|
Name |
Accession |
Description |
Interval |
E-value |
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-599 |
5.86e-116 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 356.81 E-value: 5.86e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 15 QLVQRFVRIQKVFFpsWSSQNVLMFMTLLCVTLLEQLVIY-QVGLipSQYYGV----LGNKDLDGFKALTLLAVTLIVLN 89
Cdd:COG4178 2 SLLRQFWRLARPYW--RSEEKWKAWGLLALLLLLTLASVGlNVLL--NFWNRDfydaLQARDAAAFWQQLGVFALLAAIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 90 STLKSFDQFTCNLLYVSWRKDLTEHLHHLYFRARVYYTLNVLRDDIDNPDQRISQDVERFCRQLSSVTSKLIISPFTLTY 169
Cdd:COG4178 78 ILLAVYQTYLRQRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDIRLFTETTLSLSLGLLSSVVTLIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 170 YTYQCFQSTGWLgPVSIFGYFIV--GTMV----NKTLMGPIVT-----KLV----QQEKLEGDFRFKHMQIRVNAEPAAF 234
Cdd:COG4178 158 FIGILWSLSGSL-TFTLGGYSITipGYMVwaalIYAIIGTLLThligrPLIrlnfEQQRREADFRFALVRVRENAESIAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 235 YRAGLVEHMRTDRRLQRLLQTQRELMSRELWLYIGINTFDYLGSILSYVVIAIPIFSGV--YGDLSPTelstlvsknAFV 312
Cdd:COG4178 237 YRGEAAERRRLRRRFDAVIANWRRLIRRQRNLTFFTTGYGQLAVIFPILVAAPRYFAGEitLGGLMQA---------ASA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 313 CIYLISCFTQLIDLSTTLSDVAGYTHRIGELQEALLDMSRKSQDCEALGESEwdldktpgcpttepsDTAFLLDRVSILA 392
Cdd:COG4178 308 FGQVQGALSWFVDNYQSLAEWRATVDRLAGFEEALEAADALPEAASRIETSE---------------DGALALEDLTLRT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 393 PSsDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADfgpHGVLFLPQKPFFTDGTLREQVIY 472
Cdd:COG4178 373 PD-GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAG---ARVLFLPQRPYLPLGTLREALLY 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 473 PLkeiypDSGSADDERIVRFLELAGLSSLVARtggLDQQVDWNwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTE 552
Cdd:COG4178 449 PA-----TAEAFSDAELREALEAVGLGHLAER---LDEEADWD--QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 568979103 553 EAESELYR-IGQQL-GMTFISVGHRPSLEKFHSWVLRLHGGGSWELTRI 599
Cdd:COG4178 519 ENEAALYQlLREELpGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPA 567
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-596 |
1.96e-95 |
|
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: 305.91 E-value: 1.96e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 18 QRFVRIQKVFFPSWSSQNVLMFMT----LLCVTLLEQLVIYQVGLIPSqyyGVLGNKDLDGFKAL---TLLAVTLIVLNS 90
Cdd:TIGR00954 77 GKLDFLLKILIPRVFCKETGLLILiaflLVSRTYLSVYVATLDGQIES---SIVRRSPRNFAWILfkwFLIAPPASFINS 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 91 TLKsfdqFTCNLLYVSWRKDLTEHLHHLYFRARVYYTLNVLRDDIDNPDQRISQDVERFCRQLSSVTSKLIISPFTLTYY 170
Cdd:TIGR00954 154 AIK----YLLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILY 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 171 TYQCFQSTGWLGPVSIFGYFIVgTMVNKTLMGPIVTKLVQQE-KLEGDFRFKHMQIRVNAEPAAFYRAGLVEHMRTDRRL 249
Cdd:TIGR00954 230 SFKLLTALGSVGPAGLFAYLFA-TGVVLTKLRPPIGKLTVEEqALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSF 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 250 QRL-LQTQRELMSRELWLYIGINTFDYLGSILSYVVIAIPIFSGV---YGDLSPTELSTLVSKNAFVCIYLISCFTQLID 325
Cdd:TIGR00954 309 YRLvEHLNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKThpaFLEMSEEELMQEFYNNGRLLLKAADALGRLML 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 326 LSTTLSDVAGYTHRIGELQEALLDMSR------KSQDCEALGESEWDLDKTPGCPTTEPSDTAFLLDRVSILAPSSDKpL 399
Cdd:TIGR00954 389 AGRDMTRLAGFTARVDTLLQVLDDVKSgnfkrpRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDV-L 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 400 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGsvqMLADFGPHGVLFLPQKPFFTDGTLREQVIYPL-KEIY 478
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG---RLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDsSEDM 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 479 PDSGSADDErIVRFLELAGLSSLVARTGGLDQQVDWNwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESEL 558
Cdd:TIGR00954 545 KRRGLSDKD-LEQILDNVQLTHILEREGGWSAVQDWM--DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM 621
|
570 580 590
....*....|....*....|....*....|....*...
gi 568979103 559 YRIGQQLGMTFISVGHRPSLEKFHSWVLRLHGGGSWEL 596
Cdd:TIGR00954 622 YRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
23-290 |
1.02e-93 |
|
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family of ABC transporters and shares sequence similarity with pfam00664. Mutations in this domain in Swiss:P28288 are believed responsible for Zellweger Syndrome-2; mutations in Swiss:P33897 are responsible for recessive X-linked adrenoleukodystrophy. A Saccharomyces cerevisiae homolog is involved in the import of long-chain fatty acids.
Pssm-ID: 399466 Cd Length: 269 Bit Score: 288.74 E-value: 1.02e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 23 IQKVFFPSWSSQNVLMFMTLLCVTLLEQLVIYQVGLIPSQYYGVLGNKDLDGFKALTLLAVTLIVLNSTLKSFDQFTCNL 102
Cdd:pfam06472 1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 103 LYVSWRKDLTEHLHHLYFRARVYYTLNVLRDDIDNPDQRISQDVERFCRQLSSVTSKLIISPFTLTYYTYQCFQSTGWLG 182
Cdd:pfam06472 81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 183 PVSIFGYFIVGTMVNKTLMGPIVTKLVQQEKLEGDFRFKHMQIRVNAEPAAFYRAGLVEHMRTDRRLQRLLQTQRELMSR 262
Cdd:pfam06472 161 PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILRR 240
|
250 260
....*....|....*....|....*....
gi 568979103 263 ELWLYIGINTF-DYLGSILSYVVIAIPIF 290
Cdd:pfam06472 241 RLWYGFIEDFVlKYTWSILGYVLVALPIF 269
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
383-594 |
2.44e-74 |
|
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: 234.74 E-value: 2.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 383 FLLDRVSILAPSsDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADfgpHGVLFLPQKPFFT 462
Cdd:cd03223 1 IELENLSLATPD-GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG---EDLLFLPQRPYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 463 DGTLREQVIYPlkeiypdsgsadderivrflelaglsslvartggldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAV 542
Cdd:cd03223 77 LGTLREQLIYP------------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568979103 543 LDEATSALTEEAESELYRIGQQLGMTFISVGHRPSLEKFHSWVLRLHGGGSW 594
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
66-591 |
1.73e-33 |
|
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: 136.12 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 66 VLGNKDLDGFKALTLLAVTLIVLNSTLKSFDQF----TCNLLYVSWRKDLTEHLHHL---YFRARvyYTlnvlrddidnP 138
Cdd:COG2274 186 VLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYlllrLGQRIDLRLSSRFFRHLLRLplsFFESR--SV----------G 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 139 D--QRIsQDVERFCRQLSSVTSKLIIS-PFTLTYYTYQCFQStGWLGPVSIFG---YFIVGTmvnktLMGPIVTKLVQQE 212
Cdd:COG2274 254 DlaSRF-RDVESIREFLTGSLLTALLDlLFVLIFLIVLFFYS-PPLALVVLLLiplYVLLGL-----LFQPRLRRLSREE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 213 -KLEGDFR------FKHMQ-IRV-NAEPAAFYRaglvehmrTDRRLQRLLQTQRELMSRELWLYIGINTFdylgSILSYV 283
Cdd:COG2274 327 sEASAKRQsllvetLRGIEtIKAlGAESRFRRR--------WENLLAKYLNARFKLRRLSNLLSTLSGLL----QQLATV 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 284 VIaipIFSGVY----GDLSpteLSTLVsknAFVCI--YLISCFTQLIDLSTTLSDVAGYTHRIGELQEAlldmsrksqdc 357
Cdd:COG2274 395 AL---LWLGAYlvidGQLT---LGQLI---AFNILsgRFLAPVAQLIGLLQRFQDAKIALERLDDILDL----------- 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 358 ealgESEWDLDKTPgcPTTEPSDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGM 437
Cdd:COG2274 455 ----PPEREEGRSK--LSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 438 KGSVQM----LADFGPH------GVlfLPQKPFFTDGTLREQVIYplkeiypDSGSADDERIVRFLELAGLSSLVAR-TG 506
Cdd:COG2274 529 SGRILIdgidLRQIDPAslrrqiGV--VLQDVFLFSGTIRENITL-------GDPDATDEEIIEAARLAGLHDFIEAlPM 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 507 GLDQQVDwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQL--GMTFISVGHRPSLEKFHSW 584
Cdd:COG2274 600 GYDTVVG-EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLlkGRTVIIIAHRLSTIRLADR 678
|
....*..
gi 568979103 585 VLRLHGG 591
Cdd:COG2274 679 IIVLDKG 685
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
36-577 |
6.11e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 115.26 E-value: 6.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 36 VLMFMTLLCVTLLEQLVIYQVGLIPSQyygVLGNKDLDGFKALTLLAVTLIVLNSTLKSFDQFTCNLLYVS----WRKDL 111
Cdd:COG1132 24 ILALLLLLLSALLELLLPLLLGRIIDA---LLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRvvadLRRDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 112 TEHLHHL---YF-RARVYYTLNVLRDDIDNpdqrisqdVERFcrqLSSVTSKLIISPFTLTYYTYQCFQSTGWLGPVSIF 187
Cdd:COG1132 101 FEHLLRLplsFFdRRRTGDLLSRLTNDVDA--------VEQF---LAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 188 GyFIVGTMVNKTLMGPIVTKLVQQEKLEGDFrFKHMQ-----IRV----NAEPAafyraglvEHMRTDRRLQRLLQTQRE 258
Cdd:COG1132 170 V-LPLLLLVLRLFGRRLRKLFRRVQEALAEL-NGRLQeslsgIRVvkafGREER--------ELERFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 259 LMSRELWLYIGINTFDYLGSILSYVVIAIPIFSGvygDLSPTELSTLVSknafvciYLISCFTQLIDLSTTLSDvagyth 338
Cdd:COG1132 240 AARLSALFFPLMELLGNLGLALVLLVGGLLVLSG---SLTVGDLVAFIL-------YLLRLFGPLRQLANVLNQ------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 339 rigeLQEALLDMSRksqdCEALGESEWDLDKTPGCPTTEPSDTAFLLDRVSiLAPSSDKPLIKDLSLKICEGQSLLITGN 418
Cdd:COG1132 304 ----LQRALASAER----IFELLDEPPEIPDPPGAVPLPPVRGEIEFENVS-FSYPGDRPVLKDISLTIPPGETVALVGP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 419 TGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPHG----VLFLPQKPFFTDGTLREQVIYPLKEiypdsgsADDERIV 490
Cdd:COG1132 375 SGSGKSTLVNLLLRFYDPTSGRILIdgvdIRDLTLESlrrqIGVVPQDTFLFSGTIRENIRYGRPD-------ATDEEVE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 491 RFLELAGLSSLVAR-TGGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSALteEAESElYRIGQQL---- 565
Cdd:COG1132 448 EAAKAAQAHEFIEAlPDGYDTVVGERGVN-LSGGQRQRIAIARALLKDPPILILDEATSAL--DTETE-ALIQEALerlm 523
|
570
....*....|...
gi 568979103 566 -GMTFISVGHRPS 577
Cdd:COG1132 524 kGRTTIVIAHRLS 536
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
395-591 |
2.65e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.82 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 395 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPHG----VLFLPQKPFFTDGTL 466
Cdd:COG4619 11 GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgKPLSAMPPPEwrrqVAYVPQEPALWGGTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 467 REQVIYPLKeiyPDSGSADDERIVRFLELAGLSSLVartggLDQQVDwnwydVLSPGEMQRLSFARLFYLQPKYAVLDEA 546
Cdd:COG4619 91 RDNLPFPFQ---LRERKFDRERALELLERLGLPPDI-----LDKPVE-----RLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568979103 547 TSAL----TEEAESELYRIGQQLGMTFISVGHRPSLEKFHSW-VLRLHGG 591
Cdd:COG4619 158 TSALdpenTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADrVLTLEAG 207
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
385-591 |
4.96e-26 |
|
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: 112.54 E-value: 4.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 385 LDRVSILAPSsDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGP----HGVLFLP 456
Cdd:COG4988 339 LEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingVDLSDLDPaswrRQIAWVP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 457 QKPFFTDGTLREQV-IYplkeiYPDsgsADDERIVRFLELAGLSSLVAR-TGGLDQQVD---WNwydvLSPGEMQRLSFA 531
Cdd:COG4988 418 QNPYLFAGTIRENLrLG-----RPD---ASDEELEAALEAAGLDEFVAAlPDGLDTPLGeggRG----LSGGQAQRLALA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568979103 532 RLFYLQPKYAVLDEATSALTEEAESELYRIGQQL--GMTFISVGHRPSLEKFHSWVLRLHGG 591
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLAQADRILVLDDG 547
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
385-578 |
6.05e-26 |
|
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: 106.13 E-value: 6.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 385 LDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV--------QMLADFGPHGVLFLP 456
Cdd:cd03245 5 FRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirQLDPADLRRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 457 QKPFFTDGTLREQVIYplkeiypDSGSADDERIVRFLELAGLSSLVARTG-GLDQQVDWNWYDvLSPGEMQRLSFARLFY 535
Cdd:cd03245 85 QDVTLFYGTLRDNITL-------GAPLADDERILRAAELAGVTDFVNKHPnGLDLQIGERGRG-LSGGQRQAVALARALL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568979103 536 LQPKYAVLDEATSALTEEAESELYRIGQQL--GMTFISVGHRPSL 578
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSL 201
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
374-578 |
2.86e-24 |
|
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: 106.99 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 374 PTTEPSDTAFLLDRVSILAPSSDkPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGP 449
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 450 HG----VLFLPQKPFFTDGTLREQVIYPLKEiypdsgsADDERIVRFLELAGLSSLV-ARTGGLDQQVDWNWYDvLSPGE 524
Cdd:TIGR02857 392 DSwrdqIAWVPQHPFLFAGTIAENIRLARPD-------ASDAEIREALERAGLDEFVaALPQGLDTPIGEGGAG-LSGGQ 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568979103 525 MQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQL--GMTFISVGHRPSL 578
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLAL 519
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
385-591 |
2.01e-23 |
|
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: 97.29 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 385 LDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM---------LADFGPHgVLFL 455
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqwdPNELGDH-VGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 456 PQKPFFTDGTLREqviyplkeiypdsgsadderivrflelaglsslvartggldqqvdwnwyDVLSPGEMQRLSFARLFY 535
Cdd:cd03246 82 PQDDELFSGSIAE-------------------------------------------------NILSGGQRQRLGLARALY 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568979103 536 LQPKYAVLDEATSALTEEAESELYRIGQQL---GMTFISVGHRPSLEKFHSWVLRLHGG 591
Cdd:cd03246 113 GNPRILVLDEPNSHLDVEGERALNQAIAALkaaGATRIVIAHRPETLASADRILVLEDG 171
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
385-591 |
4.13e-23 |
|
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: 97.54 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 385 LDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGL---------WEGMKGSVQMLADFGPH-GVLF 454
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLlgptsgevlVDGKDLTKLSLKELRRKvGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 455 lpQKP---FFTDgTLREQVIYPLkEIYPDSGSADDERIVRFLELAGLSSLvartggldqqVDWNWYDvLSPGEMQRLSFA 531
Cdd:cd03225 82 --QNPddqFFGP-TVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGL----------RDRSPFT-LSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568979103 532 RLFYLQPKYAVLDEATSALTEEAESELYRIGQQL---GMTFISVGHRPS-LEKFHSWVLRLHGG 591
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkaeGKTIIIVTHDLDlLLELADRVIVLEDG 210
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
385-591 |
4.59e-23 |
|
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: 96.30 E-value: 4.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 385 LDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPHG----VLFLP 456
Cdd:cd03228 3 FKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgVDLRDLDLESlrknIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 457 QKPFFTDGTLREqviyplkeiypdsgsadderivrflelaglsslvartggldqqvdwNwydVLSPGEMQRLSFARLFYL 536
Cdd:cd03228 83 QDPFLFSGTIRE----------------------------------------------N---ILSGGQRQRIAIARALLR 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568979103 537 QPKYAVLDEATSALTEEAESELYRIGQQL--GMTFISVGHRPSLEKFHSWVLRLHGG 591
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALakGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
395-591 |
4.11e-21 |
|
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: 92.29 E-value: 4.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 395 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGsvQMLADFGP----------HGVLFLPQKPFFTDG 464
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKG--QILIDGIDirdisrkslrSMIGVVLQDTFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 465 TLREQVIYplkeiypDSGSADDERIVRFLELAGLSSLVAR-TGGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVL 543
Cdd:cd03254 92 TIMENIRL-------GRPNATDEEVIEAAKEAGAHDFIMKlPNGYDTVLGENG-GNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568979103 544 DEATSALTEEAESelyRIGQQL-----GMTFISVGHRPSLEKFHSWVLRLHGG 591
Cdd:cd03254 164 DEATSNIDTETEK---LIQEALeklmkGRTSIIIAHRLSTIKNADKILVLDDG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
396-591 |
5.01e-20 |
|
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: 87.30 E-value: 5.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmladFGPHGVLFLPQKPfftdgtLREQVIYplk 475
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL----IDGKDIAKLPLEE------LRRRIGY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 476 eiypdsgsadderivrflelaglsslvartggLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAE 555
Cdd:cd00267 78 --------------------------------VPQ---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568979103 556 SELYRIGQQL---GMTFISVGHRPSL-EKFHSWVLRLHGG 591
Cdd:cd00267 117 ERLLELLRELaeeGRTVIIVTHDPELaELAADRVIVLKDG 156
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
278-558 |
2.54e-18 |
|
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: 88.19 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 278 SILSYVVIAIPIFSGvyGDLSPTELSTLVsknaFVCIYLISCFTQLIDLSTTLSDVAGYTHRIGELQEALLDmsrksqdc 357
Cdd:TIGR02868 251 AVLGALWAGGPAVAD--GRLAPVTLAVLV----LLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGP-------- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 358 EALGESEWDLDKTPGCPTTEPSDTAFLLDrvsilapsSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGM 437
Cdd:TIGR02868 317 VAEGSAPAAGAVGLGKPTLELRDLSAGYP--------GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 438 KGSVqMLADFGPHG---------VLFLPQKPFFTDGTLREQVIYPLKEiypdsgsADDERIVRFLELAGLSSLVART-GG 507
Cdd:TIGR02868 389 QGEV-TLDGVPVSSldqdevrrrVSVCAQDAHLFDTTVRENLRLARPD-------ATDEELWAALERVGLADWLRALpDG 460
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568979103 508 LDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESEL 558
Cdd:TIGR02868 461 LDTVLGEGG-ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL 510
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
400-548 |
7.09e-18 |
|
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: 80.77 E-value: 7.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 400 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGL---------WEGMKGSVQMLADFGpHGVLFLPQKP-FFTDGTLREQ 469
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLlsptegtilLDGQDLTDDERKSLR-KEIGYVFQDPqLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568979103 470 VIYPLKEIYPDSgSADDERIVRFLELAGLSSLVARTGGldqqvdwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATS 548
Cdd:pfam00005 80 LRLGLLLKGLSK-REKDARAEEALEKLGLGDLADRPVG-------ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
396-574 |
4.48e-17 |
|
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: 80.69 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMK-----GSVQMLAD--FGPH----------GVLFlpQK 458
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKdiYDLDvdvlelrrrvGMVF--QK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 459 PFFTDGTLREQVIYPLKeiypDSGSAD----DERIVRFLELAGLSSLVA-RTGGLDqqvdwnwydvLSPGEMQRLSFARL 533
Cdd:cd03260 90 PNPFPGSIYDNVAYGLR----LHGIKLkeelDERVEEALRKAALWDEVKdRLHALG----------LSGGQQQRLCLARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568979103 534 FYLQPKYAVLDEATSAL----TEEAESELYRIGQQlgMTFISVGH 574
Cdd:cd03260 156 LANEPEVLLLDEPTSALdpisTAKIEELIAELKKE--YTIVIVTH 198
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
397-575 |
5.78e-17 |
|
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: 80.23 E-value: 5.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 397 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPHgVL-----FLPQKPFFTDGTLR 467
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdgvdISKIGLH-DLrsrisIIPQDPVLFSGTIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 468 EQvIYPLKEiypdsgsADDERIVRFLELAGLSSLV-ARTGGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDEA 546
Cdd:cd03244 96 SN-LDPFGE-------YSDEELWQALERVGLKEFVeSLPGGLDTVVEEGG-ENLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190
....*....|....*....|....*....|....*
gi 568979103 547 TSALTEEAESELyrigQQL------GMTFISVGHR 575
Cdd:cd03244 167 TASVDPETDALI----QKTireafkDCTVLTIAHR 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
397-598 |
6.77e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.00 E-value: 6.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 397 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSvqmladfgphGVLFLPQKPFFTDGTLREQViyplke 476
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA----------GCVDVPDNQFGREASLIDAI------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 477 iyPDSGSADDerIVRFLELAGLSSLvartggldqqvdWNW---YDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE 553
Cdd:COG2401 107 --GRKGDFKD--AVELLNAVGLSDA------------VLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568979103 554 AESELYRIGQQL----GMTFISVGHRPSLEKFHS--WVLRLHGGGSWELTR 598
Cdd:COG2401 171 TAKRVARNLQKLarraGITLVVATHHYDVIDDLQpdLLIFVGYGGVPEEKR 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
396-561 |
1.43e-16 |
|
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: 78.67 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGL---------WEGmkGSVQMLADFGPHGVLFLPQKPFFTDG-T 465
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLlppsagevlWNG--EPIRDAREDYRRRLAYLGHADGLKPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 466 LREQVIYpLKEIYPDsgSADDERIVRFLELAGLSSLvartggLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDE 545
Cdd:COG4133 92 VRENLRF-WAALYGL--RADREAIDEALEAVGLAGL------ADLPV-----RQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170
....*....|....*.
gi 568979103 546 ATSALTEEAESELYRI 561
Cdd:COG4133 158 PFTALDAAGVALLAEL 173
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
393-577 |
2.58e-16 |
|
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: 78.43 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 393 PSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPHG----VLFLPQKPFFTDG 464
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdVRDYTLASlrrqIGLVSQDVFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 465 TLREQVIYPLKEiypdsgsADDERIVRFLELAGLSSLVART-GGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVL 543
Cdd:cd03251 91 TVAENIAYGRPG-------ATREEVEEAARAANAHEFIMELpEGYDTVIGERGVK-LSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 568979103 544 DEATSALTEEAESELYRIGQQL--GMTFISVGHRPS 577
Cdd:cd03251 163 DEATSALDTESERLVQAALERLmkNRTTFVIAHRLS 198
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
395-588 |
6.04e-16 |
|
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: 76.80 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 395 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQML---ADFGPHGVLFLPQKPFF-TD--GTLRE 468
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgkpLEKERKRIGYVPQRRSIdRDfpISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 469 QV---IYPLKEIYPDSGSADDERIVRFLELAGLSSLVARTggLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDE 545
Cdd:cd03235 90 VVlmgLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQ--IGE---------LSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568979103 546 ATSALTEEAESELYRIGQQL---GMTFISVGH-RPSLEKFHSWVLRL 588
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELrreGMTILVVTHdLGLVLEYFDRVLLL 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
397-591 |
1.24e-15 |
|
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: 75.99 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 397 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV------------QMLADFGPHGVLFLPQK----PF 460
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisklseKELAAFRRRHIGFVFQSfnllPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 461 FTdgtLREQVIYPLkEIYPDSGSADDERIVRFLELAGLSSLvartggLDQQVDWnwydvLSPGEMQRLSFARLFYLQPKY 540
Cdd:cd03255 97 LT---ALENVELPL-LLAGVPKKERRERAEELLERVGLGDR------LNHYPSE-----LSGGQQQRVAIARALANDPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568979103 541 AVLDEATSALTEEAESE----LYRIGQQLGMTFISVGHRPSLEKFHSWVLRLHGG 591
Cdd:cd03255 162 ILADEPTGNLDSETGKEvmelLRELNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
396-574 |
2.19e-15 |
|
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: 75.74 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH----GVLFlpQK-PFFTDGTL 466
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgKDITNLPPHkrpvNTVF--QNyALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 467 REQVIYPLKeIYPDSGSADDERIVRFLELAGLSSLVARTggLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEA 546
Cdd:cd03300 90 FENIAFGLR-LKKLPKAEIKERVAEALDLVQLEGYANRK--PSQ---------LSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190
....*....|....*....|....*....|..
gi 568979103 547 TSALT----EEAESELYRIGQQLGMTFISVGH 574
Cdd:cd03300 158 LGALDlklrKDMQLELKRLQKELGITFVFVTH 189
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
276-577 |
2.29e-15 |
|
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: 79.38 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 276 LGSILSYVVIAIPIFSGVYGDLSPTELSTLvsknafvciylISCFTQLIDLSTTLSDVAGythrigELQEALLDmsrksq 355
Cdd:TIGR02203 247 IASLALAVVLFIALFQAQAGSLTAGDFTAF-----------ITAMIALIRPLKSLTNVNA------PMQRGLAA------ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 356 dCEALGESewdLDKTPgcpttEPSDTAFLLDR---------VSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSL 426
Cdd:TIGR02203 304 -AESLFTL---LDSPP-----EKDTGTRAIERargdvefrnVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 427 LRVLGGLWEGMKGSVQM---------LADFGPHgVLFLPQKPFFTDGTLREQVIYPlkeiypDSGSADDERIVRFLELAG 497
Cdd:TIGR02203 375 VNLIPRFYEPDSGQILLdghdladytLASLRRQ-VALVSQDVVLFNDTIANNIAYG------RTEQADRAEIERALAAAY 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 498 LSSLVART-GGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQL--GMTFISVGH 574
Cdd:TIGR02203 448 AQDFVDKLpLGLDTPIGENG-VLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLmqGRTTLVIAH 526
|
...
gi 568979103 575 RPS 577
Cdd:TIGR02203 527 RLS 529
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
400-574 |
1.67e-14 |
|
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: 73.14 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 400 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGP--HGVLFLPQ-KPFFTDGTLREQVIY 472
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLngkdITNLPPekRDISYVPQnYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 473 PLKEIYPDSgSADDERIVRFLELAGLSSLVARTGGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL-- 550
Cdd:cd03299 95 GLKKRKVDK-KEIERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSALdv 162
|
170 180
....*....|....*....|....*.
gi 568979103 551 --TEEAESELYRIGQQLGMTFISVGH 574
Cdd:cd03299 163 rtKEKLREELKKIRKEFGVTVLHVTH 188
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
396-577 |
4.24e-14 |
|
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: 72.19 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPHGVL----FLPQKPFFTDGTLR 467
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgVDIRDLNLRWLRsqigLVSQEPVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 468 EQVIYPLKeiypdsgSADDERIVRFLELAGLSSLVAR-TGGLDQQVDWNwYDVLSPGEMQRLSFARLFYLQPKYAVLDEA 546
Cdd:cd03249 95 ENIRYGKP-------DATDEEVEEAAKKANIHDFIMSlPDGYDTLVGER-GSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 568979103 547 TSALteEAESElyRIGQQ------LGMTFISVGHRPS 577
Cdd:cd03249 167 TSAL--DAESE--KLVQEaldramKGRTTIVIAHRLS 199
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
396-577 |
4.89e-14 |
|
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: 71.40 E-value: 4.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH--GVLFLPQKP-FFTDGTLRE 468
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgRDVTGVPPErrNIGMVFQDYaLFPHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 469 QVIYPLKEIYPDSGSAdDERIVRFLELAGLSSLVARtggldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATS 548
Cdd:cd03259 92 NIAFGLKLRGVPKAEI-RARVRELLELVGLEGLLNR-----------YPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190
....*....|....*....|....*....|...
gi 568979103 549 AL----TEEAESELYRIGQQLGMTFISVGHRPS 577
Cdd:cd03259 160 ALdaklREELREELKELQRELGITTIYVTHDQE 192
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
387-574 |
1.02e-13 |
|
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: 70.61 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 387 RVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV------------QMLADFGpHGVLF 454
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllklsrRLRKIRR-KEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 455 LPQKPF------FTdgtLREQVIYPLKEIYPDSGSADDERIVrFLELAGLsslvartgGLDQQVdwnwYDV----LSPGE 524
Cdd:cd03257 87 VFQDPMsslnprMT---IGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGV--------GLPEEV----LNRypheLSGGQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568979103 525 MQRLSFARLFYLQPKYAVLDEATSAL--TEEAE--SELYRIGQQLGMTFISVGH 574
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALdvSVQAQilDLLKKLQEELGLTLLFITH 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
396-577 |
1.28e-13 |
|
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: 70.72 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM---------LADFGPH-GVLflPQK-PFFTDg 464
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdirevtLDSLRRAiGVV--PQDtVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 465 TLREQVIY-----PLKEIYPDSGSAD-DERIVRFLElaGLSSLVARTGGLdqqvdwnwydvLSPGEMQRLSFARLFYLQP 538
Cdd:cd03253 90 TIGYNIRYgrpdaTDEEVIEAAKAAQiHDKIMRFPD--GYDTIVGERGLK-----------LSGGEKQRVAIARAILKNP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568979103 539 KYAVLDEATSALTEEAESELYRIGQQL--GMTFISVGHRPS 577
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLS 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
385-575 |
1.73e-13 |
|
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: 73.01 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 385 LDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEG---MKGSV----QMLADFGPHG----VL 453
Cdd:COG1123 7 VRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVlldgRDLLELSEALrgrrIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 454 FLPQKPF--FTDGTLREQVIYPLkEIYPDSGSADDERIVRFLELAGLSSLVARtggldqqvdwnwY-DVLSPGEMQRLSF 530
Cdd:COG1123 87 MVFQDPMtqLNPVTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDR------------YpHQLSGGQRQRVAI 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568979103 531 ARLFYLQPKYAVLDEATSAL--TEEAE--SELYRIGQQLGMTFISVGHR 575
Cdd:COG1123 154 AMALALDPDLLIADEPTTALdvTTQAEilDLLRELQRERGTTVLLITHD 202
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
379-574 |
1.95e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.59 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 379 SDTAFLLDRVSILAPssDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPHG--- 451
Cdd:PRK10575 8 SDTTFALRNVSFRVP--GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaQPLESWSSKAfar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 452 -VLFLPQKPFFTDG-TLREQVI---YPLKEIYPDSGSADDERIVRFLELAGLSSLVARTggldqqvdwnwYDVLSPGEMQ 526
Cdd:PRK10575 86 kVAYLPQQLPAAEGmTVRELVAigrYPWHGALGRFGAADREKVEEAISLVGLKPLAHRL-----------VDSLSGGERQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568979103 527 RLSFARLFYLQPKYAVLDEATSALTEEAESE----LYRIGQQLGMTFISVGH 574
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDvlalVHRLSQERGLTVIAVLH 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
398-574 |
2.99e-13 |
|
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: 69.53 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 398 PLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPHGVLFLPQK--------PFFTDGT 465
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgTDLTLLSGKELRKARRRigmifqhfNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 466 LREQVIYPLkEIYPDSGSADDERIVRFLELAGLSslvartggldQQVDwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDE 545
Cdd:cd03258 99 VFENVALPL-EIAGVPKAEIEERVLELLELVGLE----------DKAD-AYPAQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190
....*....|....*....|....*....|...
gi 568979103 546 ATSALTEEAESE----LYRIGQQLGMTFISVGH 574
Cdd:cd03258 167 ATSALDPETTQSilalLRDINRELGLTIVLITH 199
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
396-574 |
3.76e-13 |
|
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: 69.45 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPH---------GVLFlpQKP-FF 461
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgedISGLSEAelyrlrrrmGMLF--QSGaLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 462 TDGTLREQVIYPLKEIYPDSGSADDERIVRFLELAGLSslvartGGLDQqvdwnWYDVLSPGEMQRLSFARLFYLQPKYA 541
Cdd:cd03261 90 DSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLR------GAEDL-----YPAELSGGMKKRVALARALALDPELL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 568979103 542 VLDEATSAL----TEEAESELYRIGQQLGMTFISVGH 574
Cdd:cd03261 159 LYDEPTAGLdpiaSGVIDDLIRSLKKELGLTSIMVTH 195
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
396-591 |
3.91e-13 |
|
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: 69.44 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLI-KDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVqmLADfGPHGVLFLPQkpfftdgTLREQVIYPL 474
Cdd:cd03252 13 DGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV--LVD-GHDLALADPA-------WLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 475 KEIYPDSGSADD-----------ERIVRFLELAGLSSLVARTG-GLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAV 542
Cdd:cd03252 83 QENVLFNRSIRDnialadpgmsmERVIEAAKLAGAHDFISELPeGYDTIVGEQGAG-LSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568979103 543 LDEATSALTEEAESELYRIGQQL--GMTFISVGHRPSLEKFHSWVLRLHGG 591
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNADRIIVMEKG 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
392-591 |
1.21e-12 |
|
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: 67.11 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 392 APSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMladfgPHGVLFLPQKPFFTDGTLREQVI 471
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-----PGSIAYVSQEPWIQNGTIRENIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 472 --YPLkeiypdsgsaDDERIVRFLELAGLSSLVARTGGLDQQVdwnwydV------LSPGEMQRLSFARLFYLQPKYAVL 543
Cdd:cd03250 88 fgKPF----------DEERYEKVIKACALEPDLEILPDGDLTE------IgekginLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568979103 544 DEATSALTEEAESELYR--IGQQL--GMTFISVGHRPSLEKFHSWVLRLHGG 591
Cdd:cd03250 152 DDPLSAVDAHVGRHIFEncILGLLlnNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
388-578 |
1.65e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.52 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 388 VSILAPS-SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH----GVLFLPQK 458
Cdd:TIGR00958 484 VSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgVPLVQYDHHylhrQVALVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 459 PFFTDGTLREQVIYPLKeiypdsgSADDERIVRFLELAGLSSLVAR-TGGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQ 537
Cdd:TIGR00958 564 PVLFSGSVRENIAYGLT-------DTPDEEIMAAAKAANAHDFIMEfPNGYDTEVGEKG-SQLSGGQKQRIAIARALVRK 635
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568979103 538 PKYAVLDEATSALTEEAESELYRIGQQLGMTFISVGHRPSL 578
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLST 676
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
396-574 |
3.23e-12 |
|
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: 66.12 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmladFGPHGVLFLPQKPFFTDGTLREQVIYPLK 475
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIY----IGGRDVTDLPPKDRDIAMVFQNYALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 476 EIYPDSGSADDERIVRFLELAGLSSLVARTGGLDQQVDwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALT---- 551
Cdd:cd03301 88 TVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLD-RKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklr 166
|
170 180
....*....|....*....|...
gi 568979103 552 EEAESELYRIGQQLGMTFISVGH 574
Cdd:cd03301 167 VQMRAELKRLQQRLGTTTIYVTH 189
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
399-550 |
3.84e-12 |
|
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: 65.74 E-value: 3.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 399 LIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADFGPHGVL-----FLPQKP---FFTDgTLREQV 470
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERrksigYVMQDVdyqLFTD-SVREEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 471 IYPLKEiyPDSGSADDERIVRFLELAGLsslvartggldqqVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 550
Cdd:cd03226 94 LLGLKE--LDAGNEQAETVLKDLDLYAL-------------KERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
388-592 |
4.31e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.63 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 388 VSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGL---------WEG-------------MKGSVQMLA 445
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLespsqgnvsWRGeplaklnraqrkaFRRDIQMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 446 DFGPHGVLflPQKpfftdgTLREQVIYPLKEIYPDSGSADDERIVRFLELAGLSSLVARTggLDQQvdwnwydvLSPGEM 525
Cdd:PRK10419 96 QDSISAVN--PRK------TVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDK--RPPQ--------LSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568979103 526 QRLSFARLFYLQPKYAVLDEATS----ALTEEAESELYRIGQQLGMTFISVGHRPSL-EKFHSWVLRLHGGG 592
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSnldlVLQAGVIRLLKKLQQQFGTACLFITHDLRLvERFCQRVMVMDNGQ 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
396-574 |
7.64e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 67.28 E-value: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVqMLADfgpHGVLFLP--QKP---------FFTDG 464
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI-MLDG---QDITHVPaeNRHvntvfqsyaLFPHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 465 TLREQVIYPLK-------EIYPdsgsaddeRIVRFLELAGLSSLVARTgglDQQvdwnwydvLSPGEMQRLSFARLFYLQ 537
Cdd:PRK09452 102 TVFENVAFGLRmqktpaaEITP--------RVMEALRMVQLEEFAQRK---PHQ--------LSGGQQQRVAIARAVVNK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568979103 538 PKYAVLDEATSALT----EEAESELYRIGQQLGMTFISVGH 574
Cdd:PRK09452 163 PKVLLLDESLSALDyklrKQMQNELKALQRKLGITFVFVTH 203
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
393-574 |
8.37e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 65.91 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 393 PSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADFGPH----------GVLFlpQKP--F 460
Cdd:PRK13650 16 EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenvwdirhkiGMVF--QNPdnQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 461 FTDGTLREQVIY-------PLKEIypdsgsadDERIVRFLELAGLSSLVARTGGLdqqvdwnwydvLSPGEMQRLSFARL 533
Cdd:PRK13650 94 FVGATVEDDVAFglenkgiPHEEM--------KERVNEALELVGMQDFKEREPAR-----------LSGGQKQRVAIAGA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568979103 534 FYLQPKYAVLDEATSALTEEAESELYR----IGQQLGMTFISVGH 574
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKtikgIRDDYQMTVISITH 199
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
396-574 |
1.13e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.11 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGsvQMLAD----FGPH----------GVLFlPQKPFF 461
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG--DLIVDglkvNDPKvderlirqeaGMVF-QQFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 462 TDGTLREQVIY-PLKeiYPDSGSADDERIVRflELAGLSSLVARTGGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKY 540
Cdd:PRK09493 90 PHLTALENVMFgPLR--VRGASKEEAEKQAR--ELLAKVGLAERAHHYPSE--------LSGGQQQRVAIARALAVKPKL 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 568979103 541 AVLDEATSALTEEAESELYRIGQQL---GMTFISVGH 574
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLaeeGMTMVIVTH 194
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
128-556 |
1.14e-11 |
|
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: 68.05 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 128 LNVLRDDIDNPDQRISQDVERFCRQLSSVTSKLI------------ISPFTLTYYTYQCF-----QSTGWLGPVS---IF 187
Cdd:TIGR00957 1065 VNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIvillatpiaaviIPPLGLLYFFVQRFyvassRQLKRLESVSrspVY 1144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 188 GYFivgtmvNKTLMGPIVTKLVQQEKlegdfRFKHMQ-IRVNAEPAAFYraglvEHMRTDRrlqrllqtqrelmsrelWL 266
Cdd:TIGR00957 1145 SHF------NETLLGVSVIRAFEEQE-----RFIHQSdLKVDENQKAYY-----PSIVANR-----------------WL 1191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 267 YIGintfdylgsiLSYVVIAIPIFSGVYGDLSPTELST-LVSKNAFVCIYLISCFTQLIDLSTtlsdvagythrigELQE 345
Cdd:TIGR00957 1192 AVR----------LECVGNCIVLFAALFAVISRHSLSAgLVGLSVSYSLQVTFYLNWLVRMSS-------------EMET 1248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 346 ALLDMSRKSQDCEALGESEWDLDKTPGCPTTEPSDTAFLLDRVSILAPSSDKPLiKDLSLKICEGQSLLITGNTGTGKTS 425
Cdd:TIGR00957 1249 NIVAVERLKEYSETEKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVL-RHINVTIHGGEKVGIVGRTGAGKSS 1327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 426 LLRVLGGLWEGMKGSVQM----LADFGPHGVLF----LPQKPFFTDGTLREQvIYPLkeiypdsGSADDERIVRFLELAG 497
Cdd:TIGR00957 1328 LTLGLFRINESAEGEIIIdglnIAKIGLHDLRFkitiIPQDPVLFSGSLRMN-LDPF-------SQYSDEEVWWALELAH 1399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 498 LSSLV-ARTGGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAES 556
Cdd:TIGR00957 1400 LKTFVsALPDKLDHECAEGGEN-LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
367-550 |
1.21e-11 |
|
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: 67.24 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 367 LDKTPGCPTTEPSDTAFLL--DRVSI---LAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV 441
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLLevRNLSKrypVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 442 QM------------LADFGPH-GVLFlpQKP---FFTDGTLREQVIYPLKEIYPDSGSADDERIVRFLELAGLSSLVArt 505
Cdd:COG1123 323 LFdgkdltklsrrsLRELRRRvQMVF--QDPyssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLA-- 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568979103 506 ggldqqvdwNWY-DVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 550
Cdd:COG1123 399 ---------DRYpHELSGGQRQRVAIARALALEPKLLILDEPTSAL 435
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
393-575 |
2.14e-11 |
|
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: 62.72 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 393 PSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmLADFGPHG--------VLFLPQKPFFTDG 464
Cdd:cd03247 11 PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-LDGVPVSDlekalsslISVLNQRPYLFDT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 465 TLREQVIYPlkeiypdsgsadderivrflelaglsslvartggldqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLD 544
Cdd:cd03247 90 TLRNNLGRR----------------------------------------------FSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190
....*....|....*....|....*....|...
gi 568979103 545 EATSALTEEAESELYR-IGQQL-GMTFISVGHR 575
Cdd:cd03247 124 EPTVGLDPITERQLLSlIFEVLkDKTLIWITHH 156
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
401-577 |
2.31e-11 |
|
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: 63.47 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 401 KDLSLKI---CEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----------QMLADFGPH----GVLFlPQKPFFTD 463
Cdd:cd03297 11 PDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsRKKINLPPQqrkiGLVF-QQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 464 GTLREQVIYPLKEIypdSGSADDERIVRFLELAGLSSLVARtgGLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 543
Cdd:cd03297 90 LNVRENLAFGLKRK---RNREDRISVDELLDLLGLDHLLNR--YPAQ---------LSGGEKQRVALARALAAQPELLLL 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 568979103 544 DEATSAL----TEEAESELYRIGQQLGMTFISVGHRPS 577
Cdd:cd03297 156 DEPFSALdralRLQLLPELKQIKKNLNIPVIFVTHDLS 193
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
397-574 |
3.35e-11 |
|
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: 63.26 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 397 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPH-GVLF-----LPQKpfftdgTL 466
Cdd:cd03293 17 VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepVTGPGPDrGYVFqqdalLPWL------TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 467 REQVIYPLkEIYPDSGSADDERIVRFLELAGLSSLVARtggldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLDEA 546
Cdd:cd03293 91 LDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENA-----------YPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 568979103 547 TSAL---T-EEAESELYRIGQQLGMTFISVGH 574
Cdd:cd03293 159 FSALdalTrEQLQEELLDIWRETGKTVLLVTH 190
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
398-592 |
5.26e-11 |
|
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: 65.53 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 398 PLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPHG----VLFLPQKPFFTDGTLREQ 469
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLngfsLKDIDRHTlrqfINYLPQEPYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 470 VIYPLKEiypdsgSADDERIVRFLELAGLSSLVARTG-GLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATS 548
Cdd:TIGR01193 568 LLLGAKE------NVSQDEIWAACEIAEIKDDIENMPlGYQTELSEEGSS-ISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568979103 549 ALTEEAESELyrIGQQLGM---TFISVGHRPSLEKFHSWVLRLHGGG 592
Cdd:TIGR01193 641 NLDTITEKKI--VNNLLNLqdkTIIFVAHRLSVAKQSDKIIVLDHGK 685
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
371-581 |
6.33e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 65.23 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 371 PGCPTTEPSDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LAD 446
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLngqpIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 447 FGP----HGVLFLPQKPFFTDGTLREQVIYPLKEiypdsgsADDERIVRFLELAGLSSLVARTGGLDQqvdwnWYD---- 518
Cdd:PRK11160 407 YSEaalrQAISVVSQRVHLFSATLRDNLLLAAPN-------ASDEALIEVLQQVGLEKLLEDDKGLNA-----WLGeggr 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568979103 519 VLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQL--GMTFISVGHR-PSLEKF 581
Cdd:PRK11160 475 QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHRlTGLEQF 540
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
396-578 |
8.01e-11 |
|
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: 61.30 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMladfgphgvlflpqkpfftDGTLREQviYPLK 475
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL-------------------DGKDLAS--LSPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 476 EIypdsgsAddeRIVRF----LELAGLSSLVARTggldqqvdwnwYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL- 550
Cdd:cd03214 70 EL------A---RKIAYvpqaLELLGLAHLADRP-----------FNELSGGERQRVLLARALAQEPPILLLDEPTSHLd 129
|
170 180 190
....*....|....*....|....*....|.
gi 568979103 551 ---TEEAESELYRIGQQLGMTFISVGHRPSL 578
Cdd:cd03214 130 iahQIELLELLRRLARERGKTVVMVLHDLNL 160
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
396-574 |
1.14e-10 |
|
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: 61.92 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH---------GVLF----Lpqk 458
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlvdgQDITGLSEKelyelrrriGMLFqggaL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 459 pfFTDGTLREQVIYPLKEiYPDSGSADDERIVRF-LELAGLSSlvARTggldqqvdwnwydvLSPGE----MQ-RLSFAR 532
Cdd:COG1127 94 --FDSLTVFENVAFPLRE-HTDLSEAEIRELVLEkLELVGLPG--AAD--------------KMPSElsggMRkRVALAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568979103 533 LFYLQPKYAVLDEATSAL---TEEAESELYR-IGQQLGMTFISVGH 574
Cdd:COG1127 155 ALALDPEILLYDEPTAGLdpiTSAVIDELIReLRDELGLTSVVVTH 200
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
392-574 |
5.86e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 392 APSSDKPLIkDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----------LADFGPH----GVLF-LP 456
Cdd:PRK13643 15 SPFASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskQKEIKPVrkkvGVVFqFP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 457 QKPFFTDGTLREQVIYPlkEIYPDSGSADDERIVRFLELAGLSSLVARTGGLDqqvdwnwydvLSPGEMQRLSFARLFYL 536
Cdd:PRK13643 94 ESQLFEETVLKDVAFGP--QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFE----------LSGGQMRRVAIAGILAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568979103 537 QPKYAVLDEATSALTEEAESELYRIGQ---QLGMTFISVGH 574
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQLFEsihQSGQTVVLVTH 202
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
398-575 |
6.72e-10 |
|
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: 59.35 E-value: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 398 PLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPHGV----LFLPQKPFFTDGTLREQ 469
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdgidISTIPLEDLrsslTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 470 ViyplkEIYpdsGSADDERIVRFLELAGlsslvartGGLDqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSA 549
Cdd:cd03369 102 L-----DPF---DEYSDEEIYGALRVSE--------GGLN----------LSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180
....*....|....*....|....*...
gi 568979103 550 LTEEAESELYRIGQQL--GMTFISVGHR 575
Cdd:cd03369 156 IDYATDALIQKTIREEftNSTILTIAHR 183
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
397-550 |
7.39e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.79 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 397 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPH------GVlfLPQK-----PFf 461
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLngrpLADWSPAelarrrAV--LPQHsslsfPF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 462 tdgTLREQV---IYPLkeiyPDSGSADDERIVRFLELAGLSSLVARTggldqqvdwnwYDVLSPGEMQRLSFAR-LFYL- 536
Cdd:PRK13548 92 ---TVEEVVamgRAPH----GLSRAEDDALVAAALAQVDLAHLAGRD-----------YPQLSGGEQQRVQLARvLAQLw 153
|
170
....*....|....*...
gi 568979103 537 ----QPKYAVLDEATSAL 550
Cdd:PRK13548 154 epdgPPRWLLLDEPTSAL 171
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
398-559 |
7.55e-10 |
|
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: 62.24 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 398 PLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmladfgpHG--VLFLPQKPFFTDGTLREQVIYPLk 475
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-------HSgrISFSPQTSWIMPGTIKDNIIFGL- 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 476 eiypdsgSADDERIVRFLELAGLSSLVARTGGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAE 555
Cdd:TIGR01271 512 -------SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
....
gi 568979103 556 SELY 559
Cdd:TIGR01271 585 KEIF 588
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
399-591 |
1.15e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.21 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 399 LIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV-------QMLAD-------FGPHGVLFLPQK------ 458
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtiNLVRDkdgqlkvADKNQLRLLRTRltmvfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 459 --PFFTDGTLREQVIYPLKEIYPDSGSADDERIVRFLELAGLsslvartgglDQQVDWNWYDVLSPGEMQRLSFARLFYL 536
Cdd:PRK10619 100 hfNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGI----------DERAQGKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568979103 537 QPKYAVLDEATSALTEEAESELYRIGQQL---GMTFISVGHRPSLEK-FHSWVLRLHGG 591
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLaeeGKTMVVVTHEMGFARhVSSHVIFLHQG 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
393-574 |
1.36e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.26 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 393 PSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMladFGPH-------------GVLFlpQKP 459
Cdd:PRK13635 16 PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV---GGMVlseetvwdvrrqvGMVF--QNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 460 --FFTDGTLREQVIYPLKeiypDSGSADDERIVRF---LELAGLSSLvartggLDQQVDwnwydVLSPGEMQRLSFARLF 534
Cdd:PRK13635 91 dnQFVGATVQDDVAFGLE----NIGVPREEMVERVdqaLRQVGMEDF------LNREPH-----RLSGGQKQRVAIAGVL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568979103 535 YLQPKYAVLDEATSALT----EEAESELYRIGQQLGMTFISVGH 574
Cdd:PRK13635 156 ALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITH 199
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
396-574 |
1.39e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 60.11 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQ--SLLitGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH----GVLFlpQK----PFF 461
Cdd:COG3842 17 DVTALDDVSLSIEPGEfvALL--GPSGCGKTTLLRMIAGFETPDSGRIlldgRDVTGLPPEkrnvGMVF--QDyalfPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 462 tdgTLREQVIYPLK-------EIypdsgsadDERIVRFLELAGLSSLVARtggldqqvdwnwY-DVLSPGEMQRLSFARL 533
Cdd:COG3842 93 ---TVAENVAFGLRmrgvpkaEI--------RARVAELLELVGLEGLADR------------YpHQLSGGQQQRVALARA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568979103 534 FYLQPKYAVLDEATSAL----TEEAESELYRIGQQLGMTFISVGH 574
Cdd:COG3842 150 LAPEPRVLLLDEPLSALdaklREEMREELRRLQRELGITFIYVTH 194
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
396-574 |
1.71e-09 |
|
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: 57.20 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQML-ADFGPHGVLFLPQKP----FFTDGTL---- 466
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgEDLTDLEDELPPLRRrigmVFQDFALfphl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 467 --REQVIYPLkeiypdSGsadderivrflelaglsslvartggldqqvdwnwydvlspGEMQRLSFARLFYLQPKYAVLD 544
Cdd:cd03229 92 tvLENIALGL------SG----------------------------------------GQQQRVALARALAMDPDVLLLD 125
|
170 180 190
....*....|....*....|....*....|....
gi 568979103 545 EATSAL----TEEAESELYRIGQQLGMTFISVGH 574
Cdd:cd03229 126 EPTSALdpitRREVRALLKSLQAQLGITVVLVTH 159
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
393-550 |
1.91e-09 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 58.05 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 393 PSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMK---GSV-----QMLADFGPHGVLFLPQKPFFTDG 464
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQIlfngqPRKPDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 465 -TLREQVIY----PLKEIYPDSGSADDERIVRFLELAglsslvartgglDQQVDWNWYDVLSPGEMQRLSFARLFYLQPK 539
Cdd:cd03234 96 lTVRETLTYtailRLPRKSSDAIRKKRVEDVLLRDLA------------LTRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170
....*....|.
gi 568979103 540 YAVLDEATSAL 550
Cdd:cd03234 164 VLILDEPTSGL 174
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
378-574 |
2.96e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 58.27 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 378 PSDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLW------------EGMKGSVQMLA 445
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpddnpnskitvDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 446 DFGPH-GVLFlpQKP--FFTDGTLREQVIYPLKeiypDSGSADDE--RIVRflelaglsSLVARTGGLDQQVDWNWYdvL 520
Cdd:PRK13640 81 DIREKvGIVF--QNPdnQFVGATVGDDVAFGLE----NRAVPRPEmiKIVR--------DVLADVGMLDYIDSEPAN--L 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568979103 521 SPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQL----GMTFISVGH 574
Cdd:PRK13640 145 SGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITH 202
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
398-559 |
3.00e-09 |
|
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: 58.33 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 398 PLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmladfgpHG--VLFLPQKPFFTDGTLREQVIYPLk 475
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-------HSgrISFSSQFSWIMPGTIKENIIFGV- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 476 eiypdsgSADDERIVRFLELAGLSSLVARTGGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAE 555
Cdd:cd03291 123 -------SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
....
gi 568979103 556 SELY 559
Cdd:cd03291 196 KEIF 199
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
398-574 |
3.21e-09 |
|
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: 57.73 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 398 PLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH--GVLFLPQK-PFFTDGTLREQV 470
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggEDATDVPVQerNVGFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 471 IYPLKeIYPDSGSAD----DERIVRFLELAGLSSLVARtggldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLDEA 546
Cdd:cd03296 96 AFGLR-VKPRSERPPeaeiRAKVHELLKLVQLDWLADR-----------YPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190
....*....|....*....|....*....|..
gi 568979103 547 TSALTEEAESEL----YRIGQQLGMTFISVGH 574
Cdd:cd03296 164 FGALDAKVRKELrrwlRRLHDELHVTTVFVTH 195
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
312-575 |
3.58e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 312 VCIYLISCFTQL--------IDLSTTLSDVAGYTHRIGELQEALLDMSRKSQD----CEALGE-----SEW-DLDKTPGC 373
Cdd:PLN03232 1146 VMIWLTATFAVLrngnaenqAGFASTMGLLLSYTLNITTLLSGVLRQASKAENslnsVERVGNyidlpSEAtAIIENNRP 1225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 374 PTTEPSDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGP 449
Cdd:PLN03232 1226 VSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIddcdVAKFGL 1305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 450 HGVL----FLPQKPFFTDGTLREQvIYPLKEiypdsgsADDERIVRFLELAGLSSLVARTG-GLDQQVdWNWYDVLSPGE 524
Cdd:PLN03232 1306 TDLRrvlsIIPQSPVLFSGTVRFN-IDPFSE-------HNDADLWEALERAHIKDVIDRNPfGLDAEV-SEGGENFSVGQ 1376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568979103 525 MQRLSFARLFYLQPKYAVLDEATSALTEEAESELYR-IGQQL-GMTFISVGHR 575
Cdd:PLN03232 1377 RQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRtIREEFkSCTMLVIAHR 1429
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
146-550 |
3.73e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 146 VERFCRQLSSVTSkliiSPFTLTYYTYQCFQStgwLGPVSIFGYFIVGTMV-NKTLMGPIVTKLVQqeklEGdfrFKHMQ 224
Cdd:PLN03232 411 LQQIAEQLHGLWS----APFRIIVSMVLLYQQ---LGVASLFGSLILFLLIpLQTLIVRKMRKLTK----EG---LQWTD 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 225 IRVNAEPAAFYRAGLVEHMRTDRRLQRLLQTQR-ELMS--RELWLYIGINTFdYLGSILSYV-VIAIPIFSGVYGDLSPT 300
Cdd:PLN03232 477 KRVGIINEILASMDTVKCYAWEKSFESRIQGIRnEELSwfRKAQLLSAFNSF-ILNSIPVVVtLVSFGVFVLLGGDLTPA 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 301 ElstlvsknAFVCIYLISCF-TQLIDLSTTLSDVAGYTHRIGELQEALLDMSRKSQDCEALgesewdldkTPGCPTTEPS 379
Cdd:PLN03232 556 R--------AFTSLSLFAVLrSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPL---------QPGAPAISIK 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 380 DTAFLLDRvsilapSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLR-VLGGLWEGMKGSVQMLADfgphgVLFLPQK 458
Cdd:PLN03232 619 NGYFSWDS------KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-----VAYVPQV 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 459 PFFTDGTLREQVIYplkeiypdsGSA-DDERIVRFLELAGLSSLVARTGGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQ 537
Cdd:PLN03232 688 SWIFNATVRENILF---------GSDfESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSN 758
|
410
....*....|...
gi 568979103 538 PKYAVLDEATSAL 550
Cdd:PLN03232 759 SDIYIFDDPLSAL 771
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
396-552 |
4.36e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.03 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPHG----VLFLPQKPFFTDGTLR 467
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegEDISTLKPEIyrqqVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 468 EQVIYP--LKEIYPDsgsadDERIVRFLELAGLSSLVartggLDQQVDwnwydVLSPGEMQRLSFARLFYLQPKYAVLDE 545
Cdd:PRK10247 99 DNLIFPwqIRNQQPD-----PAIFLDDLERFALPDTI-----LTKNIA-----ELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
....*..
gi 568979103 546 ATSALTE 552
Cdd:PRK10247 164 ITSALDE 170
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
395-576 |
4.95e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.36 E-value: 4.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 395 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM---LADFGPH-------------GVLFLPQK 458
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkVLYFGKDifqidaiklrkevGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 459 PFfTDGTLREQVIYPLKEiypdSGSADDERIVRFLElaglSSLvaRTGGLDQQVdwnwYD-------VLSPGEMQRLSFA 531
Cdd:PRK14246 101 PF-PHLSIYDNIAYPLKS----HGIKEKREIKKIVE----ECL--RKVGLWKEV----YDrlnspasQLSGGQQQRLTIA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568979103 532 RLFYLQPKYAVLDEATSALTEEAESELYRIGQQLG--MTFISVGHRP 576
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKneIAIVIVSHNP 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
395-558 |
5.96e-09 |
|
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: 56.71 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 395 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGsvQMLADFGP---------HGVLFL-PQKPFFTDG 464
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGG--QVLLDGKPisqyehkylHSKVSLvGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 465 TLREQVIYPLkeiypdsGSADDERIVRFLELAGLSSLVAR-TGGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVL 543
Cdd:cd03248 103 SLQDNIAYGL-------QSCSFECVKEAAQKAHAHSFISElASGYDTEVGEKG-SQLSGGQKQRVAIARALIRNPQVLIL 174
|
170
....*....|....*
gi 568979103 544 DEATSALteEAESEL 558
Cdd:cd03248 175 DEATSAL--DAESEQ 187
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
396-577 |
1.30e-08 |
|
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: 57.91 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH------GVLflPQKP-FFTDg 464
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgQDIRDVTQAslraaiGIV--PQDTvLFND- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 465 TLREQVIYPLkeiyPDsgsADDERIVRFLELAGLSSLVART-GGLDQQVdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 543
Cdd:COG5265 447 TIAYNIAYGR----PD---ASEEEVEAAARAAQIHDFIESLpDGYDTRVger-glkLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190
....*....|....*....|....*....|....*...
gi 568979103 544 DEATSAL---TEEA-ESELYRIGQqlGMTFISVGHRPS 577
Cdd:COG5265 519 DEATSALdsrTERAiQAALREVAR--GRTTLVIAHRLS 554
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
400-574 |
1.50e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.97 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 400 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGsvQMLADfgphGVLFLPqkpfFTDGTLRE------QVIYP 473
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG--QVLID----GVDIAK----ISDAELREvrrkkiAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 474 LKEIYPDSGSADDERIvrFLELAGLSSLVARTGGLD--QQVDWNWY-----DVLSPGEMQRLSFARLFYLQPKYAVLDEA 546
Cdd:PRK10070 114 SFALMPHMTVLDNTAF--GMELAGINAEERREKALDalRQVGLENYahsypDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190
....*....|....*....|....*....|..
gi 568979103 547 TSALT----EEAESELYRIGQQLGMTFISVGH 574
Cdd:PRK10070 192 FSALDplirTEMQDELVKLQAKHQRTIVFISH 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
394-578 |
1.64e-08 |
|
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: 55.65 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 394 SSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmladFGPHGVLFLPQKPF----------FTD 463
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL----IDGTDINKLKGKALrqlrrqigmiFQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 464 GTL--REQVI-----------YPLKEIYPDSGSADDERIVRFLELAGLSSLV-ARTggldqqvdwnwyDVLSPGEMQRLS 529
Cdd:cd03256 87 FNLieRLSVLenvlsgrlgrrSTWRSLFGLFPKEEKQRALAALERVGLLDKAyQRA------------DQLSGGQQQRVA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568979103 530 FARLFYLQPKYAVLDEATSAL----TEEAESELYRIGQQLGMTFISVGHRPSL 578
Cdd:cd03256 155 IARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLHQVDL 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
400-575 |
1.65e-08 |
|
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: 55.52 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 400 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH-----GVL--FlpQKP-FFTDGTLR 467
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgEDITGLPPHeiarlGIGrtF--QIPrLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 468 EQVI---------YPLKEIYPDSGSADDERIVRFLELAGLSSLVARTGGLdqqvdwnwydvLSPGEMQRLSFARLFYLQP 538
Cdd:cd03219 94 ENVMvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGE-----------LSYGQQRRLEIARALATDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568979103 539 KYAVLDEATSALTEEaesELYRIGQ------QLGMTFISVGHR 575
Cdd:cd03219 163 KLLLLDEPAAGLNPE---ETEELAElirelrERGITVLLVEHD 202
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
400-574 |
1.74e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.18 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 400 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMladfGPH------------------GVLF-LPQKPF 460
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI----GERvitagkknkklkplrkkvGIVFqFPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 461 FTDGTLREQVIYPLKEIYPDsgsADDERIVR-FLELAGLS-SLVARTGgldqqvdwnwYDvLSPGEMQRLSFARLFYLQP 538
Cdd:PRK13634 99 FEETVEKDICFGPMNFGVSE---EDAKQKAReMIELVGLPeELLARSP----------FE-LSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568979103 539 KYAVLDEATSALTEEAESEL----YRIGQQLGMTFISVGH 574
Cdd:PRK13634 165 EVLVLDEPTAGLDPKGRKEMmemfYKLHKEKGLTTVLVTH 204
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
396-550 |
2.44e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.49 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmLADFGPHGVLFLPQ----------KPFFtdgT 465
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK-LDGGDIDDPDVAEAchylghrnamKPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 466 LREQVIYpLKEIYpdsgSADDERIVRFLELAGLSSLVARTGGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDE 545
Cdd:PRK13539 90 VAENLEF-WAAFL----GGEELDIAAALEAVGLAPLAHLPFG-----------YLSAGQKRRVALARLLVSNRPIWILDE 153
|
....*
gi 568979103 546 ATSAL 550
Cdd:PRK13539 154 PTAAL 158
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
410-595 |
2.56e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.79 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 410 GQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQML------------ADFGPHGVLFLPQKpFFTDGTL--REQVIYPlK 475
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVgqplhqmdeearAKLRAKHVGFVFQS-FMLIPTLnaLENVELP-A 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 476 EIYPDSGSADDERIVRFLELAGLSSlvaRTGGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAE 555
Cdd:PRK10584 114 LLRGESSRQSRNGAKALLEQLGLGK---RLDHLPAQ--------LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568979103 556 SE----LYRIGQQLGMTFISVGHRPSLEKFHSWVLRLHGGGSWE 595
Cdd:PRK10584 183 DKiadlLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
400-591 |
4.90e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.41 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 400 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVqMLAD----FGPHGVLFLPQKPFFTDGTLR---EQVI- 471
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL-LIDDhplhFGDYSYRSQRIRMIFQDPSTSlnpRQRIs 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 472 ----YPLKEIYPDSGSADDERIVRFLELAGLSSLVArtggldqqvdwNWY-DVLSPGEMQRLSFARLFYLQPKYAVLDEA 546
Cdd:PRK15112 108 qildFPLRLNTDLEPEQREKQIIETLRQVGLLPDHA-----------SYYpHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568979103 547 TSALTEEAESELYRIGQQL----GMTFISVGHRPSLEKFHS-WVLRLHGG 591
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELqekqGISYIYVTQHLGMMKHISdQVLVMHQG 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
379-574 |
5.65e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 54.23 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 379 SDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMladfgphgvlflpqk 458
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 459 pfftDGTL--REQVIYPLKEI-----YPDS---GSADDERIVRFLELAGLSSLVARTGGLD--QQVDWNWY-----DVLS 521
Cdd:PRK13632 69 ----DGITisKENLKEIRKKIgiifqNPDNqfiGATVEDDIAFGLENKKVPPKKMKDIIDDlaKKVGMEDYldkepQNLS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568979103 522 PGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQL----GMTFISVGH 574
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITH 201
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
383-591 |
7.19e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.33 E-value: 7.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 383 FLLDRVSILAPSsDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADFgphGVLFLPQKPFFT 462
Cdd:TIGR03719 5 YTMNRVSKVVPP-KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI---KVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 463 DG-TLREQV----------IYPLKEIYPDSGSADDERIVRFLELAGLSSLVARTGG--LDQQVD----------WNWyDV 519
Cdd:TIGR03719 81 PTkTVRENVeegvaeikdaLDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAwdLDSQLEiamdalrcppWDA-DV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568979103 520 --LSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQLGMTFISVGH-RPSLEKFHSWVLRLHGG 591
Cdd:TIGR03719 160 tkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHdRYFLDNVAGWILELDRG 234
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
390-557 |
1.03e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 54.85 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 390 ILAPSsDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEgMKGSVQM----LADFGP----HGVLFLPQKPFF 461
Cdd:PRK11174 357 ILSPD-GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKIngieLRELDPeswrKHLSWVGQNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 462 TDGTLREQVIyplkeiyPDSGSADDERIVRFLELAGLSSLVAR-TGGLDQQV-DWNwyDVLSPGEMQRLSFARLFYLQPK 539
Cdd:PRK11174 435 PHGTLRDNVL-------LGNPDASDEQLQQALENAWVSEFLPLlPQGLDTPIgDQA--AGLSVGQAQRLALARALLQPCQ 505
|
170
....*....|....*...
gi 568979103 540 YAVLDEATSALteEAESE 557
Cdd:PRK11174 506 LLLLDEPTASL--DAHSE 521
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
397-550 |
1.06e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 397 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVqmladFGPHGVLFLPQKPFFTDGTLREQVIYplke 476
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----WAERSIAYVPQQAWIMNATVRGNILF---- 743
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568979103 477 iYPDSGSADDERIVRFLEL-AGLSSLvarTGGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 550
Cdd:PTZ00243 744 -FDEEDAARLADAVRVSQLeADLAQL---GGGLETEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
396-574 |
1.09e-07 |
|
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: 52.53 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH--------GVLFlPQKPFFTD 463
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidgLKLTDDKKNinelrqkvGMVF-QQFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 464 GTLREQVIYPLKEIYPDSGSADDERIVRFLELAGLSslvartgglDQQvdwNWY-DVLSPGEMQRLSFARLFYLQPKYAV 542
Cdd:cd03262 91 LTVLENITLAPIKVKGMSKAEAEERALELLEKVGLA---------DKA---DAYpAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190
....*....|....*....|....*....|....*
gi 568979103 543 LDEATSALTEEAESELYRIGQQL---GMTFISVGH 574
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLaeeGMTMVVVTH 193
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
385-577 |
1.27e-07 |
|
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: 54.58 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 385 LDRVSiLAPSSDKPLI-KDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH------GVL 453
Cdd:TIGR03797 454 VDRVT-FRYRPDGPLIlDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVfydgQDLAGLDVQavrrqlGVV 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 454 FlpQKPFFTDGTLREQVI----YPLKEIYPD---SGSADDeriVRFLELaGLSSLVARTGGldqqvdwnwydVLSPGEMQ 526
Cdd:TIGR03797 533 L--QNGRLMSGSIFENIAggapLTLDEAWEAarmAGLAED---IRAMPM-GMHTVISEGGG-----------TLSGGQRQ 595
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568979103 527 RLSFARLFYLQPKYAVLDEATSAL---TEEAESELYrigQQLGMTFISVGHRPS 577
Cdd:TIGR03797 596 RLLIARALVRKPRILLFDEATSALdnrTQAIVSESL---ERLKVTRIVIAHRLS 646
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
395-574 |
1.73e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.17 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 395 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADFGPH----------GVLFLPQKPFFTDG 464
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAenvwnlrrkiGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 465 TLREQVIYPLKeiypDSGSADDERIVRFLE-LAGLSSLVARTGGLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 543
Cdd:PRK13642 98 TVEDDVAFGME----NQGIPREEMIKRVDEaLLAVNMLDFKTREPAR---------LSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190
....*....|....*....|....*....|....*
gi 568979103 544 DEATSALTEEAESELYRIGQQLG----MTFISVGH 574
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKekyqLTVLSITH 199
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
402-574 |
2.00e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.82 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 402 DLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQML----------ADFGP----HGVLF-LPQKPFFTDGTL 466
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtlitstsknKDIKQirkkVGLVFqFPESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 467 REQVIYPL-----KEiypdsgsaDDERIVR-FLELAGLSslvartgglDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKY 540
Cdd:PRK13649 105 KDVAFGPQnfgvsQE--------EAEALAReKLALVGIS---------ESLFEKNPFE-LSGGQMRRVAIAGILAMEPKI 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 568979103 541 AVLDEATSALTEEAESELYRIGQQL---GMTFISVGH 574
Cdd:PRK13649 167 LVLDEPTAGLDPKGRKELMTLFKKLhqsGMTIVLVTH 203
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
399-583 |
2.75e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 399 LIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGG-LWEGMK-GSVQMLADFGPHGV--------------LFLPQ--KPF 460
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGApRGARVTGDVTLNGEplaaidaprlarlrAVLPQaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 461 FTdGTLREQVI---YPLKEIYPDSGSADDERIVRFLELAGLSSLVARtggldqqvdwnwyDV--LSPGEMQRLSFARLF- 534
Cdd:PRK13547 96 FA-FSAREIVLlgrYPHARRAGALTHRDGEIAWQALALAGATALVGR-------------DVttLSGGELARVQFARVLa 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568979103 535 --------YLQPKYAVLDEATSALTEEAESELY----RIGQQLGMTFISVGHRPSLEKFHS 583
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLdtvrRLARDWNLGVLAIVHDPNLAARHA 222
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
398-550 |
2.84e-07 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 51.21 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 398 PLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM-------LADFGPHGVLFLPQKPFF-TDGTLREQ 469
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWngtplaeQRDEPHENILYLGHLPGLkPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 470 viypLKEIYPDSGSADDErIVRFLELAGLSSLVARTGGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDEATSA 549
Cdd:TIGR01189 94 ----LHFWAAIHGGAQRT-IEDALAAVGLTGFEDLPAA-----------QLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
.
gi 568979103 550 L 550
Cdd:TIGR01189 158 L 158
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
396-547 |
2.95e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 53.14 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMladfgPHG--VLFLPQKPFFTDG-TLREQVIY 472
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-----PKGlrIGYLPQEPPLDDDlTVLDTVLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 473 PLKEIY------------PDSGSADDERI----VRFLELAG----------LSSLVARTGGLDQQVdwnwyDVLSPGEMQ 526
Cdd:COG0488 85 GDAELRaleaeleeleakLAEPDEDLERLaelqEEFEALGGweaearaeeiLSGLGFPEEDLDRPV-----SELSGGWRR 159
|
170 180
....*....|....*....|.
gi 568979103 527 RLSFARLFYLQPKYAVLDEAT 547
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPT 180
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
397-558 |
3.39e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 53.04 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 397 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM---------LADFGPH-GVLFlpQKPFFTDGTL 466
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdgtdirtvtRASLRRNiAVVF--QDAGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 467 REQviypLKEIYPDsgsADDERIVRFLELAGLSSLVAR-TGGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDE 545
Cdd:PRK13657 426 EDN----IRVGRPD---ATDEEMRAAAERAQAHDFIERkPDGYDTVVGERG-RQLSGGERQRLAIARALLKDPPILILDE 497
|
170
....*....|...
gi 568979103 546 ATSALTEEAESEL 558
Cdd:PRK13657 498 ATSALDVETEAKV 510
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
399-558 |
3.74e-07 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 50.95 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 399 LIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM-------LADFGPHGVLFLPQKPFFTdGTLreQVI 471
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnggpldfQRDSIARGLLYLGHAPGIK-TTL--SVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 472 YPLKEIYPDSGSADDERIVRFLELAGLSSLVARTggldqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALT 551
Cdd:cd03231 92 ENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQ--------------LSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
....*..
gi 568979103 552 EEAESEL 558
Cdd:cd03231 158 KAGVARF 164
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
397-574 |
5.00e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 52.15 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 397 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPHgvlflpQKP---------FFTD 463
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgVDLSHVPPY------QRPinmmfqsyaLFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 464 GTLREQVIYPLKEIYPDSGSADDeRIVRFLELAGLSSLVARTgglDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 543
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLPKAEIAS-RVNEMLGLVHMQEFAKRK---PHQ--------LSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190
....*....|....*....|....*....|....*
gi 568979103 544 DEATSALT----EEAESELYRIGQQLGMTFISVGH 574
Cdd:PRK11607 174 DEPMGALDkklrDRMQLEVVDILERVGVTCVMVTH 208
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
396-550 |
5.68e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.57 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV---------------QMLADFGPH-GVlflpqKP 459
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgepirrqrdeyhQDLLYLGHQpGI-----KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 460 fftDGTLREQviypLKEIYPDSGSADDERIVRFLE---LAGLSSLVARTggldqqvdwnwydvLSPGEMQRLSFARLFYL 536
Cdd:PRK13538 88 ---ELTALEN----LRFYQRLHGPGDDEALWEALAqvgLAGFEDVPVRQ--------------LSAGQQRRVALARLWLT 146
|
170
....*....|....
gi 568979103 537 QPKYAVLDEATSAL 550
Cdd:PRK13538 147 RAPLWILDEPFTAI 160
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
386-555 |
6.87e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 52.33 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 386 DRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM---------LADFGPHGVLFLP 456
Cdd:PRK11176 345 RNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdghdlrdytLASLRNQVALVSQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 457 QKPFFTDgTLREQVIYPLKEIYpdsgsaDDERIVRFLELA-----------GLSSLVARTGGLdqqvdwnwydvLSPGEM 525
Cdd:PRK11176 425 NVHLFND-TIANNIAYARTEQY------SREQIEEAARMAyamdfinkmdnGLDTVIGENGVL-----------LSGGQR 486
|
170 180 190
....*....|....*....|....*....|
gi 568979103 526 QRLSFARLFYLQPKYAVLDEATSALTEEAE 555
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESE 516
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
400-591 |
6.88e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 51.20 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 400 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMladfgpHGVLFLPQKPFFTDgtLREQV----IYP-- 473
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII------DGVDITDKKVKLSD--IRKKVglvfQYPey 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 474 -LKE--IYPD-------SGSADDE---RIVRFLELAGLSslvartggLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKY 540
Cdd:PRK13637 95 qLFEetIEKDiafgpinLGLSEEEienRVKRAMNIVGLD--------YEDYKDKSPFE-LSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568979103 541 AVLDEATSALTEEAESELYRIGQQL----GMTFISVGHrpSLE---KFHSWVLRLHGG 591
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELhkeyNMTIILVSH--SMEdvaKLADRIIVMNKG 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
400-568 |
1.22e-06 |
|
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: 49.74 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 400 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPH-----GVLFLPQ-KPFFTDGTLREQ 469
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrdITGLPPHeraraGIGYVPEgRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 470 ViypLKEIYPDSGSADDERIVRFLELagLSSLVARtggLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSA 549
Cdd:cd03224 96 L---LLGAYARRRAKRKARLERVYEL--FPRLKER---RKQLA-----GTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180
....*....|....*....|..
gi 568979103 550 LTEEAESELYRIGQQL---GMT 568
Cdd:cd03224 163 LAPKIVEEIFEAIRELrdeGVT 184
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
395-550 |
1.89e-06 |
|
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: 51.10 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 395 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADfgphgVLFLPQKPFFTDGTLREQVIY-- 472
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----VAYVPQQAWIQNDSLRENILFgk 723
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568979103 473 PLKEIYPDSgsadderivrFLE-LAGLSSLVARTGGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 550
Cdd:TIGR00957 724 ALNEKYYQQ----------VLEaCALLPDLEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
396-571 |
2.05e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 49.62 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLA---DFGPHGVLFL-----------PQKPFF 461
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkplDYSKRGLLALrqqvatvfqdpEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 462 TDgtLREQVIYPLKEIypdsGSADDErIVRFLELAglSSLVARTGGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYA 541
Cdd:PRK13638 93 TD--IDSDIAFSLRNL----GVPEAE-ITRRVDEA--LTLVDAQHFRHQPI-----QCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190
....*....|....*....|....*....|....
gi 568979103 542 VLDEATSALTEEAESELY----RIGQQLGMTFIS 571
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIaiirRIVAQGNHVIIS 192
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
396-574 |
2.12e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 49.24 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGP----HGVLFLPQKPFFTDG-TL 466
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVflgdKPISMLSSrqlaRRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 467 REQVIY---PLKEIYPDSGSADDERIVRFLELAGLSSLVartgglDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVL 543
Cdd:PRK11231 94 RELVAYgrsPWLSLWGRLSAEDNARVNQAMEQTRINHLA------DRRL-----TDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190
....*....|....*....|....*....|....
gi 568979103 544 DEATSALTEEAESELYRIGQQL---GMTFISVGH 574
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELntqGKTVVTVLH 196
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
390-574 |
2.16e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.83 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 390 ILAPSS--DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV-----QMLADFGPHG----------V 452
Cdd:PRK13641 11 IYSPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyHITPETGNKNlkklrkkvslV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 453 LFLPQKPFFTDGTLREQVIYPLkeiypDSGSADDE---RIVRFLELAGLSSLVARTGGLDqqvdwnwydvLSPGEMQRLS 529
Cdd:PRK13641 91 FQFPEAQLFENTVLKDVEFGPK-----NFGFSEDEakeKALKWLKKVGLSEDLISKSPFE----------LSGGQMRRVA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568979103 530 FARLFYLQPKYAVLDEATSALTEEAESELYRI---GQQLGMTFISVGH 574
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLfkdYQKAGHTVILVTH 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
396-591 |
2.90e-06 |
|
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: 47.78 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQML-ADFGPHGVL------FLPQKP-FFTDGTLR 467
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLgKDIKKEPEEvkrrigYLPEEPsLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 468 EQVIYplkeiypdsgsadderivrflelaglsslvartggldqqvdwnwydvlSPGEMQRLSFARLFYLQPKYAVLDEAT 547
Cdd:cd03230 92 ENLKL------------------------------------------------SGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568979103 548 SALTEEAESELYRIGQQL---GMTFISVGHRPS-LEKFHSWVLRLHGG 591
Cdd:cd03230 124 SGLDPESRREFWELLRELkkeGKTILLSSHILEeAERLCDRVAILNNG 171
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
384-554 |
3.52e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.02 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 384 LLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM--------LADFGPHgVLFL 455
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFerqsikkdLCTYQKQ-LCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 456 PQK----PFFtdgTLREQVIYplkEIYPDSGSADDERIVRFLElagLSSLVARTGGLdqqvdwnwydvLSPGEMQRLSFA 531
Cdd:PRK13540 80 GHRsginPYL---TLRENCLY---DIHFSPGAVGITELCRLFS---LEHLIDYPCGL-----------LSSGQKRQVALL 139
|
170 180
....*....|....*....|...
gi 568979103 532 RLFYLQPKYAVLDEATSALTEEA 554
Cdd:PRK13540 140 RLWMSKAKLWLLDEPLVALDELS 162
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
379-574 |
3.69e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 48.98 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 379 SDTAFLLDRVSilapssdkplikdlsLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV---------QMLADFGP 449
Cdd:PRK13648 19 SDASFTLKDVS---------------FNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitdDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 450 H-GVLFlpQKP--FFTDGTLREQVIYPLKEiypDSGSADD-ERIVrflelaglSSLVARTGGLDQQVDWNwyDVLSPGEM 525
Cdd:PRK13648 84 HiGIVF--QNPdnQFVGSIVKYDVAFGLEN---HAVPYDEmHRRV--------SEALKQVDMLERADYEP--NALSGGQK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568979103 526 QRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQL----GMTFISVGH 574
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITH 201
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
395-577 |
4.82e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.30 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 395 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWE-----GMKGSVQMLA------DFGP------HGVLFLPQ 457
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGrniyspDVDPievrreVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 458 KPFfTDGTLREQVIYPLKeiypdsgsadderivrflelagLSSLVARTGGLDQQVDWN------WYDV----------LS 521
Cdd:PRK14267 95 NPF-PHLTIYDNVAIGVK----------------------LNGLVKSKKELDERVEWAlkkaalWDEVkdrlndypsnLS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 522 PGEMQRLSFARLFYLQPKYAVLDEATSAL----TEEAESELYRIGQQLgmTFISVGHRPS 577
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIdpvgTAKIEELLFELKKEY--TIVLVTHSPA 209
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
400-574 |
5.12e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 48.69 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 400 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV---QMLADFGPHGVLFL----------PQKPFFTdGTL 466
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdGKPIDYSRKGLMKLresvgmvfqdPDNQLFS-ASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 467 REQVIY-------PLKEIYpdsgsaddERIVRFLELAGLSSLVartgglDQQVDWnwydvLSPGEMQRLSFARLFYLQPK 539
Cdd:PRK13636 101 YQDVSFgavnlklPEDEVR--------KRVDNALKRTGIEHLK------DKPTHC-----LSFGQKKRVAIAGVLVMEPK 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 568979103 540 YAVLDEATSALTEEAESELYRI----GQQLGMTFISVGH 574
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLlvemQKELGLTIIIATH 200
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
397-558 |
5.35e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.16 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 397 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM--LADFGP---HGVLF-----LPQKpfftdgTL 466
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgKPVEGPgaeRGVVFqneglLPWR------NV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 467 REQVIYPLKEiypdSGSADDERIVRFLELAGLSSLVartgGLDQQVDWNwydvLSPGEMQRLSFARLFYLQPKYAVLDE- 545
Cdd:PRK11248 88 QDNVAFGLQL----AGVEKMQRLEIAHQMLKKVGLE----GAEKRYIWQ----LSGGQRQRVGIARALAANPQLLLLDEp 155
|
170
....*....|....*
gi 568979103 546 --ATSALTEEAESEL 558
Cdd:PRK11248 156 fgALDAFTREQMQTL 170
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
394-591 |
1.46e-05 |
|
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: 46.56 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 394 SSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV------------QMLADFGPHGVLFLPQKPFF 461
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfEATRSRNRYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 462 TDGTLREQVIYplkeiypdsGSA-DDERIVRFLELAGLSSLVARTGGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKY 540
Cdd:cd03290 91 LNATVEENITF---------GSPfNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568979103 541 AVLDEATSALTEEAESELYRIG-----QQLGMTFISVGHRPSLEKFHSWVLRLHGG 591
Cdd:cd03290 162 VFLDDPFSALDIHLSDHLMQEGilkflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
520-575 |
1.72e-05 |
|
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: 45.50 E-value: 1.72e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568979103 520 LSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQL---GMTFISVGHR 575
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraqGVAVIFISHR 141
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
398-549 |
1.78e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 398 PLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGP---HGVL-FLPQKPFFTDGTLREQ 469
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIdgcdISKFGLmdlRKVLgIIPQAPVLFSGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 470 vIYPLKEiypdsgsADDERIVRFLELAGLSSLVARTG-GLDQQVDwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATS 548
Cdd:PLN03130 1333 -LDPFNE-------HNDADLWESLERAHLKDVIRRNSlGLDAEVS-EAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
.
gi 568979103 549 A 549
Cdd:PLN03130 1404 A 1404
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
394-550 |
2.00e-05 |
|
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: 47.98 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 394 SSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVL-------------GGLWEgmkgSVQMLADFGPHGVlfLPQKPF 460
Cdd:TIGR01271 1229 EAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALlrllstegeiqidGVSWN----SVTLQTWRKAFGV--IPQKVF 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 461 FTDGTLReqviyplKEIYPDSGSADDErIVRFLELAGLSSLVAR-TGGLDQQVDWNWYdVLSPGEMQRLSFARLFYLQPK 539
Cdd:TIGR01271 1303 IFSGTFR-------KNLDPYEQWSDEE-IWKVAEEVGLKSVIEQfPDKLDFVLVDGGY-VLSNGHKQLMCLARSILSKAK 1373
|
170
....*....|.
gi 568979103 540 YAVLDEATSAL 550
Cdd:TIGR01271 1374 ILLLDEPSAHL 1384
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
399-580 |
2.12e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 46.35 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 399 LIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QML--------ADFGPHGVLFLPQ-KPFFTDGT 465
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngQPMsklssaakAELRNQKLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 466 LREQVIYPLKeiypDSGSADDERIVRFLELagLSSLvartgGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDE 545
Cdd:PRK11629 104 ALENVAMPLL----IGKKKPAEINSRALEM--LAAV-----GLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 568979103 546 ATSALTEEAESELYRIGQQL----GMTFISVGHRPSLEK 580
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELnrlqGTAFLVVTHDLQLAK 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
400-550 |
2.74e-05 |
|
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: 45.65 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 400 IKDLSLKICEGQSLLItGNTGTGKTSLLRVLGGLWEGMKGSVQMLADFGP------HGVL-FLPQKP-FFTDGTLREQVI 471
Cdd:cd03264 16 LDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLkqpqklRRRIgYLPQEFgVYPNFTVREFLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 472 YP--LKEIyPDSGSadDERIVRFLELAGLSSLVARTGGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDEATSA 549
Cdd:cd03264 95 YIawLKGI-PSKEV--KARVDEVLELVNLGDRAKKKIG-----------SLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
.
gi 568979103 550 L 550
Cdd:cd03264 161 L 161
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
395-577 |
3.11e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 47.02 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 395 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMlaDFGP-----HGVL-----FLPQKP----- 459
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL--DGRPlsslsHSVLrqgvaMVQQDPvvlad 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 460 -FFTDGTLREQViyplkeiypdsgsaDDERIVRFLELAGLSSLV-ARTGGLDQQVDwNWYDVLSPGEMQRLSFARLFYLQ 537
Cdd:PRK10790 430 tFLANVTLGRDI--------------SEEQVWQALETVQLAELArSLPDGLYTPLG-EQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568979103 538 PKYAVLDEATSAL---TEEAeselyrIGQQLGM-----TFISVGHRPS 577
Cdd:PRK10790 495 PQILILDEATANIdsgTEQA------IQQALAAvrehtTLVVIAHRLS 536
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
147-550 |
3.34e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 147 ERFCRQLSSVTSkliiSPFTLTYYTYQCFQStgwLGPVSIFGYFIVgtmvnkTLMGPIVTKLVQQ-EKL--EG----DFR 219
Cdd:PLN03130 412 QQICQQLHTLWS----APFRIIIAMVLLYQQ---LGVASLIGSLML------VLMFPIQTFIISKmQKLtkEGlqrtDKR 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 220 FKHMqirvNAEPAAFyraGLVEHMRTDRRLQRLLQTQR--ELM-SRELWLYIGINTFdYLGSILSYV-VIAIPIFSGVYG 295
Cdd:PLN03130 479 IGLM----NEVLAAM---DTVKCYAWENSFQSKVQTVRddELSwFRKAQLLSAFNSF-ILNSIPVLVtVVSFGVFTLLGG 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 296 DLSP----TELStLVSKNAFVCIYLISCFTQLIDLSTTLSdvagythrigELQEALLDMSRKSQDCEALgesewdldkTP 371
Cdd:PLN03130 551 DLTParafTSLS-LFAVLRFPLFMLPNLITQAVNANVSLK----------RLEELLLAEERVLLPNPPL---------EP 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 372 GCPTTEPSDTAFLLDrvsilaPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLR-VLGGLWEGMKGSVQMLADfgph 450
Cdd:PLN03130 611 GLPAISIKNGYFSWD------SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT---- 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 451 gVLFLPQKPFFTDGTLREQVIYplkeiypdsGSA-DDERIVRFLELAGLSSLVARTGGLDQQ------VDwnwydvLSPG 523
Cdd:PLN03130 681 -VAYVPQVSWIFNATVRDNILF---------GSPfDPERYERAIDVTALQHDLDLLPGGDLTeigergVN------ISGG 744
|
410 420
....*....|....*....|....*..
gi 568979103 524 EMQRLSFARLFYLQPKYAVLDEATSAL 550
Cdd:PLN03130 745 QKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
396-574 |
3.46e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQML--ADFGphgvlFLPQ---KPFFTDGTLREQV 470
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenANIG-----YYAQdhaYDFENDLTLFDWM 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 471 IYPLKEiypdsgsADDERIVRflelAGLSSLVARTGGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 550
Cdd:PRK15064 406 SQWRQE-------GDDEQAVR----GTLGRLLFSQDDIKKSV-----KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHM 469
|
170 180 190
....*....|....*....|....*....|
gi 568979103 551 TEEA-ES-----ELYRiGqqlgmTFISVGH 574
Cdd:PRK15064 470 DMESiESlnmalEKYE-G-----TLIFVSH 493
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
396-555 |
3.93e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV-----QMLADFGPH------GVLflPQKPFFTDG 464
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindsHNLKDINLKwwrskiGVV--SQDPLLFSN 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 465 TLREQV---IYPLKEI------YPDSGSAD----DERIVRFLELAGLSSLVARTGGLDQ--QVDWNW------------- 516
Cdd:PTZ00265 475 SIKNNIkysLYSLKDLealsnyYNEDGNDSqenkNKRNSCRAKCAGDLNDMSNTTDSNEliEMRKNYqtikdsevvdvsk 554
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568979103 517 --------------YDVL--------SPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAE 555
Cdd:PTZ00265 555 kvlihdfvsalpdkYETLvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
396-550 |
4.25e-05 |
|
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: 44.96 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPHGVLFLPQ-KPFFTDGTLREQV 470
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkpLDIAARNRIGYLPEeRGLYPKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 471 IYpLKEIYPDSGSADDERIVRFLELAGLSSLVARTggLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 550
Cdd:cd03269 92 VY-LAQLKGLKKEEARRRIDEWLERLELSEYANKR--VEE---------LSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
399-550 |
7.07e-05 |
|
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: 44.85 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 399 LIKDLSLKICEGQSLLITGNTGTGKTSLLRVL-------------GGLWEGMKGSvQMLADFGphgvlFLPQKPFFTDGT 465
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFlrllntegdiqidGVSWNSVPLQ-KWRKAFG-----VIPQKVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 466 LReqviyplKEIYPdSGSADDERIVRFLELAGLSSLVAR-TGGLDQQVDWNWYdVLSPGEMQRLSFARLFYLQPKYAVLD 544
Cdd:cd03289 93 FR-------KNLDP-YGKWSDEEIWKVAEEVGLKSVIEQfPGQLDFVLVDGGC-VLSHGHKQLMCLARSVLSKAKILLLD 163
|
....*.
gi 568979103 545 EATSAL 550
Cdd:cd03289 164 EPSAHL 169
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
396-547 |
7.85e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 45.44 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVqmlaDFGPHGVL-FLPQKPFFTDGTLReqviyPL 474
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----KLGETVKIgYFDQHQEELDPDKT-----VL 397
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568979103 475 KEIYPDSGSADDERIVRFLELAGLSslvartgGLDQQ--VdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEAT 547
Cdd:COG0488 398 DELRDGAPGGTEQEVRGYLGRFLFS-------GDDAFkpV-----GVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
377-549 |
8.66e-05 |
|
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: 44.06 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 377 EPSDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQML----ADFGPhGV 452
Cdd:cd03220 15 GGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRgrvsSLLGL-GG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 453 LFLPqkpfftDGTLREQvIYPLKEIYPDSGSADDERIVRFLELAGLsslvartGG-LDQQVdwnwyDVLSPGEMQRLSFA 531
Cdd:cd03220 94 GFNP------ELTGREN-IYLNGRLLGLSRKEIDEKIDEIIEFSEL-------GDfIDLPV-----KTYSSGMKARLAFA 154
|
170
....*....|....*...
gi 568979103 532 RLFYLQPKYAVLDEATSA 549
Cdd:cd03220 155 IATALEPDILLIDEVLAV 172
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
400-574 |
1.11e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.23 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 400 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLA---DFGPHGVL--------FLPQKPFFT---DGT 465
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqriDTLSPGKLqalrrdiqFIFQDPYASldpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 466 LREQVIYPLKEIYPDSGSADDERIVRFLELAGLSSLVArtggldqqvdWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDE 545
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHA----------WRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190
....*....|....*....|....*....|...
gi 568979103 546 ATSALTEEAESE----LYRIGQQLGMTFISVGH 574
Cdd:PRK10261 490 AVSALDVSIRGQiinlLLDLQRDFGIAYLFISH 522
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
397-565 |
1.18e-04 |
|
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: 43.69 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 397 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH-----GVLFLPQKP-FFTDGTL 466
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgQDITKLPMHkrarlGIGYLPQEAsIFRKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 467 REQVIYPLkEIYPDSGSADDERIVRFLELAGLSSLVARTGgldqqvdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEA 546
Cdd:cd03218 93 EENILAVL-EIRGLSKKEREEKLEELLEEFHITHLRKSKA-----------SSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170
....*....|....*....
gi 568979103 547 TSALTEEAESELYRIGQQL 565
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKIL 179
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
410-591 |
1.37e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 43.71 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 410 GQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmladFGPHGVLFLPQK--PF--------------FTDGTLREQVIYP 473
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIW----FSGHDITRLKNRevPFlrrqigmifqdhhlLMDRTVYDNVAIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 474 LkeIYPDSGSADDERIVrflelaglSSLVARTGGLDQQVdwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE 553
Cdd:PRK10908 104 L--IIAGASGDDIRRRV--------SAALDKVGLLDKAK--NFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568979103 554 AESELYRIGQQ---LGMTFISVGHRPSLEKFHSWVL------RLHGG 591
Cdd:PRK10908 172 LSEGILRLFEEfnrVGVTVLMATHDIGLISRRSYRMltlsdgHLHGG 218
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
375-443 |
1.60e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 43.30 E-value: 1.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568979103 375 TTEPSDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM 443
Cdd:PRK13543 2 IEPLHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI 70
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
397-574 |
3.19e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 43.05 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 397 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPHGV-----LFLPQKPFFTDGTLR 467
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgEHIQHYASKEVarrigLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 468 EQVI---YPLKEIYPDSGSADDERIVRFLELAGLSSLVartgglDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLD 544
Cdd:PRK10253 100 ELVArgrYPHQPLFTRWRKEDEEAVTKAMQATGITHLA------DQSV-----DTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190
....*....|....*....|....*....|....
gi 568979103 545 EATSALTEEAESELYRIGQQL----GMTFISVGH 574
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELnrekGYTLAAVLH 202
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
387-593 |
3.27e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 42.72 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 387 RVSILAPSSD-KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEgMKGSVQMLADfgphgVLFLPQKPF---FT 462
Cdd:PRK14258 9 KVNNLSFYYDtQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGR-----VEFFNQNIYerrVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 463 DGTLREQV--IYPLKEIYPDS---GSADDERIVRF---LELAGLSSLVARTGGLDQQVDWNWYDV---LSPGEMQRLSFA 531
Cdd:PRK14258 83 LNRLRRQVsmVHPKPNLFPMSvydNVAYGVKIVGWrpkLEIDDIVESALKDADLWDEIKHKIHKSaldLSGGQQQRLCIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568979103 532 RLFYLQPKYAVLDEATSALTEEAESELYRIGQQLG----MTFISVGHR-PSLEKFHSWVLRLHGGGS 593
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNlHQVSRLSDFTAFFKGNEN 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
400-550 |
5.11e-04 |
|
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: 41.97 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 400 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmLADFGPHgvlflpQKP--------FFTDG------- 464
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT-VDGFDVV------KEPaearrrlgFVSDStglydrl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 465 TLREQVIY--PLKEIYPDSGSADDERIVRFLELAGLssLVARTGGldqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAV 542
Cdd:cd03266 94 TARENLEYfaGLYGLKGDELTARLEELADRLGMEEL--LDRRVGG------------FSTGMRQKVAIARALVHDPPVLL 159
|
....*...
gi 568979103 543 LDEATSAL 550
Cdd:cd03266 160 LDEPTTGL 167
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
401-550 |
5.16e-04 |
|
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: 42.75 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 401 KDLSLKICEGQSLLITGNTGTGKTSLLRVLGGL-------------WEGMKGSvQMLA---DFGphgVLFlpQKPFftdG 464
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLipsegeirfdgqdLDGLSRR-ALRPlrrRMQ---VVF--QDPF---G 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 465 TL--R---EQVIY-PLKEIYPDSGSAD-DERIVRFLELAGLSSlvartggldqqvdwnwyDVL-------SPGEMQRLSF 530
Cdd:COG4172 374 SLspRmtvGQIIAeGLRVHGPGLSAAErRARVAEALEEVGLDP-----------------AARhryphefSGGQRQRIAI 436
|
170 180
....*....|....*....|
gi 568979103 531 ARLFYLQPKYAVLDEATSAL 550
Cdd:COG4172 437 ARALILEPKLLVLDEPTSAL 456
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
398-575 |
5.77e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.23 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 398 PLI-KDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLA-DFGPHGV-----LF--LPQKPFFTDGTLRE 468
Cdd:PTZ00243 1323 PLVlRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGrEIGAYGLrelrrQFsmIPQDPVLFDGTVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 469 QViYPLKEiypdsgsADDERIVRFLELAGLSSLVA-RTGGLDQQV---DWNWydvlSPGEMQRLSFAR-LFYLQPKYAVL 543
Cdd:PTZ00243 1403 NV-DPFLE-------ASSAEVWAALELVGLRERVAsESEGIDSRVlegGSNY----SVGQRQLMCMARaLLKKGSGFILM 1470
|
170 180 190
....*....|....*....|....*....|....*...
gi 568979103 544 DEATSALteeaESELYRIGQQLGM------TFISVGHR 575
Cdd:PTZ00243 1471 DEATANI----DPALDRQIQATVMsafsayTVITIAHR 1504
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
417-571 |
5.93e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 417 GNTGTGKTSLLRVLGGLWEGMKGSVQMLA---DFGP------HGVLFLPQKpffTDGTLREQVI-------YPLKEIYPD 480
Cdd:PRK10982 31 GENGAGKSTLLKCLFGIYQKDSGSILFQGkeiDFKSskealeNGISMVHQE---LNLVLQRSVMdnmwlgrYPTKGMFVD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 481 SGSADDERIVRFLELaglsslvartgglDQQVDWN-WYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELY 559
Cdd:PRK10982 108 QDKMYRDTKAIFDEL-------------DIDIDPRaKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLF 174
|
170
....*....|....*..
gi 568979103 560 RIGQQL-----GMTFIS 571
Cdd:PRK10982 175 TIIRKLkergcGIVYIS 191
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
520-575 |
6.65e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.09 E-value: 6.65e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 520 LSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYR----IGQQLGMTFISVGHR 575
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKtivdIKDKADKTIITIAHR 1418
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
520-571 |
1.09e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 41.94 E-value: 1.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568979103 520 LSPGEMQRLSFARLFYLQPKYAVLDEATSALT-EEAEsELYRIGQQL---GMT--FIS 571
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPTAVLTpQEAD-ELFEILRRLaaeGKSiiFIT 198
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
520-575 |
1.21e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.54 E-value: 1.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 520 LSPGEMQRLSFARLFYLQPKYAVLDEATSALTeEAESE-LYRIGQQL---GMTFISVGHR 575
Cdd:COG1129 141 LSVAQQQLVEIARALSRDARVLILDEPTASLT-EREVErLFRIIRRLkaqGVAIIYISHR 199
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
396-576 |
2.90e-03 |
|
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: 40.56 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 396 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGL--WEGMKGSV-------------------------------Q 442
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvgepcpvcggtleP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 443 MLADF-GPHGVLF---------LPQKPF--FTDGTLREQVIYPLKEIypdsGSADDERIVRFLELAGLSSLVARTGGLDQ 510
Cdd:TIGR03269 92 EEVDFwNLSDKLRrrirkriaiMLQRTFalYGDDTVLDNVLEALEEI----GYEGKEAVGRAVDLIEMVQLSHRITHIAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979103 511 QvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEA----ESELYRIGQQLGMTFISVGHRP 576
Cdd:TIGR03269 168 D--------LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTaklvHNALEEAVKASGISMVLTSHWP 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
395-436 |
6.38e-03 |
|
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: 38.40 E-value: 6.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 568979103 395 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEG 436
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEG 59
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
406-445 |
7.18e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 37.53 E-value: 7.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 568979103 406 KICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLA 445
Cdd:cd17933 8 LVLRNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAA 47
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