|
Name |
Accession |
Description |
Interval |
E-value |
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
35-619 |
8.40e-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: 8.40e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 35 QLVQRFVRIQKVFFpsWSSQNVLMFMTLLCVTLLEQLVIY-QVGLipSQYYGV----LGNKDLDGFKALTLLAVTLIVLN 109
Cdd:COG4178 2 SLLRQFWRLARPYW--RSEEKWKAWGLLALLLLLTLASVGlNVLL--NFWNRDfydaLQARDAAAFWQQLGVFALLAAIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 110 STLKSFDQFTCNLLYVSWRKDLTEHLHHLYFRARVYYTLNVLRDDIDNPDQRISQDVERFCRQLSSVTSKLIISPFTLTY 189
Cdd:COG4178 78 ILLAVYQTYLRQRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDIRLFTETTLSLSLGLLSSVVTLIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 190 YTYQCFQSTGWLgPVSIFGYFIV--GTMV----NKTLMGPIVT-----KLV----QQEKLEGDFRFKHMQIRVNAEPAAF 254
Cdd:COG4178 158 FIGILWSLSGSL-TFTLGGYSITipGYMVwaalIYAIIGTLLThligrPLIrlnfEQQRREADFRFALVRVRENAESIAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 255 YRAGLVEHMRTDRRLQRLLQTQRELMSRELWLYIGINTFDYLGSILSYVVIAIPIFSGV--YGDLSPTelstlvsknAFV 332
Cdd:COG4178 237 YRGEAAERRRLRRRFDAVIANWRRLIRRQRNLTFFTTGYGQLAVIFPILVAAPRYFAGEitLGGLMQA---------ASA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 333 CIYLISCFTQLIDLSTTLSDVAGYTHRIGELQEALLDMSRKSQDCEALGESEwdldktpgcpttepsDTAFLLDRVSILA 412
Cdd:COG4178 308 FGQVQGALSWFVDNYQSLAEWRATVDRLAGFEEALEAADALPEAASRIETSE---------------DGALALEDLTLRT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 413 PSsDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADfgpHGVLFLPQKPFFTDGTLREQVIY 492
Cdd:COG4178 373 PD-GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAG---ARVLFLPQRPYLPLGTLREALLY 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 493 PLkeiypDSGSADDERIVRFLELAGLSSLVARtggLDQQVDWNwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTE 572
Cdd:COG4178 449 PA-----TAEAFSDAELREALEAVGLGHLAER---LDEEADWD--QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 148670868 573 EAESELYR-IGQQL-GMTFISVGHRPSLEKFHSWVLRLHGGGSWELTRI 619
Cdd:COG4178 519 ENEAALYQlLREELpGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPA 567
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
25-616 |
2.17e-96 |
|
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: 309.37 E-value: 2.17e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 25 RAGARPRLDLQLVQRFVRIQKVFFPSWSSQNVLMFMT----LLCVTLLEQLVIYQVGLIPSqyyGVLGNKDLDGFKAL-- 98
Cdd:TIGR00954 64 GAKKKAHVNGVFLGKLDFLLKILIPRVFCKETGLLILiaflLVSRTYLSVYVATLDGQIES---SIVRRSPRNFAWILfk 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 99 -TLLAVTLIVLNSTLKsfdqFTCNLLYVSWRKDLTEHLHHLYFRARVYYTLNVLRDDIDNPDQRISQDVERFCRQLSSVT 177
Cdd:TIGR00954 141 wFLIAPPASFINSAIK----YLLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELY 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 178 SKLIISPFTLTYYTYQCFQSTGWLGPVSIFGYFIVgTMVNKTLMGPIVTKLVQQE-KLEGDFRFKHMQIRVNAEPAAFYR 256
Cdd:TIGR00954 217 SNLTKPILDVILYSFKLLTALGSVGPAGLFAYLFA-TGVVLTKLRPPIGKLTVEEqALEGEYRYVHSRLIMNSEEIAFYQ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 257 AGLVEHMRTDRRLQRL-LQTQRELMSRELWLYIGINTFDYLGSILSYVVIAIPIFSGV---YGDLSPTELSTLVSKNAFV 332
Cdd:TIGR00954 296 GNKVEKETVMSSFYRLvEHLNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKThpaFLEMSEEELMQEFYNNGRL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 333 CIYLISCFTQLIDLSTTLSDVAGYTHRIGELQEALLDMSR------KSQDCEALGESEWDLDKTPGCPTTEPSDTAFLLD 406
Cdd:TIGR00954 376 LLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSgnfkrpRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKFE 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 407 RVSILAPSSDKpLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGsvqMLADFGPHGVLFLPQKPFFTDGTL 486
Cdd:TIGR00954 456 NIPLVTPNGDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG---RLTKPAKGKLFYVPQRPYMTLGTL 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 487 REQVIYPL-KEIYPDSGSADDErIVRFLELAGLSSLVARTGGLDQQVDWNwyDVLSPGEMQRLSFARLFYLQPKYAVLDE 565
Cdd:TIGR00954 532 RDQIIYPDsSEDMKRRGLSDKD-LEQILDNVQLTHILEREGGWSAVQDWM--DVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 148670868 566 ATSALTEEAESELYRIGQQLGMTFISVGHRPSLEKFHSWVLRLHGGGSWEL 616
Cdd:TIGR00954 609 CTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
43-310 |
3.79e-94 |
|
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: 290.28 E-value: 3.79e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 43 IQKVFFPSWSSQNVLMFMTLLCVTLLEQLVIYQVGLIPSQYYGVLGNKDLDGFKALTLLAVTLIVLNSTLKSFDQFTCNL 122
Cdd:pfam06472 1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 123 LYVSWRKDLTEHLHHLYFRARVYYTLNVLRDDIDNPDQRISQDVERFCRQLSSVTSKLIISPFTLTYYTYQCFQSTGWLG 202
Cdd:pfam06472 81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 203 PVSIFGYFIVGTMVNKTLMGPIVTKLVQQEKLEGDFRFKHMQIRVNAEPAAFYRAGLVEHMRTDRRLQRLLQTQRELMSR 282
Cdd:pfam06472 161 PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILRR 240
|
250 260
....*....|....*....|....*....
gi 148670868 283 ELWLYIGINTF-DYLGSILSYVVIAIPIF 310
Cdd:pfam06472 241 RLWYGFIEDFVlKYTWSILGYVLVALPIF 269
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
403-614 |
1.55e-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: 235.51 E-value: 1.55e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 403 FLLDRVSILAPSsDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADfgpHGVLFLPQKPFFT 482
Cdd:cd03223 1 IELENLSLATPD-GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG---EDLLFLPQRPYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 483 DGTLREQVIYPlkeiypdsgsadderivrflelaglsslvartggldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAV 562
Cdd:cd03223 77 LGTLREQLIYP------------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148670868 563 LDEATSALTEEAESELYRIGQQLGMTFISVGHRPSLEKFHSWVLRLHGGGSW 614
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-611 |
8.59e-34 |
|
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: 137.27 E-value: 8.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 20 PGPTARAGARPRLDLQLVQRFVRIQKVFFpswssqnVLMFMTLLCVTLLeqlviyqvGLIPSQYYG-----VLGNKDLDG 94
Cdd:COG2274 130 PTPEFDKRGEKPFGLRWFLRLLRRYRRLL-------LQVLLASLLINLL--------ALATPLFTQvvidrVLPNQDLST 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 95 FKALTLLAVTLIVLNSTLKSFDQF----TCNLLYVSWRKDLTEHLHHL---YFRARvyYTlnvlrddidnPD--QRIsQD 165
Cdd:COG2274 195 LWVLAIGLLLALLFEGLLRLLRSYlllrLGQRIDLRLSSRFFRHLLRLplsFFESR--SV----------GDlaSRF-RD 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 166 VERFCRQLSSVTSKLIIS-PFTLTYYTYQCFQStGWLGPVSIFG---YFIVGTmvnktLMGPIVTKLVQQE-KLEGDFR- 239
Cdd:COG2274 262 VESIREFLTGSLLTALLDlLFVLIFLIVLFFYS-PPLALVVLLLiplYVLLGL-----LFQPRLRRLSREEsEASAKRQs 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 240 -----FKHMQ-IRV-NAEPAAFYRaglvehmrTDRRLQRLLQTQRELMSRELWLYIGINTFdylgSILSYVVIaipIFSG 312
Cdd:COG2274 336 llvetLRGIEtIKAlGAESRFRRR--------WENLLAKYLNARFKLRRLSNLLSTLSGLL----QQLATVAL---LWLG 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 313 VY----GDLSpteLSTLVsknAFVCI--YLISCFTQLIDLSTTLSDVAGYTHRIGELQEAlldmsrksqdcealgESEWD 386
Cdd:COG2274 401 AYlvidGQLT---LGQLI---AFNILsgRFLAPVAQLIGLLQRFQDAKIALERLDDILDL---------------PPERE 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 387 LDKTPgcPTTEPSDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM--- 463
Cdd:COG2274 460 EGRSK--LSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgi 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 464 -LADFGPH------GVlfLPQKPFFTDGTLREQVIYplkeiypDSGSADDERIVRFLELAGLSSLVAR-TGGLDQQVDwN 535
Cdd:COG2274 538 dLRQIDPAslrrqiGV--VLQDVFLFSGTIRENITL-------GDPDATDEEIIEAARLAGLHDFIEAlPMGYDTVVG-E 607
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148670868 536 WYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQL--GMTFISVGHRPSLEKFHSWVLRLHGG 611
Cdd:COG2274 608 GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLlkGRTVIIIAHRLSTIRLADRIIVLDKG 685
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
56-597 |
8.77e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 114.88 E-value: 8.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 56 VLMFMTLLCVTLLEQLVIYQVGLIPSQyygVLGNKDLDGFKALTLLAVTLIVLNSTLKSFDQFTCNLLYVS----WRKDL 131
Cdd:COG1132 24 ILALLLLLLSALLELLLPLLLGRIIDA---LLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRvvadLRRDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 132 TEHLHHL---YF-RARVYYTLNVLRDDIDNpdqrisqdVERFcrqLSSVTSKLIISPFTLTYYTYQCFQSTGWLGPVSIF 207
Cdd:COG1132 101 FEHLLRLplsFFdRRRTGDLLSRLTNDVDA--------VEQF---LAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 208 GyFIVGTMVNKTLMGPIVTKLVQQEKLEGDFrFKHMQ-----IRV----NAEPAafyraglvEHMRTDRRLQRLLQTQRE 278
Cdd:COG1132 170 V-LPLLLLVLRLFGRRLRKLFRRVQEALAEL-NGRLQeslsgIRVvkafGREER--------ELERFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 279 LMSRELWLYIGINTFDYLGSILSYVVIAIPIFSGvygDLSPTELSTLVSknafvciYLISCFTQLIDLSTTLSDvagyth 358
Cdd:COG1132 240 AARLSALFFPLMELLGNLGLALVLLVGGLLVLSG---SLTVGDLVAFIL-------YLLRLFGPLRQLANVLNQ------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 359 rigeLQEALLDMSRksqdCEALGESEWDLDKTPGCPTTEPSDTAFLLDRVSiLAPSSDKPLIKDLSLKICEGQSLLITGN 438
Cdd:COG1132 304 ----LQRALASAER----IFELLDEPPEIPDPPGAVPLPPVRGEIEFENVS-FSYPGDRPVLKDISLTIPPGETVALVGP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 439 TGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPHG----VLFLPQKPFFTDGTLREQVIYPLKEiypdsgsADDERIV 510
Cdd:COG1132 375 SGSGKSTLVNLLLRFYDPTSGRILIdgvdIRDLTLESlrrqIGVVPQDTFLFSGTIRENIRYGRPD-------ATDEEVE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 511 RFLELAGLSSLVAR-TGGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSALteEAESElYRIGQQL---- 585
Cdd:COG1132 448 EAAKAAQAHEFIEAlPDGYDTVVGERGVN-LSGGQRQRIAIARALLKDPPILILDEATSAL--DTETE-ALIQEALerlm 523
|
570
....*....|...
gi 148670868 586 -GMTFISVGHRPS 597
Cdd:COG1132 524 kGRTTIVIAHRLS 536
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
415-611 |
2.10e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 107.21 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 415 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPHG----VLFLPQKPFFTDGTL 486
Cdd:COG4619 11 GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgKPLSAMPPPEwrrqVAYVPQEPALWGGTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 487 REQVIYPLKeiyPDSGSADDERIVRFLELAGLSSLVartggLDQQVDwnwydVLSPGEMQRLSFARLFYLQPKYAVLDEA 566
Cdd:COG4619 91 RDNLPFPFQ---LRERKFDRERALELLERLGLPPDI-----LDKPVE-----RLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 148670868 567 TSAL----TEEAESELYRIGQQLGMTFISVGHRPSLEKFHSW-VLRLHGG 611
Cdd:COG4619 158 TSALdpenTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADrVLTLEAG 207
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
405-598 |
6.79e-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: 6.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 405 LDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV--------QMLADFGPHGVLFLP 476
Cdd:cd03245 5 FRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirQLDPADLRRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 477 QKPFFTDGTLREQVIYplkeiypDSGSADDERIVRFLELAGLSSLVARTG-GLDQQVDWNWYDvLSPGEMQRLSFARLFY 555
Cdd:cd03245 85 QDVTLFYGTLRDNITL-------GAPLADDERILRAAELAGVTDFVNKHPnGLDLQIGERGRG-LSGGQRQAVALARALL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 148670868 556 LQPKYAVLDEATSALTEEAESELYRIGQQL--GMTFISVGHRPSL 598
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSL 201
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
405-611 |
8.68e-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: 111.77 E-value: 8.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 405 LDRVSILAPSsDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGP----HGVLFLP 476
Cdd:COG4988 339 LEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingVDLSDLDPaswrRQIAWVP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 477 QKPFFTDGTLREQV-IYplkeiYPDsgsADDERIVRFLELAGLSSLVAR-TGGLDQQVD---WNwydvLSPGEMQRLSFA 551
Cdd:COG4988 418 QNPYLFAGTIRENLrLG-----RPD---ASDEELEAALEAAGLDEFVAAlPDGLDTPLGeggRG----LSGGQAQRLALA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148670868 552 RLFYLQPKYAVLDEATSALTEEAESELYRIGQQL--GMTFISVGHRPSLEKFHSWVLRLHGG 611
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLAQADRILVLDDG 547
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
394-598 |
8.94e-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: 105.45 E-value: 8.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 394 PTTEPSDTAFLLDRVSILAPSSDkPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGP 469
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 470 HG----VLFLPQKPFFTDGTLREQVIYPLKEiypdsgsADDERIVRFLELAGLSSLV-ARTGGLDQQVDWNWYDvLSPGE 544
Cdd:TIGR02857 392 DSwrdqIAWVPQHPFLFAGTIAENIRLARPD-------ASDAEIREALERAGLDEFVaALPQGLDTPIGEGGAG-LSGGQ 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148670868 545 MQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQL--GMTFISVGHRPSL 598
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLAL 519
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
405-611 |
2.85e-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: 98.31 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 405 LDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGL---------WEGMKGSVQMLADFGPH-GVLF 474
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLlgptsgevlVDGKDLTKLSLKELRRKvGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 475 lpQKP---FFTDgTLREQVIYPLkEIYPDSGSADDERIVRFLELAGLSSLvartggldqqVDWNWYDvLSPGEMQRLSFA 551
Cdd:cd03225 82 --QNPddqFFGP-TVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGL----------RDRSPFT-LSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148670868 552 RLFYLQPKYAVLDEATSALTEEAESELYRIGQQL---GMTFISVGHRPS-LEKFHSWVLRLHGG 611
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkaeGKTIIIVTHDLDlLLELADRVIVLEDG 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
405-611 |
2.88e-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: 96.90 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 405 LDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM---------LADFGPHgVLFL 475
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqwdPNELGDH-VGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 476 PQKPFFTDGTLREqviyplkeiypdsgsadderivrflelaglsslvartggldqqvdwnwyDVLSPGEMQRLSFARLFY 555
Cdd:cd03246 82 PQDDELFSGSIAE-------------------------------------------------NILSGGQRQRLGLARALY 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 148670868 556 LQPKYAVLDEATSALTEEAESELYRIGQQL---GMTFISVGHRPSLEKFHSWVLRLHGG 611
Cdd:cd03246 113 GNPRILVLDEPNSHLDVEGERALNQAIAALkaaGATRIVIAHRPETLASADRILVLEDG 171
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
405-611 |
4.38e-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: 4.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 405 LDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPHG----VLFLP 476
Cdd:cd03228 3 FKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgVDLRDLDLESlrknIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 477 QKPFFTDGTLREqviyplkeiypdsgsadderivrflelaglsslvartggldqqvdwNwydVLSPGEMQRLSFARLFYL 556
Cdd:cd03228 83 QDPFLFSGTIRE----------------------------------------------N---ILSGGQRQRIAIARALLR 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148670868 557 QPKYAVLDEATSALTEEAESELYRIGQQL--GMTFISVGHRPSLEKFHSWVLRLHGG 611
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALakGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
415-611 |
2.91e-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: 93.06 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 415 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGsvQMLADfG------PHGVL-----FLPQKPFFTD 483
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKG--QILID-GidirdiSRKSLrsmigVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 484 GTLREQVIYplkeiypDSGSADDERIVRFLELAGLSSLVAR-TGGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAV 562
Cdd:cd03254 91 GTIMENIRL-------GRPNATDEEVIEAAKEAGAHDFIMKlPNGYDTVLGENG-GNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148670868 563 LDEATSALTEEAESelyRIGQQL-----GMTFISVGHRPSLEKFHSWVLRLHGG 611
Cdd:cd03254 163 LDEATSNIDTETEK---LIQEALeklmkGRTSIIIAHRLSTIKNADKILVLDDG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
416-611 |
4.56e-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: 4.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmladFGPHGVLFLPQKPfftdgtLREQVIYplk 495
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL----IDGKDIAKLPLEE------LRRRIGY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 496 eiypdsgsadderivrflelaglsslvartggLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAE 575
Cdd:cd00267 78 --------------------------------VPQ---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148670868 576 SELYRIGQQL---GMTFISVGHRPSL-EKFHSWVLRLHGG 611
Cdd:cd00267 117 ERLLELLRELaeeGRTVIIVTHDPELaELAADRVIVLKDG 156
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
420-568 |
5.96e-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: 81.16 E-value: 5.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 420 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGL---------WEGMKGSVQMLADFGpHGVLFLPQKP-FFTDGTLREQ 489
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLlsptegtilLDGQDLTDDERKSLR-KEIGYVFQDPqLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148670868 490 VIYPLKEIYPDSgSADDERIVRFLELAGLSSLVARTGGldqqvdwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATS 568
Cdd:pfam00005 80 LRLGLLLKGLSK-REKDARAEEALEKLGLGDLADRPVG-------ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
298-578 |
1.09e-17 |
|
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: 86.65 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 298 SILSYVVIAIPIFSGvyGDLSPTELSTLVsknaFVCIYLISCFTQLIDLSTTLSDVAGYTHRIGELQEALLDmsrksqdc 377
Cdd:TIGR02868 251 AVLGALWAGGPAVAD--GRLAPVTLAVLV----LLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGP-------- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 378 EALGESEWDLDKTPGCPTTEPSDTAFLLDrvsilapsSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGM 457
Cdd:TIGR02868 317 VAEGSAPAAGAVGLGKPTLELRDLSAGYP--------GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 458 KGSVqMLADFGPHG---------VLFLPQKPFFTDGTLREQVIYPLKEiypdsgsADDERIVRFLELAGLSSLVART-GG 527
Cdd:TIGR02868 389 QGEV-TLDGVPVSSldqdevrrrVSVCAQDAHLFDTTVRENLRLARPD-------ATDEELWAALERVGLADWLRALpDG 460
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 148670868 528 LDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESEL 578
Cdd:TIGR02868 461 LDTVLGEGG-ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL 510
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
416-594 |
4.82e-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: 4.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMK-----GSVQMLAD--FGPH----------GVLFlpQK 478
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKdiYDLDvdvlelrrrvGMVF--QK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 479 PFFTDGTLREQVIYPLKeiypDSGSAD----DERIVRFLELAGLSSLVA-RTGGLDqqvdwnwydvLSPGEMQRLSFARL 553
Cdd:cd03260 90 PNPFPGSIYDNVAYGLR----LHGIKLkeelDERVEEALRKAALWDEVKdRLHALG----------LSGGQQQRLCLARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 148670868 554 FYLQPKYAVLDEATSAL----TEEAESELYRIGQQlgMTFISVGH 594
Cdd:cd03260 156 LANEPEVLLLDEPTSALdpisTAKIEELIAELKKE--YTIVIVTH 198
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
417-595 |
5.29e-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: 5.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 417 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPHgVL-----FLPQKPFFTDGTLR 487
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdgvdISKIGLH-DLrsrisIIPQDPVLFSGTIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 488 EQvIYPLKEiypdsgsADDERIVRFLELAGLSSLV-ARTGGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDEA 566
Cdd:cd03244 96 SN-LDPFGE-------YSDEELWQALERVGLKEFVeSLPGGLDTVVEEGG-ENLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190
....*....|....*....|....*....|....*
gi 148670868 567 TSALTEEAESELyrigQQL------GMTFISVGHR 595
Cdd:cd03244 167 TASVDPETDALI----QKTireafkDCTVLTIAHR 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
417-618 |
8.40e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.62 E-value: 8.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 417 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSvqmladfgphGVLFLPQKPFFTDGTLREQViyplke 496
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA----------GCVDVPDNQFGREASLIDAI------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 497 iyPDSGSADDerIVRFLELAGLSSLvartggldqqvdWNW---YDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE 573
Cdd:COG2401 107 --GRKGDFKD--AVELLNAVGLSDA------------VLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148670868 574 AESELYRIGQQL----GMTFISVGHRPSLEKFHS--WVLRLHGGGSWELTR 618
Cdd:COG2401 171 TAKRVARNLQKLarraGITLVVATHHYDVIDDLQpdLLIFVGYGGVPEEKR 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
416-581 |
2.05e-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: 78.29 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGL---------WEGmkGSVQMLADFGPHGVLFLPQKPFFTDG-T 485
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLlppsagevlWNG--EPIRDAREDYRRRLAYLGHADGLKPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 486 LREQVIYpLKEIYPDsgSADDERIVRFLELAGLSSLvartggLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDE 565
Cdd:COG4133 92 VRENLRF-WAALYGL--RADREAIDEALEAVGLAGL------ADLPV-----RQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170
....*....|....*.
gi 148670868 566 ATSALTEEAESELYRI 581
Cdd:COG4133 158 PFTALDAAGVALLAEL 173
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
413-597 |
2.93e-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: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 413 PSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPHG----VLFLPQKPFFTDG 484
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdVRDYTLASlrrqIGLVSQDVFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 485 TLREQVIYPLKEiypdsgsADDERIVRFLELAGLSSLVART-GGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVL 563
Cdd:cd03251 91 TVAENIAYGRPG-------ATREEVEEAARAANAHEFIMELpEGYDTVIGERGVK-LSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 148670868 564 DEATSALTEEAESELYRIGQQL--GMTFISVGHRPS 597
Cdd:cd03251 163 DEATSALDTESERLVQAALERLmkNRTTFVIAHRLS 198
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
415-608 |
5.79e-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: 77.19 E-value: 5.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 415 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQML---ADFGPHGVLFLPQKPFF-TD--GTLRE 488
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgkpLEKERKRIGYVPQRRSIdRDfpISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 489 QV---IYPLKEIYPDSGSADDERIVRFLELAGLSSLVARTggLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDE 565
Cdd:cd03235 90 VVlmgLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQ--IGE---------LSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 148670868 566 ATSALTEEAESELYRIGQQL---GMTFISVGH-RPSLEKFHSWVLRL 608
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELrreGMTILVVTHdLGLVLEYFDRVLLL 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
417-611 |
1.14e-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: 76.37 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 417 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV------------QMLADFGPHGVLFLPQK----PF 480
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisklseKELAAFRRRHIGFVFQSfnllPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 481 FTdgtLREQVIYPLkEIYPDSGSADDERIVRFLELAGLSSLvartggLDQQVDWnwydvLSPGEMQRLSFARLFYLQPKY 560
Cdd:cd03255 97 LT---ALENVELPL-LLAGVPKKERRERAEELLERVGLGDR------LNHYPSE-----LSGGQQQRVAIARALANDPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 148670868 561 AVLDEATSALTEEAESE----LYRIGQQLGMTFISVGHRPSLEKFHSWVLRLHGG 611
Cdd:cd03255 162 ILADEPTGNLDSETGKEvmelLRELNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
416-594 |
1.84e-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: 76.12 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH----GVLFlpQK-PFFTDGTL 486
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgKDITNLPPHkrpvNTVF--QNyALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 487 REQVIYPLKeIYPDSGSADDERIVRFLELAGLSSLVARTggLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEA 566
Cdd:cd03300 90 FENIAFGLR-LKKLPKAEIKERVAEALDLVQLEGYANRK--PSQ---------LSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190
....*....|....*....|....*....|..
gi 148670868 567 TSALT----EEAESELYRIGQQLGMTFISVGH 594
Cdd:cd03300 158 LGALDlklrKDMQLELKRLQKELGITFVFVTH 189
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
408-597 |
3.35e-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: 78.99 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 408 VSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM---------LADFGPHgVLFLPQK 478
Cdd:TIGR02203 336 VTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLdghdladytLASLRRQ-VALVSQD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 479 PFFTDGTLREQVIYPlkeiypDSGSADDERIVRFLELAGLSSLVART-GGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQ 557
Cdd:TIGR02203 415 VVLFNDTIANNIAYG------RTEQADRAEIERALAAAYAQDFVDKLpLGLDTPIGENG-VLLSGGQRQRLAIARALLKD 487
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148670868 558 PKYAVLDEATSALTEEAESELYRIGQQL--GMTFISVGHRPS 597
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLmqGRTTLVIAHRLS 529
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
420-594 |
1.75e-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: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 420 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGP--HGVLFLPQ-KPFFTDGTLREQVIY 492
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLngkdITNLPPekRDISYVPQnYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 493 PLKEIYPDSgSADDERIVRFLELAGLSSLVARTGGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL-- 570
Cdd:cd03299 95 GLKKRKVDK-KEIERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSALdv 162
|
170 180
....*....|....*....|....*.
gi 148670868 571 --TEEAESELYRIGQQLGMTFISVGH 594
Cdd:cd03299 163 rtKEKLREELKKIRKEFGVTVLHVTH 188
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
416-597 |
4.48e-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: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPHGVL----FLPQKPFFTDGTLR 487
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgVDIRDLNLRWLRsqigLVSQEPVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 488 EQVIYPLKeiypdsgSADDERIVRFLELAGLSSLVAR-TGGLDQQVDWNwYDVLSPGEMQRLSFARLFYLQPKYAVLDEA 566
Cdd:cd03249 95 ENIRYGKP-------DATDEEVEEAAKKANIHDFIMSlPDGYDTLVGER-GSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 148670868 567 TSALteEAESElyRIGQQ------LGMTFISVGHRPS 597
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 ... |
416-597 |
5.15e-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: 5.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH--GVLFLPQKP-FFTDGTLRE 488
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgRDVTGVPPErrNIGMVFQDYaLFPHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 489 QVIYPLKEIYPDSGSAdDERIVRFLELAGLSSLVARtggldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATS 568
Cdd:cd03259 92 NIAFGLKLRGVPKAEI-RARVRELLELVGLEGLLNR-----------YPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190
....*....|....*....|....*....|...
gi 148670868 569 AL----TEEAESELYRIGQQLGMTFISVGHRPS 597
Cdd:cd03259 160 ALdaklREELREELKELQRELGITTIYVTHDQE 192
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
407-594 |
9.39e-14 |
|
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: 71.00 E-value: 9.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 407 RVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV------------QMLADFGpHGVLF 474
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllklsrRLRKIRR-KEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 475 LPQKPF------FTdgtLREQVIYPLKEIYPDSGSADDERIVrFLELAGLsslvartgGLDQQVdwnwYDV----LSPGE 544
Cdd:cd03257 87 VFQDPMsslnprMT---IGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGV--------GLPEEV----LNRypheLSGGQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148670868 545 MQRLSFARLFYLQPKYAVLDEATSAL--TEEAE--SELYRIGQQLGMTFISVGH 594
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALdvSVQAQilDLLKKLQEELGLTLLFITH 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
416-597 |
1.33e-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: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM---------LADFGPH-GVLflPQK-PFFTDg 484
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdirevtLDSLRRAiGVV--PQDtVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 485 TLREQVIY-----PLKEIYPDSGSAD-DERIVRFLElaGLSSLVARTGGLdqqvdwnwydvLSPGEMQRLSFARLFYLQP 558
Cdd:cd03253 90 TIGYNIRYgrpdaTDEEVIEAAKAAQiHDKIMRFPD--GYDTIVGERGLK-----------LSGGEKQRVAIARAILKNP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148670868 559 KYAVLDEATSALTEEAESELYRIGQQL--GMTFISVGHRPS 597
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLS 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
405-595 |
2.63e-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: 72.63 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 405 LDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEG---MKGSV----QMLADFGPHG----VL 473
Cdd:COG1123 7 VRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVlldgRDLLELSEALrgrrIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 474 FLPQKPF--FTDGTLREQVIYPLkEIYPDSGSADDERIVRFLELAGLSSLVARtggldqqvdwnWYDVLSPGEMQRLSFA 551
Cdd:COG1123 87 MVFQDPMtqLNPVTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDR-----------YPHQLSGGQRQRVAIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 148670868 552 RLFYLQPKYAVLDEATSAL--TEEAE--SELYRIGQQLGMTFISVGHR 595
Cdd:COG1123 155 MALALDPDLLIADEPTTALdvTTQAEilDLLRELQRERGTTVLLITHD 202
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
399-594 |
2.73e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.20 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 399 SDTAFLLDRVSILAPssDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPHG--- 471
Cdd:PRK10575 8 SDTTFALRNVSFRVP--GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaQPLESWSSKAfar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 472 -VLFLPQKPFFTDG-TLREQVI---YPLKEIYPDSGSADDERIVRFLELAGLSSLVARTggldqqvdwnwYDVLSPGEMQ 546
Cdd:PRK10575 86 kVAYLPQQLPAAEGmTVRELVAigrYPWHGALGRFGAADREKVEEAISLVGLKPLAHRL-----------VDSLSGGERQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148670868 547 RLSFARLFYLQPKYAVLDEATSALTEEAESE----LYRIGQQLGMTFISVGH 594
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDvlalVHRLSQERGLTVIAVLH 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
418-594 |
3.10e-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: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 418 PLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPHGVLFLPQK--------PFFTDGT 485
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgTDLTLLSGKELRKARRRigmifqhfNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 486 LREQVIYPLkEIYPDSGSADDERIVRFLELAGLSslvartggldQQVDwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDE 565
Cdd:cd03258 99 VFENVALPL-EIAGVPKAEIEERVLELLELVGLE----------DKAD-AYPAQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190
....*....|....*....|....*....|...
gi 148670868 566 ATSALTEEAESE----LYRIGQQLGMTFISVGH 594
Cdd:cd03258 167 ATSALDPETTQSilalLRDINRELGLTIVLITH 199
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
416-594 |
3.32e-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: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPH---------GVLFlpQKP-FF 481
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgedISGLSEAelyrlrrrmGMLF--QSGaLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 482 TDGTLREQVIYPLKEIYPDSGSADDERIVRFLELAGLSslvartGGLDQqvdwnWYDVLSPGEMQRLSFARLFYLQPKYA 561
Cdd:cd03261 90 DSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLR------GAEDL-----YPAELSGGMKKRVALARALALDPELL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 148670868 562 VLDEATSAL----TEEAESELYRIGQQLGMTFISVGH 594
Cdd:cd03261 159 LYDEPTAGLdpiaSGVIDDLIRSLKKELGLTSIMVTH 195
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
416-611 |
4.09e-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: 4.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLI-KDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVqmLADfGPHGVLFLPQkpfftdgTLREQVIYPL 494
Cdd:cd03252 13 DGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV--LVD-GHDLALADPA-------WLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 495 KEIYPDSGSADD-----------ERIVRFLELAGLSSLVARTG-GLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAV 562
Cdd:cd03252 83 QENVLFNRSIRDnialadpgmsmERVIEAAKLAGAHDFISELPeGYDTIVGEQGAG-LSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148670868 563 LDEATSALTEEAESELYRIGQQL--GMTFISVGHRPSLEKFHSWVLRLHGG 611
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNADRIIVMEKG 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
412-611 |
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 148670868 412 APSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMladfgPHGVLFLPQKPFFTDGTLREQVI 491
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-----PGSIAYVSQEPWIQNGTIRENIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 492 --YPLkeiypdsgsaDDERIVRFLELAGLSSLVARTGGLDQQVdwnwydV------LSPGEMQRLSFARLFYLQPKYAVL 563
Cdd:cd03250 88 fgKPF----------DEERYEKVIKACALEPDLEILPDGDLTE------IgekginLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148670868 564 DEATSALTEEAESELYR--IGQQL--GMTFISVGHRPSLEKFHSWVLRLHGG 611
Cdd:cd03250 152 DDPLSAVDAHVGRHIFEncILGLLlnNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
387-598 |
1.54e-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: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 387 LDKTPGCPTTEPSDTAFLLDR-----VSILAPS-SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGS 460
Cdd:TIGR00958 458 LDRKPNIPLTGTLAPLNLEGLiefqdVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQ 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 461 V----QMLADFGPH----GVLFLPQKPFFTDGTLREQVIYPLKeiypdsgSADDERIVRFLELAGLSSLVAR-TGGLDQQ 531
Cdd:TIGR00958 538 VlldgVPLVQYDHHylhrQVALVGQEPVLFSGSVRENIAYGLT-------DTPDEEIMAAAKAANAHDFIMEfPNGYDTE 610
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148670868 532 VDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQLGMTFISVGHRPSL 598
Cdd:TIGR00958 611 VGEKG-SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLST 676
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
419-570 |
3.37e-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: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 419 LIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADFGPHGVL-----FLPQKP---FFTDgTLREQV 490
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERrksigYVMQDVdyqLFTD-SVREEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 491 IYPLKEiyPDSGSADDERIVRFLELAGLsslvartggldqqVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 570
Cdd:cd03226 94 LLGLKE--LDAGNEQAETVLKDLDLYAL-------------KERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
416-594 |
3.37e-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: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmladFGPHGVLFLPQKPFFTDGTLREQVIYPLK 495
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIY----IGGRDVTDLPPKDRDIAMVFQNYALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 496 EIYPDSGSADDERIVRFLELAGLSSLVARTGGLDQQVDwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALT---- 571
Cdd:cd03301 88 TVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLD-RKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklr 166
|
170 180
....*....|....*....|...
gi 148670868 572 EEAESELYRIGQQLGMTFISVGH 594
Cdd:cd03301 167 VQMRAELKRLQQRLGTTTIYVTH 189
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
413-594 |
5.18e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 66.68 E-value: 5.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 413 PSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADFGPH----------GVLFlpQKP--F 480
Cdd:PRK13650 16 EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenvwdirhkiGMVF--QNPdnQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 481 FTDGTLREQVIY-------PLKEIypdsgsadDERIVRFLELAGLSSLVARTGGLdqqvdwnwydvLSPGEMQRLSFARL 553
Cdd:PRK13650 94 FVGATVEDDVAFglenkgiPHEEM--------KERVNEALELVGMQDFKEREPAR-----------LSGGQKQRVAIAGA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 148670868 554 FYLQPKYAVLDEATSALTEEAESELYR----IGQQLGMTFISVGH 594
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKtikgIRDDYQMTVISITH 199
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
416-594 |
5.73e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 67.66 E-value: 5.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVqMLADfgpHGVLFLP--QKP---------FFTDG 484
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI-MLDG---QDITHVPaeNRHvntvfqsyaLFPHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 485 TLREQVIYPLK-------EIYPdsgsaddeRIVRFLELAGLSSLVARTgglDQQvdwnwydvLSPGEMQRLSFARLFYLQ 557
Cdd:PRK09452 102 TVFENVAFGLRmqktpaaEITP--------RVMEALRMVQLEEFAQRK---PHQ--------LSGGQQQRVAIARAVVNK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148670868 558 PKYAVLDEATSALT----EEAESELYRIGQQLGMTFISVGH 594
Cdd:PRK09452 163 PKVLLLDESLSALDyklrKQMQNELKALQRKLGITFVFVTH 203
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
408-612 |
5.95e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.25 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 408 VSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGL---------WEG-------------MKGSVQMLA 465
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLespsqgnvsWRGeplaklnraqrkaFRRDIQMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 466 DFGPHGVLflPQKpfftdgTLREQVIYPLKEIYPDSGSADDERIVRFLELAGLSSLVARTggLDQQvdwnwydvLSPGEM 545
Cdd:PRK10419 96 QDSISAVN--PRK------TVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDK--RPPQ--------LSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148670868 546 QRLSFARLFYLQPKYAVLDEATS----ALTEEAESELYRIGQQLGMTFISVGHRPSL-EKFHSWVLRLHGGG 612
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSnldlVLQAGVIRLLKKLQQQFGTACLFITHDLRLvERFCQRVMVMDNGQ 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
148-576 |
1.07e-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: 68.43 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 148 LNVLRDDIDNPDQRISQDVERFCRQLSSVTSKLI------------ISPFTLTYYTYQCF-----QSTGWLGPVS---IF 207
Cdd:TIGR00957 1065 VNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIvillatpiaaviIPPLGLLYFFVQRFyvassRQLKRLESVSrspVY 1144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 208 GYFivgtmvNKTLMGPIVTKLVQQEKlegdfRFKHMQ-IRVNAEPAAFYraglvEHMRTDRrlqrllqtqrelmsrelWL 286
Cdd:TIGR00957 1145 SHF------NETLLGVSVIRAFEEQE-----RFIHQSdLKVDENQKAYY-----PSIVANR-----------------WL 1191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 287 YIGintfdylgsiLSYVVIAIPIFSGVYGDLSPTELST-LVSKNAFVCIYLISCFTQLIDLSTtlsdvagythrigELQE 365
Cdd:TIGR00957 1192 AVR----------LECVGNCIVLFAALFAVISRHSLSAgLVGLSVSYSLQVTFYLNWLVRMSS-------------EMET 1248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 366 ALLDMSRKSQDCEALGESEWDLDKTPGCPTTEPSDTAFLLDRVSILAPSSDKPLiKDLSLKICEGQSLLITGNTGTGKTS 445
Cdd:TIGR00957 1249 NIVAVERLKEYSETEKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVL-RHINVTIHGGEKVGIVGRTGAGKSS 1327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 446 LLRVLGGLWEGMKGSVQM----LADFGPHGVLF----LPQKPFFTDGTLREQvIYPLkeiypdsGSADDERIVRFLELAG 517
Cdd:TIGR00957 1328 LTLGLFRINESAEGEIIIdglnIAKIGLHDLRFkitiIPQDPVLFSGSLRMN-LDPF-------SQYSDEEVWWALELAH 1399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 518 LSSLV-ARTGGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAES 576
Cdd:TIGR00957 1400 LKTFVsALPDKLDHECAEGGEN-LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
413-595 |
1.14e-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: 63.87 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 413 PSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmLADFGPHG--------VLFLPQKPFFTDG 484
Cdd:cd03247 11 PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-LDGVPVSDlekalsslISVLNQRPYLFDT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 485 TLREQVIYPlkeiypdsgsadderivrflelaglsslvartggldqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLD 564
Cdd:cd03247 90 TLRNNLGRR----------------------------------------------FSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190
....*....|....*....|....*....|...
gi 148670868 565 EATSALTEEAESELYR-IGQQL-GMTFISVGHR 595
Cdd:cd03247 124 EPTVGLDPITERQLLSlIFEVLkDKTLIWITHH 156
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
416-594 |
1.18e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.11 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGsvQMLAD----FGPH----------GVLFlPQKPFF 481
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG--DLIVDglkvNDPKvderlirqeaGMVF-QQFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 482 TDGTLREQVIY-PLKeiYPDSGSADDERIVRflELAGLSSLVARTGGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKY 560
Cdd:PRK09493 90 PHLTALENVMFgPLR--VRGASKEEAEKQAR--ELLAKVGLAERAHHYPSE--------LSGGQQQRVAIARALAVKPKL 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 148670868 561 AVLDEATSALTEEAESELYRIGQQL---GMTFISVGH 594
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLaeeGMTMVIVTH 194
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
421-597 |
1.59e-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: 64.24 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 421 KDLSLKI---CEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----------QMLADFGPH----GVLFlPQKPFFTD 483
Cdd:cd03297 11 PDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsRKKINLPPQqrkiGLVF-QQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 484 GTLREQVIYPLKEIypdSGSADDERIVRFLELAGLSSLVARtgGLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 563
Cdd:cd03297 90 LNVRENLAFGLKRK---RNREDRISVDELLDLLGLDHLLNR--YPAQ---------LSGGEKQRVALARALAAQPELLLL 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 148670868 564 DEATSAL----TEEAESELYRIGQQLGMTFISVGHRPS 597
Cdd:cd03297 156 DEPFSALdralRLQLLPELKQIKKNLNIPVIFVTHDLS 193
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
387-570 |
1.72e-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: 66.85 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 387 LDKTPGCPTTEPSDTAFLL--DRVSI---LAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV 461
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLLevRNLSKrypVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 462 QM------------LADFGPH-GVLFlpQKP---FFTDGTLREQVIYPLKEIYPDSGSADDERIVRFLELAGLSSLVArt 525
Cdd:COG1123 323 LFdgkdltklsrrsLRELRRRvQMVF--QDPyssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLA-- 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 148670868 526 ggldqqvdwNWY-DVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 570
Cdd:COG1123 399 ---------DRYpHELSGGQRQRVAIARALALEPKLLILDEPTSAL 435
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
418-612 |
3.13e-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: 66.30 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 418 PLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPHG----VLFLPQKPFFTDGTLREQ 489
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLngfsLKDIDRHTlrqfINYLPQEPYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 490 VIYPLKEiypdsgSADDERIVRFLELAGLSSLVARTG-GLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATS 568
Cdd:TIGR01193 568 LLLGAKE------NVSQDEIWAACEIAEIKDDIENMPlGYQTELSEEGSS-ISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 148670868 569 ALTEEAESELyrIGQQLGM---TFISVGHRPSLEKFHSWVLRLHGGG 612
Cdd:TIGR01193 641 NLDTITEKKI--VNNLLNLqdkTIIFVAHRLSVAKQSDKIIVLDHGK 685
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
417-594 |
3.66e-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: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 417 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPH-GVLF-----LPQKpfftdgTL 486
Cdd:cd03293 17 VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepVTGPGPDrGYVFqqdalLPWL------TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 487 REQVIYPLkEIYPDSGSADDERIVRFLELAGLSSLVARtggldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLDEA 566
Cdd:cd03293 91 LDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENA-----------YPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 148670868 567 TSAL---T-EEAESELYRIGQQLGMTFISVGH 594
Cdd:cd03293 159 FSALdalTrEQLQEELLDIWRETGKTVLLVTH 190
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
391-601 |
5.83e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 65.23 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 391 PGCPTTEPSDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LAD 466
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLngqpIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 467 FGP----HGVLFLPQKPFFTDGTLREQVIYPLKEiypdsgsADDERIVRFLELAGLSSLVARTGGLDQqvdwnWYD---- 538
Cdd:PRK11160 407 YSEaalrQAISVVSQRVHLFSATLRDNLLLAAPN-------ASDEALIEVLQQVGLEKLLEDDKGLNA-----WLGeggr 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148670868 539 VLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQL--GMTFISVGHR-PSLEKF 601
Cdd:PRK11160 475 QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHRlTGLEQF 540
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
416-598 |
7.50e-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: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMladfgphgvlflpqkpfftDGTLREQviYPLK 495
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL-------------------DGKDLAS--LSPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 496 EIypdsgsAddeRIVRF----LELAGLSSLVARTggldqqvdwnwYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL- 570
Cdd:cd03214 70 EL------A---RKIAYvpqaLELLGLAHLADRP-----------FNELSGGERQRVLLARALAQEPPILLLDEPTSHLd 129
|
170 180 190
....*....|....*....|....*....|.
gi 148670868 571 ---TEEAESELYRIGQQLGMTFISVGHRPSL 598
Cdd:cd03214 130 iahQIELLELLRRLARERGKTVVMVLHDLNL 160
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
416-594 |
1.01e-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: 62.30 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH---------GVLF----Lpqk 478
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlvdgQDITGLSEKelyelrrriGMLFqggaL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 479 pfFTDGTLREQVIYPLKEiYPDSGSADDERIVRF-LELAGLSSlvARTggldqqvdwnwydvLSPGE----MQ-RLSFAR 552
Cdd:COG1127 94 --FDSLTVFENVAFPLRE-HTDLSEAEIRELVLEkLELVGLPG--AAD--------------KMPSElsggMRkRVALAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 148670868 553 LFYLQPKYAVLDEATSAL---TEEAESELYR-IGQQLGMTFISVGH 594
Cdd:COG1127 155 ALALDPEILLYDEPTAGLdpiTSAVIDELIReLRDELGLTSVVVTH 200
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
418-579 |
6.13e-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: 62.62 E-value: 6.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 418 PLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmladfgpHG--VLFLPQKPFFTDGTLREQVIYPLk 495
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-------HSgrISFSPQTSWIMPGTIKDNIIFGL- 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 496 eiypdsgSADDERIVRFLELAGLSSLVARTGGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAE 575
Cdd:TIGR01271 512 -------SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
....
gi 148670868 576 SELY 579
Cdd:TIGR01271 585 KEIF 588
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
412-594 |
6.13e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 6.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 412 APSSDKPLIkDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----------LADFGPH----GVLF-LP 476
Cdd:PRK13643 15 SPFASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskQKEIKPVrkkvGVVFqFP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 477 QKPFFTDGTLREQVIYPlkEIYPDSGSADDERIVRFLELAGLSSLVARTGGLDqqvdwnwydvLSPGEMQRLSFARLFYL 556
Cdd:PRK13643 94 ESQLFEETVLKDVAFGP--QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFE----------LSGGQMRRVAIAGILAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148670868 557 QPKYAVLDEATSALTEEAESELYRIGQ---QLGMTFISVGH 594
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 ... |
418-595 |
6.25e-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: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 418 PLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPHGV----LFLPQKPFFTDGTLREQ 489
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdgidISTIPLEDLrsslTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 490 ViyplkEIYpdsGSADDERIVRFLELAGlsslvartGGLDqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSA 569
Cdd:cd03369 102 L-----DPF---DEYSDEEIYGALRVSE--------GGLN----------LSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180
....*....|....*....|....*...
gi 148670868 570 LTEEAESELYRIGQQL--GMTFISVGHR 595
Cdd:cd03369 156 IDYATDALIQKTIREEftNSTILTIAHR 183
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
417-570 |
1.12e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.40 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 417 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPH------GVlfLPQK-----PFf 481
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLngrpLADWSPAelarrrAV--LPQHsslsfPF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 482 tdgTLREQV---IYPLkeiyPDSGSADDERIVRFLELAGLSSLVARTggldqqvdwnwYDVLSPGEMQRLSFAR-LFYL- 556
Cdd:PRK13548 92 ---TVEEVVamgRAPH----GLSRAEDDALVAAALAQVDLAHLAGRD-----------YPQLSGGEQQRVQLARvLAQLw 153
|
170
....*....|....*...
gi 148670868 557 ----QPKYAVLDEATSAL 570
Cdd:PRK13548 154 epdgPPRWLLLDEPTSAL 171
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
419-611 |
1.14e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.60 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 419 LIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV-------QMLAD-------FGPHGVLFLPQK------ 478
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtiNLVRDkdgqlkvADKNQLRLLRTRltmvfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 479 --PFFTDGTLREQVIYPLKEIYPDSGSADDERIVRFLELAGLsslvartgglDQQVDWNWYDVLSPGEMQRLSFARLFYL 556
Cdd:PRK10619 100 hfNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGI----------DERAQGKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 148670868 557 QPKYAVLDEATSALTEEAESELYRIGQQL---GMTFISVGHRPSLEK-FHSWVLRLHGG 611
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLaeeGKTMVVVTHEMGFARhVSSHVIFLHQG 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
413-594 |
1.42e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.26 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 413 PSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMladFGPH-------------GVLFlpQKP 479
Cdd:PRK13635 16 PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV---GGMVlseetvwdvrrqvGMVF--QNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 480 --FFTDGTLREQVIYPLKeiypDSGSADDERIVRF---LELAGLSSLvartggLDQQVDwnwydVLSPGEMQRLSFARLF 554
Cdd:PRK13635 91 dnQFVGATVQDDVAFGLE----NIGVPREEMVERVdqaLRQVGMEDF------LNREPH-----RLSGGQKQRVAIAGVL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 148670868 555 YLQPKYAVLDEATSALT----EEAESELYRIGQQLGMTFISVGH 594
Cdd:PRK13635 156 ALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITH 199
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
416-594 |
1.51e-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: 57.58 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQML-ADFGPHGVLFLPQKP----FFTDGTL---- 486
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgEDLTDLEDELPPLRRrigmVFQDFALfphl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 487 --REQVIYPLkeiypdSGsadderivrflelaglsslvartggldqqvdwnwydvlspGEMQRLSFARLFYLQPKYAVLD 564
Cdd:cd03229 92 tvLENIALGL------SG----------------------------------------GQQQRVALARALAMDPDVLLLD 125
|
170 180 190
....*....|....*....|....*....|....
gi 148670868 565 EATSAL----TEEAESELYRIGQQLGMTFISVGH 594
Cdd:cd03229 126 EPTSALdpitRREVRALLKSLQAQLGITVVLVTH 159
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
416-594 |
1.74e-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: 59.73 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQ--SLLitGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH----GVLFlpQK----PFF 481
Cdd:COG3842 17 DVTALDDVSLSIEPGEfvALL--GPSGCGKTTLLRMIAGFETPDSGRIlldgRDVTGLPPEkrnvGMVF--QDyalfPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 482 tdgTLREQVIYPLK-------EIypdsgsadDERIVRFLELAGLSSLVARtggldqqvdwnwY-DVLSPGEMQRLSFARL 553
Cdd:COG3842 93 ---TVAENVAFGLRmrgvpkaEI--------RARVAELLELVGLEGLADR------------YpHQLSGGQQQRVALARA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 148670868 554 FYLQPKYAVLDEATSAL----TEEAESELYRIGQQLGMTFISVGH 594
Cdd:COG3842 150 LAPEPRVLLLDEPLSALdaklREEMREELRRLQRELGITFIYVTH 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
413-570 |
1.83e-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: 58.44 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 413 PSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMK---GSV-----QMLADFGPHGVLFLPQKPFFTDG 484
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQIlfngqPRKPDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 485 -TLREQVIY----PLKEIYPDSGSADDERIVRFLELAglsslvartgglDQQVDWNWYDVLSPGEMQRLSFARLFYLQPK 559
Cdd:cd03234 96 lTVRETLTYtailRLPRKSSDAIRKKRVEDVLLRDLA------------LTRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170
....*....|.
gi 148670868 560 YAVLDEATSAL 570
Cdd:cd03234 164 VLILDEPTSGL 174
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
166-570 |
2.15e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.76 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 166 VERFCRQLSSVTSkliiSPFTLTYYTYQCFQStgwLGPVSIFGYFIVGTMV-NKTLMGPIVTKLVQqeklEGdfrFKHMQ 244
Cdd:PLN03232 411 LQQIAEQLHGLWS----APFRIIVSMVLLYQQ---LGVASLFGSLILFLLIpLQTLIVRKMRKLTK----EG---LQWTD 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 245 IRVNAEPAAFYRAGLVEHMRTDRRLQRLLQTQR-ELMS--RELWLYIGINTFdYLGSILSYV-VIAIPIFSGVYGDLSPT 320
Cdd:PLN03232 477 KRVGIINEILASMDTVKCYAWEKSFESRIQGIRnEELSwfRKAQLLSAFNSF-ILNSIPVVVtLVSFGVFVLLGGDLTPA 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 321 ElstlvsknAFVCIYLISCF-TQLIDLSTTLSDVAGYTHRIGELQEALLDMSRKSQDCEALgesewdldkTPGCPTTEPS 399
Cdd:PLN03232 556 R--------AFTSLSLFAVLrSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPL---------QPGAPAISIK 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 400 DTAFLLDRvsilapSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLR-VLGGLWEGMKGSVQMLADfgphgVLFLPQK 478
Cdd:PLN03232 619 NGYFSWDS------KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-----VAYVPQV 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 479 PFFTDGTLREQVIYplkeiypdsGSA-DDERIVRFLELAGLSSLVARTGGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQ 557
Cdd:PLN03232 688 SWIFNATVRENILF---------GSDfESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSN 758
|
410
....*....|...
gi 148670868 558 PKYAVLDEATSAL 570
Cdd:PLN03232 759 SDIYIFDDPLSAL 771
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
332-595 |
2.46e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.76 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 332 VCIYLISCFTQL--------IDLSTTLSDVAGYTHRIGELQEALLDMSRKSQD----CEALGE-----SEW-DLDKTPGC 393
Cdd:PLN03232 1146 VMIWLTATFAVLrngnaenqAGFASTMGLLLSYTLNITTLLSGVLRQASKAENslnsVERVGNyidlpSEAtAIIENNRP 1225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 394 PTTEPSDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGP 469
Cdd:PLN03232 1226 VSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIddcdVAKFGL 1305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 470 HGVL----FLPQKPFFTDGTLREQvIYPLKEiypdsgsADDERIVRFLELAGLSSLVARTG-GLDQQVdWNWYDVLSPGE 544
Cdd:PLN03232 1306 TDLRrvlsIIPQSPVLFSGTVRFN-IDPFSE-------HNDADLWEALERAHIKDVIDRNPfGLDAEV-SEGGENFSVGQ 1376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 148670868 545 MQRLSFARLFYLQPKYAVLDEATSALTEEAESELYR-IGQQL-GMTFISVGHR 595
Cdd:PLN03232 1377 RQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRtIREEFkSCTMLVIAHR 1429
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
418-579 |
2.74e-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: 58.71 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 418 PLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmladfgpHG--VLFLPQKPFFTDGTLREQVIYPLk 495
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-------HSgrISFSSQFSWIMPGTIKENIIFGV- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 496 eiypdsgSADDERIVRFLELAGLSSLVARTGGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAE 575
Cdd:cd03291 123 -------SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
....
gi 148670868 576 SELY 579
Cdd:cd03291 196 KEIF 199
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
398-594 |
3.10e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 58.27 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 398 PSDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLW------------EGMKGSVQMLA 465
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpddnpnskitvDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 466 DFGPH-GVLFlpQKP--FFTDGTLREQVIYPLKeiypDSGSADDE--RIVRflelaglsSLVARTGGLDQQVDWNWYdvL 540
Cdd:PRK13640 81 DIREKvGIVF--QNPdnQFVGATVGDDVAFGLE----NRAVPRPEmiKIVR--------DVLADVGMLDYIDSEPAN--L 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 148670868 541 SPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQL----GMTFISVGH 594
Cdd:PRK13640 145 SGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITH 202
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
416-572 |
3.13e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.42 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPHG----VLFLPQKPFFTDGTLR 487
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegEDISTLKPEIyrqqVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 488 EQVIYP--LKEIYPDsgsadDERIVRFLELAGLSSLVartggLDQQVDwnwydVLSPGEMQRLSFARLFYLQPKYAVLDE 565
Cdd:PRK10247 99 DNLIFPwqIRNQQPD-----PAIFLDDLERFALPDTI-----LTKNIA-----ELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
....*..
gi 148670868 566 ATSALTE 572
Cdd:PRK10247 164 ITSALDE 170
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
418-594 |
3.48e-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: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 418 PLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH--GVLFLPQK-PFFTDGTLREQV 490
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggEDATDVPVQerNVGFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 491 IYPLKeIYPDSGSAD----DERIVRFLELAGLSSLVARtggldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLDEA 566
Cdd:cd03296 96 AFGLR-VKPRSERPPeaeiRAKVHELLKLVQLDWLADR-----------YPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190
....*....|....*....|....*....|..
gi 148670868 567 TSALTEEAESELYR----IGQQLGMTFISVGH 594
Cdd:cd03296 164 FGALDAKVRKELRRwlrrLHDELHVTTVFVTH 195
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
415-596 |
3.55e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.13 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 415 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM---LADFGPH-------------GVLFLPQK 478
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkVLYFGKDifqidaiklrkevGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 479 PFfTDGTLREQVIYPLKEiypdSGSADDERIVRFLElaglSSLvaRTGGLDQQVdwnwYD-------VLSPGEMQRLSFA 551
Cdd:PRK14246 101 PF-PHLSIYDNIAYPLKS----HGIKEKREIKKIVE----ECL--RKVGLWKEV----YDrlnspasQLSGGQQQRLTIA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 148670868 552 RLFYLQPKYAVLDEATSALTEEAESELYRIGQQLG--MTFISVGHRP 596
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKneIAIVIVSHNP 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
415-578 |
7.57e-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: 56.33 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 415 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGsvQMLADFGP---------HGVLFL-PQKPFFTDG 484
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGG--QVLLDGKPisqyehkylHSKVSLvGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 485 TLREQVIYPLkeiypdsGSADDERIVRFLELAGLSSLVAR-TGGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVL 563
Cdd:cd03248 103 SLQDNIAYGL-------QSCSFECVKEAAQKAHAHSFISElASGYDTEVGEKG-SQLSGGQKQRVAIARALIRNPQVLIL 174
|
170
....*....|....*
gi 148670868 564 DEATSALteEAESEL 578
Cdd:cd03248 175 DEATSAL--DAESEQ 187
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
416-597 |
1.52e-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: 57.52 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH------GVLflPQKP-FFTDg 484
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgQDIRDVTQAslraaiGIV--PQDTvLFND- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 485 TLREQVIYPLkeiyPDsgsADDERIVRFLELAGLSSLVART-GGLDQQVdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 563
Cdd:COG5265 447 TIAYNIAYGR----PD---ASEEEVEAAARAAQIHDFIESLpDGYDTRVger-glkLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190
....*....|....*....|....*....|....*...
gi 148670868 564 DEATSAL---TEEA-ESELYRIGQqlGMTFISVGHRPS 597
Cdd:COG5265 519 DEATSALdsrTERAiQAALREVAR--GRTTLVIAHRLS 554
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
420-594 |
1.76e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.97 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 420 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGsvQMLADfgphGVLFLPqkpfFTDGTLRE------QVIYP 493
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG--QVLID----GVDIAK----ISDAELREvrrkkiAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 494 LKEIYPDSGSADDERIvrFLELAGLSSLVARTGGLD--QQVDWNWY-----DVLSPGEMQRLSFARLFYLQPKYAVLDEA 566
Cdd:PRK10070 114 SFALMPHMTVLDNTAF--GMELAGINAEERREKALDalRQVGLENYahsypDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190
....*....|....*....|....*....|..
gi 148670868 567 TSALT----EEAESELYRIGQQLGMTFISVGH 594
Cdd:PRK10070 192 FSALDplirTEMQDELVKLQAKHQRTIVFISH 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
420-594 |
1.82e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.18 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 420 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMladfGPH------------------GVLF-LPQKPF 480
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI----GERvitagkknkklkplrkkvGIVFqFPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 481 FTDGTLREQVIYPLKEIYPDsgsADDERIVR-FLELAGLS-SLVARTGgldqqvdwnwYDvLSPGEMQRLSFARLFYLQP 558
Cdd:PRK13634 99 FEETVEKDICFGPMNFGVSE---EDAKQKAReMIELVGLPeELLARSP----------FE-LSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148670868 559 KYAVLDEATSALTEEAESEL----YRIGQQLGMTFISVGH 594
Cdd:PRK13634 165 EVLVLDEPTAGLDPKGRKEMmemfYKLHKEKGLTTVLVTH 204
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
414-598 |
1.92e-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: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 414 SSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmladFGPHGVLFLPQKPF----------FTD 483
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL----IDGTDINKLKGKALrqlrrqigmiFQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 484 GTL--REQVI-----------YPLKEIYPDSGSADDERIVRFLELAGLSSLV-ARTggldqqvdwnwyDVLSPGEMQRLS 549
Cdd:cd03256 87 FNLieRLSVLenvlsgrlgrrSTWRSLFGLFPKEEKQRALAALERVGLLDKAyQRA------------DQLSGGQQQRVA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148670868 550 FARLFYLQPKYAVLDEATSAL----TEEAESELYRIGQQLGMTFISVGHRPSL 598
Cdd:cd03256 155 IARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLHQVDL 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
420-595 |
2.22e-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: 55.14 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 420 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH-----GVL--FlpQKP-FFTDGTLR 487
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgEDITGLPPHeiarlGIGrtF--QIPrLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 488 EQVI---------YPLKEIYPDSGSADDERIVRFLELAGLSSLVARTGGLdqqvdwnwydvLSPGEMQRLSFARLFYLQP 558
Cdd:cd03219 94 ENVMvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGE-----------LSYGQQRRLEIARALATDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148670868 559 KYAVLDEATSALTEEaesELYRIGQ------QLGMTFISVGHR 595
Cdd:cd03219 163 KLLLLDEPAAGLNPE---ETEELAElirelrERGITVLLVEHD 202
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
430-615 |
2.78e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.79 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 430 GQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQML------------ADFGPHGVLFLPQKpFFTDGTL--REQVIYPlK 495
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVgqplhqmdeearAKLRAKHVGFVFQS-FMLIPTLnaLENVELP-A 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 496 EIYPDSGSADDERIVRFLELAGLSSlvaRTGGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAE 575
Cdd:PRK10584 114 LLRGESSRQSRNGAKALLEQLGLGK---RLDHLPAQ--------LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 148670868 576 SE----LYRIGQQLGMTFISVGHRPSLEKFHSWVLRLHGGGSWE 615
Cdd:PRK10584 183 DKiadlLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
416-570 |
3.47e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.11 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmLADFGPHGVLFLPQ----------KPFFtdgT 485
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK-LDGGDIDDPDVAEAchylghrnamKPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 486 LREQVIYpLKEIYpdsgSADDERIVRFLELAGLSSLVARTGGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDE 565
Cdd:PRK13539 90 VAENLEF-WAAFL----GGEELDIAAALEAVGLAPLAHLPFG-----------YLSAGQKRRVALARLLVSNRPIWILDE 153
|
....*
gi 148670868 566 ATSAL 570
Cdd:PRK13539 154 PTAAL 158
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
420-611 |
4.98e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.41 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 420 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSvqmladfgphgvLFLPQKPF-FTDGTLREQVIyplKEIY 498
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGE------------LLIDDHPLhFGDYSYRSQRI---RMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 499 PDSGSADD--ERIVRFLEL-----AGLSSlVARTGGLDQ---QVDW-----NWY-DVLSPGEMQRLSFARLFYLQPKYAV 562
Cdd:PRK15112 94 QDPSTSLNprQRISQILDFplrlnTDLEP-EQREKQIIEtlrQVGLlpdhaSYYpHMLAPGQKQRLGLARALILRPKVII 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148670868 563 LDEATSALTEEAESELYRIGQQL----GMTFISVGHRPSLEKFHS-WVLRLHGG 611
Cdd:PRK15112 173 ADEALASLDMSMRSQLINLMLELqekqGISYIYVTQHLGMMKHISdQVLVMHQG 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
399-594 |
5.91e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 54.23 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 399 SDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMladfgphgvlflpqk 478
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 479 pfftDGTL--REQVIYPLKEI-----YPDS---GSADDERIVRFLELAGLSSLVARTGGLD--QQVDWNWY-----DVLS 541
Cdd:PRK13632 69 ----DGITisKENLKEIRKKIgiifqNPDNqfiGATVEDDIAFGLENKKVPPKKMKDIIDDlaKKVGMEDYldkepQNLS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148670868 542 PGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQL----GMTFISVGH 594
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITH 201
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
403-611 |
7.56e-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: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 403 FLLDRVSILAPSsDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADFgphGVLFLPQKPFFT 482
Cdd:TIGR03719 5 YTMNRVSKVVPP-KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI---KVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 483 DG-TLREQV----------IYPLKEIYPDSGSADDERIVRFLELAGLSSLVARTGG--LDQQVD----------WNWyDV 539
Cdd:TIGR03719 81 PTkTVRENVeegvaeikdaLDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAwdLDSQLEiamdalrcppWDA-DV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148670868 540 --LSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQLGMTFISVGH-RPSLEKFHSWVLRLHGG 611
Cdd:TIGR03719 160 tkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHdRYFLDNVAGWILELDRG 234
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
410-577 |
8.89e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 55.24 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 410 ILAPSsDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEgMKGSVQM----LADFGP----HGVLFLPQKPFF 481
Cdd:PRK11174 357 ILSPD-GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKIngieLRELDPeswrKHLSWVGQNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 482 TDGTLREQVIyplkeiyPDSGSADDERIVRFLELAGLSSLVAR-TGGLDQQV-DWNwyDVLSPGEMQRLSFARLFYLQPK 559
Cdd:PRK11174 435 PHGTLRDNVL-------LGNPDASDEQLQQALENAWVSEFLPLlPQGLDTPIgDQA--AGLSVGQAQRLALARALLQPCQ 505
|
170
....*....|....*...
gi 148670868 560 YAVLDEATSALteEAESE 577
Cdd:PRK11174 506 LLLLDEPTASL--DAHSE 521
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
416-594 |
1.08e-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: 52.92 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH--------GVLFlPQKPFFTD 483
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidgLKLTDDKKNinelrqkvGMVF-QQFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 484 GTLREQVIYPLKEIYPDSGSADDERIVRFLELAGLSslvartgglDQQvdwNWY-DVLSPGEMQRLSFARLFYLQPKYAV 562
Cdd:cd03262 91 LTVLENITLAPIKVKGMSKAEAEERALELLEKVGLA---------DKA---DAYpAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190
....*....|....*....|....*....|....*
gi 148670868 563 LDEATSALTEEAESELYRIGQQL---GMTFISVGH 594
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLaeeGMTMVVVTH 193
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
417-570 |
1.31e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 417 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVqmladFGPHGVLFLPQKPFFTDGTLREQVIYplke 496
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----WAERSIAYVPQQAWIMNATVRGNILF---- 743
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148670868 497 iYPDSGSADDERIVRFLEL-AGLSSLvarTGGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 570
Cdd:PTZ00243 744 -FDEEDAARLADAVRVSQLeADLAQL---GGGLETEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
422-594 |
1.57e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.21 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 422 DLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQML----------ADFGP----HGVLF-LPQKPFFTDGTL 486
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtlitstsknKDIKQirkkVGLVFqFPESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 487 REQVIYPL-----KEiypdsgsaDDERIVR-FLELAGLSslvartgglDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKY 560
Cdd:PRK13649 105 KDVAFGPQnfgvsQE--------EAEALAReKLALVGIS---------ESLFEKNPFE-LSGGQMRRVAIAGILAMEPKI 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 148670868 561 AVLDEATSALTEEAESELYRIGQQL---GMTFISVGH 594
Cdd:PRK13649 167 LVLDEPTAGLDPKGRKELMTLFKKLhqsGMTIVLVTH 203
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
415-594 |
1.81e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.17 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 415 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADFGPH----------GVLFLPQKPFFTDG 484
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAenvwnlrrkiGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 485 TLREQVIYPLKeiypDSGSADDERIVRFLE-LAGLSSLVARTGGLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 563
Cdd:PRK13642 98 TVEDDVAFGME----NQGIPREEMIKRVDEaLLAVNMLDFKTREPAR---------LSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190
....*....|....*....|....*....|....*
gi 148670868 564 DEATSALTEEAESELYRIGQQLG----MTFISVGH 594
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKekyqLTVLSITH 199
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
405-597 |
1.88e-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: 54.19 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 405 LDRVSiLAPSSDKPLI-KDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH------GVL 473
Cdd:TIGR03797 454 VDRVT-FRYRPDGPLIlDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVfydgQDLAGLDVQavrrqlGVV 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 474 FlpQKPFFTDGTLREQVI----YPLKEIYPD---SGSADDeriVRFLELaGLSSLVARTGGldqqvdwnwydVLSPGEMQ 546
Cdd:TIGR03797 533 L--QNGRLMSGSIFENIAggapLTLDEAWEAarmAGLAED---IRAMPM-GMHTVISEGGG-----------TLSGGQRQ 595
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148670868 547 RLSFARLFYLQPKYAVLDEATSAL---TEEAESELYrigQQLGMTFISVGHRPS 597
Cdd:TIGR03797 596 RLLIARALVRKPRILLFDEATSALdnrTQAIVSESL---ERLKVTRIVIAHRLS 646
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
416-567 |
2.52e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 53.53 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMladfgPHG--VLFLPQKPFFTDG-TLREQVIY 492
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-----PKGlrIGYLPQEPPLDDDlTVLDTVLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 493 PLKEIY------------PDSGSADDERI----VRFLELAG----------LSSLVARTGGLDQQVdwnwyDVLSPGEMQ 546
Cdd:COG0488 85 GDAELRaleaeleeleakLAEPDEDLERLaelqEEFEALGGweaearaeeiLSGLGFPEEDLDRPV-----SELSGGWRR 159
|
170 180
....*....|....*....|.
gi 148670868 547 RLSFARLFYLQPKYAVLDEAT 567
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPT 180
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
419-603 |
2.88e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 419 LIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGG-LWEGMK-GSVQMLADFGPHGV--------------LFLPQ--KPF 480
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGApRGARVTGDVTLNGEplaaidaprlarlrAVLPQaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 481 FTdGTLREQVI---YPLKEIYPDSGSADDERIVRFLELAGLSSLVARtggldqqvdwnwyDV--LSPGEMQRLSFARLF- 554
Cdd:PRK13547 96 FA-FSAREIVLlgrYPHARRAGALTHRDGEIAWQALALAGATALVGR-------------DVttLSGGELARVQFARVLa 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148670868 555 --------YLQPKYAVLDEATSALTEEAESELY----RIGQQLGMTFISVGHRPSLEKFHS 603
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLdtvrRLARDWNLGVLAIVHDPNLAARHA 222
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
418-570 |
3.64e-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: 50.82 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 418 PLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM-------LADFGPHGVLFLPQKPFF-TDGTLREQ 489
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWngtplaeQRDEPHENILYLGHLPGLkPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 490 viypLKEIYPDSGSADDErIVRFLELAGLSSLVARTGGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDEATSA 569
Cdd:TIGR01189 94 ----LHFWAAIHGGAQRT-IEDALAAVGLTGFEDLPAA-----------QLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
.
gi 148670868 570 L 570
Cdd:TIGR01189 158 L 158
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
417-578 |
4.46e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 53.04 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 417 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM---------LADFGPH-GVLFlpQKPFFTDGTL 486
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdgtdirtvtRASLRRNiAVVF--QDAGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 487 REQviypLKEIYPDsgsADDERIVRFLELAGLSSLVAR-TGGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDE 565
Cdd:PRK13657 426 EDN----IRVGRPD---ATDEEMRAAAERAQAHDFIERkPDGYDTVVGERG-RQLSGGERQRLAIARALLKDPPILILDE 497
|
170
....*....|...
gi 148670868 566 ATSALTEEAESEL 578
Cdd:PRK13657 498 ATSALDVETEAKV 510
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
419-578 |
5.16e-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: 50.57 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 419 LIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM-------LADFGPHGVLFLPQKPFFTdGTLreQVI 491
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnggpldfQRDSIARGLLYLGHAPGIK-TTL--SVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 492 YPLKEIYPDSGSADDERIVRFLELAGLSSLVARTggldqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALT 571
Cdd:cd03231 92 ENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQ--------------LSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
....*..
gi 148670868 572 EEAESEL 578
Cdd:cd03231 158 KAGVARF 164
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
417-594 |
5.24e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 52.15 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 417 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPHgvlflpQKP---------FFTD 483
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgVDLSHVPPY------QRPinmmfqsyaLFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 484 GTLREQVIYPLKEIYPDSGSADDeRIVRFLELAGLSSLVARTgglDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 563
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLPKAEIAS-RVNEMLGLVHMQEFAKRK---PHQ--------LSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190
....*....|....*....|....*....|....*
gi 148670868 564 DEATSALT----EEAESELYRIGQQLGMTFISVGH 594
Cdd:PRK11607 174 DEPMGALDkklrDRMQLEVVDILERVGVTCVMVTH 208
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
416-570 |
6.14e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.57 E-value: 6.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV---------------QMLADFGPH-GVlflpqKP 479
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgepirrqrdeyhQDLLYLGHQpGI-----KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 480 fftDGTLREQviypLKEIYPDSGSADDERIVRFLE---LAGLSSLVARTggldqqvdwnwydvLSPGEMQRLSFARLFYL 556
Cdd:PRK13538 88 ---ELTALEN----LRFYQRLHGPGDDEALWEALAqvgLAGFEDVPVRQ--------------LSAGQQRRVALARLWLT 146
|
170
....*....|....
gi 148670868 557 QPKYAVLDEATSAL 570
Cdd:PRK13538 147 RAPLWILDEPFTAI 160
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
406-575 |
7.02e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 52.33 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 406 DRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM---------LADFGPHGVLFLP 476
Cdd:PRK11176 345 RNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdghdlrdytLASLRNQVALVSQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 477 QKPFFTDgTLREQVIYPLKEIYpdsgsaDDERIVRFLELA-----------GLSSLVARTGGLdqqvdwnwydvLSPGEM 545
Cdd:PRK11176 425 NVHLFND-TIANNIAYARTEQY------SREQIEEAARMAyamdfinkmdnGLDTVIGENGVL-----------LSGGQR 486
|
170 180 190
....*....|....*....|....*....|
gi 148670868 546 QRLSFARLFYLQPKYAVLDEATSALTEEAE 575
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESE 516
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
420-611 |
7.19e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 51.20 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 420 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMladfgpHGVLFLPQKPFFTDgtLREQV----IYP-- 493
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII------DGVDITDKKVKLSD--IRKKVglvfQYPey 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 494 -LKE--IYPD-------SGSADDE---RIVRFLELAGLSslvartggLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKY 560
Cdd:PRK13637 95 qLFEetIEKDiafgpinLGLSEEEienRVKRAMNIVGLD--------YEDYKDKSPFE-LSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 148670868 561 AVLDEATSALTEEAESELYRIGQQL----GMTFISVGHrpSLE---KFHSWVLRLHGG 611
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 ... |
420-588 |
1.51e-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: 49.35 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 420 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPH-----GVLFLPQ-KPFFTDGTLREQ 489
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrdITGLPPHeraraGIGYVPEgRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 490 ViypLKEIYPDSGSADDERIVRFLELagLSSLVARtggLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSA 569
Cdd:cd03224 96 L---LLGAYARRRAKRKARLERVYEL--FPRLKER---RKQLA-----GTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180
....*....|....*....|..
gi 148670868 570 LTEEAESELYRIGQQL---GMT 588
Cdd:cd03224 163 LAPKIVEEIFEAIRELrdeGVT 184
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
416-594 |
1.93e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 49.63 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGP----HGVLFLPQKPFFTDG-TL 486
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVflgdKPISMLSSrqlaRRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 487 REQVIY---PLKEIYPDSGSADDERIVRFLELAGLSSLVartgglDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVL 563
Cdd:PRK11231 94 RELVAYgrsPWLSLWGRLSAEDNARVNQAMEQTRINHLA------DRRL-----TDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190
....*....|....*....|....*....|....
gi 148670868 564 DEATSALTEEAESELYRIGQQL---GMTFISVGH 594
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELntqGKTVVTVLH 196
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
415-570 |
1.95e-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: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 415 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADfgphgVLFLPQKPFFTDGTLREQVIY-- 492
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----VAYVPQQAWIQNDSLRENILFgk 723
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148670868 493 PLKEIYPDSgsadderivrFLE-LAGLSSLVARTGGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 570
Cdd:TIGR00957 724 ALNEKYYQQ----------VLEaCALLPDLEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
416-591 |
2.14e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 49.62 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLA---DFGPHGVLFL-----------PQKPFF 481
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkplDYSKRGLLALrqqvatvfqdpEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 482 TDgtLREQVIYPLKEIypdsGSADDErIVRFLELAglSSLVARTGGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYA 561
Cdd:PRK13638 93 TD--IDSDIAFSLRNL----GVPEAE-ITRRVDEA--LTLVDAQHFRHQPI-----QCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190
....*....|....*....|....*....|....
gi 148670868 562 VLDEATSALTEEAESELY----RIGQQLGMTFIS 591
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIaiirRIVAQGNHVIIS 192
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
416-611 |
2.14e-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: 48.16 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQML-ADFGPHGVL------FLPQKP-FFTDGTLR 487
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLgKDIKKEPEEvkrrigYLPEEPsLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 488 EQVIYplkeiypdsgsadderivrflelaglsslvartggldqqvdwnwydvlSPGEMQRLSFARLFYLQPKYAVLDEAT 567
Cdd:cd03230 92 ENLKL------------------------------------------------SGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 148670868 568 SALTEEAESELYRIGQQL---GMTFISVGHRPS-LEKFHSWVLRLHGG 611
Cdd:cd03230 124 SGLDPESRREFWELLRELkkeGKTILLSSHILEeAERLCDRVAILNNG 171
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
410-594 |
2.26e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.83 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 410 ILAPSS--DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV-----QMLADFGPHG----------V 472
Cdd:PRK13641 11 IYSPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyHITPETGNKNlkklrkkvslV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 473 LFLPQKPFFTDGTLREQVIYPLkeiypDSGSADDE---RIVRFLELAGLSSLVARTGGLDqqvdwnwydvLSPGEMQRLS 549
Cdd:PRK13641 91 FQFPEAQLFENTVLKDVEFGPK-----NFGFSEDEakeKALKWLKKVGLSEDLISKSPFE----------LSGGQMRRVA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 148670868 550 FARLFYLQPKYAVLDEATSALTEEAESELYRI---GQQLGMTFISVGH 594
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLfkdYQKAGHTVILVTH 203
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
404-574 |
2.30e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 404 LLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM--------LADFGPHgVLFL 475
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFerqsikkdLCTYQKQ-LCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 476 PQK----PFFtdgTLREQVIYplkEIYPDSGSADDERIVRFLElagLSSLVARTGGLdqqvdwnwydvLSPGEMQRLSFA 551
Cdd:PRK13540 80 GHRsginPYL---TLRENCLY---DIHFSPGAVGITELCRLFS---LEHLIDYPCGL-----------LSSGQKRQVALL 139
|
170 180
....*....|....*....|...
gi 148670868 552 RLFYLQPKYAVLDEATSALTEEA 574
Cdd:PRK13540 140 RLWMSKAKLWLLDEPLVALDELS 162
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
399-594 |
3.85e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 48.98 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 399 SDTAFLLDRVSilapssdkplikdlsLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV---------QMLADFGP 469
Cdd:PRK13648 19 SDASFTLKDVS---------------FNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitdDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 470 H-GVLFlpQKP--FFTDGTLREQVIYPLKEiypDSGSADD-ERIVrflelaglSSLVARTGGLDQQVDWNwyDVLSPGEM 545
Cdd:PRK13648 84 HiGIVF--QNPdnQFVGSIVKYDVAFGLEN---HAVPYDEmHRRV--------SEALKQVDMLERADYEP--NALSGGQK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148670868 546 QRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQL----GMTFISVGH 594
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITH 201
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
420-594 |
4.16e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 48.69 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 420 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV---QMLADFGPHGVLFL----------PQKPFFTdGTL 486
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdGKPIDYSRKGLMKLresvgmvfqdPDNQLFS-ASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 487 REQVIY-------PLKEIYpdsgsaddERIVRFLELAGLSSLVartgglDQQVDWnwydvLSPGEMQRLSFARLFYLQPK 559
Cdd:PRK13636 101 YQDVSFgavnlklPEDEVR--------KRVDNALKRTGIEHLK------DKPTHC-----LSFGQKKRVAIAGVLVMEPK 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 148670868 560 YAVLDEATSALTEEAESELYRI----GQQLGMTFISVGH 594
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLlvemQKELGLTIIIATH 200
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
415-597 |
4.30e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.68 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 415 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWE-----GMKGSVQMLA------DFGP------HGVLFLPQ 477
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGrniyspDVDPievrreVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 478 KPFfTDGTLREQVIYPLKeiypdsgsadderivrflelagLSSLVARTGGLDQQVDWN------WYDV----------LS 541
Cdd:PRK14267 95 NPF-PHLTIYDNVAIGVK----------------------LNGLVKSKKELDERVEWAlkkaalWDEVkdrlndypsnLS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 542 PGEMQRLSFARLFYLQPKYAVLDEATSAL----TEEAESELYRIGQQLgmTFISVGHRPS 597
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIdpvgTAKIEELLFELKKEY--TIVLVTHSPA 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
417-578 |
7.00e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.77 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 417 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM--LADFGP---HGVLF-----LPQKpfftdgTL 486
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgKPVEGPgaeRGVVFqneglLPWR------NV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 487 REQVIYPLKEiypdSGSADDERIVRFLELAGLSSLVartgGLDQQVDWNwydvLSPGEMQRLSFARLFYLQPKYAVLDE- 565
Cdd:PRK11248 88 QDNVAFGLQL----AGVEKMQRLEIAHQMLKKVGLE----GAEKRYIWQ----LSGGQRQRVGIARALAANPQLLLLDEp 155
|
170
....*....|....*
gi 148670868 566 --ATSALTEEAESEL 578
Cdd:PRK11248 156 fgALDAFTREQMQTL 170
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
414-611 |
1.48e-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: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 414 SSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV------------QMLADFGPHGVLFLPQKPFF 481
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfEATRSRNRYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 482 TDGTLREQVIYplkeiypdsGSA-DDERIVRFLELAGLSSLVARTGGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKY 560
Cdd:cd03290 91 LNATVEENITF---------GSPfNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148670868 561 AVLDEATSALTEEAESELYRIG-----QQLGMTFISVGHRPSLEKFHSWVLRLHGG 611
Cdd:cd03290 162 VFLDDPFSALDIHLSDHLMQEGilkflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
414-570 |
1.66e-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: 48.37 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 414 SSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVL-------------GGLWEgmkgSVQMLADFGPHGVlfLPQKPF 480
Cdd:TIGR01271 1229 EAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALlrllstegeiqidGVSWN----SVTLQTWRKAFGV--IPQKVF 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 481 FTDGTLReqviyplKEIYPDSGSADDErIVRFLELAGLSSLVAR-TGGLDQQVDWNWYdVLSPGEMQRLSFARLFYLQPK 559
Cdd:TIGR01271 1303 IFSGTFR-------KNLDPYEQWSDEE-IWKVAEEVGLKSVIEQfPDKLDFVLVDGGY-VLSNGHKQLMCLARSILSKAK 1373
|
170
....*....|.
gi 148670868 560 YAVLDEATSAL 570
Cdd:TIGR01271 1374 ILLLDEPSAHL 1384
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
418-569 |
1.74e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 418 PLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGP---HGVL-FLPQKPFFTDGTLREQ 489
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIdgcdISKFGLmdlRKVLgIIPQAPVLFSGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 490 vIYPLKEiypdsgsADDERIVRFLELAGLSSLVARTG-GLDQQVDwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATS 568
Cdd:PLN03130 1333 -LDPFNE-------HNDADLWESLERAHLKDVIRRNSlGLDAEVS-EAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
.
gi 148670868 569 A 569
Cdd:PLN03130 1404 A 1404
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
540-595 |
1.79e-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: 1.79e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 148670868 540 LSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQL---GMTFISVGHR 595
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraqGVAVIFISHR 141
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
419-600 |
2.11e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 46.35 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 419 LIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QML--------ADFGPHGVLFLPQ-KPFFTDGT 485
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngQPMsklssaakAELRNQKLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 486 LREQVIYPLKeiypDSGSADDERIVRFLELagLSSLvartgGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDE 565
Cdd:PRK11629 104 ALENVAMPLL----IGKKKPAEINSRALEM--LAAV-----GLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 148670868 566 ATSALTEEAESELYRIGQQL----GMTFISVGHRPSLEK 600
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELnrlqGTAFLVVTHDLQLAK 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
420-570 |
2.88e-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: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 420 IKDLSLKICEGQSLLItGNTGTGKTSLLRVLGGLWEGMKGSVQMLADFGP------HGVL-FLPQKP-FFTDGTLREQVI 491
Cdd:cd03264 16 LDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLkqpqklRRRIgYLPQEFgVYPNFTVREFLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 492 YP--LKEIyPDSGSadDERIVRFLELAGLSSLVARTGGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDEATSA 569
Cdd:cd03264 95 YIawLKGI-PSKEV--KARVDEVLELVNLGDRAKKKIG-----------SLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
.
gi 148670868 570 L 570
Cdd:cd03264 161 L 161
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
167-570 |
3.14e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 167 ERFCRQLSSVTSkliiSPFTLTYYTYQCFQStgwLGPVSIFGYFIVgtmvnkTLMGPIVTKLVQQ-EKL--EG----DFR 239
Cdd:PLN03130 412 QQICQQLHTLWS----APFRIIIAMVLLYQQ---LGVASLIGSLML------VLMFPIQTFIISKmQKLtkEGlqrtDKR 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 240 FKHMqirvNAEPAAFyraGLVEHMRTDRRLQRLLQTQR--ELM-SRELWLYIGINTFdYLGSILSYV-VIAIPIFSGVYG 315
Cdd:PLN03130 479 IGLM----NEVLAAM---DTVKCYAWENSFQSKVQTVRddELSwFRKAQLLSAFNSF-ILNSIPVLVtVVSFGVFTLLGG 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 316 DLSP----TELStLVSKNAFVCIYLISCFTQLIDLSTTLSdvagythrigELQEALLDMSRKSQDCEALgesewdldkTP 391
Cdd:PLN03130 551 DLTParafTSLS-LFAVLRFPLFMLPNLITQAVNANVSLK----------RLEELLLAEERVLLPNPPL---------EP 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 392 GCPTTEPSDTAFLLDrvsilaPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLR-VLGGLWEGMKGSVQMLADfgph 470
Cdd:PLN03130 611 GLPAISIKNGYFSWD------SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT---- 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 471 gVLFLPQKPFFTDGTLREQVIYplkeiypdsGSA-DDERIVRFLELAGLSSLVARTGGLDQQ------VDwnwydvLSPG 543
Cdd:PLN03130 681 -VAYVPQVSWIFNATVRDNILF---------GSPfDPERYERAIDVTALQHDLDLLPGGDLTeigergVN------ISGG 744
|
410 420
....*....|....*....|....*..
gi 148670868 544 EMQRLSFARLFYLQPKYAVLDEATSAL 570
Cdd:PLN03130 745 QKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
415-597 |
3.38e-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: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 415 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMlaDFGP-----HGVL-----FLPQKP----- 479
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL--DGRPlsslsHSVLrqgvaMVQQDPvvlad 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 480 -FFTDGTLREQViyplkeiypdsgsaDDERIVRFLELAGLSSLV-ARTGGLDQQVDwNWYDVLSPGEMQRLSFARLFYLQ 557
Cdd:PRK10790 430 tFLANVTLGRDI--------------SEEQVWQALETVQLAELArSLPDGLYTPLG-EQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 148670868 558 PKYAVLDEATSAL---TEEAeselyrIGQQLGM-----TFISVGHRPS 597
Cdd:PRK10790 495 PQILILDEATANIdsgTEQA------IQQALAAvrehtTLVVIAHRLS 536
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
416-570 |
3.41e-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: 45.35 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM----LADFGPHGVLFLPQ-KPFFTDGTLREQV 490
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkpLDIAARNRIGYLPEeRGLYPKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 491 IYpLKEIYPDSGSADDERIVRFLELAGLSSLVARTggLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 570
Cdd:cd03269 92 VY-LAQLKGLKKEEARRRIDEWLERLELSEYANKR--VEE---------LSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
416-594 |
3.59e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQML--ADFGphgvlFLPQ---KPFFTDGTLREQV 490
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenANIG-----YYAQdhaYDFENDLTLFDWM 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 491 IYPLKEiypdsgsADDERIVRflelAGLSSLVARTGGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 570
Cdd:PRK15064 406 SQWRQE-------GDDEQAVR----GTLGRLLFSQDDIKKSV-----KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHM 469
|
170 180 190
....*....|....*....|....*....|
gi 148670868 571 TEEA-ES-----ELYRiGqqlgmTFISVGH 594
Cdd:PRK15064 470 DMESiESlnmalEKYE-G-----TLIFVSH 493
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
416-575 |
4.11e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV-----QMLADFGPH------GVLflPQKPFFTDG 484
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindsHNLKDINLKwwrskiGVV--SQDPLLFSN 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 485 TLREQV---IYPLKEI------YPDSGSAD----DERIVRFLELAGLSSLVARTGGLDQ--QVDWNW------------- 536
Cdd:PTZ00265 475 SIKNNIkysLYSLKDLealsnyYNEDGNDSqenkNKRNSCRAKCAGDLNDMSNTTDSNEliEMRKNYqtikdsevvdvsk 554
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148670868 537 --------------YDVL--------SPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAE 575
Cdd:PTZ00265 555 kvlihdfvsalpdkYETLvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
419-570 |
6.17e-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: 45.23 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 419 LIKDLSLKICEGQSLLITGNTGTGKTSLLRVL-------------GGLWEGMKGSvQMLADFGphgvlFLPQKPFFTDGT 485
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFlrllntegdiqidGVSWNSVPLQ-KWRKAFG-----VIPQKVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 486 LReqviyplKEIYPdSGSADDERIVRFLELAGLSSLVAR-TGGLDQQVDWNWYdVLSPGEMQRLSFARLFYLQPKYAVLD 564
Cdd:cd03289 93 FR-------KNLDP-YGKWSDEEIWKVAEEVGLKSVIEQfPGQLDFVLVDGGC-VLSHGHKQLMCLARSVLSKAKILLLD 163
|
....*.
gi 148670868 565 EATSAL 570
Cdd:cd03289 164 EPSAHL 169
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
416-567 |
6.85e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 45.83 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVqmlaDFGPHGVL-FLPQKPFFTDGTLReqviyPL 494
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----KLGETVKIgYFDQHQEELDPDKT-----VL 397
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148670868 495 KEIYPDSGSADDERIVRFLELAGLSslvartgGLDQQ--VdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEAT 567
Cdd:COG0488 398 DELRDGAPGGTEQEVRGYLGRFLFS-------GDDAFkpV-----GVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
397-569 |
9.27e-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: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 397 EPSDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQML----ADFGPhGV 472
Cdd:cd03220 15 GGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRgrvsSLLGL-GG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 473 LFLPqkpfftDGTLREQvIYPLKEIYPDSGSADDERIVRFLELAGLsslvartGG-LDQQVdwnwyDVLSPGEMQRLSFA 551
Cdd:cd03220 94 GFNP------ELTGREN-IYLNGRLLGLSRKEIDEKIDEIIEFSEL-------GDfIDLPV-----KTYSSGMKARLAFA 154
|
170
....*....|....*...
gi 148670868 552 RLFYLQPKYAVLDEATSA 569
Cdd:cd03220 155 IATALEPDILLIDEVLAV 172
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
417-585 |
1.11e-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: 44.07 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 417 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPH-----GVLFLPQKP-FFTDGTL 486
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgQDITKLPMHkrarlGIGYLPQEAsIFRKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 487 REQVIYPLkEIYPDSGSADDERIVRFLELAGLSSLVARTGgldqqvdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEA 566
Cdd:cd03218 93 EENILAVL-EIRGLSKKEREEKLEELLEEFHITHLRKSKA-----------SSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170
....*....|....*....
gi 148670868 567 TSALTEEAESELYRIGQQL 585
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKIL 179
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
420-594 |
1.19e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.23 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 420 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLA---DFGPHGVL--------FLPQKPFFT---DGT 485
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqriDTLSPGKLqalrrdiqFIFQDPYASldpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 486 LREQVIYPLKEIYPDSGSADDERIVRFLELAGLSSLVArtggldqqvdWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDE 565
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHA----------WRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190
....*....|....*....|....*....|...
gi 148670868 566 ATSALTEEAESE----LYRIGQQLGMTFISVGH 594
Cdd:PRK10261 490 AVSALDVSIRGQiinlLLDLQRDFGIAYLFISH 522
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
395-463 |
1.80e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 43.30 E-value: 1.80e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148670868 395 TTEPSDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQM 463
Cdd:PRK13543 2 IEPLHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI 70
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
430-611 |
1.81e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 43.32 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 430 GQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmladFGPHGVLFLPQK--PF--------------FTDGTLREQVIYP 493
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIW----FSGHDITRLKNRevPFlrrqigmifqdhhlLMDRTVYDNVAIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 494 LkeIYPDSGSADDERIVrflelaglSSLVARTGGLDQQVdwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE 573
Cdd:PRK10908 104 L--IIAGASGDDIRRRV--------SAALDKVGLLDKAK--NFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 148670868 574 AESELYRIGQQ---LGMTFISVGHRPSLEKFHSWVL------RLHGG 611
Cdd:PRK10908 172 LSEGILRLFEEfnrVGVTVLMATHDIGLISRRSYRMltlsdgHLHGG 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
417-594 |
3.32e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 43.05 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 417 KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSV----QMLADFGPHGV-----LFLPQKPFFTDGTLR 487
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgEHIQHYASKEVarrigLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 488 EQVI---YPLKEIYPDSGSADDERIVRFLELAGLSSLVartgglDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLD 564
Cdd:PRK10253 100 ELVArgrYPHQPLFTRWRKEDEEAVTKAMQATGITHLA------DQSV-----DTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190
....*....|....*....|....*....|....
gi 148670868 565 EATSALTEEAESELYRIGQQL----GMTFISVGH 594
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELnrekGYTLAAVLH 202
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
407-613 |
3.41e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 42.72 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 407 RVSILAPSSD-KPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEgMKGSVQMLADfgphgVLFLPQKPF---FT 482
Cdd:PRK14258 9 KVNNLSFYYDtQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGR-----VEFFNQNIYerrVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 483 DGTLREQV--IYPLKEIYPDS---GSADDERIVRF---LELAGLSSLVARTGGLDQQVDWNWYDV---LSPGEMQRLSFA 551
Cdd:PRK14258 83 LNRLRRQVsmVHPKPNLFPMSvydNVAYGVKIVGWrpkLEIDDIVESALKDADLWDEIKHKIHKSaldLSGGQQQRLCIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148670868 552 RLFYLQPKYAVLDEATSALTEEAESELYRIGQQLG----MTFISVGHR-PSLEKFHSWVLRLHGGGS 613
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNlHQVSRLSDFTAFFKGNEN 229
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
437-591 |
5.26e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 437 GNTGTGKTSLLRVLGGLWEGMKGSVQMLA---DFGP------HGVLFLPQKpffTDGTLREQVI-------YPLKEIYPD 500
Cdd:PRK10982 31 GENGAGKSTLLKCLFGIYQKDSGSILFQGkeiDFKSskealeNGISMVHQE---LNLVLQRSVMdnmwlgrYPTKGMFVD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 501 SGSADDERIVRFLELaglsslvartgglDQQVDWN-WYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELY 579
Cdd:PRK10982 108 QDKMYRDTKAIFDEL-------------DIDIDPRaKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLF 174
|
170
....*....|....*..
gi 148670868 580 RIGQQL-----GMTFIS 591
Cdd:PRK10982 175 TIIRKLkergcGIVYIS 191
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
421-570 |
6.03e-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: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 421 KDLSLKICEGQSLLITGNTGTGKTSLLRVLGGL-------------WEGMKGSvQMLA---DFGphgVLFlpQKPFftdG 484
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLipsegeirfdgqdLDGLSRR-ALRPlrrRMQ---VVF--QDPF---G 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 485 TL--R---EQVIY-PLKEIYPDSGSAD-DERIVRFLELAGLSSlvartggldqqvdwnwyDVL-------SPGEMQRLSF 550
Cdd:COG4172 374 SLspRmtvGQIIAeGLRVHGPGLSAAErRARVAEALEEVGLDP-----------------AARhryphefSGGQRQRIAI 436
|
170 180
....*....|....*....|
gi 148670868 551 ARLFYLQPKYAVLDEATSAL 570
Cdd:COG4172 437 ARALILEPKLLVLDEPTSAL 456
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
420-570 |
6.74e-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: 41.58 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 420 IKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQmLADFGPHgvlflpQKP--------FFTDG------- 484
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT-VDGFDVV------KEPaearrrlgFVSDStglydrl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 485 TLREQVIY--PLKEIYPDSGSADDERIVRFLELAGLssLVARTGGldqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAV 562
Cdd:cd03266 94 TARENLEYfaGLYGLKGDELTARLEELADRLGMEEL--LDRRVGG------------FSTGMRQKVAIARALVHDPPVLL 159
|
....*...
gi 148670868 563 LDEATSAL 570
Cdd:cd03266 160 LDEPTTGL 167
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
540-595 |
6.96e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.09 E-value: 6.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 540 LSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYR----IGQQLGMTFISVGHR 595
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKtivdIKDKADKTIITIAHR 1418
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
418-595 |
7.27e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 418 PLI-KDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLA-DFGPHGV-----LF--LPQKPFFTDGTLRE 488
Cdd:PTZ00243 1323 PLVlRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGrEIGAYGLrelrrQFsmIPQDPVLFDGTVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 489 QViYPLKEiypdsgsADDERIVRFLELAGLSSLVA-RTGGLDQQV---DWNWydvlSPGEMQRLSFAR-LFYLQPKYAVL 563
Cdd:PTZ00243 1403 NV-DPFLE-------ASSAEVWAALELVGLRERVAsESEGIDSRVlegGSNY----SVGQRQLMCMARaLLKKGSGFILM 1470
|
170 180 190
....*....|....*....|....*....|....*...
gi 148670868 564 DEATSALteeaESELYRIGQQLGM------TFISVGHR 595
Cdd:PTZ00243 1471 DEATANI----DPALDRQIQATVMsafsayTVITIAHR 1504
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
540-591 |
1.31e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 41.55 E-value: 1.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 148670868 540 LSPGEMQRLSFARLFYLQPKYAVLDEATSALT-EEAEsELYRIGQQL---GMT--FIS 591
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPTAVLTpQEAD-ELFEILRRLaaeGKSiiFIT 198
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
540-595 |
1.34e-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: 1.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 540 LSPGEMQRLSFARLFYLQPKYAVLDEATSALTeEAESE-LYRIGQQL---GMTFISVGHR 595
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 ... |
416-596 |
3.03e-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: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 416 DKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGL--WEGMKGSV-------------------------------Q 462
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvgepcpvcggtleP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 463 MLADF-GPHGVLF---------LPQKPF--FTDGTLREQVIYPLKEIypdsGSADDERIVRFLELAGLSSLVARTGGLDQ 530
Cdd:TIGR03269 92 EEVDFwNLSDKLRrrirkriaiMLQRTFalYGDDTVLDNVLEALEEI----GYEGKEAVGRAVDLIEMVQLSHRITHIAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670868 531 QvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEA----ESELYRIGQQLGMTFISVGHRP 596
Cdd:TIGR03269 168 D--------LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTaklvHNALEEAVKASGISMVLTSHWP 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
415-456 |
6.34e-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: 6.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 148670868 415 SDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEG 456
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. ... |
426-465 |
8.27e-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: 8.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 148670868 426 KICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLA 465
Cdd:cd17933 8 LVLRNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAA 47
|
|
| |
