNQEEIVAqtkVQSY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 963 LHKTIVNLDTIKGYSVLSFFRENHKNSLRKSWEAFKRRAFWTSLGFAINNSLLYFVRALLFYCSSIFISKEFYTVEQMVQ 1042
Cdd:cd18555 183 LTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIA 262
|
170
....*....|....*....
gi 162312251 1043 VLSLATFTLLMASTCIMSL 1061
Cdd:cd18555 263 FSSLAGSFLTPIVSLINSY 281
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
467-628 |
9.85e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.17 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 467 IIGPSGSGKSTF---ISLLLRYFSPTYGNIYLDDFPLEEIDehvlgstitlvCQQPVIFDMTIReNIIMRNENASESDFE 543
Cdd:cd03279 33 ICGPTGAGKSTIldaITYALYGKTPRYGRQENLRSVFAPGE-----------DTAEVSFTFQLG-GKKYRVERSRGLDYD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312251 544 EVCRLALV--DEFALTFDQSYDTpckeasLSGGQQQRIALARAL-LRDT---------EILILDEPTSALDPITKNLVMD 611
Cdd:cd03279 101 QFTRIVLLpqGEFDRFLARPVST------LSGGETFLASLSLALaLSEVlqnrggarlEALFIDEGFGTLDPEALEAVAT 174
|
170
....*....|....*...
gi 162312251 612 AIRA-HRKGKTTLVITHD 628
Cdd:cd03279 175 ALELiRTENRMVGVISHV 192
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