|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-631 |
0e+00 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 1316.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETPALPQAA 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 LEYVIDGDREYRQLEAQLHDANERNDGQAIATIHGKLDAIDAWSIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNL 160
Cdd:PRK10636 81 LEYVIDGDREYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMFEYTGNYSSFEVQRAT 240
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 241 RLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFRFSFRAPESLPNPLLKMEKVSA 320
Cdd:PRK10636 241 RLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEYLRADESPIQHLAR 400
Cdd:PRK10636 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLAR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 401 LAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGAL 480
Cdd:PRK10636 401 LAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 481 VVVSHDRHLLRSTTDDLYLVHDRKVEPFDGDLEDYQQWLSDVQKQENQADEAPKE-NANSAQARKDQKRREAELRAQTQP 559
Cdd:PRK10636 481 VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQENQTDEAPKEnNANSAQARKDQKRREAELRTQTQP 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557484 560 LRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQML 631
Cdd:PRK10636 561 LRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQML 632
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-518 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 749.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 4 FSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETPALPQA-ALE 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLtVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 83 YVIDGDREYRQLEAQLHDANER-----NDGQAIATIHGKLDAIDAWSIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMR 157
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKlaepdEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMFEYTGNYSSFEVQ 237
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 238 RATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFRFSFRAPESLPNPLLKMEK 317
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKVLELEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQlEYLRADESPIQH 397
Cdd:COG0488 321 LSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDPDKTVLDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 398 LARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFE 477
Cdd:COG0488 400 LRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 446557484 478 GALVVVSHDRHLLRSTTDDLYLVHDRKVEPFDGDLEDYQQW 518
Cdd:COG0488 480 GTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-519 |
2.02e-133 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 407.71 E-value: 2.02e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEiSADGgsytFPGSWQLAWVNQETPALPQAAL 81
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMH-AIDG----IPKNCQILHVEQEVVGDDTTAL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 EYVIDGDREYRQL---EAQLHDANERND---------------------GQAIATIHGKLDAIDAWSIRSRAASLLHGLG 137
Cdd:PLN03073 253 QCVLNTDIERTQLleeEAQLVAQQRELEfetetgkgkgankdgvdkdavSQRLEEIYKRLELIDAYTAEARAASILAGLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 138 FSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
Cdd:PLN03073 333 FTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDIL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 218 HIEQQSMFEYTGNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNP 297
Cdd:PLN03073 413 HLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLGHVDAVVNDPD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 298 FRFSFRAPESLPN-PLLKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGI 375
Cdd:PLN03073 493 YKFEFPTPDDRPGpPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 376 KLGYFAQHQLEYLRADESPIQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
Cdd:PLN03073 573 RMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLD 652
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557484 456 EPTNHLDLDMRQALTEALIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKVEPFDGDLEDYQQWL 519
Cdd:PLN03073 653 EPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKTL 716
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-515 |
1.22e-101 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 319.53 E-value: 1.22e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETPALPQ-A 79
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEfT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 80 ALEYVIDGDREYRQLEAQ------LHDANErNDGQAIATIHGKLDAIDAWSIRSRAASLLHGLGFSNEQLERPVSDFSGG 153
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQErdriyaLPEMSE-EDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMFEYTGNYSS 233
Cdd:PRK15064 160 WKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 234 FEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMEL--IAPAHVDNPF-RFSFRapESLPN 310
Cdd:PRK15064 240 YMTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLeeVKPSSRQNPFiRFEQD--KKLHR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEYLRA 390
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFEN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 DESPIQHLARLA-PQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
Cdd:PRK15064 398 DLTLFDWMSQWRqEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESL 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446557484 470 TEALIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKVEPFDGDLEDY 515
Cdd:PRK15064 478 NMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-626 |
1.35e-88 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 288.39 E-value: 1.35e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETP-ALPQAALEYVIDGDRE---- 90
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPrNVEGTVYDFVAEGIEEqaey 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 91 ---YRQLEAQL-HDANERNDGQaIATIHGKLDAIDAWSIRSRAASLLHGLGFSNEQlerPVSDFSGGWRMRLNLAQALIC 166
Cdd:PRK11147 98 lkrYHDISHLVeTDPSEKNLNE-LAKLQEQLDHHNLWQLENRINEVLAQLGLDPDA---ALSSLSGGWLRKAALGRALVS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 167 RSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMFEYTGNYSSFEVQRATRL---A 243
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALrveE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 244 QQQAMYESQ--QERVAHLQSYIDRF-----RAKATKAKQaQSRIKMLERMElIAPAHVDNPFR-----Fsfrapeslpnp 311
Cdd:PRK11147 254 LQNAEFDRKlaQEEVWIRQGIKARRtrnegRVRALKALR-RERSERREVMG-TAKMQVEEASRsgkivF----------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 llKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQlEYLRAD 391
Cdd:PRK11147 321 --EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHR-AELDPE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 392 ESPIQHLARlAPQELEQKLRD-----YLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
Cdd:PRK11147 398 KTVMDNLAE-GKQEVMVNGRPrhvlgYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 467 QALTEALIEFEGALVVVSHDRHLLRSTTDDLYLVH-DRKVEPFDGDLEDYQQWLSDVQKQENQADEAPKENAnsAQARKD 545
Cdd:PRK11147 477 ELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIGRYVGGYHDARQQQAQYLALKQPAVKKKEEAA--APKAET 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 546 QKRREAELRAQtqpLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKaELTACLQQQASAKSGLEECEMAW--LEA 623
Cdd:PRK11147 555 VKRSSKKLSYK---LQRELEQLPQLLEDLEAEIEALQAQVADADFFSQPHE-QTQKVLADLADAEQELEVAFERWeeLEA 630
|
...
gi 446557484 624 QEQ 626
Cdd:PRK11147 631 LKN 633
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-518 |
8.75e-85 |
|
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: 276.05 E-value: 8.75e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLL---ALLKNEIsaDGGSYTFPGsWQLAWVNQEtPAL--PQAALEYVIDGD 88
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLrimAGVDKDF--NGEARPQPG-IKVGYLPQE-PQLdpTKTVRENVEEGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 89 REYRQLEAQLHD-----ANERNDGQAIATIHGKL----DAIDAWSIRSRAASLLHGLGFSNEqlERPVSDFSGGWRMRLN 159
Cdd:TIGR03719 94 AEIKDALDRFNEisakyAEPDADFDKLAAEQAELqeiiDAADAWDLDSQLEIAMDALRCPPW--DADVTKLSGGERRRVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 160 LAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMFEYTGNYSSFEVQRA 239
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 240 TRLAQQQAMYESQQERVAHLQSYIdRFRAKATKAKQaQSRIKMLERMELIAPAHVDNPFRFSFRAPESLPNPLLKMEKVS 319
Cdd:TIGR03719 252 KRLEQEEKEESARQKTLKRELEWV-RQSPKGRQAKS-KARLARYEELLSQEFQKRNETAEIYIPPGPRLGDKVIEAENLT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 320 AGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQlEYLRADESPIQHLA 399
Cdd:TIGR03719 330 KAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSR-DALDPNKTVWEEIS 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 400 ------RLAPQELEQklRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
Cdd:TIGR03719 409 ggldiiKLGKREIPS--RAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446557484 474 IEFEGALVVVSHDRHLL-RSTTDDLYLVHDRKVEPFDGDLEDYQQW 518
Cdd:TIGR03719 487 LNFAGCAVVISHDRWFLdRIATHILAFEGDSHVEWFEGNFSEYEED 532
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-518 |
2.50e-79 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 261.59 E-value: 2.50e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLL---ALLKNEIsaDGGSYTFPGsWQLAWVNQETPALP-QAALEYVIDGDR 89
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLrimAGVDKEF--EGEARPAPG-IKVGYLPQEPQLDPeKTVRENVEEGVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 90 EYRQLEAQLHD-----ANERNDGQAIATIHGKL----DAIDAWSIRSraasllhglgfsneQLER------------PVS 148
Cdd:PRK11819 97 EVKAALDRFNEiyaayAEPDADFDALAAEQGELqeiiDAADAWDLDS--------------QLEIamdalrcppwdaKVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 149 DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMFEYT 228
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 229 GNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIdRFRAKATKAK-----------QAQSRIKMLERMELIAPahvdnp 297
Cdd:PRK11819 243 GNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWV-RQSPKARQAKskarlaryeelLSEEYQKRNETNEIFIP------ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 298 frfsfrAPESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKL 377
Cdd:PRK11819 316 ------PGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 378 GYFAQHQlEYLRADESPIQHLA------RLAPQELEQklRDYLGGFGF----QGDKVTEetrrFSGGEKARLVLALIVWQ 447
Cdd:PRK11819 390 AYVDQSR-DALDPNKTVWEEISggldiiKVGNREIPS--RAYVGRFNFkggdQQKKVGV----LSGGERNRLHLAKTLKQ 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557484 448 RPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVVVSHDRHLL-RSTTDDLYLVHDRKVEPFDGDLEDYQQW 518
Cdd:PRK11819 463 GGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLdRIATHILAFEGDSQVEWFEGNFQEYEED 534
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
313-504 |
2.45e-57 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 189.97 E-value: 2.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQhqleylrade 392
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 spiqhlarlapqeleqklrdylggfgfqgdkvteetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
Cdd:cd03221 71 --------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEA 112
|
170 180 190
....*....|....*....|....*....|..
gi 446557484 473 LIEFEGALVVVSHDRHLLRSTTDDLYLVHDRK 504
Cdd:cd03221 113 LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
315-584 |
3.45e-57 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 201.45 E-value: 3.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 315 MEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQH----------- 383
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEppldddltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 384 ------------QLEYLRADESP------IQHLARLAPQ-------ELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKAR 438
Cdd:COG0488 81 tvldgdaelralEAELEELEAKLaepdedLERLAELQEEfealggwEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 439 LVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKVEPFDGdleDYQQW 518
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPG---NYSAY 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446557484 519 LsdVQKQENQadeapkenansAQARKDQKRREAELRAQTQPLRKEIAR---------LEKEMEKLNAQLAQAEEK 584
Cdd:COG0488 238 L--EQRAERL-----------EQEAAAYAKQQKKIAKEEEFIRRFRAKarkakqaqsRIKALEKLEREEPPRRDK 299
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-222 |
8.37e-48 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 164.16 E-value: 8.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQetpalpqaal 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 eyvidgdreyrqleaqlhdanerndgqaiatihgkldaidawsirsraasllhglgfsneqlerpvsdFSGGWRMRLNLA 161
Cdd:cd03221 71 --------------------------------------------------------------------LSGGEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 162 QALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQ 222
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-235 |
9.09e-48 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 175.64 E-value: 9.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETPALP--Q 78
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDpdK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 79 AALEYVIDGDREYRQLEaqlhdanerndgqaiatihgkldaidawsirsrAASLLHGLGFSNEQLERPVSDFSGGWRMRL 158
Cdd:COG0488 395 TVLDELRDGAPGGTEQE---------------------------------VRGYLGRFLFSGDDAFKPVGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMFEYTGNYSSFE 235
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYL 518
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-514 |
2.30e-37 |
|
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: 145.82 E-value: 2.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADG---GSYTFPG-----------SWQLAWVNQ 71
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGrdllelsealrGRRIGMVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 72 EtpalPQAALEYVIDGDREYRQLEAQLHDANErndgqaiatihgkldaidawsIRSRAASLLHGLGFSnEQLERPVSDFS 151
Cdd:COG1123 91 D----PMTQLNPVTVGDQIAEALENLGLSRAE---------------------ARARVLELLEAVGLE-RRLDRYPHQLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 152 GGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQG-TLILISHDRDFLDPIVDKIIHIEQQSMFEy 227
Cdd:COG1123 145 GGQRQRVAIAMALALDPDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRIVE- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 228 tgnyssfevqratrlaqqqamyesqqervahlqsyidrfrakATKAKQAQSRIKMLERMELIAPAhvdnpfRFSFRAPES 307
Cdd:COG1123 224 ------------------------------------------DGPPEEILAAPQALAAVPRLGAA------RGRAAPAAA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 308 LPNPLLKMEKVSAGY-----GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQ 382
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI-LFDGKDLTKLSR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 383 HQLEYLRAD----------------------ESPIQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLV 440
Cdd:COG1123 335 RSLRELRRRvqmvfqdpysslnprmtvgdiiAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVA 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 441 LA--LIVwqRPNLLLLDEPTNHLDLDMRQALTEALI----EFEGALVVVSHDRHLLRSTTDDLYLVHD-RKVEpfDGDLE 513
Cdd:COG1123 415 IAraLAL--EPKLLILDEPTSALDVSVQAQILNLLRdlqrELGLTYLFISHDLAVVRYIADRVAVMYDgRIVE--DGPTE 490
|
.
gi 446557484 514 D 514
Cdd:COG1123 491 E 491
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
217-300 |
3.37e-34 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 124.99 E-value: 3.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 217 IHIEQQSMFEYTGNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDN 296
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK 80
|
....*
gi 446557484 297 P-FRF 300
Cdd:pfam12848 81 PkLRF 85
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
315-591 |
3.07e-32 |
|
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: 131.60 E-value: 3.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 315 MEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQH-QL------- 385
Cdd:TIGR03719 7 MNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEpQLdptktvr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 386 EYLRADESPIQHL-------------------ARLAPQ-ELEQKLrDYLGGFGFQ--------------GD-KVTEetrr 430
Cdd:TIGR03719 87 ENVEEGVAEIKDAldrfneisakyaepdadfdKLAAEQaELQEII-DAADAWDLDsqleiamdalrcppWDaDVTK---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 431 FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVVVSHDRHLLRSTTDDLyLVHDR-KVEPFD 509
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWI-LELDRgRGIPWE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 510 GdleDYQQWLSdvQKQENQADEAPKEnansaQARKDQKRREAELRAQTQPLR--KEIARLEKeMEKLNAQlaQAEEKLGD 587
Cdd:TIGR03719 241 G---NYSSWLE--QKQKRLEQEEKEE-----SARQKTLKRELEWVRQSPKGRqaKSKARLAR-YEELLSQ--EFQKRNET 307
|
....
gi 446557484 588 SELY 591
Cdd:TIGR03719 308 AEIY 311
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
313-505 |
1.46e-30 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 117.88 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgIKLGYfaqhqlEYLRADE 392
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEI-----KVLGK------DIKKEPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 SPIQHLArLAPQEleqklrdylggFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
Cdd:cd03230 70 EVKRRIG-YLPEE-----------PSLYENLTVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWEL 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 446557484 473 LIEF--EGALVVV-SHDRHLLRSTTDDLYLVHDRKV 505
Cdd:cd03230 138 LRELkkEGKTILLsSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
314-505 |
1.31e-29 |
|
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: 115.23 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 314 KMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEYLRADEs 393
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI---------LLDGKDLASLSPKE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 394 piqhLAR---LAPQELEQklrdyLGGFGFQGDKVTEetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470
Cdd:cd03214 71 ----LARkiaYVPQALEL-----LGLAHLADRPFNE----LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELL 137
|
170 180 190
....*....|....*....|....*....|....*....
gi 446557484 471 EAL----IEFEGALVVVSHDRHLLRSTTDDLYLVHDRKV 505
Cdd:cd03214 138 ELLrrlaRERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
315-591 |
1.58e-29 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 123.31 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 315 MEKVSAGYG-DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQH-QLeylraDE 392
Cdd:PRK11819 9 MNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEpQL-----DP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 S------------PIQH-LARL------------------APQ-ELEQKLrDYLGGFGFQ--------------GD-KVT 425
Cdd:PRK11819 84 EktvrenveegvaEVKAaLDRFneiyaayaepdadfdalaAEQgELQEII-DAADAWDLDsqleiamdalrcppWDaKVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 426 eetrRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVVVSHDRHLLrsttDD-----LYLv 500
Cdd:PRK11819 163 ----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFL----DNvagwiLEL- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 501 hDR-KVEPFDGdleDYQQWLsdVQKQENQADEAPKEnansaQARkdQKRREAELR--AQTQPLR--KEIARLEKeMEKLN 575
Cdd:PRK11819 234 -DRgRGIPWEG---NYSSWL--EQKAKRLAQEEKQE-----AAR--QKALKRELEwvRQSPKARqaKSKARLAR-YEELL 299
|
330
....*....|....*.
gi 446557484 576 AQlaQAEEKLGDSELY 591
Cdd:PRK11819 300 SE--EYQKRNETNEIF 313
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
314-504 |
3.32e-29 |
|
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: 113.49 E-value: 3.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 314 KMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgyfaqhqleylRADES 393
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI-------------------LIDGK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 394 PIqhlARLAPQELEQKLrdylgGFGFQgdkvteetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
Cdd:cd00267 62 DI---AKLPLEELRRRI-----GYVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELL 123
|
170 180 190
....*....|....*....|....*....|....
gi 446557484 474 IEF--EG-ALVVVSHDRHLLRSTTDDLYLVHDRK 504
Cdd:cd00267 124 RELaeEGrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
309-515 |
4.00e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.96 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 309 PNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL------AKGIKLGYFAQ 382
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 383 HqleyLRADES-PI-------------QHLARLAPQELEQKLRDYL---GGFGFQGDKVTEetrrFSGGEKARLVLA--L 443
Cdd:COG1121 83 R----AEVDWDfPItvrdvvlmgrygrRGLFRRPSRADREAVDEALervGLEDLADRPIGE----LSGGQQQRVLLAraL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446557484 444 IvwQRPNLLLLDEPTNHLDLDMRQALTEALIEF--EG-ALVVVSHDRHLLRSTTDDLYLVHDRKVepFDGDLEDY 515
Cdd:COG1121 155 A--QDPDLLLLDEPFAGVDAATEEALYELLRELrrEGkTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPPEEV 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
312-505 |
1.38e-28 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 114.57 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI---KLGYFAQHQLEYL 388
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSI-LIDGEdvrKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 389 rADESP----------IQHLARLAP---QELEQKLRDYLGGFGFQGDKVTeETRRFSGGEKARLVLALIVWQRPNLLLLD 455
Cdd:COG4555 80 -PDERGlydrltvrenIRYFAELYGlfdEELKKRIEELIELLGLEEFLDR-RVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446557484 456 EPTNHLDLDMRQALTEALIEF--EGALVVVS-HDRHLLRSTTDDLYLVHDRKV 505
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALkkEGKTVLFSsHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
314-504 |
1.42e-28 |
|
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: 113.33 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 314 KMEKVSAGYGD--RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGY------------ 379
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEV-LVDGKDLTKlslkelrrkvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 380 ---FAQHQLEYLRADE----SPIQhlARLAPQELEQKLRDYLGGFGFQGDKvTEETRRFSGGEKARLVLALIVWQRPNLL 452
Cdd:cd03225 80 vfqNPDDQFFGPTVEEevafGLEN--LGLPEEEIEERVEEALELVGLEGLR-DRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446557484 453 LLDEPTNHLDLDMRQALTEALIEF--EG-ALVVVSHDRHLLRSTTDDLYLVHDRK 504
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-221 |
2.52e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.60 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSW-----------QLAWVN 70
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 71 QEtPALPqaaleyvidGDREYRQLEAQLHDANERNDgqaiatihgkldaidawsiRSRAASLLHGLGFSNEQLERPVSDF 150
Cdd:COG4619 81 QE-PALW---------GGTVRDNLPFPFQLRERKFD-------------------RERALELLERLGLPPDILDKPVERL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446557484 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVI-WLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:COG4619 132 SGGERQRLALIRALLLQPDVLLLDEPTSALDPEntrRVEeLLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
322-484 |
2.68e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 113.23 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---GL-----AKGIK--LGYFAQHQ--LEYLR 389
Cdd:COG1131 10 YGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlGEdvardPAEVRrrIGYVPQEPalYPDLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 390 ADESpIQHLARLAP---QELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
Cdd:COG1131 90 VREN-LRFFARLYGlprKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEAR 167
|
170 180
....*....|....*....|
gi 446557484 467 QALTEALIEF--EGALVVVS 484
Cdd:COG1131 168 RELWELLRELaaEGKTVLLS 187
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-221 |
5.84e-28 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 112.64 E-value: 5.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnqetpalpqaa 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 lEYVIDGDREYRQLEAQLHDANERNDG-------QAIATIHGKLDAidawSIRSRAASLLHGLGFSnEQLERPVSDFSGG 153
Cdd:COG4555 63 -EDVRKEPREARRQIGVLPDERGLYDRltvreniRYFAELYGLFDE----ELKKRIEELIELLGLE-EFLDRRVGELSTG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY--QGTLILIS-HDRDFLDPIVDKIIHIEQ 221
Cdd:COG4555 137 MKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkEGKTVLFSsHIMQEVEALCDRVVILHK 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
312-486 |
6.43e-28 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 112.83 E-value: 6.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---G----------LAKgiKLG 378
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldGrdlaslsrreLAR--RIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 379 YFAQHQ--------LEYLRadespiqhLARLApqeleqklrdYLGGFGFQGDK----VTE----------ETRRF---SG 433
Cdd:COG1120 79 YVPQEPpapfgltvRELVA--------LGRYP----------HLGLFGRPSAEdreaVEEalertglehlADRPVdelSG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 434 GEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTE---ALIEFEG-ALVVVSHD 486
Cdd:COG1120 141 GERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLEllrRLARERGrTVVMVLHD 197
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-242 |
2.85e-27 |
|
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: 116.57 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETPALpqaaleyviDGDREY 91
Cdd:TIGR03719 333 GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDAL---------DPNKTV 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 92 RQleaqlhdanERNDGQAIATIhGKLDaidawsIRSRAasLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
Cdd:TIGR03719 404 WE---------EISGGLDIIKL-GKRE------IPSRA--YVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557484 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMFE-YTGNYSSFEVQRATRL 242
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEwFEGNFSEYEEDKKRRL 537
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-288 |
2.96e-27 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 116.97 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETPAL-PQAAleyVIDgdreyr 92
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELdPEKT---VMD------ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 93 qleaqlhdanerN--DGQAIATIHGkldaidawsiRSRaasllHGLG------FSNEQLERPVSDFSGGWRMRLNLAQAL 164
Cdd:PRK11147 403 ------------NlaEGKQEVMVNG----------RPR-----HVLGylqdflFHPKRAMTPVKALSGGERNRLLLARLF 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 165 ICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMF-EYTGNYSSFEVQRATRLA 243
Cdd:PRK11147 456 LKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIgRYVGGYHDARQQQAQYLA 535
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446557484 244 QQQAMYESQQERVAhlqsyidrfrAKATKAKQAQSRIKMLERMEL 288
Cdd:PRK11147 536 LKQPAVKKKEEAAA----------PKAETVKRSSKKLSYKLQREL 570
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
313-514 |
8.13e-27 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 108.96 E-value: 8.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLgyfAQHQLEYLR-- 389
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEV-LVDGKDI---TKKNLRELRrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 390 -----------------ADE---SPIQHlaRLAPQELEQKLRDYLGGFGFQG--DKvteETRRFSGGEKARLVLALIVWQ 447
Cdd:COG1122 77 vglvfqnpddqlfaptvEEDvafGPENL--GLPREEIRERVEEALELVGLEHlaDR---PPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 448 RPNLLLLDEPTNHLDLDMRQALTEALIEF--EG-ALVVVSHDRHLLRSTTDDLYLVHDRKVEpFDGDLED 514
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADRVIVLDDGRIV-ADGTPRE 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-217 |
8.70e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 109.00 E-value: 8.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSytfpgswqlAWVNQETPA-LPQAA 80
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGE---------VRVLGEDVArDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 LE---YVIDGDREYRQLeaqlhdanernDGQAIATIHGKLDAIDAWSIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMR 157
Cdd:COG1131 72 RRrigYVPQEPALYPDL-----------TVRENLRFFARLYGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY--QGTLILIS-HDRDFLDPIVDKII 217
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaEGKTVLLStHYLEEAERLCDRVA 202
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-221 |
2.25e-26 |
|
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: 106.79 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQlawvnQETPALPQAA 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-----RDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 LEYVIDGDREYRQL--EAQLhdanerndgQAIATIHGKLDAidawsiRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRL 158
Cdd:COG4133 77 LAYLGHADGLKPELtvRENL---------RFWAALYGLRAD------REAIDEALEAVGLA-GLADLPVRQLSAGQKRRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY--QGTLILI-SHDRDFLDPivDKIIHIEQ 221
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlaRGGAVLLtTHQPLELAA--ARVLDLGD 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
328-459 |
2.39e-26 |
|
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: 105.04 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAK-----------GIKLGYFAQH-QLEY-LRADE-- 392
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslRKEIGYVFQDpQLFPrLTVREnl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 ---SPIQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
Cdd:pfam00005 81 rlgLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-221 |
4.50e-26 |
|
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: 106.40 E-value: 4.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQaaleyvi 85
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDG--------KDLTKLSL------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 86 dgdREYRQL--------EAQL--HDANE------RNDGQAIATIhgkldaidawsiRSRAASLLHGLGFSnEQLERPVSD 149
Cdd:cd03225 71 ---KELRRKvglvfqnpDDQFfgPTVEEevafglENLGLPEEEI------------EERVEEALELVGLE-GLRDRSPFT 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446557484 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03225 135 LSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-486 |
4.67e-26 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 112.98 E-value: 4.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWqlawvnqetpalpqaalEYVIDgdrEYRQLEaqLHDAN 102
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSW-----------------DEVLK---RFRGTE--LQNYF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 103 ERNDGQAIATIH-------------GK----LDAIDAwsiRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALI 165
Cdd:PRK13409 153 KKLYNGEIKVVHkpqyvdlipkvfkGKvrelLKKVDE---RGKLDEVVERLGLEN-ILDRDISELSGGELQRVAIAAALL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 166 CRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG--TLILISHDRDFLDPIVDkIIHIeqqsMFEYTGNYSSFEVQRATRLA 243
Cdd:PRK13409 229 RDADFYFFDEPTSYLDIRQRLNVARLIRELAEgkYVLVVEHDLAVLDYLAD-NVHI----AYGEPGAYGVVSKPKGVRVG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 244 QQQamyesqqervaHLQSYID----RFRakatkakqaqsrikmlermeliapahvDNPFRFSFRAPESLPN--PLLKMEK 317
Cdd:PRK13409 304 INE-----------YLKGYLPeenmRIR---------------------------PEPIEFEERPPRDESEreTLVEYPD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 318 VSAGYGDriildsIKLNLVPGSR-----IGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkgIKLGYFAQhqleYLRAD- 391
Cdd:PRK13409 346 LTKKLGD------FSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--LKISYKPQ----YIKPDy 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 392 ----------------ESPIQH-------LARLapqeLEQKLRDylggfgfqgdkvteetrrFSGGEKARLVLALIVWQR 448
Cdd:PRK13409 414 dgtvedllrsitddlgSSYYKSeiikplqLERL----LDKNVKD------------------LSGGELQRVAIAACLSRD 471
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 446557484 449 PNLLLLDEPTNHLDLDMRQALTEA---LIE-FEGALVVVSHD 486
Cdd:PRK13409 472 ADLYLLDEPSAHLDVEQRLAVAKAirrIAEeREATALVVDHD 513
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
313-505 |
1.99e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 104.51 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQLE----YL 388
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYL-DGKPLSAMPPPEWRrqvaYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 389 RA-----DESPIQHLA---RLAPQEL-EQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
Cdd:COG4619 80 PQepalwGGTVRDNLPfpfQLRERKFdRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446557484 460 HLDLDMRQALTEALIEF----EGALVVVSHDRHLLRSTTDDLYLVHDRKV 505
Cdd:COG4619 160 ALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
314-505 |
3.08e-25 |
|
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: 103.77 E-value: 3.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 314 KMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA------KGIKLGYFAQHqLEY 387
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgkplekERKRIGYVPQR-RSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 388 LRadESPI--QHLARLApqeleqkLRDYLGGFGFQG----DKVTE----------ETRRF---SGGEKARLVLALIVWQR 448
Cdd:cd03235 80 DR--DFPIsvRDVVLMG-------LYGHKGLFRRLSkadkAKVDEalervglselADRQIgelSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 449 PNLLLLDEPTNHLDLDMRQALTEALIEF--EG-ALVVVSHDRHLLRSTTDDLYLVhDRKV 505
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELrrEGmTILVVTHDLGLVLEYFDRVLLL-NRTV 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-221 |
5.83e-25 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 101.71 E-value: 5.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnqetpalpqaal 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 EYVIDGDREYRQLeaqlhdanerndgqaIATIHGKLDAIDAWSIRsraasllhglgfsnEQLerpvsDFSGGWRMRLNLA 161
Cdd:cd03230 62 KDIKKEPEEVKRR---------------IGYLPEEPSLYENLTVR--------------ENL-----KLSGGMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 162 QALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY--QGTLILI-SHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELkkEGKTILLsSHILEEAERLCDRVAILNN 170
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
313-491 |
8.22e-25 |
|
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: 101.31 E-value: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRI--ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLgyfAQHQLEYLRa 390
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI-LIDGVDL---RDLDLESLR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 despiQHLArLAPQEleqklrDYLggfgFQGdkvteeTRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
Cdd:cd03228 76 -----KNIA-YVPQD------PFL----FSG------TIReniLSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180
....*....|....*....|....*.
gi 446557484 468 ALTEALIEFEG--ALVVVSHDRHLLR 491
Cdd:cd03228 134 LILEALRALAKgkTVIVIAHRLSTIR 159
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
304-490 |
1.37e-24 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 108.31 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 304 APESLPNPL-LKMEKVSAGY--GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYF 380
Cdd:COG4987 324 EPAPAPGGPsLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG-GVDLRDL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 381 AQHQL-------------------EYLR-----ADESPIQH---LARLAP--QELEQKLRDYLGgfgfqgdkvtEETRRF 431
Cdd:COG4987 403 DEDDLrrriavvpqrphlfdttlrENLRlarpdATDEELWAaleRVGLGDwlAALPDGLDTWLG----------EGGRRL 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 432 SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEF--EGALVVVSHDRHLL 490
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAGL 533
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-221 |
1.88e-24 |
|
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: 100.01 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 4 FSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpgswqlawvnqetpalpqaaley 83
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI----------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 84 vidgdreyrqleaqlhdanernDGQAIAtihgkldAIDAWSIRSRAASLLhglgfsneQLerpvsdfSGGWRMRLNLAQA 163
Cdd:cd00267 59 ----------------------DGKDIA-------KLPLEELRRRIGYVP--------QL-------SGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
311-493 |
2.50e-24 |
|
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: 101.02 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLG-----YFAQ--- 382
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEV-LWNGEPIRdaredYRRRlay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 383 --HQLEyLRADESPIQHL---ARLAPQEL-EQKLRDYLGGFGFQG--DKvteETRRFSGGEKARLVLA-LIVWQRPnLLL 453
Cdd:COG4133 80 lgHADG-LKPELTVRENLrfwAALYGLRAdREAIDEALEAVGLAGlaDL---PVRQLSAGQKRRVALArLLLSPAP-LWL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446557484 454 LDEPTNHLDLDMRQALTEALIEF---EGALVVVSHDRHLLRST 493
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
312-527 |
3.43e-24 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 107.34 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLG------------- 378
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVArlqqdpprnvegt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 379 ---YFA---QHQLEYLRA------------DESPIQHLARLAPQ-------ELEQKLRDYLGGFGFQGDKVTEEtrrFSG 433
Cdd:PRK11147 83 vydFVAegiEEQAEYLKRyhdishlvetdpSEKNLNELAKLQEQldhhnlwQLENRINEVLAQLGLDPDAALSS---LSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 434 G--EKARLVLALIVwqRPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVVVSHDRHLLRSTTD---DLylvhDR-KVEP 507
Cdd:PRK11147 160 GwlRKAALGRALVS--NPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATrivDL----DRgKLVS 233
|
250 260
....*....|....*....|
gi 446557484 508 FDGdleDYQQWLSDvqKQEN 527
Cdd:PRK11147 234 YPG---NYDQYLLE--KEEA 248
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-178 |
1.28e-23 |
|
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: 97.33 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgsWQLAWVNQETPALPQAALEYVIDGDREYRQLEA 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIL----LDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 97 QlhdanernDGQAIATIHGKLDAIDAWSIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
Cdd:pfam00005 77 R--------ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 446557484 177 TN 178
Cdd:pfam00005 149 TA 150
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-486 |
1.32e-23 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 105.25 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 26 PGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWqlawvnqetpalpqaalEYVIDgdrEYRQLEAQLHDANERN 105
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSW-----------------DEVLK---RFRGTELQDYFKKLAN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 106 DG-------QAIATI----HGK----LDAIDAwsiRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALICRSDL 170
Cdd:COG1245 158 GEikvahkpQYVDLIpkvfKGTvrelLEKVDE---RGKLDELAEKLGLEN-ILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 171 LLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDkIIHIeqqsMFEYTGNYSSFEVQRATRLAQQQa 247
Cdd:COG1245 234 YFFDEPSSYLDIYQRLNVARLIRELAEegkYVLVVEHDLAILDYLAD-YVHI----LYGEPGVYGVVSKPKSVRVGINQ- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 248 myesqqervaHLQSYID----RFRakatkakqaqsrikmlermeliapahvDNPFRFSFRAPESLPN--PLLKMEKVSAG 321
Cdd:COG1245 308 ----------YLDGYLPeenvRIR---------------------------DEPIEFEVHAPRREKEeeTLVEYPDLTKS 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 322 YGDriildsIKLNLVPGS-----RIGLLGRNGAGKSTLIKLLAGELAPVSGEIGlaKGIKLGYFAQhqleYLRADespiq 396
Cdd:COG1245 351 YGG------FSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKISYKPQ----YISPD----- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 397 hlarlAPQELEQKLRDYLGGfGFQGDKVTEE-TRRF-------------SGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:COG1245 414 -----YDGTVEEFLRSANTD-DFGSSYYKTEiIKPLgleklldknvkdlSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
490 500
....*....|....*....|....*...
gi 446557484 463 LDMRQALTEA---LIEFEGALV-VVSHD 486
Cdd:COG1245 488 VEQRLAVAKAirrFAENRGKTAmVVDHD 515
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-242 |
1.79e-23 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 104.82 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETPALpqaaleyviDGDREY 91
Cdd:PRK11819 335 GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDAL---------DPNKTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 92 RQleaqlhdanERNDGQAIATIHGKldaidawSIRSRAasLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
Cdd:PRK11819 406 WE---------EISGGLDIIKVGNR-------EIPSRA--YVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557484 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMFE-YTGNYSSFEVQRATRL 242
Cdd:PRK11819 468 LLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDSQVEwFEGNFQEYEEDKKRRL 539
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
283-486 |
1.85e-23 |
|
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: 104.36 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 283 LERMELIAPAHVDNPFRFSFRA-PESLPNPLLKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG 360
Cdd:TIGR02868 304 AERIVEVLDAAGPVAEGSAPAAgAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 361 ELAPVSGEIGL-----------AKGIKLGYFAQ--H--------QLEYLRADESPIQHLARLAPQELEQKLRDYLGGFgf 419
Cdd:TIGR02868 384 LLDPLQGEVTLdgvpvssldqdEVRRRVSVCAQdaHlfdttvreNLRLARPDATDEELWAALERVGLADWLRALPDGL-- 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 420 qGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI--EFEGALVVVSHD 486
Cdd:TIGR02868 462 -DTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLaaLSGRTVVLITHH 529
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
310-485 |
2.21e-23 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 99.77 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE----IGLAKG------IK--L 377
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlFGERRGgedvweLRkrI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 378 GYFAQHQLEYLRADESPIQ----------HLARLAPQELEQKLRDYLGGFGFQGDKvteeTRRF---SGGEKaRLVL--- 441
Cdd:COG1119 81 GLVSPALQLRFPRDETVLDvvlsgffdsiGLYREPTDEQRERARELLELLGLAHLA----DRPFgtlSQGEQ-RRVLiar 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446557484 442 ALIvwQRPNLLLLDEPTNHLDLDMRQALTEALIEF--EG--ALVVVSH 485
Cdd:COG1119 156 ALV--KDPELLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTH 201
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
321-499 |
2.28e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.69 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHqleyLRADES------- 393
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQR----SEVPDSlpltvrd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 394 -----------PIQHLARLAPQELEQKLrDYLGGFGFQGDKVTEetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:NF040873 77 lvamgrwarrgLWRRLTRDDRAAVDDAL-ERVGLADLAGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446557484 463 LDMRQALTEALIEF--EGALVV-VSHDRHLLRSTTDDLYL 499
Cdd:NF040873 152 AESRERIIALLAEEhaRGATVVvVTHDLELVRRADPCVLL 191
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
2.58e-23 |
|
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: 104.45 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGV-RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---------PGSW--QLAWV 69
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIngvdlsdldPASWrrQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 70 NQeTPALPQAALEYVIdgdREYRqleaqlHDANErndgqaiatihgklDAIDAWSIRSRAASLLHGLgfsNEQLERPVSD 149
Cdd:COG4988 417 PQ-NPYLFAGTIRENL---RLGR------PDASD--------------EELEAALEAAGLDEFVAAL---PDGLDTPLGE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 150 ----FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD--AVIW--LEKWLKSYqgTLILISHDRDFLDpIVDKIIHIEQ 221
Cdd:COG4988 470 ggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAEteAEILqaLRRLAKGR--TVILITHRLALLA-QADRILVLDD 546
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
311-497 |
1.98e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 97.11 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHqleyLRA 390
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK----LYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 DES---PIQHLARLAPQeleQKLRDYLGGFG-FQGDKVTEE-TRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
Cdd:PRK09544 79 DTTlplTVNRFLRLRPG---TKKEDILPALKrVQAGHLIDApMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 446557484 466 RQALTEaLI-----EFEGALVVVSHDRHLLRSTTDDL 497
Cdd:PRK09544 156 QVALYD-LIdqlrrELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-221 |
2.42e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 95.36 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpgsWQLAWVNQETPALPQAAL 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF---DGKSYQKNIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 eyvIDGDREYRQLEAqlhdaneRNDGQAIATIHGKLDaidawsirSRAASLLHGLGFSNEQlERPVSDFSGGWRMRLNLA 161
Cdd:cd03268 78 ---IEAPGFYPNLTA-------RENLRLLARLLGIRK--------KRIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 162 QALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY--QGTLILI-SHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLrdQGITVLIsSHLLSEIQKVADRIGIINK 201
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-205 |
3.57e-22 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 96.27 E-value: 3.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----SW-------QLAWV 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaSLsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 70 NQETPA-LPQAALEYVIDGDREYRQLEAQLHDAnernDGQAIATIhgkLDAIDAWSIRsraasllhglgfsneqlERPVS 148
Cdd:COG1120 81 PQEPPApFGLTVRELVALGRYPHLGLFGRPSAE----DREAVEEA---LERTGLEHLA-----------------DRPVD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 149 DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVI----WLEKWLKSYQGTLILISHD 205
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLevleLLRRLARERGRTVVMVLHD 197
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
5-205 |
4.03e-22 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 96.04 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 5 SSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGS-----------WQLAWVNQET 73
Cdd:TIGR03873 5 SRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVdlhglsrraraRRVALVEQDS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 74 P-ALPQAALEYVIDGDREYRQLEA--QLHDAnerndgqaiatihgklDAIDAWSIRSRAASLLhglgfsneqlERPVSDF 150
Cdd:TIGR03873 85 DtAVPLTVRDVVALGRIPHRSLWAgdSPHDA----------------AVVDRALARTELSHLA----------DRDMSTL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQGTLILISHD 205
Cdd:TIGR03873 139 SGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAqleTLALVRELAATGVTVVAALHD 196
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
313-500 |
4.07e-22 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 96.04 E-value: 4.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQ------LE 386
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARarrvalVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 387 YLRADESP-----------IQHLARLA--PQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLL 453
Cdd:TIGR03873 82 QDSDTAVPltvrdvvalgrIPHRSLWAgdSPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446557484 454 LDEPTNHLDLDMRQALTEALIEF--EGALVVVS-HDRHLLRSTTDDLYLV 500
Cdd:TIGR03873 161 LDEPTNHLDVRAQLETLALVRELaaTGVTVVAAlHDLNLAASYCDHVVVL 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-505 |
4.77e-22 |
|
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: 100.26 E-value: 4.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLALLK--NEISADGGS--YTFPGSWQLAWVN------QETPALPQAAL 81
Cdd:TIGR03269 12 GKEVL-KNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmDQYEPTSGRiiYHVALCEKCGYVErpskvgEPCPVCGGTLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 EYVID----GDREYRQLEAQLHDANERN-----DGQAIATIHGKLDAI--DAWSIRSRAASLLHGLGFSNeQLERPVSDF 150
Cdd:TIGR03269 91 PEEVDfwnlSDKLRRRIRKRIAIMLQRTfalygDDTVLDNVLEALEEIgyEGKEAVGRAVDLIEMVQLSH-RITHIARDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLD-LDAVI---WLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMFE 226
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKLvhnALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 227 ytgnyssfevqratrlaqqqamyESQQERVahlqsyIDRFrakatkakqaQSRIKMLERMELIapahvdnpfrfsfrape 306
Cdd:TIGR03269 250 -----------------------EGTPDEV------VAVF----------MEGVSEVEKECEV----------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 307 SLPNPLLKMEKVSAGYG--DRIIL---DSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKG------I 375
Cdd:TIGR03269 274 EVGEPIIKVRNVSKRYIsvDRGVVkavDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvdmT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 376 KLGYFAQ----------HQLEYLRADESPIQHLARLA----PQELEQKLRDY-LGGFGFQGDKVTEETRRF----SGGEK 436
Cdd:TIGR03269 354 KPGPDGRgrakryigilHQEYDLYPHRTVLDNLTEAIglelPDELARMKAVItLKMVGFDEEKAEEILDKYpdelSEGER 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 437 ARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTE----ALIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKV 505
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsilkAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
313-491 |
6.23e-22 |
|
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: 100.68 E-value: 6.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDR--IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLgyfAQHQLEYLR- 389
Cdd:COG2274 474 IELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI-LIDGIDL---RQIDPASLRr 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 390 --------------------------ADESPIQHLARLApqELEQKLRDYLGGFGFQgdkVTEETRRFSGGEKARLVLAL 443
Cdd:COG2274 550 qigvvlqdvflfsgtirenitlgdpdATDEEIIEAARLA--GLHDFIEALPMGYDTV---VGEGGSNLSGGQRQRLAIAR 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446557484 444 IVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEG--ALVVVSHDRHLLR 491
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIR 674
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-205 |
1.65e-21 |
|
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: 92.11 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 5 SSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----SWQLAWVNQETPALPQAa 80
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGkdlaSLSPKELARKIAYVPQA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 LEYVidgdreyrqleaqlhdanerndgqaiatihgkldaidawsirsRAASLLHglgfsneqleRPVSDFSGGWRMRLNL 160
Cdd:cd03214 82 LELL-------------------------------------------GLAHLAD----------RPFNELSGGERQRVLL 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446557484 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLK----SYQGTLILISHD 205
Cdd:cd03214 109 ARALAQEPPILLLDEPTSHLDIAHQIELLELLRrlarERGKTVVMVLHD 157
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-221 |
1.88e-21 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 93.55 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnqetpalpqaaLEYVIDGDREYRQ 93
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDG------------------KDITKKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 94 L--------EAQLHDAN--E------RNDGQAIATIhgkldaidawsiRSRAASLLHGLGFSnEQLERPVSDFSGGWRMR 157
Cdd:COG1122 76 KvglvfqnpDDQLFAPTveEdvafgpENLGLPREEI------------RERVEEALELVGLE-HLADRPPHELSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
3.87e-21 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 92.84 E-value: 3.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG------SWQLAWVnqetp 74
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprraRRRIGYV----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 75 alPQAALeyvIDGD-----RE------YRQLeaqlhdanerndgqaiaTIHGKLDAIDawsiRSRAASLLHGLGFSnEQL 143
Cdd:COG1121 81 --PQRAE---VDWDfpitvRDvvlmgrYGRR-----------------GLFRRPSRAD----REAVDEALERVGLE-DLA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 144 ERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIHIE 220
Cdd:COG1121 134 DRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLN 213
|
..
gi 446557484 221 QQ 222
Cdd:COG1121 214 RG 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-217 |
4.19e-21 |
|
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: 92.57 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQAaleyvi 85
Cdd:cd03257 10 SFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDG--------KDLLKLSRR------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 86 dgDREYRQLEAQL--HDANERND-----GQAIA---TIHGKLDaiDAWSIRSRAASLLHGLGFSNEQLERPVSDFSGGWR 155
Cdd:cd03257 76 --LRKIRRKEIQMvfQDPMSSLNprmtiGEQIAeplRIHGKLS--KKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 156 MRLNLAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKS-YQGTLILISHDRDFLDPIVDKII 217
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVsvqAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVA 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-221 |
4.53e-21 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 97.14 E-value: 4.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----SW-------QLAWVNQETP---------- 74
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrDLdeddlrrRIAVVPQRPHlfdttlrenl 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 75 --ALPQAaleyvidGDREYRQ-LE-AQLHDAnerndgqaIATIHGKLDAIdawsirsraasllhgLGFSNEQLerpvsdf 150
Cdd:COG4987 430 rlARPDA-------TDEELWAaLErVGLGDW--------LAALPDGLDTW---------------LGEGGRRL------- 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLD-LDAVIWLEKWLKSYQG-TLILISHDRDFLDpIVDKIIHIEQ 221
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDaATEQALLADLLEALAGrTVLLITHRLAGLE-RMDRILVLED 544
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
313-568 |
5.82e-21 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 97.62 E-value: 5.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLA----------GELAPVSGEIGLAKGIKLGYFAQ 382
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipknCQILHVEQEVVGDDTTALQCVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 383 HQLEYLRADESPIQHLAR------------------------LAPQELEQ---------------KLRDYLGGFGFQGDK 423
Cdd:PLN03073 258 TDIERTQLLEEEAQLVAQqrelefetetgkgkgankdgvdkdAVSQRLEEiykrlelidaytaeaRAASILAGLSFTPEM 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 424 VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVVVSHDRHLLRSTTDDLYLVHDR 503
Cdd:PLN03073 338 QVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQ 417
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446557484 504 KVEPFDGDLEDYQQWLSDVQKQENQADEAPKENANSAQARKDQKRREAELRAQTQPLRKEIARLE 568
Cdd:PLN03073 418 KLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLG 482
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
303-491 |
1.31e-20 |
|
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: 95.98 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 303 RAPESLPNPLLKMEKVSAGYGD-RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFA 381
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI-LINGVDLSDLD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 382 QHQL-------------------EYLR-----ADESPIQHLARLApqELEQKLRDYLGGFGFQgdkVTEETRRFSGGEKA 437
Cdd:COG4988 406 PASWrrqiawvpqnpylfagtirENLRlgrpdASDEELEAALEAA--GLDEFVAALPDGLDTP---LGEGGRGLSGGQAQ 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 438 RLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIE-FEGALV-VVSHDRHLLR 491
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlAKGRTViLITHRLALLA 536
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
313-505 |
1.49e-20 |
|
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: 89.20 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGD--RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgyfaqhqleylra 390
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 despiqhlaRLAPQELEQKLRDYLGGF-GF--QGDKVTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
Cdd:cd03246 60 ---------RLDGADISQWDPNELGDHvGYlpQDDELFSGSIAeniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446557484 465 MRQALTEALIEFEGA---LVVVSHDRHLLRStTDDLYLVHDRKV 505
Cdd:cd03246 131 GERALNQAIAALKAAgatRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
315-517 |
1.52e-20 |
|
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: 91.02 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 315 MEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEYLRA---- 390
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEV-LIDGEDISGLSEAELYRLRRrmgm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 ---------DESPIQHLA-------RLAPQELEQKLRDYLGGFGFQG--DKVTEEtrrFSGGEKARLVLALIVWQRPNLL 452
Cdd:cd03261 82 lfqsgalfdSLTVFENVAfplrehtRLSEEEIREIVLEKLEAVGLRGaeDLYPAE---LSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 453 LLDEPTNHLDlDMRQALTEALI-----EFEGALVVVSHDRHLLRSTTDDLYLVHDRKVEpFDGDLEDYQQ 517
Cdd:cd03261 159 LYDEPTAGLD-PIASGVIDDLIrslkkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIV-AEGTPEELRA 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
313-502 |
2.10e-20 |
|
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: 88.78 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgyfaqhqleylRADE 392
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI-------------------LIDG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 SPIQHLARLAPqELEQKLrdylgGFGFQ----------GDKVTEetrRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:cd03229 62 EDLTDLEDELP-PLRRRI-----GMVFQdfalfphltvLENIAL---GLSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446557484 463 LDMR---QALTEALIEFEG-ALVVVSHDRHLLRSTTDDLYLVHD 502
Cdd:cd03229 133 PITRrevRALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRD 176
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
312-505 |
3.11e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 90.56 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEYLRA- 390
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLN-GRPLAAWSPWELARRRAv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 -------------DE------SPIQHLARLAPQELEQKL----------RDYlggfgfqgdkvteetRRFSGGEKARLVL 441
Cdd:COG4559 80 lpqhsslafpftvEEvvalgrAPHGSSAAQDRQIVREALalvglahlagRSY---------------QTLSGGEQQRVQL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557484 442 A--LI-VWQ----RPNLLLLDEPTNHLDLDMRQALTEALIEF---EGALVVVSHDRHLLRSTTDDLYLVHDRKV 505
Cdd:COG4559 145 ArvLAqLWEpvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
313-484 |
4.64e-20 |
|
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: 88.79 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSrIGLLGRNGAGKSTLIKLLAGELAPVSGEI------GLAKGIK----LGYFAQ 382
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIridgqdVLKQPQKlrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 383 HQLEY--LRADESpIQHLARL-------APQELEQKLRDyLGGFGFQGDKVTEetrrFSGGEKARLVLALIVWQRPNLLL 453
Cdd:cd03264 80 EFGVYpnFTVREF-LDYIAWLkgipskeVKARVDEVLEL-VNLGDRAKKKIGS----LSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190
....*....|....*....|....*....|..
gi 446557484 454 LDEPTNHLDLDMRQALTEALIEF-EGALVVVS 484
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELgEDRIVILS 185
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
307-491 |
5.79e-20 |
|
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: 93.51 E-value: 5.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 307 SLPNPLLKMEKVSAGYGDR-IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKL-------- 377
Cdd:TIGR02857 316 AAPASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN-GVPLadadadsw 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 378 ----GYFAQHQ-------LEYLR-----ADESPIQHLARLAP-QELEQKLRDYLggfgfqGDKVTEETRRFSGGEKARLV 440
Cdd:TIGR02857 395 rdqiAWVPQHPflfagtiAENIRlarpdASDAEIREALERAGlDEFVAALPQGL------DTPIGEGGAGLSGGQAQRLA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446557484 441 LALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEF-EGALV-VVSHDRHLLR 491
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaQGRTVlLVTHRLALAA 521
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
313-505 |
7.51e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 88.49 E-value: 7.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEYLRADE 392
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV-LFDGKPLDIAARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 ---------SPIQHLARLA---PQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
Cdd:cd03269 80 glypkmkviDQLVYLAQLKglkKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446557484 461 LDLDMRQALTEALIEFEGA---LVVVSHDRHLLRSTTDDLYLVHDRKV 505
Cdd:cd03269 159 LDPVNVELLKDVIRELARAgktVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
311-486 |
9.16e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.45 E-value: 9.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEYLRA 390
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLN-GRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 ------------------------DESPIQHLARLAPQELEQ------KLRDYlggfgfqgdkvteetRRFSGGEKARLV 440
Cdd:PRK13548 80 vlpqhsslsfpftveevvamgrapHGLSRAEDDALVAAALAQvdlahlAGRDY---------------PQLSGGEQQRVQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 441 LALI---VWQ---RPNLLLLDEPTNHLDLDMRQALTEALIEF----EGALVVVSHD 486
Cdd:PRK13548 145 LARVlaqLWEpdgPPRWLLLDEPTSALDLAHQHHVLRLARQLaherGLAVIVVLHD 200
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
313-492 |
9.18e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 88.19 E-value: 9.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEYLR-- 389
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-GQDLSRLKRREIPYLRrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 390 -----------ADESPIQHLA------RLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVL--ALIVwqRPN 450
Cdd:COG2884 81 igvvfqdfrllPDRTVYENVAlplrvtGKSRKEIRRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAIarALVN--RPE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446557484 451 LLLLDEPTNHLDLDMRQALTEALIEF--EG-ALVVVSHDRHLLRS 492
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELVDR 202
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
313-490 |
1.02e-19 |
|
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: 86.98 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYG--DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLakgiklgyfaqhqleylra 390
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 DESPIqhlarlapQELEQKLRDYLG-----GFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
Cdd:cd03247 62 DGVPV--------SDLEKALSSLISvlnqrPYLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180
....*....|....*....|....*..
gi 446557484 466 RQALTEALIEF--EGALVVVSHdrHLL 490
Cdd:cd03247 134 ERQLLSLIFEVlkDKTLIWITH--HLT 158
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
313-505 |
1.48e-19 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 87.27 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKL--------------- 377
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI-TFDGKSYqkniealrrigalie 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 378 --GYF----AQHQLEYLRAdespiqhLARLAPQELEQKLRdyLGGFGFQGDKvteETRRFSGGEKARLVLALIVWQRPNL 451
Cdd:cd03268 80 apGFYpnltARENLRLLAR-------LLGIRKKRIDEVLD--VVGLKDSAKK---KVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 452 LLLDEPTNHLD----LDMRQaLTEALIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKV 505
Cdd:cd03268 148 LILDEPTNGLDpdgiKELRE-LILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-220 |
2.39e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 86.54 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 6 SLQIRRGVRVLlDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETPALPQAALEYVI 85
Cdd:cd03226 6 SFSYKKGTEIL-DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDVDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 86 DGDREYRQLEAQLHDANERNdgQAIATIHGKLDaidawsirsraaslLHGLGfsneqlERPVSDFSGGWRMRLNLAQALI 165
Cdd:cd03226 85 FTDSVREELLLGLKELDAGN--EQAETVLKDLD--------------LYALK------ERHPLSLSGGQKQRLAIAAALL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 166 CRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIHIE 220
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-217 |
3.22e-19 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 86.65 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 8 QIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlAWVNQEtPALPQAALEYVIDG 87
Cdd:cd03266 12 RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG----FDVVKE-PAEARRRLGFVSDS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 88 DREYRQLEAqlhdaneRNDGQAIATIHG-KLDAIDAwsirsRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALIC 166
Cdd:cd03266 87 TGLYDRLTA-------RENLEYFAGLYGlKGDELTA-----RLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446557484 167 RSDLLLLDEPTNHLDLDAV-IWLE--KWLKSYQGTLILISHDRDFLDPIVDKII 217
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATrALREfiRQLRALGKCILFSTHIMQEVERLCDRVV 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
316-490 |
3.41e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 86.16 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 316 EKVSAGYGDRI-ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKL-------GYFAQ---H 383
Cdd:cd03226 3 ENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLnGKPIKAkerrksiGYVMQdvdY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 384 QL-------E-YLRADESPiqhlarLAPQELEQKLRDyLGGFGFQgdkvTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
Cdd:cd03226 83 QLftdsvreElLLGLKELD------AGNEQAETVLKD-LDLYALK----ERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 446557484 456 EPTNHLDLDMRQALTEALIEFEG---ALVVVSHDRHLL 490
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFL 189
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
321-486 |
3.99e-19 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 86.40 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAK----------GIKLGYFAQH--QLEYL 388
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaaRQSLGYCPQFdaLFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 389 radeSPIQHL---ARL-------APQELEQKLRdylgGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
Cdd:cd03263 91 ----TVREHLrfyARLkglpkseIKEEVELLLR----VLGLT-DKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190
....*....|....*....|....*....|
gi 446557484 459 NHLDLDMRQALTEALIEFEG--ALVVVSHD 486
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-221 |
4.40e-19 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 87.17 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 8 QIRRGVRVLlDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSwqlawvnqetpALPQAAleyvidg 87
Cdd:COG1124 13 QGGRRVPVL-KDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR-----------PVTRRR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 88 DREYR---QL-----EAQLHDAneRNDGQAIA---TIHGKLDaidawsIRSRAASLLHGLGFSNEQLERPVSDFSGGWRM 156
Cdd:COG1124 74 RKAFRrrvQMvfqdpYASLHPR--HTVDRILAeplRIHGLPD------REERIAELLEQVGLPPSFLDRYPHQLSGGQRQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 157 RLNLAQALICRSDLLLLDEPTNHLDL--DAVIW--LEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVsvQAEILnlLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
313-486 |
4.55e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.38 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQLEylrade 392
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFL-GDKPISMLSSRQLA------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 spiQHLARLaPQELE-------QKLRDY-----LGGFGFQGDK----VT---EET-------RR---FSGGEKARLVLAL 443
Cdd:PRK11231 76 ---RRLALL-PQHHLtpegitvRELVAYgrspwLSLWGRLSAEdnarVNqamEQTrinhladRRltdLSGGQRQRAFLAM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446557484 444 IVWQRPNLLLLDEPTNHLDLDMRQALTEALIEF--EGALVV-VSHD 486
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELntQGKTVVtVLHD 197
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
320-510 |
7.06e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 85.66 E-value: 7.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 320 AGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIK----LGYFAQHQLE-----YLRA 390
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSsllgLGGGFNPELTgreniYLNG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 despiqHLARLAPQELEQKLRDYLgGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT----NHLDLDMR 466
Cdd:cd03220 110 ------RLLGLSRKEIDEKIDEII-EFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLavgdAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446557484 467 QALTEaLIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKVEpFDG 510
Cdd:cd03220 183 RRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR-FDG 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-219 |
9.21e-19 |
|
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: 90.04 E-value: 9.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIR-RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG---------SW--QLAWV 69
Cdd:TIGR02857 322 LEFSGVSVAyPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadSWrdQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 70 NQeTPALPQAALEYVIdgdreyrqleaqlhdanerndgqAIATIHGKLDAIDAWSIRSRAASLLHGLGfsnEQLERPVSD 149
Cdd:TIGR02857 402 PQ-HPFLFAGTIAENI-----------------------RLARPDASDAEIREALERAGLDEFVAALP---QGLDTPIGE 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 150 ----FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD-AVIWLEKWLKSYQG-TLILISHDRDFLdPIVDKIIHI 219
Cdd:TIGR02857 455 ggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAEtEAEVLEALRALAQGrTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
328-485 |
1.19e-18 |
|
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: 84.95 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI------------KLGYFAQH-QLEY--LR--- 389
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV-LLDGTdirqldpadlrrNIGYVPQDvTLFYgtLRdni 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 390 ------ADESPIQHLARLApqELEQKLRDYLGGFGFQgdkVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
Cdd:cd03245 99 tlgaplADDERILRAAELA--GVTDFVNKHPNGLDLQ---IGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
|
170 180
....*....|....*....|....
gi 446557484 464 DMRQALTEALIEFEG--ALVVVSH 485
Cdd:cd03245 174 NSEERLKERLRQLLGdkTLIIITH 197
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
17-221 |
1.90e-18 |
|
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: 84.46 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQAALeyvidgdREYR---- 92
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDG--------TDISKLSEKEL-------AAFRrrhi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 93 ----QleaQLHDANERNDGQAIATIhGKLDAIDAWSIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALICRS 168
Cdd:cd03255 85 gfvfQ---SFNLLPDLTALENVELP-LLLAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 169 DLLLLDEPTNHLDLD---AVIWLEKWLKSYQG-TLILISHDRDfLDPIVDKIIHIEQ 221
Cdd:cd03255 160 KIILADEPTGNLDSEtgkEVMELLRELNKEAGtTIVVVTHDPE-LAEYADRIIELRD 215
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-223 |
1.95e-18 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 84.79 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGS--YTFPGSW-----------------QLAWVNQETPALP 77
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGWvdlaqaspreilalrrrTIGYVSQFLRVIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 78 -QAALEYVIdgdreyrqlEAQLhdanERNDGQAIAtihgkldaidawsiRSRAASLLHGLGFSNEQLERPVSDFSGGWRM 156
Cdd:COG4778 107 rVSALDVVA---------EPLL----ERGVDREEA--------------RARARELLARLNLPERLWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 157 RLNLAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKSyQGTLIL-ISHDRDFLDPIVDKIIHIEQQS 223
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAanrAVVVELIEEAKA-RGTAIIgIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-221 |
4.52e-18 |
|
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: 82.05 E-value: 4.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----SWQLAWVNQETPALPQaaleyvidgdr 89
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrDLDLESLRKNIAYVPQ----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 90 eyrqlEAQLHDAnerndgqaiatihgkldaidawSIRSraaSLLhglgfsneqlerpvsdfSGGWRMRLNLAQALICRSD 169
Cdd:cd03228 84 -----DPFLFSG----------------------TIRE---NIL-----------------SGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 170 LLLLDEPTNHLDLD--AVIW--LEKWLKSYqgTLILISHdRDFLDPIVDKIIHIEQ 221
Cdd:cd03228 117 ILILDEATSALDPEteALILeaLRALAKGK--TVIVIAH-RLSTIRDADRIIVLDD 169
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-221 |
8.49e-18 |
|
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: 82.58 E-value: 8.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 4 FSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG------SWQLAWVNQET---P 74
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekeRKRIGYVPQRRsidR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 75 ALPQAALEYVIDGDREYRQLeaqlhdanerndgqaiatiHGKLDAIDawsiRSRAASLLHGLGFSnEQLERPVSDFSGGW 154
Cdd:cd03235 82 DFPISVRDVVLMGLYGHKGL-------------------FRRLSKAD----KAKVDEALERVGLS-ELADRQIGELSGGQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 155 RMRLNLAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03235 138 QQRVLLARALVQDPDLLLLDEPFAGVDPktqEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNR 207
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
312-505 |
9.73e-18 |
|
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: 82.55 E-value: 9.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGYGDRI----ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEY 387
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSI-IFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 388 LRAD-----------------------ESPIQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALI 444
Cdd:cd03257 80 RRKEiqmvfqdpmsslnprmtigeqiaEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 445 VWQRPNLLLLDEPTNHLDLDMrQALTEALI-----EFEGALVVVSHDRHLLRSTTDDLYLVHDRKV 505
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSV-QAQILDLLkklqeELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
298-520 |
3.46e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.28 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 298 FRFSFRAPESLPNPLLKMEKvsAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------- 369
Cdd:COG1134 14 YRLYHEPSRSLKELLLRRRR--TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVevngrvsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 370 --GLAKGIklgyfaQHQL---E--YLRAdespiqHLARLAPQELEQKLRDY-----LGGFGFQgdKVteetRRFSGGEKA 437
Cdd:COG1134 92 llELGAGF------HPELtgrEniYLNG------RLLGLSRKEIDEKFDEIvefaeLGDFIDQ--PV----KTYSSGMRA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 438 RLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEF---EGALVVVSHDRHLLRSTTDDLYLVHDRKVEpFDGDLED 514
Cdd:COG1134 154 RLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELresGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV-MDGDPEE 232
|
250
....*....|
gi 446557484 515 ----YQQWLS 520
Cdd:COG1134 233 viaaYEALLA 242
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
313-493 |
3.63e-17 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 80.53 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRII-LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEYLRAD 391
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTI-RVNGQDVSDLRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 392 ESPIQHLARL-------------------APQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLL 452
Cdd:cd03292 80 IGVVFQDFRLlpdrnvyenvafalevtgvPPREIRKRVPAALELVGLS-HKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446557484 453 LLDEPTNHLDLDMRQALTEAL--IEFEGALVVVS-HDRHLLRST 493
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLkkINKAGTTVVVAtHAKELVDTT 202
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-221 |
4.21e-17 |
|
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: 80.71 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG--SWQL---------AWVNQEtPALPQAALeyvi 85
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdIRQLdpadlrrniGYVPQD-VTLFYGTL---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 86 dgdREYRQLEAQLHDANERndgQAIATIHGKLDAIDawsirsraaslLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALI 165
Cdd:cd03245 95 ---RDNITLGAPLADDERI---LRAAELAGVTDFVN-----------KHPNGLDLQIGERGRG-LSGGQRQAVALARALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 166 CRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG--TLILISHDRDFLDpIVDKIIHIEQ 221
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLD-LVDRIIVMDS 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-205 |
4.40e-17 |
|
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: 80.59 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG------SWQLAWVNQETPALP-QAALE 82
Cdd:cd03293 13 GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpGPDRGYVFQQDALLPwLTVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 83 YVIDGdreyrqLEAQLHDANERndgqaiatihgkldaidawsiRSRAASLLH--GL-GFSN---EQLerpvsdfSGGWRM 156
Cdd:cd03293 93 NVALG------LELQGVPKAEA---------------------RERAEELLElvGLsGFENaypHQL-------SGGMRQ 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446557484 157 RLNLAQALICRSDLLLLDEPTNHLD----LDAVIWLEKWLKSYQGTLILISHD 205
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
313-485 |
4.54e-17 |
|
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: 79.01 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEYLRADE 392
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI---------LVDGKEVSFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 SpIQHLARLAPQeleqklrdylggfgfqgdkvteetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDldmrQALTEA 472
Cdd:cd03216 72 A-RRAGIAMVYQ--------------------------LSVGERQMVEIARALARNARLLILDEPTAALT----PAEVER 120
|
170 180
....*....|....*....|
gi 446557484 473 LIEF------EG-ALVVVSH 485
Cdd:cd03216 121 LFKVirrlraQGvAVIFISH 140
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-221 |
5.23e-17 |
|
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: 84.89 E-value: 5.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---------PGSW--QLAWVNQET----------- 73
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidlrqidPASLrrQIGVVLQDVflfsgtireni 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 74 ----PALPQAALEYVIDgdreyrqlEAQLHDAnerndgqaiatihgkldaidawsIRSRAasllhglgfsnEQLERPVSD 149
Cdd:COG2274 570 tlgdPDATDEEIIEAAR--------LAGLHDF-----------------------IEALP-----------MGYDTVVGE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 150 ----FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD--AVIW--LEKWLKsyQGTLILISHDRDFLDpIVDKIIHIEQ 221
Cdd:COG2274 608 ggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAEteAIILenLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDK 684
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-207 |
5.42e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.59 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQET---PALPQAALEYVIDGdRE 90
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSevpDSLPLTVRDLVAMG-RW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 91 YRQLEAQLHDANERndgqaiATIHGKLDAIDawsirsraaslLHGLgfsneqLERPVSDFSGGWRMRLNLAQALICRSDL 170
Cdd:NF040873 84 ARRGLWRRLTRDDR------AAVDDALERVG-----------LADL------AGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446557484 171 LLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRD 207
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLE 180
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
309-487 |
7.60e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 82.45 E-value: 7.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 309 PNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEYL 388
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRI---------LLDGRDVTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 389 RADESPI----QHLA------------------RLAPQELEQKLRDYL-----GGFGfqgdkvteetRRF----SGGEKA 437
Cdd:COG3842 73 PPEKRNVgmvfQDYAlfphltvaenvafglrmrGVPKAEIRARVAELLelvglEGLA----------DRYphqlSGGQQQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 438 RLVLA--LIVwqRPNLLLLDEPTNHLDL----DMRQALTEALIEFEGALVVVSHDR 487
Cdd:COG3842 143 RVALAraLAP--EPRVLLLDEPLSALDAklreEMREELRRLQRELGITFIYVTHDQ 196
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
322-471 |
1.07e-16 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 79.34 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA--------KGIK--LGYFAQhqleYLRAD 391
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghdvvrepREVRrrIGIVFQ----DLSVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 392 E--SPIQHL---ARLA---PQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
Cdd:cd03265 86 DelTGWENLyihARLYgvpGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
....*...
gi 446557484 464 DMRQALTE 471
Cdd:cd03265 165 QTRAHVWE 172
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
328-486 |
1.11e-16 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 80.14 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGS-----RIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQhqleYLRADEspiqhlarla 402
Cdd:cd03237 10 LGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQ----YIKADY---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 403 PQELEQKLRDYLGGFG------------FQGDKVTE-ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
Cdd:cd03237 75 EGTVRDLLSSITKDFYthpyfkteiakpLQIEQILDrEVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180
....*....|....*....|.
gi 446557484 470 TEALIEF----EGALVVVSHD 486
Cdd:cd03237 155 SKVIRRFaennEKTAFVVEHD 175
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
311-486 |
1.27e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.11 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLkMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAkgiklgyfAQHQLEYLRA 390
Cdd:PRK11247 12 PLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LA--------GTAPLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 DESPIQHLARLAPQeleQKLRDYLgGFGFQG----------------DKVTEETRRFSGGEKARLVLALIVWQRPNLLLL 454
Cdd:PRK11247 82 DTRLMFQDARLLPW---KKVIDNV-GLGLKGqwrdaalqalaavglaDRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 446557484 455 DEPTNHLD----LDMrQALTEALIEFEGALVV-VSHD 486
Cdd:PRK11247 158 DEPLGALDaltrIEM-QDLIESLWQQHGFTVLlVTHD 193
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
313-514 |
1.30e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.92 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQLEYL---- 388
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW-DGEPLDPEDRRRIGYLpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 389 ------RADESpIQHLARL---APQELEQKLRDYLGGFGFqGDKVTEETRRFSGGE--KARLVLALIvwQRPNLLLLDEP 457
Cdd:COG4152 81 glypkmKVGEQ-LVYLARLkglSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNqqKVQLIAALL--HDPELLILDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 458 TNHLDLDMRQALTEALIEF--EGALVVVS-HDRHLLRSTTDDLYLVHD-RKVepFDGDLED 514
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELaaKGTTVIFSsHQMELVEELCDRIVIINKgRKV--LSGSVDE 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
327-505 |
1.73e-16 |
|
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: 78.69 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGI----------------KLGY-FAQHQL-EYL 388
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD-GTdisklsekelaafrrrHIGFvFQSFNLlPDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 389 RADE--SPIQHLARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLA--LIvwQRPNLLLLDEPTNHLDLD 464
Cdd:cd03255 98 TALEnvELPLLLAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIAraLA--NDPKIILADEPTGNLDSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446557484 465 MRQALTEALIEF---EG-ALVVVSHDRHLLrSTTDDLYLVHDRKV 505
Cdd:cd03255 175 TGKEVMELLRELnkeAGtTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-216 |
2.34e-16 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 78.32 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSytfpgswqlAWVN----QETPALPQAALEYVI 85
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGT---------AYINgysiRTDRKAARQSLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 86 DGDREYRQLEAQLHdanerndgqaiATIHGKLDAIDAWSIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALI 165
Cdd:cd03263 82 QFDALFDELTVREH-----------LRFYARLKGLPKSEIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 166 CRSDLLLLDEPTnhLDLDAV----IWleKWLKSYQG--TLILISHDRDFLDPIVDKI 216
Cdd:cd03263 150 GGPSVLLLDEPT--SGLDPAsrraIW--DLILEVRKgrSIILTTHSMDEAEALCDRI 202
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
313-487 |
2.79e-16 |
|
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: 77.94 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA-----------KGIklGYFA 381
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvtgvpperRNI--GMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 382 QHQLEY------------LRADESPIQHLARLAPQELEQ-KLRDYLGgfgfqgdkvtEETRRFSGGEKARLVLA--LIVw 446
Cdd:cd03259 79 QDYALFphltvaeniafgLKLRGVPKAEIRARVRELLELvGLEGLLN----------RYPHELSGGQQQRVALAraLAR- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446557484 447 qRPNLLLLDEPTNHLDLDMRQALTEALIEFEGAL----VVVSHDR 487
Cdd:cd03259 148 -EPSLLLLDEPLSALDAKLREELREELKELQRELgittIYVTHDQ 191
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-217 |
3.40e-16 |
|
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: 78.31 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQAal 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDG--------EDISGLSEA-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 eyvidgdrEYRQLEAQ---------LHDAneRNDGQAIA---TIHGKLDAidaWSIRSRAASLLHGLGFSNEQLERPvSD 149
Cdd:cd03261 71 --------ELYRLRRRmgmlfqsgaLFDS--LTVFENVAfplREHTRLSE---EEIREIVLEKLEAVGLRGAEDLYP-AE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557484 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLK-SYQGTLILISHDRDFLDPIVDKII 217
Cdd:cd03261 137 LSGGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKkELGLTSIMVTHDLDTAFAIADRIA 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-216 |
3.42e-16 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 77.80 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSytfpgswqlAWVnqetpalpqAAL 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGR---------ATV---------AGH 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 EYVIDGD--REYRQLEAQLHDANERNDGQAIATIHGKLDAIDAWSIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLN 159
Cdd:cd03265 63 DVVREPRevRRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLE 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 160 LAQALICRSDLLLLDEPTNHLDLDAV--IW--LEKWLKSYQGTLILISHDRDFLDPIVDKI 216
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQTRahVWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRV 202
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
273-508 |
4.18e-16 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 81.72 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 273 AKQAQSRIKML--------ERMELIAPAHVdnpfrfsfrapeslpnplLKMEKVSAGY--GDRIILDSIKLNLVPGSRIG 342
Cdd:COG4618 301 ARQAYRRLNELlaavpaepERMPLPRPKGR------------------LSVENLTVVPpgSKRPILRGVSFSLEPGEVLG 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 343 LLGRNGAGKSTLIKLLAGELAPVSGEIGL-----------AKGIKLGYFAQhQLEYLR------------ADESPIQHLA 399
Cdd:COG4618 363 VIGPSGSGKSTLARLLVGVWPPTAGSVRLdgadlsqwdreELGRHIGYLPQ-DVELFDgtiaeniarfgdADPEKVVAAA 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 400 RLAP-QELEQKLRDylgGFGFQgdkVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEF-- 476
Cdd:COG4618 442 KLAGvHEMILRLPD---GYDTR---IGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALka 515
|
250 260 270
....*....|....*....|....*....|...
gi 446557484 477 EGA-LVVVSHDRHLLRStTDDLYLVHDRKVEPF 508
Cdd:COG4618 516 RGAtVVVITHRPSLLAA-VDKLLVLRDGRVQAF 547
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
17-217 |
4.89e-16 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 77.43 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGS--YTFPGSW-----------------QLAWVNQETPALP 77
Cdd:TIGR02324 24 LKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRilVRHEGAWvdlaqasprevlevrrkTIGYVSQFLRVIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 78 Q-AALEYVIDgdreyrqleaqlhDANERNDGQAIAtihgkldaidawsiRSRAASLLHGLGFSNEQLERPVSDFSGGWRM 156
Cdd:TIGR02324 104 RvSALEVVAE-------------PLLERGVPREAA--------------RARARELLARLNIPERLWHLPPATFSGGEQQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557484 157 RLNLAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
Cdd:TIGR02324 157 RVNIARGFIADYPILLLDEPTASLDAanrQVVVELIAEAKARGAALIGIFHDEEVRELVADRVM 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
310-491 |
5.38e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 77.39 E-value: 5.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 310 NPLLKMEKVS----AGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLA 372
Cdd:COG1136 2 SPLLELRNLTksygTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlidgqdisslserELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 373 K--GIKLGY-FAQHQL-EYLRADES---PiQHLARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEK-----ARlv 440
Cdd:COG1136 82 RlrRRHIGFvFQFFNLlPELTALENvalP-LLLAGVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQQqrvaiAR-- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446557484 441 lALIvwQRPNLLLLDEPTNHLDLDMRQALTEALIEF---EG-ALVVVSHDRHLLR 491
Cdd:COG1136 158 -ALV--NRPKLILADEPTGNLDSKTGEEVLELLRELnreLGtTIVMVTHDPELAA 209
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
311-458 |
6.82e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 77.33 E-value: 6.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEYLRA 390
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSI---------RFDGEDITGLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 DEspiqhLARL----APQE--------LEQKLRdyLGGFGFQGDKVTEETR-----RF--------------SGGEK--- 436
Cdd:COG0410 73 HR-----IARLgigyVPEGrrifpsltVEENLL--LGAYARRDRAEVRADLervyeLFprlkerrrqragtlSGGEQqml 145
|
170 180
....*....|....*....|....
gi 446557484 437 --ARlvlALIvwQRPNLLLLDEPT 458
Cdd:COG0410 146 aiGR---ALM--SRPKLLLLDEPS 164
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
328-505 |
6.91e-16 |
|
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: 77.02 E-value: 6.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGI-----------KLGYFAQHQLEYLR--ADESp 394
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD-GFdvvkepaearrRLGFVSDSTGLYDRltAREN- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 395 IQHLARL---APQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTE 471
Cdd:cd03266 99 LEYFAGLyglKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALRE 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 446557484 472 ALIEF--EG-ALVVVSHDRHLLRSTTDDLYLVHDRKV 505
Cdd:cd03266 178 FIRQLraLGkCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
328-507 |
9.64e-16 |
|
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: 76.56 E-value: 9.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNL---VPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL--------AKGI-------KLGY-FAQHQL-EY 387
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdsRKKInlppqqrKIGLvFQQYALfPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 388 LRADESPIQHLARLAPQELEQKLRDYLGGFGFQGdKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
Cdd:cd03297 90 LNVRENLAFGLKRKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446557484 468 A----LTEALIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKVEP 507
Cdd:cd03297 169 QllpeLKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
313-514 |
2.27e-15 |
|
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: 75.94 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQ-------- 384
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV-LFDGEDITGLPPHEiarlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 385 -------------LE------YLRADESPIQHLARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIV 445
Cdd:cd03219 80 tfqiprlfpeltvLEnvmvaaQARTGSGLLLARARREEREARERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 446 WQRPNLLLLDEPTNHLDLDMRQALTE---ALIEFEGALVVVSHDRHLLRSTTDDLY-LVHDRKVepFDGDLED 514
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAElirELRERGITVLLVEHDMDVVMSLADRVTvLDQGRVI--AEGTPDE 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
313-517 |
3.61e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 75.35 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEYLRADE 392
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI---------LLDGKDITNLPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 SPI----QH------------------LARLAPQELEQKLRDYLG--GFGFQGDKVTEEtrrFSGGEKARLVLALIVWQR 448
Cdd:cd03300 72 RPVntvfQNyalfphltvfeniafglrLKKLPKAEIKERVAEALDlvQLEGYANRKPSQ---LSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 449 PNLLLLDEPTNHLDLDMRQALTEALIEFEGAL----VVVSHDRHLLRSTTDDLYLVHDRKVEPFDGDLEDYQQ 517
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKELgitfVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
327-501 |
3.61e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 76.00 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEYLRAD--------------- 391
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFR-GQDLYQLDRKQRRAFRRDvqlvfqdspsavnpr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 392 -------ESPIQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
Cdd:TIGR02769 105 mtvrqiiGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446557484 465 MR----QALTEALIEFEGALVVVSHDRHLLRSTTDDLYLVH 501
Cdd:TIGR02769 185 LQavilELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMD 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
309-495 |
3.83e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 75.85 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 309 PNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI--------GLA------KG 374
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlfdgrditGLPphriarLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 375 I-------------------KLGYFAQHQLEYLRADESPIQHLARLApqELEQKLRDYLGGFGFqGDKVTEETRRFSGGE 435
Cdd:COG0411 81 IartfqnprlfpeltvlenvLVAAHARLGRGLLAALLRLPRARREER--EARERAEELLERVGL-ADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557484 436 KARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI----EFEGALVVVSHDRHLLRSTTD 495
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRrlrdERGITILLIEHDMDLVMGLAD 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
313-495 |
3.92e-15 |
|
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: 75.30 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGD-RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------GLAKGIKL------- 377
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdiNKLKGKALrqlrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 378 GY-FAQHQL-EYLRADE----------SPIQHLARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIV 445
Cdd:cd03256 81 GMiFQQFNLiERLSVLEnvlsgrlgrrSTWRSLFGLFPKEEKQRALAALERVGLL-DKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446557484 446 WQRPNLLLLDEPTNHLDLDMRQALTEALIEF---EGALVVVS-HDRHLLRSTTD 495
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQVDLAREYAD 213
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
324-506 |
4.15e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.70 E-value: 4.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAP-VSGEIGLAKGIKLGYFAQH----------QLEYLRADE 392
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPyGSGRIARPAGARVLFLPQRpylplgtlreALLYPATAE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 SpiqhlarLAPQELEQKLRDY-LGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTE 471
Cdd:COG4178 454 A-------FSDAELREALEAVgLGHLAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ 526
|
170 180 190
....*....|....*....|....*....|....*..
gi 446557484 472 ALIE--FEGALVVVSHdrhllRSTTDDLylvHDRKVE 506
Cdd:COG4178 527 LLREelPGTTVISVGH-----RSTLAAF---HDRVLE 555
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
328-491 |
4.52e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 75.26 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAPVSGEIGLAkGIKL------------GYFAQHQL--------EY 387
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLN-GRPLsdwsaaelarhrAYLSQQQSppfampvfQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 388 LRadespiQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLA---LIVWQRPN----LLLLDEPTNH 460
Cdd:COG4138 90 LA------LHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAavlLQVWPTINpegqLLLLDEPMNS 163
|
170 180 190
....*....|....*....|....*....|....*
gi 446557484 461 LDLDMRQALTEALIEF--EGALVVVS-HD-RHLLR 491
Cdd:COG4138 164 LDVAQQAALDRLLRELcqQGITVVMSsHDlNHTLR 198
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
311-486 |
4.87e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.35 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLAKGIK- 376
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqlrdlyALSEAERr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 377 ------LGYFAQHQLEYLRADESPIQHLA-RLAPQ------ELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLAL 443
Cdd:PRK11701 85 rllrteWGFVHQHPRDGLRMQVSAGGNIGeRLMAVgarhygDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446557484 444 IVWQRPNLLLLDEPTNHLD-------LDMRQALTEaliEFEGALVVVSHD 486
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDvsvqarlLDLLRGLVR---ELGLAVVIVTHD 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-219 |
5.35e-15 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 75.12 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALlkneISAD-----GGSYTF----PGSW------- 64
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSL----ITGDlpptyGNDVRLfgerRGGEdvwelrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 65 QLAWVnqeTPALPQA------ALEYVIDGdreyrqleaqlhdanerndgqAIATI--HGKLDAIDawsiRSRAASLLHGL 136
Cdd:COG1119 79 RIGLV---SPALQLRfprdetVLDVVLSG---------------------FFDSIglYREPTDEQ----RERARELLELL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 137 GFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA----VIWLEKWLKSYQGTLILISHdrdFLDPI 212
Cdd:COG1119 131 GLA-HLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH---HVEEI 206
|
....*..
gi 446557484 213 VDKIIHI 219
Cdd:COG1119 207 PPGITHV 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-205 |
5.37e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.05 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLA----LLK---NEISADGGSYTFPGSWQLAwvnQET 73
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKcfarLLTpqsGTVFLGDKPISMLSSRQLA---RRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 74 PALPQAAL--------EYVIDGDREYRQLEAQLHDANERNDGQAIATIHgkldaidawsirsraasllhglgfSNEQLER 145
Cdd:PRK11231 79 ALLPQHHLtpegitvrELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTR------------------------INHLADR 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 146 PVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHD 205
Cdd:PRK11231 135 RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTqgkTVVTVLHD 197
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
312-491 |
7.36e-15 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 74.84 E-value: 7.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGYG----DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-----GLAKGIKLGYFAQ 382
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 383 HQLEY----------LRADES---PIQHLARLAPQELEQKLRDYLGgfgfqgdkVTEETR-RF----SGGEKARLVL--A 442
Cdd:COG1124 81 VQMVFqdpyaslhprHTVDRIlaePLRIHGLPDREERIAELLEQVG--------LPPSFLdRYphqlSGGQRQRVAIarA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446557484 443 LIVwqRPNLLLLDEPTNHLDLDMrQALTEALI-----EFEGALVVVSHDRHLLR 491
Cdd:COG1124 153 LIL--EPELLLLDEPTSALDVSV-QAEILNLLkdlreERGLTYLFVSHDLAVVA 203
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-205 |
7.54e-15 |
|
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: 77.79 E-value: 7.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQAALEYVIDGDREyrqlEA 96
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG--------VPVSSLDQDEVRRRVSVCAQ----DA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 97 QLHDANERND---GQAIATIHGKLDAIDAWSIRSRAASLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLL 173
Cdd:TIGR02868 419 HLFDTTVRENlrlARPDATDEELWAALERVGLADWLRALPDGL---DTVLGEGGARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....
gi 446557484 174 DEPTNHLDLD-AVIWLEKWLKSYQG-TLILISHD 205
Cdd:TIGR02868 496 DEPTEHLDAEtADELLEDLLAALSGrTVVLITHH 529
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
317-462 |
7.69e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 73.35 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 317 KVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP--VSGEIgLAKGIKL---------GYFAQHQ- 384
Cdd:cd03213 14 KSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEV-LINGRPLdkrsfrkiiGYVPQDDi 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 385 -LEYLRADESpIQHLARLapqeleqklrdylggfgfqgdkvteetRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:cd03213 93 lHPTLTVRET-LMFAAKL---------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
308-473 |
7.89e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.61 E-value: 7.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 308 LPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQH---- 383
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLC-GEPVPSRARHarqr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 384 -----QLEYLRADESPIQHL---AR---LAPQELEQKLRDYLgGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLL 452
Cdd:PRK13537 82 vgvvpQFDNLDPDFTVRENLlvfGRyfgLSAAAARALVPPLL-EFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180
....*....|....*....|.
gi 446557484 453 LLDEPTNHLDLDMRQALTEAL 473
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERL 181
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
299-485 |
8.02e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.56 E-value: 8.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 299 RFSFRAPESLPNPLLKMEKVSAGYGDR--IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIK 376
Cdd:PRK11160 325 TFPTTSTAAADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLN-GQP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 377 LGYFAQHQleyLRADESPI------------QHLARLAPQELEQKLRDYLGGFGF----QGDK-----VTEETRRFSGGE 435
Cdd:PRK11160 404 IADYSEAA---LRQAISVVsqrvhlfsatlrDNLLLAAPNASDEALIEVLQQVGLekllEDDKglnawLGEGGRQLSGGE 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446557484 436 KARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEF--EGALVVVSH 485
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITH 532
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
313-487 |
9.37e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 77.51 E-value: 9.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLgyfAQHQLEYLR-- 389
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI-LIDGVDI---RDLTLESLRrq 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 390 -------------------------ADESPIQHLARLApqELEQKLRDYLGGFGFQgdkVTEETRRFSGGEKARLVLALI 444
Cdd:COG1132 416 igvvpqdtflfsgtirenirygrpdATDEEVEEAAKAA--QAHEFIEALPDGYDTV---VGERGVNLSGGQRQRIAIARA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446557484 445 VWQRPNLLLLDEPTNHLDldmrqALTEALIefEGALVVVSHDR 487
Cdd:COG1132 491 LLKDPPILILDEATSALD-----TETEALI--QEALERLMKGR 526
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-181 |
1.11e-14 |
|
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: 73.38 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQkVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQ--- 78
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG--------QDVLKQPQklr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 79 AALEY------VIDGDREYRQLEAqlhdanerndgqaIATIHGkldaIDAWSIRSRAASLLHGLGFsNEQLERPVSDFSG 152
Cdd:cd03264 72 RRIGYlpqefgVYPNFTVREFLDY-------------IAWLKG----IPSKEVKARVDEVLELVNL-GDRAKKKIGSLSG 133
|
170 180
....*....|....*....|....*....
gi 446557484 153 GWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:cd03264 134 GMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
17-220 |
1.34e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 73.54 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQAALeyvidgdreyrqleA 96
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDG--------QDISSLSEREL--------------A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 97 QLhdaneRND--G---Q--------------AIATIhgkLDAIDAWSIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMR 157
Cdd:COG1136 82 RL-----RRRhiGfvfQffnllpeltalenvALPLL---LAGVSRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 158 LNLAQALICRSDLLLLDEPTNHLD-------LDAviwLEKWLKSYQGTLILISHDRDFLDpIVDKIIHIE 220
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDsktgeevLEL---LRELNRELGTTIVMVTHDPELAA-RADRVIRLR 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
307-486 |
1.38e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 73.97 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 307 SLPNPLLKMEKVSAGY----GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL------AKGIK 376
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 377 LGY-FAQHQL----------EY-LRadespiqhLARLAPQELEQKLRDYLGGFGFQGDKvteetRRF----SGGEKARLV 440
Cdd:COG1116 82 RGVvFQEPALlpwltvldnvALgLE--------LRGVPKAERRERARELLELVGLAGFE-----DAYphqlSGGMRQRVA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446557484 441 LA--LIVwqRPNLLLLDEPTNHLD----LDMRQALTEALIEFEGALVVVSHD 486
Cdd:COG1116 149 IAraLAN--DPEVLLMDEPFGALDaltrERLQDELLRLWQETGKTVLFVTHD 198
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-183 |
1.74e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.65 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG-----------SWQLAWV 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraaSRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 70 NQETPALPQAALEYVID-GDREYRQLEAQLHDANERNDGQAIAtihgkldaidawsiRSRAASLlhglgfsneqLERPVS 148
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEmGRTPHRSRFDTWTETDRAAVERAME--------------RTGVAQF----------ADRPVT 138
|
170 180 190
....*....|....*....|....*....|....*
gi 446557484 149 DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD 183
Cdd:PRK09536 139 SLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
313-458 |
1.78e-14 |
|
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: 72.85 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEYLRADE 392
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSI---------RFDGRDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 spiqhLAR----LAPQE--------LEQKLRdyLGGFGFQGDKVTE------------ETRR------FSGGEK-----A 437
Cdd:cd03224 72 -----RARagigYVPEGrrifpeltVEENLL--LGAYARRRAKRKArlervyelfprlKERRkqlagtLSGGEQqmlaiA 144
|
170 180
....*....|....*....|.
gi 446557484 438 RlvlALIvwQRPNLLLLDEPT 458
Cdd:cd03224 145 R---ALM--SRPKLLLLDEPS 160
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-505 |
1.85e-14 |
|
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: 76.26 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 12 GVRVLLDNATATINPGQKVGLVGKNGCGKS----TLLALLKNEISADGGSYTFPGswqlawvnQETPALPQAALeyvidg 87
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDG--------QDLLGLSEREL------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 88 dREYR--------Q-----------LEAQLhdanerndGQAIAtIHGKLDAIDAwsiRSRAASLLHGLGFSNEqlERPVS 148
Cdd:COG4172 87 -RRIRgnriamifQepmtslnplhtIGKQI--------AEVLR-LHRGLSGAAA---RARALELLERVGIPDP--ERRLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 149 DF----SGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDaviwLEKWLKSYQGT-LILISHD----RDFLDPI 212
Cdd:COG4172 152 AYphqlSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqaqiLD----LLKDLQRELGMaLLLITHDlgvvRRFADRV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 213 VdkiihieqqsmfeytgnyssfeVQRATRLAQQQAmyesqqerVAHLqsyidrFRAkatkAKQAQSRikmlermELIA-- 290
Cdd:COG4172 228 A----------------------VMRQGEIVEQGP--------TAEL------FAA----PQHPYTR-------KLLAae 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 291 PAHVDNPfrfsfrAPESLPnPLLKMEKVSAGY-----------GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLA 359
Cdd:COG4172 261 PRGDPRP------VPPDAP-PLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 360 GeLAPVSGEIGLAkGIKLGYFAQHQLEYLRADespIQ--------------------------HLARLAPQELEQKLRDY 413
Cdd:COG4172 334 R-LIPSEGEIRFD-GQDLDGLSRRALRPLRRR---MQvvfqdpfgslsprmtvgqiiaeglrvHGPGLSAAERRARVAEA 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 414 LggfgfqgDKV--TEETR-R----FSGGEKARLVLA--LIVwqRPNLLLLDEPTNHLD-------LDMRQALTEaliEFE 477
Cdd:COG4172 409 L-------EEVglDPAARhRypheFSGGQRQRIAIAraLIL--EPKLLVLDEPTSALDvsvqaqiLDLLRDLQR---EHG 476
|
570 580
....*....|....*....|....*...
gi 446557484 478 GALVVVSHDRHLLRSTTDDLYLVHDRKV 505
Cdd:COG4172 477 LAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
313-490 |
1.92e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 72.17 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--ELAPVSGEIgLAKGIKLgyfaqhqleylra 390
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEI-LFKGEDI------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 DESPIQHLAR----LAPQELEQ----KLRDYLGGfgfqgdkVTEEtrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:cd03217 67 TDLPPEERARlgifLAFQYPPEipgvKNADFLRY-------VNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190
....*....|....*....|....*....|.
gi 446557484 463 LDMRQALTEA---LIEFEGALVVVSHDRHLL 490
Cdd:cd03217 137 IDALRLVAEVinkLREEGKSVLIITHYQRLL 167
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
303-473 |
2.34e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.87 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 303 RAPESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI--------GLAKG 374
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgvpvpARARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 375 IKLGYFAQHQLEYLRADESPIQHLA------RLAPQELEQKLRDYLGgFGFQGDKVTEETRRFSGGEKARLVLALIVWQR 448
Cdd:PRK13536 112 ARARIGVVPQFDNLDLEFTVRENLLvfgryfGMSTREIEAVIPSLLE-FARLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180
....*....|....*....|....*
gi 446557484 449 PNLLLLDEPTNHLDLDMRQALTEAL 473
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERL 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
10-207 |
2.75e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 73.20 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPGSwQLAWVNQEtPAL-PQA-A 80
Cdd:COG1116 20 GGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIaglekptSGEVLVDGKPVTGPGP-DRGVVFQE-PALlPWLtV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 LEYVIDGdreyrqLEAQLHDANERndgqaiatihgkldaidawsiRSRAASLLH--GL-GFSNE---QLerpvsdfSGGW 154
Cdd:COG1116 98 LDNVALG------LELRGVPKAER---------------------RERARELLElvGLaGFEDAyphQL-------SGGM 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 155 RMRLNLAQALICRSDLLLLDEPTNHLDldaVI-------WLEKWLKSYQGTLILISHDRD 207
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALD---ALtrerlqdELLRLWQETGKTVLFVTHDVD 200
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
328-514 |
2.96e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.97 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLakgikLGYF-AQHQLEYLRA-------------DES 393
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV-----LGYVpFKRRKEFARRigvvfgqrsqlwwDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 394 PI------QHLARLAPQELEQKLRDYLGGFGfQGDKVTEETRRFSGGE--KARLVLALIvwQRPNLLLLDEPTNHLDLDM 465
Cdd:COG4586 113 AIdsfrllKAIYRIPDAEYKKRLDELVELLD-LGELLDTPVRQLSLGQrmRCELAAALL--HRPKILFLDEPTIGLDVVS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446557484 466 RQALTEALIEF---EGALVVV-SHDRHLLRSTTDDLYLVHD-RKVepFDGDLED 514
Cdd:COG4586 190 KEAIREFLKEYnreRGTTILLtSHDMDDIEALCDRVIVIDHgRII--YDGSLEE 241
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
311-487 |
3.53e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 74.49 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGyfaqHQLEYLRA 390
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLS----HVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 DESPIQHLARLAPQELEQKLrdylgGFGFQGDKVT--EETRR--------------------FSGGEKARLVLALIVWQR 448
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNI-----AFGLKQDKLPkaEIASRvnemlglvhmqefakrkphqLSGGQRQRVALARSLAKR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446557484 449 PNLLLLDEPTNHLDLDMR---QALTEALIEFEGAL-VVVSHDR 487
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRdrmQLEVVDILERVGVTcVMVTHDQ 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-205 |
6.83e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 73.23 E-value: 6.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVL--LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQAALeyvidg 87
Cdd:COG4608 25 GRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG--------QDITGLSGREL------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 88 dREYRQlEAQL--HDA----NERND-GQAIA---TIHGKLDAIDawsIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMR 157
Cdd:COG4608 91 -RPLRR-RMQMvfQDPyaslNPRMTvGDIIAeplRIHGLASKAE---RRERVAELLELVGLRPEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446557484 158 LNLAQALICRSDLLLLDEPTNHLDLD--A-VIWLEKWLKSYQG-TLILISHD 205
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSiqAqVLNLLEDLQDELGlTYLFISHD 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
311-505 |
8.26e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.72 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA------------------ 372
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsaraasrrvas 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 373 --KGIKLGY-FAQHQLeyLRADESPiqHLARLAPQE------LEQKLrDYLGGFGFQGDKVTEetrrFSGGEKARLVLAL 443
Cdd:PRK09536 82 vpQDTSLSFeFDVRQV--VEMGRTP--HRSRFDTWTetdraaVERAM-ERTGVAQFADRPVTS----LSGGERQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 444 IVWQRPNLLLLDEPTNHLDLDmRQ----ALTEALIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKV 505
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDIN-HQvrtlELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
313-486 |
8.70e-14 |
|
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: 70.96 E-value: 8.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDR----IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL------AKGIKLGY-FA 381
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYvFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 382 QHQL-EYLRADES---PIQhLARLAPQELEQKLRDYLGGFGFQG--DKVTEEtrrFSGGEKARLVLA--LIVwqRPNLLL 453
Cdd:cd03293 81 QDALlPWLTVLDNvalGLE-LQGVPKAEARERAEELLELVGLSGfeNAYPHQ---LSGGMRQRVALAraLAV--DPDVLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 446557484 454 LDEPTNHLD----LDMRQALTEALIEFEGALVVVSHD 486
Cdd:cd03293 155 LDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHD 191
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
313-509 |
8.77e-14 |
|
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: 70.52 E-value: 8.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRI--ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAqhqLEYLRA 390
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDISTIP---LEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 DESPIqhlarlaPQE---LEQKLRDYLGGFGFQGD-------KVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
Cdd:cd03369 83 SLTII-------PQDptlFSGTIRSNLDPFDEYSDeeiygalRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 461 LDLDmrqalTEALI------EFEGALVVVShdRHLLRSTTD-DLYLVHDR-KVEPFD 509
Cdd:cd03369 156 IDYA-----TDALIqktireEFTNSTILTI--AHRLRTIIDyDKILVMDAgEVKEYD 205
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
327-514 |
1.04e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.00 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQ--------------HQLEYLRADE 392
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV-IFNGQPMSKLSSaakaelrnqklgfiYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 SPIQHLA------RLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
Cdd:PRK11629 103 TALENVAmplligKKKPAEINSRALEMLAAVGLE-HRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446557484 467 QALTEALIEFE----GALVVVSHDRHLLRSTtddlylvhDRKVEPFDGDLED 514
Cdd:PRK11629 182 DSIFQLLGELNrlqgTAFLVVTHDLQLAKRM--------SRQLEMRDGRLTA 225
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
337-491 |
1.05e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 337 PGSRIGLLGRNGAGKSTLIKLLAGeLAPVSGEIGLAkGIKLGYFAQHQLEYLRA-----DESPIQ---------HLARLA 402
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFA-GQPLEAWSAAELARHRAylsqqQTPPFAmpvfqyltlHQPDKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 403 PQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLA---LIVWQRPN----LLLLDEPTNHLDLDMRQALTEALIE 475
Cdd:PRK03695 99 RTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvLQVWPDINpagqLLLLDEPMNSLDVAQQAALDRLLSE 178
|
170 180
....*....|....*....|
gi 446557484 476 FE---GALVVVSHD-RHLLR 491
Cdd:PRK03695 179 LCqqgIAVVMSSHDlNHTLR 198
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
313-513 |
1.26e-13 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 70.75 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELA--PVSGEIGLA--------------KGIK 376
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyeVTSGTILFKgqdllelepderarAGLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 377 LGYfaQHQLE--------YLRA---------DESPIQHLARLapQELEQKLRDYLGGFGFQGDKVTEEtrrFSGGEKAR- 438
Cdd:TIGR01978 81 LAF--QYPEEipgvsnleFLRSalnarrsarGEEPLDLLDFE--KLLKEKLALLDMDEEFLNRSVNEG---FSGGEKKRn 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 439 --LVLALIvwqRPNLLLLDEPTNHLDLDMRQALTEALIEF---EGALVVVSHDRHLLRSTTDD-LYLVHDRKVePFDGDL 512
Cdd:TIGR01978 154 eiLQMALL---EPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLNYIKPDyVHVLLDGRI-VKSGDV 229
|
.
gi 446557484 513 E 513
Cdd:TIGR01978 230 E 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
309-491 |
1.65e-13 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 70.54 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 309 PNPLLKMEKVSAGYGDR----IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQ 384
Cdd:COG4181 5 SAPIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLA-GQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 385 LEYLRAD--------ESPIQHLARLA----PQEL------EQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVW 446
Cdd:COG4181 84 RARLRARhvgfvfqsFQLLPTLTALEnvmlPLELagrrdaRARARALLERVGL-GHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446557484 447 QRPNLLLLDEPTNHLDLDMRQALTEALieFE-----GA-LVVVSHDRHLLR 491
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLL--FElnrerGTtLVLVTHDPALAA 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
312-490 |
1.66e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 70.29 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEYLRA 390
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKI---------WFSGHDITRLKN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 DESPI-----------QHL----------------ARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLAL 443
Cdd:PRK10908 72 REVPFlrrqigmifqdHHLlmdrtvydnvaipliiAGASGDDIRRRVSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446557484 444 IVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVVV---SHDRHLL 490
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVlmaTHDIGLI 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-205 |
1.68e-13 |
|
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: 73.18 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVL--LDNATATINPGQKVGLVGKNGCGKSTL-LALLKnEISADGgsytfpgswQLAWVNQETPALPQAALeyvid 86
Cdd:COG4172 293 RRTVGHVkaVDGVSLTLRRGETLGLVGESGSGKSTLgLALLR-LIPSEG---------EIRFDGQDLDGLSRRAL----- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 87 gdREYRQlEAQ---------LhdaNER-NDGQAIA---TIHGklDAIDAWSIRSRAASLLHGLGFSNEQLERPVSDFSGG 153
Cdd:COG4172 358 --RPLRR-RMQvvfqdpfgsL---SPRmTVGQIIAeglRVHG--PGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGG 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWL-KSYQGTLILISHD 205
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSvqaQILDLLRDLqREHGLAYLFISHD 485
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-182 |
1.85e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.57 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG-------SWQLAwvnQET 73
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwsPAELA---RRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 74 PALPQAA-------LEYVIdgdreyrQLEAQLHDANERNDGQAIATIhgkLDAIDAWSIRSRaasLLHGLgfsneqlerp 146
Cdd:PRK13548 79 AVLPQHSslsfpftVEEVV-------AMGRAPHGLSRAEDDALVAAA---LAQVDLAHLAGR---DYPQL---------- 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446557484 147 vsdfSGGWRMRLNLAQALI---CRSD---LLLLDEPTNHLDL 182
Cdd:PRK13548 136 ----SGGEQQRVQLARVLAqlwEPDGpprWLLLDEPTSALDL 173
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
328-488 |
2.24e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 70.05 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGI----KLGYFAQ-----HQLEYLRADESPI--- 395
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrRKKFLRRigvvfGQKTQLWWDLPVIdsf 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 396 ---QHLARLAPQELEQKLrDYLGGFGFQGDKVTEETRRFSGGE--KARLVLALIvwQRPNLLLLDEPTNHLDL----DMR 466
Cdd:cd03267 117 yllAAIYDLPPARFKKRL-DELSELLDLEELLDTPVRQLSLGQrmRAEIAAALL--HEPEILFLDEPTIGLDVvaqeNIR 193
|
170 180
....*....|....*....|..
gi 446557484 467 QALTEALIEFEGALVVVSHDRH 488
Cdd:cd03267 194 NFLKEYNRERGTTVLLTSHYMK 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-207 |
2.31e-13 |
|
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: 69.47 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALP--QAALEYV 84
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG--------RDVTGVPpeRRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 85 IDGDREYRQLEAqlhdanERNdgqaIAtIHGKLDAIDAWSIRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQAL 164
Cdd:cd03259 78 FQDYALFPHLTV------AEN----IA-FGLKLRGVPKAEIRARVRELLELVGLEG-LLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446557484 165 ICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRD 207
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQE 192
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
12-217 |
2.53e-13 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 70.45 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG------------------SWQlawvnqeT 73
Cdd:COG0411 16 GLVAV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrditglpphriarlgiarTFQ-------N 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 74 PALPQA--ALEYVIDGdreyrqleAQLHdaneRNDGQAIATIHGKLDAIDAWSIRSRAASLLHGLGFSnEQLERPVSDFS 151
Cdd:COG0411 88 PRLFPEltVLENVLVA--------AHAR----LGRGLLAALLRLPRARREEREARERAEELLERVGLA-DRADEPAGNLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 152 GGWRMRLNLAQALICRSDLLLLDEPT---NHLDLDAVIWLEKWLKSYQG-TLILISHDRDFLDPIVDKII 217
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIV 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
316-487 |
2.64e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 71.72 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 316 EKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAK---GIKL-------GYFAQHql 385
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlFTNLpprerrvGFVFQH-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 386 eYL--RadespiqHL------------ARLAPQELEQKLRDYLGGFGFQGdkvtEETRR---FSGGEKARLVLA--LIVw 446
Cdd:COG1118 84 -YAlfP-------HMtvaeniafglrvRPPSKAEIRARVEELLELVQLEG----LADRYpsqLSGGQRQRVALAraLAV- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446557484 447 qRPNLLLLDEPTNHLD----LDMRQALTEALIEFEGALVVVSHDR 487
Cdd:COG1118 151 -EPEVLLLDEPFGALDakvrKELRRWLRRLHDELGGTTVFVTHDQ 194
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
328-505 |
4.03e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.11 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLE--------YLRADE---SPI- 395
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEV-LIKGEPIKYDKKSLLEvrktvgivFQNPDDqlfAPTv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 396 -QHLA------RLAPQELEQKLRDYLGGFGFQGdkvTEET--RRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
Cdd:PRK13639 97 eEDVAfgplnlGLSKEEVEKRVKEALKAVGMEG---FENKppHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446557484 467 QALTEALIEF--EGALVVVS-HDRHLLRSTTDDLYLVHDRKV 505
Cdd:PRK13639 174 SQIMKLLYDLnkEGITIIIStHDVDLVPVYADKVYVMSDGKI 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
310-556 |
4.03e-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: 72.24 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 310 NPLLKMEKVSAGY--GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP---VSGEIGLA-----------K 373
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDgrdllelsealR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 374 GIKLGYFAQ---HQL----------EYLRADESPIQHLARLAPQELEQ-KLRDYLGGFGFQgdkvteetrrFSGGEKARL 439
Cdd:COG1123 82 GRRIGMVFQdpmTQLnpvtvgdqiaEALENLGLSRAEARARVLELLEAvGLERRLDRYPHQ----------LSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 440 VLALIVWQRPNLLLLDEPTNHLD----LDMRQALTEALIEFEGALVVVSHDRHLLRSTTDDLYLVHD-RKVEpfDGDLEd 514
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDgRIVE--DGPPE- 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446557484 515 yqqwlsDVQKQENQADEAPKENANSAQARKDQKRREAELRAQ 556
Cdd:COG1123 229 ------EILAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVR 264
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-204 |
4.50e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.22 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF-----PGSWQLAwvNQETPAL 76
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgepvPSRARHA--RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 77 PQAAleyVIDGDREYRQleaqlhdaNERndgqaiatIHGKLDAIDAWSIRSRAASLLHGLGFSNEQlERPVSDFSGGWRM 156
Cdd:PRK13537 86 PQFD---NLDPDFTVRE--------NLL--------VFGRYFGLSAAAARALVPPLLEFAKLENKA-DAKVGELSGGMKR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446557484 157 RLNLAQALICRSDLLLLDEPTNHLDLDA--VIWLE-KWLKSYQGTLILISH 204
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQArhLMWERlRSLLARGKTILLTTH 196
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
324-511 |
5.37e-13 |
|
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: 67.18 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAPV-SGEIGLAKGIKLGYFAQHqlEYLradespiqhlarla 402
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWgSGRIGMPEGEDLLFLPQR--PYL-------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 403 PQELeqkLRDYLggfgfqgdkVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVV 482
Cdd:cd03223 76 PLGT---LREQL---------IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVIS 143
|
170 180
....*....|....*....|....*....
gi 446557484 483 VSHdRHLLRSttddlylVHDRKVEpFDGD 511
Cdd:cd03223 144 VGH-RPSLWK-------FHDRVLD-LDGE 163
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-221 |
6.12e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.32 E-value: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtFPGSWQLAWVNQETPALPQAA- 80
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTRLMFQDAr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 ---LEYVIDgdreyrqleaqlhdanerNDGqaiatihgkLDAIDAWsiRSRAASLLHGLGFSNEQLERPVSdFSGGWRMR 157
Cdd:PRK11247 92 llpWKKVID------------------NVG---------LGLKGQW--RDAALQALAAVGLADRANEWPAA-LSGGQKQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 158 LNLAQALICRSDLLLLDEPTNHLD---------LDAVIWLEkwlksYQGTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDaltriemqdLIESLWQQ-----HGFTVLLVTHDVSEAVAMADRVLLIEE 209
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
314-486 |
6.20e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 68.96 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 314 KMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgyfaqhQLEYLRADES 393
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEV--------------LVDGLDVATT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 394 PIQHLAR-LA--PQE--LEQKL--RDyLGGFG-F---QGdKVTEETR-----------------RF----SGGEKARLVL 441
Cdd:COG4604 69 PSRELAKrLAilRQEnhINSRLtvRE-LVAFGrFpysKG-RLTAEDReiideaiayldledladRYldelSGGQRQRAFI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446557484 442 ALIVWQRPNLLLLDEPTNHLDL----DMRQALTEALIEFEGALVVVSHD 486
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
312-506 |
7.11e-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: 68.38 E-value: 7.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGYGDR----IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEY 387
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVD-GTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 388 LRADESPI-QH------------------LARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQR 448
Cdd:cd03258 80 ARRRIGMIfQHfnllssrtvfenvalpleIAGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557484 449 PNLLLLDEPTNHLDLDMRQALTEALI----EFEGALVVVSHDRHLLRSTTDDLYLVHDRKVE 506
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRdinrELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-205 |
8.30e-13 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 69.70 E-value: 8.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTL-LALLK--NEISADGGSYTFPGswqlawvnQETPALPQAALe 82
Cdd:COG0444 10 YFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaRAILGllPPPGITSGEILFDG--------EDLLKLSEKEL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 83 yvidgdREYRQLEAQL--HDA----NERND-GQAIA---TIHGKLDAIDAwsiRSRAASLLH--GLGFSNEQLER-PvSD 149
Cdd:COG0444 81 ------RKIRGREIQMifQDPmtslNPVMTvGDQIAeplRIHGGLSKAEA---RERAIELLErvGLPDPERRLDRyP-HE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAviwLEKWLKSYQGTLILISHD 205
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqaqiLNL---LKDLQRELGLAILFITHD 210
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
10-217 |
8.31e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.06 E-value: 8.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSytfpGSWQLaWVNQETPALPqaaleyVIDgdr 89
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA----GCVDV-PDNQFGREAS------LID--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 90 eyrqleaqlhdanerndgqAIATIHGKLDAIDawsirsraasLLHGLGFSNEQL-ERPVSDFSGGWRMRLNLAQALICRS 168
Cdd:COG2401 105 -------------------AIGRKGDFKDAVE----------LLNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446557484 169 DLLLLDEPTNHLDLD-----AVIWLEKWlKSYQGTLILISHDRDFLDPIV-DKII 217
Cdd:COG2401 156 KLLVIDEFCSHLDRQtakrvARNLQKLA-RRAGITLVVATHHYDVIDDLQpDLLI 209
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
318-491 |
1.07e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.56 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEYLRAD------ 391
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-GEPLAKLNRAQRKAFRRDiqmvfq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 392 ----------------ESPIQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
Cdd:PRK10419 97 dsisavnprktvreiiREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446557484 456 EPTNHLDL----DMRQALTEALIEFEGALVVVSHDRHLLR 491
Cdd:PRK10419 177 EAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVE 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
313-486 |
1.26e-12 |
|
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: 67.17 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLgYFAQHQLEYLRAD- 391
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI-IIDGLKL-TDDKKNINELRQKv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 392 --------------------ESPIQHLaRLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNL 451
Cdd:cd03262 79 gmvfqqfnlfphltvlenitLAPIKVK-GMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446557484 452 LLLDEPTNHLD-------LDMRQALTEaliefEG-ALVVVSHD 486
Cdd:cd03262 157 MLFDEPTSALDpelvgevLDVMKDLAE-----EGmTMVVVTHE 194
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-221 |
1.33e-12 |
|
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: 66.44 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSwQLAWVNQETPALpQAAL 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE-DLTDLEDELPPL-RRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 EYVIDgdreyrqlEAQLhdanerndgqaiatihgkldaidaWSIRSRAASLLHGLgfsneqlerpvsdfSGGWRMRLNLA 161
Cdd:cd03229 79 GMVFQ--------DFAL------------------------FPHLTVLENIALGL--------------SGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557484 162 QALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqlgiTVVLVTHDLDEAARLADRVVVLRD 176
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-221 |
1.60e-12 |
|
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: 67.70 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQAA 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDG--------QDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 LeyvidgdREYRQL------EAQLHDA-----NerndgqaIA---TIHGKLDAidaWSIRSRAASLLH--GLGFSNEQLe 144
Cdd:COG1127 77 L-------YELRRRigmlfqGGALFDSltvfeN-------VAfplREHTDLSE---AEIRELVLEKLElvGLPGAADKM- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 145 rPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD------LDAVIwLEkwL-KSYQGTLILISHDRDFLDPIVDKII 217
Cdd:COG1127 139 -P-SELSGGMRKRVALARALALDPEILLYDEPTAGLDpitsavIDELI-RE--LrDELGLTSVVVTHDLDSAFAIADRVA 213
|
....
gi 446557484 218 HIEQ 221
Cdd:COG1127 214 VLAD 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
313-486 |
1.69e-12 |
|
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: 67.21 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG-----ELAPVSGEIGL-AKGIklgYFAQHQLE 386
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLdGKDI---YDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 387 YLRAD-----ESP------IQHLARLAPQ---ELEQKLRDYLGGFGFQGDKVTEE------TRRFSGGEKARLVLA--LI 444
Cdd:cd03260 78 ELRRRvgmvfQKPnpfpgsIYDNVAYGLRlhgIKLKEELDERVEEALRKAALWDEvkdrlhALGLSGGQQQRLCLAraLA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446557484 445 VwqRPNLLLLDEPTNHLDLDMRQALTEALIEF--EGALVVVSHD 486
Cdd:cd03260 158 N--EPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-204 |
1.89e-12 |
|
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: 65.53 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSwqlawvnqetpalpqaalEYVIDGDREY 91
Cdd:cd03216 12 GVKAL-DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK------------------EVSFASPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 92 RQLeaqlhdanerndgqAIATIHgkldaidawsirsraasllhglgfsneQLerpvsdfSGGWRMRLNLAQALICRSDLL 171
Cdd:cd03216 73 RRA--------------GIAMVY---------------------------QL-------SVGERQMVEIARALARNARLL 104
|
170 180 190
....*....|....*....|....*....|....*.
gi 446557484 172 LLDEPTNHLDLDAVIWLEKWLKSY--QG-TLILISH 204
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLraQGvAVIFISH 140
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
310-487 |
2.15e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.05 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFA----QHQL 385
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL-LFEGEDISTLKpeiyRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 386 EY------LRADES------PIQhLARLAPQelEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLL 453
Cdd:PRK10247 84 SYcaqtptLFGDTVydnlifPWQ-IRNQQPD--PAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 446557484 454 LDEPTNHLDLDMRQALTEALIEF----EGALVVVSHDR 487
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYvreqNIAVLWVTHDK 198
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-220 |
2.23e-12 |
|
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: 66.55 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 26 PGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGS-WQLAWVNQETPalPQA-ALEYVIDgdreyrqlEAQL--HDA 101
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvLFDSRKKINLP--PQQrKIGLVFQ--------QYALfpHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 102 NERNdgqaiatIHGKLDAIDAWSIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:cd03297 92 VREN-------LAFGLKRKRNREDRISVDELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446557484 182 ----LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIE 220
Cdd:cd03297 164 ralrLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVME 206
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-221 |
2.37e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 66.97 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYT----FPGSWQLAWVNQETpalpqaaleyVIDGDREyr 92
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglVPWKRRKKFLRRIG----------VVFGQKT-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 93 QLEAQLHDAnernDGQA-IATIHGkldaIDAWSIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
Cdd:cd03267 105 QLWWDLPVI----DSFYlLAAIYD----LPPARFKKRLDELSELLDLE-ELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446557484 172 LLDEPTNHLDLDAVIWLEKWLKSY----QGTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDK 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
313-527 |
2.45e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.45 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--ELAPVSGEI--GLAKGIKLGY--------- 379
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyHVALCEKCGYverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 380 --------FAQHQLEYLRADESPIQHLARLAPQELEQKLRDY------------LGGFGFQGDK---------------- 423
Cdd:TIGR03269 81 pcpvcggtLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFALYgddtvldnvleaLEEIGYEGKEavgravdliemvqlsh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 424 -VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD----MRQALTEALIEFEGALVVVSHDRHLLRSTTDDLY 498
Cdd:TIGR03269 161 rITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtaklVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270
....*....|....*....|....*....|...
gi 446557484 499 LVHDRKV----EPfDGDLEDYQQWLSDVQKQEN 527
Cdd:TIGR03269 241 WLENGEIkeegTP-DEVVAVFMEGVSEVEKECE 272
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-205 |
2.55e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.17 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISAdGGSYTFPG----SWQL-------AWVNQETPALPQ-AALEYV 84
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGrplsDWSAaelarhrAYLSQQQSPPFAmPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 85 idgdreyrqleaQLHDANERNDGQAIATIhgkldaidawsirsraASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQAL 164
Cdd:COG4138 91 ------------ALHQPAGASSEAVEQLL----------------AQLAEALGLED-KLSRPLTQLSGGEWQRVRLAAVL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446557484 165 --ICRSD-----LLLLDEPTNHLDLDAVIWLEKWLKSY---QGTLILISHD 205
Cdd:COG4138 142 lqVWPTInpegqLLLLDEPMNSLDVAQQAALDRLLRELcqqGITVVMSSHD 192
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-220 |
2.76e-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: 65.95 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSwqLAWVNQEtPALPQAALEYVIDGDREYRQle 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQE-PWIQNGTIRENILFGKPFDE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 96 aqlhdanERNDgqaiatihgklDAIDAWSIRSRAASLLHG----LGfsneqlERPVSdFSGGWRMRLNLAQALICRSDLL 171
Cdd:cd03250 95 -------ERYE-----------KVIKACALEPDLEILPDGdlteIG------EKGIN-LSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 172 LLDEPtnhldLDAV-------IW----LEKWLKSyqGTLILISHDRDFLdPIVDKIIHIE 220
Cdd:cd03250 150 LLDDP-----LSAVdahvgrhIFenciLGLLLNN--KTRILVTHQLQLL-PHADQIVVLD 201
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
308-486 |
2.84e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 67.57 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 308 LPNPLLKMEKVSAGYGDRI-ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLE 386
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 387 yLRAD-----ESPIQHL---------------ARLAPQELEQKLRDYLGGFGFQGDKvTEETRRFSGGEKARLVLALIVW 446
Cdd:PRK13636 80 -LRESvgmvfQDPDNQLfsasvyqdvsfgavnLKLPEDEVRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446557484 447 QRPNLLLLDEPTNHLD----LDMRQALTEALIEFEGALVVVSHD 486
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-205 |
3.04e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.40 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 5 SSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGsytfpgswQLAWVNQETPALPQAaleyv 84
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQG--------NVSWRGEPLAKLNRA----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 85 idGDREYRQlEAQL--HDA----NERND-GQAIATIHGKLDAIDAWSIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMR 157
Cdd:PRK10419 83 --QRKAFRR-DIQMvfQDSisavNPRKTvREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446557484 158 LNLAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKSYQGT-LILISHD 205
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLvlqAGVIRLLKKLQQQFGTaCLFITHD 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-181 |
3.49e-12 |
|
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: 65.41 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpgswqlawvNQETPALPQAALEyvidgdreyrql 94
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL---------DGVPVSDLEKALS------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 95 eaqlhdanerndgQAIATIHGKLDAIDawsirsraASLLHGLGfsneqlERpvsdFSGGWRMRLNLAQALICRSDLLLLD 174
Cdd:cd03247 75 -------------SLISVLNQRPYLFD--------TTLRNNLG------RR----FSGGERQRLALARILLQDAPIVLLD 123
|
....*..
gi 446557484 175 EPTNHLD 181
Cdd:cd03247 124 EPTVGLD 130
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-485 |
4.22e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.89 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 5 SSLQIRRGVRVLLDNATA-----TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYT--FPGSWQLAWVNQetpalp 77
Cdd:PRK10938 2 SSLQISQGTFRLSDTKTLqlpslTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQsqFSHITRLSFEQL------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 78 QAALEyvidgdREYRQLEAQLHDANERNDGQAIATIhgKLDAIDAwsiRSRAASLLHGLGFSNeQLERPVSDFSGGWRMR 157
Cdd:PRK10938 76 QKLVS------DEWQRNNTDMLSPGEDDTGRTTAEI--IQDEVKD---PARCEQLAQQFGITA-LLDRRFKYLSTGETRK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIHIEQQSMfeytgnyssf 234
Cdd:PRK10938 144 TLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLVLNRFDEIPDFVQFAGVLADCTL---------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 235 evqraTRLAQQQAMYesQQERVAHLqsyidrfrakatkakqAQSrikmlERMELIAPAHVDNPfrfsfRAPESLP--NPL 312
Cdd:PRK10938 214 -----AETGEREEIL--QQALVAQL----------------AHS-----EQLEGVQLPEPDEP-----SARHALPanEPR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGElAPV--------------SGEIGLAKGIKLG 378
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQgysndltlfgrrrgSGETIWDIKKHIG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 379 YFA-QHQLEYlRADESPIQ----------HLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKaRLVL---ALI 444
Cdd:PRK10938 340 YVSsSLHLDY-RVSTSVRNvilsgffdsiGIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQ-RLALivrALV 417
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446557484 445 vwQRPNLLLLDEPTNHLDLDMRQAL---TEALI-EFEGALVVVSH 485
Cdd:PRK10938 418 --KHPTLLILDEPLQGLDPLNRQLVrrfVDVLIsEGETQLLFVSH 460
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
307-485 |
4.25e-12 |
|
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: 69.38 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 307 SLPNPLLKMEKVSAGYG-DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQL 385
Cdd:TIGR01193 468 NNLNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILL-NGFSLKDIDRHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 386 E----YLRADE-----SPIQHLARLAPQELEQ----------KLRDYLGGF--GFQGDkVTEETRRFSGGEKARLVLALI 444
Cdd:TIGR01193 547 RqfinYLPQEPyifsgSILENLLLGAKENVSQdeiwaaceiaEIKDDIENMplGYQTE-LSEEGSSISGGQKQRIALARA 625
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446557484 445 VWQRPNLLLLDEPTNHLDLDMRQALTEALIEF-EGALVVVSH 485
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLqDKTIIFVAH 667
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-221 |
4.64e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.84 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIR-RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGsytfpgswQLAWVNQETPALPQA 79
Cdd:COG2884 1 MIRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSG--------QVLVNGQDLSRLKRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 80 ALEY------VIDGDreYRQLeaqlhdaNERNDGQAIA---TIHGKLDAidawSIRSRAASLLH--GLGfsnEQLERPVS 148
Cdd:COG2884 73 EIPYlrrrigVVFQD--FRLL-------PDRTVYENVAlplRVTGKSRK----EIRRRVREVLDlvGLS---DKAKALPH 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 149 DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY--QGTLILI-SHDRDFLDPIVDKIIHIEQ 221
Cdd:COG2884 137 ELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRMPKRVLELED 212
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
325-505 |
4.65e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.77 E-value: 4.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGEL--------APVSGEIGLaKGIKLGYFAQHQLEYLRA------ 390
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTL-NGEPLAAIDAPRLARLRAvlpqaa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 --------DEspIQHLARL----APQELEQKLRDYL-------GGFGFQGDKVTEetrrFSGGEKARLVLALIVWQ---- 447
Cdd:PRK13547 93 qpafafsaRE--IVLLGRYpharRAGALTHRDGEIAwqalalaGATALVGRDVTT----LSGGELARVQFARVLAQlwpp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 448 -----RPNLLLLDEPTNHLDLDMRQALTEALIEFE-----GALVVVsHDRHLLRSTTDDLYLVHDRKV 505
Cdd:PRK13547 167 hdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwnlGVLAIV-HDPNLAARHADRIAMLADGAI 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
322-506 |
4.69e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.53 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA---------KGIKLGYFAQHQLEYLRAD- 391
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvrdKDGQLKVADKNQLRLLRTRl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 392 --------------------ESPIQHLArLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNL 451
Cdd:PRK10619 95 tmvfqhfnlwshmtvlenvmEAPIQVLG-LSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 452 LLLDEPTNHLD-------LDMRQALTEaliefEG-ALVVVSHDRHLLRSTTDDLYLVHDRKVE 506
Cdd:PRK10619 174 LLFDEPTSALDpelvgevLRIMQQLAE-----EGkTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
12-217 |
5.40e-12 |
|
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: 65.92 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG------------------SWQlawVNQET 73
Cdd:cd03219 12 GLVAL-DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglppheiarlgigrTFQ---IPRLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 74 PALPqaALEYVIdgdreyrqLEAQLHDANerndgqaiaTIHGKLDAIDAWSIRSRAASLLHGLGFSnEQLERPVSDFSGG 153
Cdd:cd03219 88 PELT--VLENVM--------VAAQARTGS---------GLLLARARREEREARERAEELLERVGLA-DLADRPAGELSYG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 154 WRMRLNLAQALICRSDLLLLDEPT---NHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-217 |
5.83e-12 |
|
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: 66.05 E-value: 5.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQAALeyvidgdREY 91
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDG--------TDINKLKGKAL-------RQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 92 RQ----LEAQLHDANERNDGQAIatIHGKLDAIDAWSI---------RSRAASLLHGLGFSnEQLERPVSDFSGGWRMRL 158
Cdd:cd03256 77 RRqigmIFQQFNLIERLSVLENV--LSGRLGRRSTWRSlfglfpkeeKQRALAALERVGLL-DKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 159 NLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQGTLILIS-HDRDFLDPIVDKII 217
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASsrqVMDLLKRINREEGITVIVSlHQVDLAREYADRIV 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
312-505 |
5.96e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.33 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEYLRAD 391
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LFDGENIPAMSRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 392 ES--------------------PIQHLARLAPQELEQKLRDYLGGFGFQGdKVTEETRRFSGGEKARLVLALIVWQRPNL 451
Cdd:PRK11831 86 MSmlfqsgalftdmnvfdnvayPLREHTQLPAPLLHSTVMMKLEAVGLRG-AAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 452 LLLDEPTNHLDLDMRQALTEALIEFEGAL----VVVSHDRHLLRSTTDDLYLVHDRKV 505
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALgvtcVVVSHDVPEVLSIADHAYIVADKKI 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
313-514 |
7.00e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 65.55 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIIldSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI----------------------- 369
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqdltalppaerpvsmlfqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 370 ---------------GLAKGIKLGYFAQHQLEylradespiQHLARLAPQELEQKLRDYLggfgfqgdkvteetrrfSGG 434
Cdd:COG3840 80 nnlfphltvaqniglGLRPGLKLTAEQRAQVE---------QALERVGLAGLLDRLPGQL-----------------SGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 435 EKARLVLA-LIVWQRPnLLLLDEPTNHLDLDMRQ---ALTEALIEFEGA-LVVVSHD----RHLlrstTDDLYLVHDRKV 505
Cdd:COG3840 134 QRQRVALArCLVRKRP-ILLLDEPFSALDPALRQemlDLVDELCRERGLtVLMVTHDpedaARI----ADRVLLVADGRI 208
|
....*....
gi 446557484 506 EPfDGDLED 514
Cdd:COG3840 209 AA-DGPTAA 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-226 |
7.69e-12 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 65.98 E-value: 7.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 5 SSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISadggsytfPGSWQLAWVNQETPALPQAALEYV 84
Cdd:TIGR02769 15 GGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEK--------PAQGTVSFRGQDLYQLDRKQRRAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 85 idgdreYRQLEAQLHDA----NERND-GQAIATIHGKLDAIDAWSIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLN 159
Cdd:TIGR02769 87 ------RRDVQLVFQDSpsavNPRMTvRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 160 LAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKSYQGT-LILISHDRDFLDPIVDKIIHIEQQSMFE 226
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMvlqAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
316-475 |
8.49e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.90 E-value: 8.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 316 EKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGiklgyfAQHqleylraDESPI 395
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG------DID-------DPDVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 396 QHLARLAPQE-------LEQKL---RDYLGGFGFQGDKVTE-------ETRRF---SGGEKARLVLA-LIVWQRPnLLLL 454
Cdd:PRK13539 73 EACHYLGHRNamkpaltVAENLefwAAFLGGEELDIAAALEavglaplAHLPFgylSAGQKRRVALArLLVSNRP-IWIL 151
|
170 180
....*....|....*....|.
gi 446557484 455 DEPTNHLDLDMrQALTEALIE 475
Cdd:PRK13539 152 DEPTAALDAAA-VALFAELIR 171
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
330-516 |
8.64e-12 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 67.06 E-value: 8.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 330 SIKLNL-VPGS-RIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL--------AKGI-------KLGYFAQH--------- 383
Cdd:TIGR02142 13 SLDADFtLPGQgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfdsRKGIflppekrRIGYVFQEarlfphlsv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 384 --QLEYLRADESPIQHLARlapqelEQKLRDYLGgfgfQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
Cdd:TIGR02142 93 rgNLRYGMKRARPSERRIS------FERVIELLG----IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 462 DLDMRQALTEAL----IEFEGALVVVSHDRHLLRSTTDDLYLVHDRKVEPFdGDLEDYQ 516
Cdd:TIGR02142 163 DDPRKYEILPYLerlhAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA-GPIAEVW 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
312-486 |
8.94e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 65.40 E-value: 8.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGyFAQHQLEYLRAD 391
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI-TVDGEDLT-DSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 392 ---------------------ESPIQHLaRLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEK-----ARlVLALiv 445
Cdd:COG1126 79 vgmvfqqfnlfphltvlenvtLAPIKVK-KMSKAEAEERAMELLERVGL-ADKADAYPAQLSGGQQqrvaiAR-ALAM-- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446557484 446 wqRPNLLLLDEPTNHLD-------LD-MRQaLTEaliefEG-ALVVVSHD 486
Cdd:COG1126 154 --EPKVMLFDEPTSALDpelvgevLDvMRD-LAK-----EGmTMVVVTHE 195
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
313-486 |
9.05e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.78 E-value: 9.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGI--KLGYFA 381
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdgehiqhyaSKEVarRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 382 QHQL--------EYLRADESPIQHLARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLL 453
Cdd:PRK10253 88 QNATtpgditvqELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 446557484 454 LDEPTNHLDLDMRQALTEALIEFEG----ALVVVSHD 486
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNRekgyTLAAVLHD 203
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
328-541 |
9.60e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.61 E-value: 9.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---GLAKGIKLGYFAQHQLEYLRADESPI-------QH 397
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdrnGEVSVIAISAGLSGQLTGIENIEFKMlcmgfkrKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 398 LARLAPQELEqklrdylggFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFE 477
Cdd:PRK13546 120 IKAMTPKIIE---------FSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 478 GA---LVVVSHDRHLLRSTTDDLYLVHDRKVEPFdGDLED----YQQWLSDVQKQENQADEAPKENANSAQ 541
Cdd:PRK13546 191 EQnktIFFVSHNLGQVRQFCTKIAWIEGGKLKDY-GELDDvlpkYEAFLNDFKKKSKAEQKEFRNKLDESR 260
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-221 |
1.12e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.10 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSytfpgswqlAWVNQETPALpqaaL 81
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR---------VEVNGRVSAL----L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 EY--VIDGD---REYRQLEAQLHdanerndGQAIATIHGKLDAIDAWSirsraasllhGLGfsnEQLERPVSDFSGGWRM 156
Cdd:COG1134 94 ELgaGFHPEltgRENIYLNGRLL-------GLSRKEIDEKFDEIVEFA----------ELG---DFIDQPVKTYSSGMRA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 157 RLNLAQALICRSDLLLLDEptnhldldaviWL-----------EKWLKSYQ---GTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:COG1134 154 RLAFAVATAVDPDILLVDE-----------VLavgdaafqkkcLARIRELResgRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
316-485 |
1.16e-11 |
|
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: 64.94 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 316 EKVSAGYGD-RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI------------KLGYFAQ 382
Cdd:cd03253 4 ENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSI-LIDGQdirevtldslrrAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 383 ----------HQLEYLRADESPIQ--HLARLApqeleqKLRDYLGGFGFQGD-KVTEETRRFSGGEKARLVLALIVWQRP 449
Cdd:cd03253 83 dtvlfndtigYNIRYGRPDATDEEviEAAKAA------QIHDKIMRFPDGYDtIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 446557484 450 NLLLLDEPTNHLDLDMRQALTEALIE-FEG-ALVVVSH 485
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDvSKGrTTIVIAH 194
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
312-525 |
1.17e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.78 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGYGDRI-ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQ----LE 386
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV-LVSGIDTGDFSKLQgirkLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 387 YLRADESPIQHLAR--------------LAPQELEQKLRDYLGGFGFQGDKvTEETRRFSGGEKARLVLALIVWQRPNLL 452
Cdd:PRK13644 80 GIVFQNPETQFVGRtveedlafgpenlcLPPIEIRKRVDRALAEIGLEKYR-HRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 453 LLDEPTNHLDLDMRQALTE---ALIEFEGALVVVSHDRHLLRSTtdDLYLVHDRKVEPFDGDLEDYqqwLSDVQKQ 525
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLErikKLHEKGKTIVYITHNLEELHDA--DRIIVMDRGKIVLEGEPENV---LSDVSLQ 229
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
313-485 |
1.24e-11 |
|
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: 64.30 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGiklgyfAQHQLEYLRADE 392
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT------PLAEQRDEPHEN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 SP-IQHL----ARLAPQELEQKLRDYLGGFGFQGDKVTEET----------RRFSGGEKARLVLA-LIVWQRPnLLLLDE 456
Cdd:TIGR01189 75 ILyLGHLpglkPELSALENLHFWAAIHGGAQRTIEDALAAVgltgfedlpaAQLSAGQQRRLALArLWLSRRP-LWILDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 446557484 457 PTNHLD---LDMRQALTEALIEFEGALVVVSH 485
Cdd:TIGR01189 154 PTTALDkagVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-256 |
1.45e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.16 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQAALeyvidgdreyRQ--- 93
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG--------QPIADYSEAAL----------RQais 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 94 --------LEAQLHD-----ANERNDGQAIATIH----GKL----DAIDAWsirsraasllhgLGFSNEQLerpvsdfSG 152
Cdd:PRK11160 418 vvsqrvhlFSATLRDnlllaAPNASDEALIEVLQqvglEKLleddKGLNAW------------LGEGGRQL-------SG 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 153 GWRMRLNLAQALICRSDLLLLDEPTNHLDLDA--VIwLEKWLKSYQG-TLILISHDRDFLDPIvDKIIHIEQQSMFEyTG 229
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETerQI-LELLAEHAQNkTVLMITHRLTGLEQF-DRICVMDNGQIIE-QG 555
|
250 260
....*....|....*....|....*..
gi 446557484 230 NYSSfevqratrLAQQQAMYESQQERV 256
Cdd:PRK11160 556 THQE--------LLAQQGRYYQLKQRL 574
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-224 |
1.47e-11 |
|
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: 63.39 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKneisadggsytfpGSWQlawvnqetpalPQAAlEYVIDGdreyrq 93
Cdd:cd03246 15 PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLIL-------------GLLR-----------PTSG-RVRLDG------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 94 leAQLHDANERNDGQAIATIhgkldAIDAwsirsraaSLLHGlgfsneqlerPVSD--FSGGWRMRLNLAQALICRSDLL 171
Cdd:cd03246 64 --ADISQWDPNELGDHVGYL-----PQDD--------ELFSG----------SIAEniLSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 172 LLDEPTNHLDLDAVIWLE---KWLKSYQGTLILISHDRDFLDpIVDKIIHIEQQSM 224
Cdd:cd03246 119 VLDEPNSHLDVEGERALNqaiAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
313-457 |
1.53e-11 |
|
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: 64.49 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL--------------AKGIklG 378
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLdgqditklpmhkraRLGI--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 379 YFAQHQ--------LEYLRAdespIQHLARLAPQELEQKLRDYLGGFGFqgdkvtEETR-----RFSGGEKARLVLALIV 445
Cdd:cd03218 79 YLPQEAsifrkltvEENILA----VLEIRGLSKKEREEKLEELLEEFHI------THLRkskasSLSGGERRRVEIARAL 148
|
170
....*....|..
gi 446557484 446 WQRPNLLLLDEP 457
Cdd:cd03218 149 ATNPKFLLLDEP 160
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
312-474 |
1.55e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.11 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA------KGIKLGYFAQHQ- 384
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegPGAERGVVFQNEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 385 -LEYLRADESPI--QHLARLAPQELEQKLRDYLGGFGFQGdkvtEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPT 458
Cdd:PRK11248 81 lLPWRNVQDNVAfgLQLAGVEKMQRLEIAHQMLKKVGLEG----AEKRYiwqLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170
....*....|....*.
gi 446557484 459 NHLDLDMRQALTEALI 474
Cdd:PRK11248 157 GALDAFTREQMQTLLL 172
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-247 |
1.61e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.18 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 15 VLLDNATATINPGQKVGLVGKNGCGKSTLL-ALLkneisadG-----GSYTF---------PGSW--QLAWVNQEtPALP 77
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLnALL-------GflpyqGSLKIngielreldPESWrkHLSWVGQN-PQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 78 QAAL-EYVIDGDreyrqleaqlHDANErndgqaiATIHGKLDAIDAWSIRSRaasLLHGlgfsneqLERPVSD----FSG 152
Cdd:PRK11174 436 HGTLrDNVLLGN----------PDASD-------EQLQQALENAWVSEFLPL---LPQG-------LDTPIGDqaagLSV 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 153 GWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIwleKWLKSY--QGTLILISHDRDFLDPiVDKIIHIEQQSMFEy 227
Cdd:PRK11174 489 GQAQRLALARALLQPCQLLLLDEPTASLDAHseqLVM---QALNAAsrRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQ- 563
|
250 260
....*....|....*....|...
gi 446557484 228 TGNYSSFEVQR---ATRLAQQQA 247
Cdd:PRK11174 564 QGDYAELSQAGglfATLLAHRQE 586
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
313-514 |
1.75e-11 |
|
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: 64.28 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDrIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKLGYFAQHQLEYLRAD 391
Cdd:cd03299 1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 392 ESPIQHLA-----------RLAPQ-ELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLA--LIVwqRPNLLLLDEP 457
Cdd:cd03299 80 YALFPHMTvykniayglkkRKVDKkEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIAraLVV--NPKILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 458 TNHLDLDMRQALTEALI----EFEGALVVVSHDRHLLRSTTDDLYLVHDRKVEPFdGDLED 514
Cdd:cd03299 157 FSALDVRTKEKLREELKkirkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV-GKPEE 216
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-223 |
1.83e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.14 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRR-GVRVLLDNATATINPGQKVGLVGKNGCGKSTLL-ALlkNEISADG-GSYTFPGSWQLAWvnqetpaLP 77
Cdd:COG4178 362 ALALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLrAI--AGLWPYGsGRIARPAGARVLF-------LP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 78 QAAleYVIDGDreyrqLEAQL---HDANERNDGQAIATIH--------GKLDAIDAWSIRsraasllhglgfsneqlerp 146
Cdd:COG4178 433 QRP--YLPLGT-----LREALlypATAEAFSDAELREALEavglghlaERLDEEADWDQV-------------------- 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 147 vsdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKS--YQGTLILISHdRDFLDPIVDKIIHIEQQS 223
Cdd:COG4178 486 ---LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGDG 560
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
310-457 |
1.91e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 64.28 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA--------------KGI 375
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDgedithlpmhkrarLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 376 klGYFAQH-----QL---EYLRAdespIQHLARLAPQELEQKLRDYLGGFGFqgdkvtEETRR-----FSGGEKARLVLA 442
Cdd:COG1137 81 --GYLPQEasifrKLtveDNILA----VLELRKLSKKEREERLEELLEEFGI------THLRKskaysLSGGERRRVEIA 148
|
170
....*....|....*..
gi 446557484 443 --LIVwqRPNLLLLDEP 457
Cdd:COG1137 149 raLAT--NPKFILLDEP 163
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
313-491 |
2.43e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.32 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--ELAPVSGEIGL--------------AKGIK 376
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLdgedilelspderaRAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 377 LGYfaQHQLE--------YLRADESpIQHLARLAPQELEQKLRDYLGGFGFQGDKVteetRR-----FSGGEKARL-VLA 442
Cdd:COG0396 81 LAF--QYPVEipgvsvsnFLRTALN-ARRGEELSAREFLKLLKEKMKELGLDEDFL----DRyvnegFSGGEKKRNeILQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446557484 443 LIVwQRPNLLLLDEPTNHLDLDMRQALTEALIEF---EGALVVVSHDRHLLR 491
Cdd:COG0396 154 MLL-LEPKLAILDETDSGLDIDALRIVAEGVNKLrspDRGILIITHYQRILD 204
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
328-487 |
2.66e-11 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 63.61 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKG---IKLGYFAQHQLEYLRADE----SpiQHL-- 398
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwVDLAQASPREILALRRRTigyvS--QFLrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 399 -----AR-----------LAPQELEQKLRDYLGGFGfqgdkVTEE-------TrrFSGGEKARLVLA--LIVwqRPNLLL 453
Cdd:COG4778 105 iprvsALdvvaepllergVDREEARARARELLARLN-----LPERlwdlppaT--FSGGEQQRVNIArgFIA--DPPLLL 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 446557484 454 LDEPTNHLDLDMRQALTEALIEF--EG-ALVVVSHDR 487
Cdd:COG4778 176 LDEPTASLDAANRAVVVELIEEAkaRGtAIIGIFHDE 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-217 |
2.86e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 66.35 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSytFPGSWQLAWVnqetpalPQaaleYV-IDGDREYRQLeaqLHDA 101
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE--VDEDLKISYK-------PQ----YIsPDYDGTVEEF---LRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 102 NErndgqaiatihgklDAIDAWSIRSRaasLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:COG1245 426 NT--------------DDFGSSYYKTE---IIKPLGL-EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446557484 182 LDAVIWLEKWLK----SYQGTLILISHDRDFLDPIVDKII 217
Cdd:COG1245 488 VEQRLAVAKAIRrfaeNRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-492 |
3.14e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.27 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 6 SLQIRRG--VRVLLDNATATINPGQKVGLVGKNGCGKS-TLLALLK----NEISADGGSYTFPGSW-------------- 64
Cdd:PRK15134 12 SVAFRQQqtVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRllpsPPVVYPSGDIRFHGESllhaseqtlrgvrg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 65 -QLAWVNQEtpalPQAALEYVidgdreyRQLEAQLHDANERNDGQAIATIHGK-LDAIDAWSIRSRAASLlhglgfsneq 142
Cdd:PRK15134 92 nKIAMIFQE----PMVSLNPL-------HTLEKQLYEVLSLHRGMRREAARGEiLNCLDRVGIRQAAKRL---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 143 lerpvSDF----SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDfldpIVD 214
Cdd:PRK15134 151 -----TDYphqlSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNLS----IVR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 215 KIIHieqqsmfeytgnysSFEVQRATRLAQQQamyesqqervahlqsyidrfRAKATKAKQAQSRIKMLERMEliaPAHv 294
Cdd:PRK15134 222 KLAD--------------RVAVMQNGRCVEQN--------------------RAATLFSAPTHPYTQKLLNSE---PSG- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 295 dnpfrfsfrAPESLPN---PLLKMEKVSAGY-----------GDRIILDSIKLNLVPGSRIGLLGRNGAGKST----LIK 356
Cdd:PRK15134 264 ---------DPVPLPEpasPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 357 LLAGElapvsGEIGLaKGIKLGYFAQHQLEYLRadeSPIQ--------------------------HLARLAPQELEQKL 410
Cdd:PRK15134 335 LINSQ-----GEIWF-DGQPLHNLNRRQLLPVR---HRIQvvfqdpnsslnprlnvlqiieeglrvHQPTLSAAQREQQV 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 411 RDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMrQALTEALI-----EFEGALVVVSH 485
Cdd:PRK15134 406 IAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTV-QAQILALLkslqqKHQLAYLFISH 484
|
....*..
gi 446557484 486 DRHLLRS 492
Cdd:PRK15134 485 DLHVVRA 491
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
328-505 |
3.20e-11 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 63.64 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGI------KLGYFAQHQL-EYLRADESPIQHLA 399
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQItepgpdRMVVFQNYSLlPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 400 RLAPQ----ELEQKLRDYLG--GFGFQGDKVTEEtrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
Cdd:TIGR01184 81 RVLPDlsksERRAIVEEHIAlvGLTEAADKRPGQ---LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 446557484 474 I----EFEGALVVVSHDrhllrstTDDLYLVHDRKV 505
Cdd:TIGR01184 158 MqiweEHRVTVLMVTHD-------VDEALLLSDRVV 186
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
327-495 |
3.64e-11 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 63.18 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG---LAKGIKLGYFAQHQLEYLR-ADESPIQHLARLA 402
Cdd:TIGR02324 23 VLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILvrhEGAWVDLAQASPREVLEVRrKTIGYVSQFLRVI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 403 PQE-----LEQKLRDYlggfGFQGDKVTEETRR------------------FSGGEKARLVLALIVWQRPNLLLLDEPTN 459
Cdd:TIGR02324 103 PRVsalevVAEPLLER----GVPREAARARAREllarlniperlwhlppatFSGGEQQRVNIARGFIADYPILLLDEPTA 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 446557484 460 HLDLDMRQALTEALIEFEG---ALVVVSHDRHLLRSTTD 495
Cdd:TIGR02324 179 SLDAANRQVVVELIAEAKArgaALIGIFHDEEVRELVAD 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-506 |
4.00e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 65.62 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLkneisadggSYTFP-GSW--QLAWVNQETPAlpqaalEYVIDGDR---- 89
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKIL---------SGVYPhGTWdgEIYWSGSPLKA------SNIRDTERagiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 90 ---EYRQLEAQLHDANERNDGQAIaTIHGKLDAIDAWSIRSRAasLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALIC 166
Cdd:TIGR02633 82 iihQELTLVPELSVAENIFLGNEI-TLPGGRMAYNAMYLRAKN--LLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 167 RSDLLLLDEPTNHL---DLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIeqqsmfeytgnyssfevqRATRLA 243
Cdd:TIGR02633 159 QARLLILDEPSSSLtekETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVI------------------RDGQHV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 244 QQQAMYESQQERVahlqsyidrfrakatkakqaqsrIKMLERMELIApahvdnpfrFSFRAPESLPNPLLKMEKVSAGYG 323
Cdd:TIGR02633 221 ATKDMSTMSEDDI-----------------------ITMMVGREITS---------LYPHEPHEIGDVILEARNLTCWDV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 324 D---RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGEL-APVSGEIglakgiklgYFAQHQLEyLRADESPIQHLA 399
Cdd:TIGR02633 269 InphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNV---------FINGKPVD-IRNPAQAIRAGI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 400 RLAPqelEQKLRD---------------YLGGFGFQG--DKVTEE--------------------TRRFSGGEKARLVLA 442
Cdd:TIGR02633 339 AMVP---EDRKRHgivpilgvgknitlsVLKSFCFKMriDAAAELqiigsaiqrlkvktaspflpIGRLSGGNQQKAVLA 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 443 LIVWQRPNLLLLDEPTNHLDLDMRQA---LTEALIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKVE 506
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDVGAKYEiykLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
310-486 |
4.49e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 63.88 E-value: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 310 NPLLKMEKVSAGYGD--RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKL---------- 377
Cdd:PRK13635 3 EEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG-GMVLseetvwdvrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 378 --GYFAQHQ----------------LEYlradespiQHLARlapQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARL 439
Cdd:PRK13635 82 qvGMVFQNPdnqfvgatvqddvafgLEN--------IGVPR---EEMVERVDQALRQVGME-DFLNREPHRLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446557484 440 VLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEF--EGALVVVS--HD 486
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSitHD 200
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
313-474 |
4.83e-11 |
|
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: 62.90 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGD--RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLgyfAQHQLEYLRa 390
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSI-LIDGVDI---SKIGLHDLR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 despiQHLArLAPQE--------------------------LEQ-KLRDYLGGFGFQGD-KVTEETRRFSGGEKARLVLA 442
Cdd:cd03244 78 -----SRIS-IIPQDpvlfsgtirsnldpfgeysdeelwqaLERvGLKEFVESLPGGLDtVVEEGGENLSVGQRQLLCLA 151
|
170 180 190
....*....|....*....|....*....|..
gi 446557484 443 LIVWQRPNLLLLDEPTNHLDLDmrqalTEALI 474
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPE-----TDALI 178
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-215 |
5.00e-11 |
|
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: 65.59 E-value: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 9 IRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFP-GSwqlAWVNQETPALPQA--ALEYVI 85
Cdd:TIGR03269 292 VDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGD---EWVDMTKPGPDGRgrAKRYIG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 86 DGDREYRQLEaqlHDANERNDGQAIAtihgkLDAIDAWSIRsRAASLLHGLGFSNEQ----LERPVSDFSGGWRMRLNLA 161
Cdd:TIGR03269 369 ILHQEYDLYP---HRTVLDNLTEAIG-----LELPDELARM-KAVITLKMVGFDEEKaeeiLDKYPDELSEGERHRVALA 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 162 QALICRSDLLLLDEPTNHLD-LDAVIWLEKWLKS---YQGTLILISHDRDFLDPIVDK 215
Cdd:TIGR03269 440 QVLIKEPRIVILDEPTGTMDpITKVDVTHSILKAreeMEQTFIIVSHDMDFVLDVCDR 497
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
309-458 |
5.03e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.42 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 309 PNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----------AKGIKLG 378
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdgepvrfrspRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 379 YFAQHQ----LEYLRADE-----SPIQHLARLAPQELEQKLRDYLGGFGFQGDkVTEETRRFSGGEK-----ARlvlALI 444
Cdd:COG1129 81 IAIIHQelnlVPNLSVAEniflgREPRRGGLIDWRAMRRRARELLARLGLDID-PDTPVGDLSVAQQqlveiAR---ALS 156
|
170
....*....|....
gi 446557484 445 vwQRPNLLLLDEPT 458
Cdd:COG1129 157 --RDARVLILDEPT 168
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-219 |
5.81e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.16 E-value: 5.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLallkneisadggsytfpgswqlawvnqetpalpqaaleYVID 86
Cdd:cd03217 6 LHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLA--------------------------------------KTIM 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 87 GDREYRQLEAQLhdaneRNDGQAIATIhgkldaidawSIRSRAASLLhGLGF---------SNEQLERPVSD-FSGGWRM 156
Cdd:cd03217 48 GHPKYEVTEGEI-----LFKGEDITDL----------PPEERARLGI-FLAFqyppeipgvKNADFLRYVNEgFSGGEKK 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 157 RLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIHI 219
Cdd:cd03217 112 RNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLLDYIKPDRVHV 177
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
7-185 |
6.20e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSwqlawvNQETPALPqAALEYVID 86
Cdd:PRK13539 8 LACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG------DIDDPDVA-EACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 87 GD--------REYRQLEAQLHdanerndGQAIATIHgklDAIDAWSirsraaslLHGLgfsneqLERPVSDFSGGWRMRL 158
Cdd:PRK13539 81 RNamkpaltvAENLEFWAAFL-------GGEELDIA---AALEAVG--------LAPL------AHLPFGYLSAGQKRRV 136
|
170 180
....*....|....*....|....*..
gi 446557484 159 NLAQALICRSDLLLLDEPTNHLDLDAV 185
Cdd:PRK13539 137 ALARLLVSNRPIWILDEPTAALDAAAV 163
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-205 |
6.43e-11 |
|
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: 62.58 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-----KNEISADGGSYTFPGS------------- 63
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKdiydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 64 WQLAWVNQETPALPQAALEYVIDGDReyrqleaqLHDANERndgqaiatihGKLDAIDAWSIRS-----RAASLLHGLGF 138
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLR--------LHGIKLK----------EELDERVEEALRKaalwdEVKDRLHALGL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 139 SneqlerpvsdfsGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG--TLILISHD 205
Cdd:cd03260 143 S------------GGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
325-500 |
7.24e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.28 E-value: 7.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGEL--APVSGEIGLAKGIklgyFAQhqleylraDESPIQHLARLA 402
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ----FGR--------EASLIDAIGRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 403 PqeLEQKLRdYLGGFGFqGDKVTEeTRRF---SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ----ALTEALIE 475
Cdd:COG2401 111 D--FKDAVE-LLNAVGL-SDAVLW-LRRFkelSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKrvarNLQKLARR 185
|
170 180
....*....|....*....|....*
gi 446557484 476 FEGALVVVSHDRHLLRSTTDDLYLV 500
Cdd:COG2401 186 AGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-220 |
7.95e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.08 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnqeTPALPQAAL 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG----------VPVPARARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 EYVIDG--------DREYRQLEAQLhdanerndgqaiatIHGKLDAIDAWSIRSRAASLLHglgFSneQLER----PVSD 149
Cdd:PRK13536 112 ARARIGvvpqfdnlDLEFTVRENLL--------------VFGRYFGMSTREIEAVIPSLLE---FA--RLESkadaRVSD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557484 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA--VIWLE-KWLKSYQGTLILISHDRDFLDPIVDKIIHIE 220
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHArhLIWERlRSLLARGKTILLTTHFMEEAERLCDRLCVLE 246
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-253 |
8.36e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.96 E-value: 8.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 18 DNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGsytfpgswQLAWVNQETPALPQAALeyvidgdREYRQlEAQ 97
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDG--------EVAWLGKDLLGMKDDEW-------RAVRS-DIQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 98 ------LHDANER-NDGQAIA----TIHGKLDAIDawsIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALIC 166
Cdd:PRK15079 102 mifqdpLASLNPRmTIGEIIAeplrTYHPKLSRQE---VKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 167 RSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQG-TLILISHDRDfldpiVDKiiHIEQQSMFEYTGNyssfevqrATRL 242
Cdd:PRK15079 179 EPKLIICDEPVSALDVSiqaQVVNLLQQLQREMGlSLIFIAHDLA-----VVK--HISDRVLVMYLGH--------AVEL 243
|
250
....*....|.
gi 446557484 243 AQQQAMYESQQ 253
Cdd:PRK15079 244 GTYDEVYHNPL 254
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-221 |
8.57e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 62.42 E-value: 8.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLL------------ALLKNEISADGGSYTFPGSWQLA- 67
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrcinkleeitsgDLIVDGLKVNDPKVDERLIRQEAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 68 WVNQETPALPQ-AALEYVIDGDREYRQLeaqlhdanerndgqaiatihGKLDAidawsiRSRAASLLHGLGFSNEQLERP 146
Cdd:PRK09493 81 MVFQQFYLFPHlTALENVMFGPLRVRGA--------------------SKEEA------EKQARELLAKVGLAERAHHYP 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 147 vSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:PRK09493 135 -SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPElrhEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDK 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
328-510 |
8.91e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.14 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL------AKGIKL-------GYFAQHQlEYLRADESP 394
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditDKKVKLsdirkkvGLVFQYP-EYQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 395 IQHLA------RLAPQELEQKLRDYLGGFGFQGDKVTEETR-RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
Cdd:PRK13637 102 EKDIAfgpinlGLSEEEIENRVKRAMNIVGLDYEDYKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446557484 468 ALTEALI----EFEGALVVVSHDRHLLRSTTDDLYLVHDRKVEpFDG 510
Cdd:PRK13637 182 EILNKIKelhkEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE-LQG 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
313-506 |
9.15e-11 |
|
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: 62.36 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGIKLGYFAQH 383
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggedatdvpVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 384 QLEY------------LRadespIQHLARLAP-QELEQKLRDYLGGFGFQG--DKVTEEtrrFSGGEKARLVLALIVWQR 448
Cdd:cd03296 83 YALFrhmtvfdnvafgLR-----VKPRSERPPeAEIRAKVHELLKLVQLDWlaDRYPAQ---LSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557484 449 PNLLLLDEPTNHLDLDMRQALTEALIEFEGAL----VVVSHDRHLLRSTTDDLYLVHDRKVE 506
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHDQEEALEVADRVVVMNKGRIE 216
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-205 |
9.45e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.14 E-value: 9.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWqlawVNQETPAlPQAALEyvidgDREY---R 92
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP----MSKLSSA-AKAELR-----NQKLgfiY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 93 QLEAQLHDANERNDGQAIATIHGKLDAidawSIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLL 172
Cdd:PRK11629 94 QFHHLLPDFTALENVAMPLLIGKKKPA----EINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 446557484 173 LDEPTNHLDL---DAVIWLEKWLKSYQGTLIL-ISHD 205
Cdd:PRK11629 169 ADEPTGNLDArnaDSIFQLLGELNRLQGTAFLvVTHD 205
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
309-486 |
1.01e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 309 PNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLG-----YFAQh 383
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQPLEswsskAFAR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 384 QLEYLradespiqhlarlaPQELEQ----KLRDY-----------LGGFGFQGDKVTEE--------------TRRFSGG 434
Cdd:PRK10575 86 KVAYL--------------PQQLPAaegmTVRELvaigrypwhgaLGRFGAADREKVEEaislvglkplahrlVDSLSGG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 435 EKARLVLALIVWQRPNLLLLDEPTNHLDLDMR---QALTEALIEFEGALVV-VSHD 486
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQvdvLALVHRLSQERGLTVIaVLHD 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
328-485 |
1.20e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.03 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA-KGI---------KLGYFAQ------------HQL 385
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAgKSIltnisdvhqNMGYCPQfdaiddlltgreHLY 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 386 EYLRADESPIQHLARLAPQELEQKlrdylgGFGFQGDKVTEEtrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
Cdd:TIGR01257 2035 LYARLRGVPAEEIEKVANWSIQSL------GLSLYADRLAGT---YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
170 180
....*....|....*....|...
gi 446557484 466 RQALTE---ALIEFEGALVVVSH 485
Cdd:TIGR01257 2106 RRMLWNtivSIIREGRAVVLTSH 2128
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-216 |
1.74e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.95 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSwQLAWVNQETPALPQAA 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK-PLDYSKRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 LEYVIDGDRE--YRQLEAQLHdANERNDGQAIATIHGKLDaidawsirsRAASLLHGLGFSNEqlerPVSDFSGGWRMRL 158
Cdd:PRK13638 80 ATVFQDPEQQifYTDIDSDIA-FSLRNLGVPEAEITRRVD---------EALTLVDAQHFRHQ----PIQCLSHGQKKRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY--QGTLILI-SHDRDFLDPIVDKI 216
Cdd:PRK13638 146 AIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvaQGNHVIIsSHDIDLIYEISDAV 206
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
314-503 |
1.80e-10 |
|
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: 61.47 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 314 KMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI------------KLGY- 379
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQI-LIDGIdirdisrkslrsMIGVv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 380 ------FAQHQLEYLR------ADESPIQHLARLAPQELEQKLRDylggfGFQgDKVTEETRRFSGGEKARLVLALIVWQ 447
Cdd:cd03254 83 lqdtflFSGTIMENIRlgrpnaTDEEVIEAAKEAGAHDFIMKLPN-----GYD-TVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 448 RPNLLLLDEPTNHLDLDMRQALTEALIE-FEG-ALVVVSHdrHLlrSTTD--DLYLVHDR 503
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKlMKGrTSIIIAH--RL--STIKnaDKILVLDD 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-221 |
1.81e-10 |
|
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: 61.59 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSwqlawvnqetpalpqaal 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 eyvidgdreyrqlEAQLHDANERNDG---QAIA---------------TIHGKLDAIDAWSIRSRAASLLHGLGFSNEQl 143
Cdd:cd03296 65 -------------DATDVPVQERNVGfvfQHYAlfrhmtvfdnvafglRVKPRSERPPEAEIRAKVHELLKLVQLDWLA- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 144 ERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDKII-- 217
Cdd:cd03296 131 DRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelhvTTVFVTHDQEEALEVADRVVvm 210
|
....*..
gi 446557484 218 ---HIEQ 221
Cdd:cd03296 211 nkgRIEQ 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-207 |
1.85e-10 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 61.55 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQAALE----YVI 85
Cdd:cd03295 10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG--------EDIREQDPVELRrkigYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 86 dgdreyRQLEAQLHDANERNdgqaIATIHgKLDAIDAWSIRSRAASLLHGLGFSNEQL-ERPVSDFSGGWRMRLNLAQAL 164
Cdd:cd03295 82 ------QQIGLFPHMTVEEN----IALVP-KLLKWPKEKIRERADELLALVGLDPAEFaDRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446557484 165 ICRSDLLLLDEPTNHLD-------LDAVIWLEKWLKSyqgTLILISHDRD 207
Cdd:cd03295 151 AADPPLLLMDEPFGALDpitrdqlQEEFKRLQQELGK---TIVFVTHDID 197
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
337-495 |
2.12e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 61.61 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 337 PGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE----------IGLAKGIKL-GYFAQHQLEYLRADESPiQHLARLaPQE 405
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeiLDEFRGSELqNYFTKLLEGDVKVIVKP-QYVDLI-PKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 406 LEQKLRDYLGGFGFQG--DKVTE----------ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLdmRQALTEA- 472
Cdd:cd03236 103 VKGKVGELLKKKDERGklDELVDqlelrhvldrNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI--KQRLNAAr 180
|
170 180
....*....|....*....|....*..
gi 446557484 473 ----LIEFEGALVVVSHDRHLLRSTTD 495
Cdd:cd03236 181 lireLAEDDNYVLVVEHDLAVLDYLSD 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
311-458 |
2.35e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.12 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---G-----------LAKGIk 376
Cdd:COG3845 4 PALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEIlidGkpvrirsprdaIALGI- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 377 lGYFAQH-QL-EYLRADE-----SPIQHLARLAPQELEQKLRDYLGGFGFQGD---KVteetRRFSGGEKARL--VLALi 444
Cdd:COG3845 83 -GMVHQHfMLvPNLTVAEnivlgLEPTKGGRLDRKAARARIRELSERYGLDVDpdaKV----EDLSVGEQQRVeiLKAL- 156
|
170
....*....|....
gi 446557484 445 vWQRPNLLLLDEPT 458
Cdd:COG3845 157 -YRGARILILDEPT 169
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
6-205 |
2.41e-10 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 60.91 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPGSWQLA--------WVN 70
Cdd:COG4181 17 TVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLagldrptSGTVRLAGQDLFALDEDARArlrarhvgFVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 71 QETPALPQ-AALEYVidgdreyrQLEAQLhdaneRNDGQAiatihgkldaidawsiRSRAASLLH--GLGfsnEQLE-RP 146
Cdd:COG4181 97 QSFQLLPTlTALENV--------MLPLEL-----AGRRDA----------------RARARALLErvGLG---HRLDhYP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 147 vSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKSYQG-TLILISHD 205
Cdd:COG4181 145 -AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAatgEQIIDLLFELNRERGtTLVLVTHD 206
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
17-219 |
2.57e-10 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 61.12 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALL----KNEISadGGSYTFPGSWQLAWVNQETPAL-----PQAALEyvIDG 87
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghpSYEVT--SGTILFKGQDLLELEPDERARAglflaFQYPEE--IPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 88 --DREYrqleaqLHDANErndgqAIATIHGKlDAIDAWSIRSRAASLLHGLGFSNEQLERPVSD-FSGGWRMRLNLAQAL 164
Cdd:TIGR01978 92 vsNLEF------LRSALN-----ARRSARGE-EPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEILQMA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 165 ICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIHI 219
Cdd:TIGR01978 160 LLEPKLAILDEIDSGLDIDALKIVAEGINRLREpdrSFLIITHYQRLLNYIKPDYVHV 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
316-462 |
3.00e-10 |
|
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: 60.96 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 316 EKVSAGYG--DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI------------KLGYFA 381
Cdd:cd03252 4 EHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-LVDGHdlaladpawlrrQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 382 QHQLEYLR--------ADESP----IQHLARLA-PQELEQKLRDylggfGFqGDKVTEETRRFSGGEKARLVLALIVWQR 448
Cdd:cd03252 83 QENVLFNRsirdnialADPGMsmerVIEAAKLAgAHDFISELPE-----GY-DTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170
....*....|....
gi 446557484 449 PNLLLLDEPTNHLD 462
Cdd:cd03252 157 PRILIFDEATSALD 170
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
303-485 |
3.01e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 303 RAPESLPnPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKLGYFA 381
Cdd:PRK13543 3 EPLHTAP-PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATRGDRS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 382 QH-----QLEYLRADESPIQHLARLA------PQELEQKLRDYLGGFGFQGDKVteetRRFSGGEKARLVLALIvWQRPN 450
Cdd:PRK13543 82 RFmaylgHLPGLKADLSTLENLHFLCglhgrrAKQMPGSALAIVGLAGYEDTLV----RQLSAGQKKRLALARL-WLSPA 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 446557484 451 -LLLLDEPTNHLDLD---MRQALTEALIEFEGALVVVSH 485
Cdd:PRK13543 157 pLWLLDEPYANLDLEgitLVNRMISAHLRGGGAALVTTH 195
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-220 |
3.21e-10 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 60.50 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISadggsytfPGSWQLAWVNQETPALPQAALEYVidgdreYRQLEA 96
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEEL--------PTSGTIRVNGQDVSDLRGRAIPYL------RRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 97 QLHDAN---ERN--DGQAIAtihgkLDAIDA--WSIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSD 169
Cdd:cd03292 83 VFQDFRllpDRNvyENVAFA-----LEVTGVppREIRKRVPAALELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446557484 170 LLLLDEPTNHLDLDAVIWLEKWLKSYQ--GTLILIS-HDRDFLDPIVDKIIHIE 220
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINkaGTTVVVAtHAKELVDTTRHRVIALE 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-282 |
3.44e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.20 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSwQLAWVNQEtpALPQAALEYVIDGDREYRQLEa 96
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ-DVATLDAD--ALAQLRREHFGFIFQRYHLLS- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 97 qlHDANERNDgqaiatihgKLDAIDAWSIRS----RAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLL 172
Cdd:PRK10535 100 --HLTAAQNV---------EVPAVYAGLERKqrllRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 173 LDEPTNHLDL---DAVIWLEKWLKSYQGTLILISHdrdflDPIV----DKIIHIEQQSMFEYTGNYSSFEVQRATrlaqq 245
Cdd:PRK10535 168 ADEPTGALDShsgEEVMAILHQLRDRGHTVIIVTH-----DPQVaaqaERVIEIRDGEIVRNPPAQEKVNVAGGT----- 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 446557484 246 qamyESQQERVAHLQSYIDRFRAKATKAKQAQSRIKM 282
Cdd:PRK10535 238 ----EPVVNTASGWRQFVSGFREALTMAWRAMAANKM 270
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-217 |
3.87e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGG--------SYTfpgswqlawvnqetpalPQaaleYV-IDGDREYRQ 93
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGevdpelkiSYK-----------------PQ----YIkPDYDGTVED 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 94 LeaqlhdanerndgqaIATIHGKLDAIDAWSirsraaSLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLL 173
Cdd:PRK13409 420 L---------------LRSITDDLGSSYYKS------EIIKPLQL-ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446557484 174 DEPTNHLDLDAVIWLEKWLKSY----QGTLILISHDRDFLDPIVDKII 217
Cdd:PRK13409 478 DEPSAHLDVEQRLAVAKAIRRIaeerEATALVVDHDIYMIDYISDRLM 525
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
312-500 |
3.94e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.29 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGY------GDRIILDsIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQL 385
Cdd:PRK13643 1 MIKFEKVNYTYqpnspfASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 386 EYLRA--------------DESPIQHLArLAPQ-------ELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALI 444
Cdd:PRK13643 80 KPVRKkvgvvfqfpesqlfEETVLKDVA-FGPQnfgipkeKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 445 VWQRPNLLLLDEPTNHLDLDMR---QALTEALIEFEGALVVVSHDRHLLRSTTDDLYLV 500
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARiemMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLL 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
333-485 |
4.02e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 60.37 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 333 LNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI--------------------------------------GLAKG 374
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdhtttppsrrpvsmlfqennlfshltvaqniglGLNPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 375 IKLGYFAQHQLEYLRADESPIQHLARLaPQELeqklrdylggfgfqgdkvteetrrfSGGEKARLVLA-LIVWQRPnLLL 453
Cdd:PRK10771 100 LKLNAAQREKLHAIARQMGIEDLLARL-PGQL-------------------------SGGQRQRVALArCLVREQP-ILL 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 446557484 454 LDEPTNHLDLDMRQA----LTEALIEFEGALVVVSH 485
Cdd:PRK10771 153 LDEPFSALDPALRQEmltlVSQVCQERQLTLLMVSH 188
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-458 |
4.53e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 62.34 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQE-TPALPQAALEyvidgdre 90
Cdd:COG1129 16 GVKAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG--------EPvRFRSPRDAQA-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 91 yrqleaqlhdanerndgQAIATIH---------------------GKLDAIDAWSIRSRAASLLHGLGFsNEQLERPVSD 149
Cdd:COG1129 79 -----------------AGIAIIHqelnlvpnlsvaeniflgrepRRGGLIDWRAMRRRARELLARLGL-DIDPDTPVGD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWL----EKwLKSyQG-TLILISHdrdFLDPIvdkiihieqqsm 224
Cdd:COG1129 141 LSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLfriiRR-LKA-QGvAIIYISH---RLDEV------------ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 225 feytgnyssFEV-QRAT-----RLAQQQAMYESQQERVAHLqsyidrfrakatkakqaqsrikMLERmeliapaHVDNPF 298
Cdd:COG1129 204 ---------FEIaDRVTvlrdgRLVGTGPVAELTEDELVRL----------------------MVGR-------ELEDLF 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 299 RfsfRAPESLPNPLLKMEKVSAGYGdriiLDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL------- 371
Cdd:COG1129 246 P---KRAAAPGEVVLEVEGLSVGGV----VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLdgkpvri 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 372 ---AKGIKLGyFAqhqleYLRAD--------ESPIQ------HLARLA------PQELEQKLRDYLGGFGFQGDKVTEET 428
Cdd:COG1129 319 rspRDAIRAG-IA-----YVPEDrkgeglvlDLSIRenitlaSLDRLSrgglldRRRERALAEEYIKRLRIKTPSPEQPV 392
|
490 500 510
....*....|....*....|....*....|..
gi 446557484 429 RRFSGGEKARLVLA--LIvwQRPNLLLLDEPT 458
Cdd:COG1129 393 GNLSGGNQQKVVLAkwLA--TDPKVLILDEPT 422
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-227 |
4.56e-10 |
|
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: 59.81 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIR--RGVRVLLDNATATINPGQKVGLVGKNGCGKSTL-LALLKnEISADGGSYTFPG------------SwQL 66
Cdd:cd03244 3 IEFKNVSLRyrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLlLALFR-LVELSSGSILIDGvdiskiglhdlrS-RI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 67 AWVNQEtPALPQAALEYVIDGDREYRqlEAQLHDANER-NDGQAIATIHGKLDAIDAwsirsraasllhgLGFSNeqler 145
Cdd:cd03244 81 SIIPQD-PVLFSGTIRSNLDPFGEYS--DEELWQALERvGLKEFVESLPGGLDTVVE-------------EGGEN----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 146 pvsdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL--DAVIW--LEKWLKSYqgTLILISHdRdfLDPIV--DKIIHI 219
Cdd:cd03244 140 ----LSVGQRQLLCLARALLRKSKILVLDEATASVDPetDALIQktIREAFKDC--TVLTIAH-R--LDTIIdsDRILVL 210
|
....*...
gi 446557484 220 EQQSMFEY 227
Cdd:cd03244 211 DKGRVVEF 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-204 |
4.63e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.82 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGS-----------WQLAWVNQEtPALPQAALEYVI 85
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhRQVALVGQE-PVLFSGSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 86 DGDREYRQLEAQLHDANERNdgqAIATIHGKLDAIDAwsirsraasllhGLGFSNEQLerpvsdfSGGWRMRLNLAQALI 165
Cdd:TIGR00958 576 AYGLTDTPDEEIMAAAKAAN---AHDFIMEFPNGYDT------------EVGEKGSQL-------SGGQKQRIAIARALV 633
|
170 180 190
....*....|....*....|....*....|....*....
gi 446557484 166 CRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISH 204
Cdd:TIGR00958 634 RKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
311-490 |
4.85e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.43 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELA--PVSGEIgLAKGI-----------KL 377
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDI-LFKGEsildlepeeraHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 378 GYFA--QHQLE--------YLRA---DESPIQHLARLAPQELEQKLRDYLGGFG----FQGDKVTEEtrrFSGGEKAR-- 438
Cdd:CHL00131 85 GIFLafQYPIEipgvsnadFLRLaynSKRKFQGLPELDPLEFLEIINEKLKLVGmdpsFLSRNVNEG---FSGGEKKRne 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 439 -LVLALIvwqRPNLLLLDEPTNHLDLDMRQALTEALIEF---EGALVVVSHDRHLL 490
Cdd:CHL00131 162 iLQMALL---DSELAILDETDSGLDIDALKIIAEGINKLmtsENSIILITHYQRLL 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-227 |
5.44e-10 |
|
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: 59.85 E-value: 5.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG--SWQLAwvnqetpalPQAALEYVIDG 87
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLG---------LGGGFNPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 88 dREYRQLEAQLHdanerndGQAIATIHGKLDAIDAWSirsraasllhGLGfsnEQLERPVSDFSGGWRMRLNLAQALICR 167
Cdd:cd03220 102 -RENIYLNGRLL-------GLSRKEIDEKIDEIIEFS----------ELG---DFIDLPVKTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557484 168 SDLLLLDEPT----NHLDLDAVIWLEKWLKSyQGTLILISHDRDFLDPIVDKIIHIEQQSMFEY 227
Cdd:cd03220 161 PDILLIDEVLavgdAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
322-505 |
5.76e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.41 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQ-----------------HQ 384
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLDYSKRgllalrqqvatvfqdpeQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 385 LEYLRADESPIQHLARL--APQELEQKLRDYLGGFGFQGDKvTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:PRK13638 90 IFYTDIDSDIAFSLRNLgvPEAEITRRVDEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446557484 463 LDMRQ---ALTEALIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKV 505
Cdd:PRK13638 169 PAGRTqmiAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
337-496 |
5.98e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 58.15 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 337 PGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgyfaqhqlEYLRADESPIQHLARLapqeleqklrdylgg 416
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV----------------IYIDGEDILEEVLDQL--------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 417 fgfQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVVVSHDRHLLRSTTDD 496
Cdd:smart00382 50 ---LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDE 126
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
317-486 |
6.01e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.11 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 317 KVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL-------AGELApVSG-----------EIGLAKGIklg 378
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLI-VDGlkvndpkvderLIRQEAGM--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 379 YFAQHQL-EYLRADES----PIqHLARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLL 453
Cdd:PRK09493 82 VFQQFYLfPHLTALENvmfgPL-RVRGASKEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 446557484 454 LDEPTNHLDLDMRQ---ALTEALIEfEG-ALVVVSHD 486
Cdd:PRK09493 160 FDEPTSALDPELRHevlKVMQDLAE-EGmTMVIVTHE 195
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-226 |
6.54e-10 |
|
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: 59.94 E-value: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGS-----------WQLAWVNQETPaLPQAALE 82
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldslrRAIGVVPQDTV-LFNDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 83 YVIdgdrEYrqleaqlhdanerndgqaiatihGKLDAIDAWSIRSRAASLLHGL------GFSNEQLERPVSdFSGGWRM 156
Cdd:cd03253 93 YNI----RY-----------------------GRPDATDEEVIEAAKAAQIHDKimrfpdGYDTIVGERGLK-LSGGEKQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 157 RLNLAQALICRSDLLLLDEPTNHLD-------LDAviwLEKWLKSYqgTLILISHDrdfLDPIV--DKIIHIEQQSMFE 226
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDthtereiQAA---LRDVSKGR--TTIVIAHR---LSTIVnaDKIIVLKDGRIVE 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
338-485 |
7.20e-10 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 59.43 E-value: 7.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYF--AQHQLEYLRADESPIQHLA-------------RLA 402
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRV-LINGVDVTAAppADRPVSMLFQENNLFAHLTveqnvglglspglKLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 403 PQElEQKLRDYLGGFGFQGdKVTEETRRFSGGEKARLVLA-LIVWQRPnLLLLDEPTNHLDLDMRQALTEALIEF----E 477
Cdd:cd03298 103 AED-RQAIEVALARVGLAG-LEKRLPGELSGGERQRVALArVLVRDKP-VLLLDEPFAALDPALRAEMLDLVLDLhaetK 179
|
....*...
gi 446557484 478 GALVVVSH 485
Cdd:cd03298 180 MTVLMVTH 187
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
23-217 |
7.26e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.89 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 23 TINPGQKVGLVGKNGCGKS-TLLALL----KNEISadGGSYTFPGswqlawvnQETPALPQAALE--------------- 82
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSqTAFALMgllaANGRI--GGSATFNG--------REILNLPEKELNklraeqismifqdpm 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 83 -----YVIDGDREYRQLeaQLHDANERNdgQAIATIHGKLDAIDAWSIRSRAASLLHglgfsneqlerpvsDFSGGWRMR 157
Cdd:PRK09473 108 tslnpYMRVGEQLMEVL--MLHKGMSKA--EAFEESVRMLDAVKMPEARKRMKMYPH--------------EFSGGMRQR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557484 158 LNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQGT-LILISHDRDFLDPIVDKII 217
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELKREFNTaIIMITHDLGVVAGICDKVL 233
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
306-462 |
7.53e-10 |
|
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: 58.81 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 306 ESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP---VSGEIgLAKGIKLGYFA- 381
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDI-HYNGIPYKEFAe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 382 --QHQLEYLRADESpiqHLARLAPQE-LEQKLRdylggfgFQGDKVTeetRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
Cdd:cd03233 80 kyPGEIIYVSEEDV---HFPTLTVREtLDFALR-------CKGNEFV---RGISGGERKRVSIAEALVSRASVLCWDNST 146
|
....
gi 446557484 459 NHLD 462
Cdd:cd03233 147 RGLD 150
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-219 |
7.74e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 60.07 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 26 PGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQlawvnqetpalpqaaleyviDGDREYRQLEAQLHDANERN 105
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWD--------------------EILDEFRGSELQNYFTKLLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 106 DGQAIATIHGKLDAIDAwSIRSRAASLL---HGLGFSNEQ---------LERPVSDFSGGWRMRLNLAQALICRSDLLLL 173
Cdd:cd03236 85 GDVKVIVKPQYVDLIPK-AVKGKVGELLkkkDERGKLDELvdqlelrhvLDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446557484 174 DEPTNHLD----LDAVIwLEKWLKSYQGTLILISHDRDFLDPIVDkIIHI 219
Cdd:cd03236 164 DEPSSYLDikqrLNAAR-LIRELAEDDNYVLVVEHDLAVLDYLSD-YIHC 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
313-486 |
8.20e-10 |
|
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: 59.19 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEYLRADE 392
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI---------YIGGRDVTDLPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 SPI----QHLA------------------RLAPQELEQKLRD---------YLGgfgfqgdkvtEETRRFSGGEKARLVL 441
Cdd:cd03301 72 RDIamvfQNYAlyphmtvydniafglklrKVPKDEIDERVREvaellqiehLLD----------RKPKQLSGGQRQRVAL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446557484 442 ALIVWQRPNLLLLDEPTNHLD----LDMRQALTEALIEFEGALVVVSHD 486
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
311-506 |
9.25e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 60.73 E-value: 9.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiklgyfaqHQLEYLRA 390
Cdd:PRK09452 13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG---------QDITHVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 DESPI----QHLArLAPQeleQKLRDYLgGFGFQGDKVTEE-------------------TRR---FSGGEKARLVLALI 444
Cdd:PRK09452 84 ENRHVntvfQSYA-LFPH---MTVFENV-AFGLRMQKTPAAeitprvmealrmvqleefaQRKphqLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 445 VWQRPNLLLLDEPTNHLDLDMRQALTEAL--------IEFegalVVVSHDRHLLRSTTDDLYLVHDRKVE 506
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELkalqrklgITF----VFVTHDQEEALTMSDRIVVMRDGRIE 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-205 |
9.34e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 59.88 E-value: 9.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPGSWQlAWVNQETPALP-QAAL 81
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIagflapsSGEITLDGVPVTGPGADR-GVVFQKDALLPwLNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 EYVIDGdreyrqLEAQLHDANERndgqaiatihgkldaidawsiRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLA 161
Cdd:COG4525 95 DNVAFG------LRLRGVPKAER---------------------RARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446557484 162 QALICRSDLLLLDEPTNHLDLDA-----VIWLEKWLKSYQGTLiLISHD 205
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTreqmqELLLDVWQRTGKGVF-LITHS 194
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
10-181 |
1.04e-09 |
|
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: 59.09 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLlDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG--------SW---QLAWVNQEtPALPQ 78
Cdd:cd03249 13 RPDVPIL-KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirdlnlRWlrsQIGLVSQE-PVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 79 AALEYVI---DGDREYRQLEAQLHDANerndgqaiatIHgklDAIdawsirsraASLLHG----LGFSNEQLerpvsdfS 151
Cdd:cd03249 91 GTIAENIrygKPDATDEEVEEAAKKAN----------IH---DFI---------MSLPDGydtlVGERGSQL-------S 141
|
170 180 190
....*....|....*....|....*....|
gi 446557484 152 GGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:cd03249 142 GGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-181 |
1.04e-09 |
|
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: 61.27 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGsytfpgswqlawvnqetpalpqaalEYVIDGD--REY 91
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSG-------------------------QILLDGHdlADY 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 92 --RQLEAQL----HDANERNDGQAIATIHGKLDAIDAWSIRS--RAASLLHGLGFSNEQLERPVSD----FSGGWRMRLN 159
Cdd:TIGR02203 400 tlASLRRQValvsQDVVLFNDTIANNIAYGRTEQADRAEIERalAAAYAQDFVDKLPLGLDTPIGEngvlLSGGQRQRLA 479
|
170 180
....*....|....*....|..
gi 446557484 160 LAQALICRSDLLLLDEPTNHLD 181
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALD 501
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
308-584 |
1.11e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.68 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 308 LPNPLLKME----KVSAGY------GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGiKL 377
Cdd:PLN03130 603 LPNPPLEPGlpaiSIKNGYfswdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRG-TV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 378 GYFAQ-------------------HQLEYLRA-DESPIQHLARLAPqeleqklrdylggfgfqGDKVTEETRR---FSGG 434
Cdd:PLN03130 682 AYVPQvswifnatvrdnilfgspfDPERYERAiDVTALQHDLDLLP-----------------GGDLTEIGERgvnISGG 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 435 EKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFE---GALVVVSHDRHLLrSTTDDLYLVHDRKVEPfDGD 511
Cdd:PLN03130 745 QKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDElrgKTRVLVTNQLHFL-SQVDRIILVHEGMIKE-EGT 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 512 LED-------YQQWLSDVQKQENQADEAPKENansaqarkDQKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEK 584
Cdd:PLN03130 823 YEElsnngplFQKLMENAGKMEEYVEENGEEE--------DDQTSSKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEER 894
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-207 |
1.15e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 60.55 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 6 SLQI-----RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLkneisadggsytfpgswqlawvnqetpalpqAA 80
Cdd:COG1118 2 SIEVrniskRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII-------------------------------AG 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 LEY------VIDGdreyRQLEAQLHdANERNDG---------------QAIA---TIHGKLDAidawSIRSRAASLLH-- 134
Cdd:COG1118 51 LETpdsgriVLNG----RDLFTNLP-PRERRVGfvfqhyalfphmtvaENIAfglRVRPPSKA----EIRARVEELLElv 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 135 GL-GFSNE---QLerpvsdfSGGWRMRLNLAQALICRSDLLLLDEPTNHLDlDAVIW-LEKWL----KSYQGTLILISHD 205
Cdd:COG1118 122 QLeGLADRypsQL-------SGGQRQRVALARALAVEPEVLLLDEPFGALD-AKVRKeLRRWLrrlhDELGGTTVFVTHD 193
|
..
gi 446557484 206 RD 207
Cdd:COG1118 194 QE 195
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-227 |
1.20e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPGSWQLAWVNQ---ETPAL 76
Cdd:PLN03232 1242 LRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALfriveleKGRIMIDDCDVAKFGLTDLRRVLSiipQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 77 PQAALEYVIDGDREYRqlEAQLHDANERndgqaiatIHGKlDAIDAWSIrsraasllhGLgfsNEQLERPVSDFSGGWRM 156
Cdd:PLN03232 1322 FSGTVRFNIDPFSEHN--DADLWEALER--------AHIK-DVIDRNPF---------GL---DAEVSEGGENFSVGQRQ 1378
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 157 RLNLAQALICRSDLLLLDEPTNHLDL--DAVIW--LEKWLKSYqgTLILISHDrdfLDPIV--DKIIHIEQQSMFEY 227
Cdd:PLN03232 1379 LLSLARALLRRSKILVLDEATASVDVrtDSLIQrtIREEFKSC--TMLVIAHR---LNTIIdcDKILVLSSGQVLEY 1450
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-220 |
1.27e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 58.39 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 4 FSSLQIRrGVRVLLDNATATINPGQKVgLVGKNGCGKSTLLALLKNEISADggsyTFPGSWQLAWVNQ---ETPALPQAA 80
Cdd:cd03240 1 IDKLSIR-NIRSFHERSEIEFFSPLTL-IVGQNGAGKTTIIEALKYALTGE----LPPNSKGGAHDPKlirEGEVRAQVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 LEYVIDGDREYrqleaqlhdanerndgqaiaTIHGKLDAIdawsirsRAASLLHGlGFSNEQLERPVSDFSGGWRM---- 156
Cdd:cd03240 75 LAFENANGKKY--------------------TITRSLAIL-------ENVIFCHQ-GESNWPLLDMRGRCSGGEKVlasl 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 157 --RLNLAQALICRSDLLLLDEPTNHLDLDAV-IWLEKWLKSYQGT----LILISHDRDFLDPIvDKIIHIE 220
Cdd:cd03240 127 iiRLALAETFGSNCGILALDEPTTNLDEENIeESLAEIIEERKSQknfqLIVITHDEELVDAA-DHIYRVE 196
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
330-477 |
1.46e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.42 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 330 SIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGY----FAQHQLEYLRADES----PIQHLAR- 400
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL-LIDDHPLHFgdysYRSQRIRMIFQDPStslnPRQRISQi 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 401 ----------LAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470
Cdd:PRK15112 110 ldfplrlntdLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI 189
|
....*..
gi 446557484 471 EALIEFE 477
Cdd:PRK15112 190 NLMLELQ 196
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
17-204 |
1.63e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 60.56 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADG---GSYTfPGSW--QLAWVNQETP---------- 74
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLlrfydptSGRILIDGvdiRDLT-LESLrrQIGVVPQDTFlfsgtireni 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 75 --ALPQAALEYVIDGDReyrqlEAQLHDanerndgqAIATIHGKLDAIdawsIRSRAASLlhglgfsneqlerpvsdfSG 152
Cdd:COG1132 435 ryGRPDATDEEVEEAAK-----AAQAHE--------FIEALPDGYDTV----VGERGVNL------------------SG 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 153 GWRMRLNLAQALICRSDLLLLDEPTNHLDL--DAVIW--LEKWLKsyQGTLILISH 204
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTetEALIQeaLERLMK--GRTTIVIAH 533
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-205 |
1.74e-09 |
|
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: 58.40 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPqaal 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG--------KDITNLP---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 eyvidgdreyrqleaqlhdANERNDG---QAIA-----TIHG------KLDAIDAWSIRSRAASLLHGLGFSnEQLERPV 147
Cdd:cd03300 69 -------------------PHKRPVNtvfQNYAlfphlTVFEniafglRLKKLPKAEIKERVAEALDLVQLE-GYANRKP 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557484 148 SDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHD 205
Cdd:cd03300 129 SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHD 190
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
310-503 |
1.85e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 59.73 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------------- 369
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvthrsiqqrdicmv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 370 ----GLAKGIKLGYFAQHQLEYLRADESPIQHLARLApqeLEqkLRDyLGGFgfqGDKVTEEtrrFSGGEKARLVLALIV 445
Cdd:PRK11432 84 fqsyALFPHMSLGENVGYGLKMLGVPKEERKQRVKEA---LE--LVD-LAGF---EDRYVDQ---ISGGQQQRVALARAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 446 WQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVVVShdrhllrsttddLYLVHDR 503
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITS------------LYVTHDQ 197
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
24-205 |
1.92e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 58.25 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSwQLAWVNQETPALPQA-----------------ALEYVid 86
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQ-PLHQMDEEARAKLRAkhvgfvfqsfmliptlnALENV-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 87 gdreyrQLEAQLHDANERNDgqaiatihgkldaidawsiRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALIC 166
Cdd:PRK10584 110 ------ELPALLRGESSRQS-------------------RNGAKALLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446557484 167 RSDLLLLDEPTNHLD-------LDAVIWLEkwlKSYQGTLILISHD 205
Cdd:PRK10584 164 RPDVLFADEPTGNLDrqtgdkiADLLFSLN---REHGTTLILVTHD 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
313-491 |
1.93e-09 |
|
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: 57.86 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDR-----IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIklGYFAQ---HQ 384
Cdd:cd03250 1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--AYVSQepwIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 385 LEYLRADespIQHLARLAPQELEQKLR--------DYLGGfgfqGDK--VTEETRRFSGGEKARLVLALIVWQRPNLLLL 454
Cdd:cd03250 79 NGTIREN---ILFGKPFDEERYEKVIKacalepdlEILPD----GDLteIGEKGINLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446557484 455 DEPTNHLDLDMRQALTEALIEFEGAL----VVVSHDRHLLR 491
Cdd:cd03250 152 DDPLSAVDAHVGRHIFENCILGLLLNnktrILVTHQLQLLP 192
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-205 |
1.93e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 21 TATINPGQKVGLVGKNGCGKSTLLALLKNeISADGGSYTFPG----SWQL-------AWVNQETPALPQAAL-EYVidgd 88
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGqpleAWSAaelarhrAYLSQQQTPPFAMPVfQYL---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 89 reyrqleaQLHdaneRNDGQAIATIHGKLDAIdawsirsraASLLhGLGfsnEQLERPVSDFSGGWRMRLNLAQALI--- 165
Cdd:PRK03695 91 --------TLH----QPDKTRTEAVASALNEV---------AEAL-GLD---DKLGRSVNQLSGGEWQRVRLAAVVLqvw 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446557484 166 ----CRSDLLLLDEPTNHLDLDAVIWLEKWLK--SYQGTLILIS-HD 205
Cdd:PRK03695 146 pdinPAGQLLLLDEPMNSLDVAQQAALDRLLSelCQQGIAVVMSsHD 192
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
316-473 |
1.93e-09 |
|
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: 58.40 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 316 EKVSAGYGD--RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLE------- 386
Cdd:cd03251 4 KNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRI-LIDGHDVRDYTLASLRrqiglvs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 387 ---------------YLRADESP--IQHLARLA-PQELEQKLRDylggfGFQgDKVTEETRRFSGGEKARLVLALIVWQR 448
Cdd:cd03251 83 qdvflfndtvaeniaYGRPGATReeVEEAARAAnAHEFIMELPE-----GYD-TVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180
....*....|....*....|....*
gi 446557484 449 PNLLLLDEPTNHLDLDMRQALTEAL 473
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAAL 181
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-227 |
2.24e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.69 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLL-ALLK-----NEISADGGSYTfpgSWQLAWVNQETPALPQAAleYVIDG 87
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLsALLRllsteGEIQIDGVSWN---SVTLQTWRKAFGVIPQKV--FIFSG 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 88 drEYRQleaQLhDANERNDGQAIATIhgkldaIDAWSIRSRAASLLHGLGFsneQLERPVSDFSGGWRMRLNLAQALICR 167
Cdd:TIGR01271 1307 --TFRK---NL-DPYEQWSDEEIWKV------AEEVGLKSVIEQFPDKLDF---VLVDGGYVLSNGHKQLMCLARSILSK 1371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 168 SDLLLLDEPTNHLDLDAVIWLEKWLK-SYQGTLILISHDRdfLDPIVD--KIIHIEQQSMFEY 227
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVTLQIIRKTLKqSFSNCTVILSEHR--VEALLEcqQFLVIEGSSVKQY 1432
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
310-462 |
2.56e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 58.46 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 310 NPLLKMEKVSAGYGD--RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLgyfAQHQLEY 387
Cdd:PRK13632 5 SVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI-DGITI---SKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 388 LRA---------DESPIQHLA-----------RLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQ 447
Cdd:PRK13632 81 IRKkigiifqnpDNQFIGATVeddiafglenkKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170
....*....|....*
gi 446557484 448 RPNLLLLDEPTNHLD 462
Cdd:PRK13632 160 NPEIIIFDESTSMLD 174
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
323-500 |
2.73e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.66 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQ------LEYLRADE---S 393
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV-LIRGEPITKENIREvrkfvgLVFQNPDDqifS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 394 PI--QHLA------RLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
Cdd:PRK13652 94 PTveQDIAfgpinlGLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 446557484 466 RQAL---TEALIEFEGALVVVS-HDRHLLRSTTDDLYLV 500
Cdd:PRK13652 173 VKELidfLNDLPETYGMTVIFStHQLDLVPEMADYIYVM 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
313-487 |
2.90e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 59.33 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGIKLGYFAQH 383
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtdvsrlhARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 384 Q---------------LEYLRADESP---------------IQ--HLARLAPQELeqklrdylggfgfqgdkvteetrrf 431
Cdd:PRK10851 83 YalfrhmtvfdniafgLTVLPRRERPnaaaikakvtqllemVQlaHLADRYPAQL------------------------- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 432 SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI----EFEGALVVVSHDR 487
Cdd:PRK10851 138 SGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRqlheELKFTSVFVTHDQ 197
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-217 |
2.98e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.19 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG---SWQLAWVNQETPALPQAALEYVIDGDREYRQLEAQLH 99
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvSYKPQYIKADYEGTVRDLLSSITKDFYTHPYFKTEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 100 DANerndgqaiatihgKLDAIdawsirsraasllhglgfsneqLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNH 179
Cdd:cd03237 101 KPL-------------QIEQI----------------------LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446557484 180 LDLDAVIWLEKWLKSY----QGTLILISHDRDFLDPIVDKII 217
Cdd:cd03237 146 LDVEQRLMASKVIRRFaennEKTAFVVEHDIIMIDYLADRLI 187
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-187 |
3.55e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.41 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGS---WQLAWVNQETPALPQ-AALEYVIDGdREYR 92
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsilTNISDVHQNMGYCPQfDAIDDLLTG-REHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 93 QLEAQLHDANERndgqaiatihgKLDAIDAWSIRSRAASLLhglgfsneqLERPVSDFSGGWRMRLNLAQALICRSDLLL 172
Cdd:TIGR01257 2034 YLYARLRGVPAE-----------EIEKVANWSIQSLGLSLY---------ADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170
....*....|....*..
gi 446557484 173 LDEPTNHLDLDA--VIW 187
Cdd:TIGR01257 2094 LDEPTTGMDPQArrMLW 2110
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-182 |
4.02e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.91 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADG--------GSYTFPG-------SWQ 65
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGeplaaidAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 66 LAWV-----NQETPALPQAALEYVIDGdreyRQLEAQLHDANERNDGQAiatihgkldaidAWSIRSRA-ASLLHGlgfs 139
Cdd:PRK13547 81 LARLravlpQAAQPAFAFSAREIVLLG----RYPHARRAGALTHRDGEI------------AWQALALAgATALVG---- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446557484 140 neqleRPVSDFSGGWRMRLNLAQAL---------ICRSDLLLLDEPTNHLDL 182
Cdd:PRK13547 141 -----RDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-486 |
4.05e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.75 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLA-------------GELAPVSGEIGLAKGIKLgyfaQHQLEYLRA 390
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydskikvdGKVLYFGKDIFQIDAIKL----RKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 DESPIQHLA-----------------RLAPQELEQKLRDyLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLL 453
Cdd:PRK14246 98 QPNPFPHLSiydniayplkshgikekREIKKIVEECLRK-VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190
....*....|....*....|....*....|....*
gi 446557484 454 LDEPTNHLDLDMRQALTEALIEF--EGALVVVSHD 486
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELknEIAIVIVSHN 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-231 |
4.36e-09 |
|
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: 59.37 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGV-RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----SWQLAWVNQETPAL 76
Cdd:TIGR01193 474 IVINDVSYSYGYgSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 77 PQAAleYVIDGDreyrQLEAQLHDANERndgqaiATIHGKLDAIDAWSIRSRAASLLHGLGFSneqLERPVSDFSGGWRM 156
Cdd:TIGR01193 554 PQEP--YIFSGS----ILENLLLGAKEN------VSQDEIWAACEIAEIKDDIENMPLGYQTE---LSEEGSSISGGQKQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 157 RLNLAQALICRSDLLLLDEPTNHLDL--DAVIwLEKWLKSYQGTLILISHdRDFLDPIVDKIIHIEQQSMFEyTGNY 231
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDTitEKKI-VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIE-QGSH 692
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
304-506 |
4.65e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 59.35 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 304 APESLpNPLLKMEKVSAGY---GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI----- 375
Cdd:TIGR00958 471 APLNL-EGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV-LLDGVplvqy 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 376 -------KLGYFAQHQLEYLRADESPIQHLARLAPQE------LEQKLRDYLGGFGFQGDKVTEETRRF-SGGEKARLVL 441
Cdd:TIGR00958 549 dhhylhrQVALVGQEPVLFSGSVRENIAYGLTDTPDEeimaaaKAANAHDFIMEFPNGYDTEVGEKGSQlSGGQKQRIAI 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446557484 442 ALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKVE 506
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
326-511 |
5.31e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 59.38 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLaGELAPVSGEIgLAKGIKLGYFAQHQLEY-----LRAD----ESPIQ 396
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYGGR-LTKPAKGKLFYVPQRPYmtlgtLRDQiiypDSSED 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 397 HLAR-LAPQELEQ-----KLRDYL---GGFgfqgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
Cdd:TIGR00954 544 MKRRgLSDKDLEQildnvQLTHILereGGW----SAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG 619
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446557484 468 ALTEALIEFEGALVVVSHDRHLLRSTTddlYLVHdrkvepFDGD 511
Cdd:TIGR00954 620 YMYRLCREFGITLFSVSHRKSLWKYHE---YLLY------MDGR 654
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
313-503 |
5.35e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.92 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYG-----DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA----------KGIK- 376
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhitpetgnKNLKk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 377 -------LGYFAQHQLEylradESPIQHLARLAP-------QELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLA 442
Cdd:PRK13641 83 lrkkvslVFQFPEAQLF-----ENTVLKDVEFGPknfgfseDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446557484 443 LIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGA---LVVVSHDRHLLRSTTDD-LYLVHDR 503
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDvLVLEHGK 222
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-462 |
5.48e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.86 E-value: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---------PGSWQLAW---VNQETPALPQA 79
Cdd:PRK10762 16 GVKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgkevtfngPKSSQEAGigiIHQELNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 80 ALEYVIDGDREYRqleaqlhdanerndgqaiatihGKLDAIDAWSIRSRAASLLHGLGFSNEQlERPVSDFSGGWRMRLN 159
Cdd:PRK10762 95 TIAENIFLGREFV----------------------NRFGRIDWKKMYAEADKLLARLNLRFSS-DKLVGELSIGEQQMVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 160 LAQALICRSDLLLLDEPTNHL------DLDAVIwleKWLKSyQGTLIL-ISHDRDFLDPIVDKIIhieqqsmfeytgnys 232
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALtdteteSLFRVI---RELKS-QGRGIVyISHRLKEIFEICDDVT--------------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 233 sfeVQRATRLAQQQAMYESQQERVahlqsyidrfrakatkakqaqsrIKML--ERMELIAPaHVDNPfrfsfrapeslPN 310
Cdd:PRK10762 213 ---VFRDGQFIAEREVADLTEDSL-----------------------IEMMvgRKLEDQYP-RLDKA-----------PG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PL-LKMEKVSaGYGdriiLDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI--------------GLAKGI 375
Cdd:PRK10762 255 EVrLKVDNLS-GPG----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVtldghevvtrspqdGLANGI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 376 K------------LGYFAQHQ-----LEYLRADESPIQHlarlapQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKAR 438
Cdd:PRK10762 330 VyisedrkrdglvLGMSVKENmsltaLRYFSRAGGSLKH------ADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQK 403
|
490 500
....*....|....*....|....
gi 446557484 439 LVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:PRK10762 404 VAIARGLMTRPKVLILDEPTRGVD 427
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-221 |
5.63e-09 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 58.20 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 26 PGQKV-GLVGKNGCGKSTLLALLKNEISADGGSYTFPGS-WQLAWVNQETPAlPQAALEYVIDgdreyrqlEAQL--HDA 101
Cdd:TIGR02142 21 PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtLFDSRKGIFLPP-EKRRIGYVFQ--------EARLfpHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 102 NERNdgqaiaTIHGKLDAiDAWSIRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:TIGR02142 92 VRGN------LRYGMKRA-RPSERRISFERVIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446557484 182 L---DAVI-WLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:TIGR02142 164 DprkYEILpYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLED 207
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
10-219 |
5.75e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 56.65 E-value: 5.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGS-----------WQLAWVNQeTPALpq 78
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrQQVSYCAQ-TPTL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 79 aaleyviDGDREYRQLeaqlhdanerndgqaiatihgkldaIDAWSIRSRA---ASLLHGL---GFSNEQLERPVSDFSG 152
Cdd:PRK10247 93 -------FGDTVYDNL-------------------------IFPWQIRNQQpdpAIFLDDLerfALPDTILTKNIAELSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 153 GWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY---QGTLIL-ISHDRDFLDPiVDKIIHI 219
Cdd:PRK10247 141 GEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvreQNIAVLwVTHDKDEINH-ADKVITL 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
17-207 |
5.98e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.31 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLkneisadgGSYTFPGSWQLAWVNQETPALPqaalEYVIDGDREYRQLEA 96
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRML--------AGFEQPTAGQIMLDGVDLSHVP----PYQRPINMMFQSYAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 97 QLHDANERNDGQAIatihgKLDAIDAWSIRSRAASLLhGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
Cdd:PRK11607 103 FPHMTVEQNIAFGL-----KQDKLPKAEIASRVNEML-GLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 446557484 177 TNHLD--------LDAVIWLEKwlksYQGTLILISHDRD 207
Cdd:PRK11607 177 MGALDkklrdrmqLEVVDILER----VGVTCVMVTHDQE 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-263 |
7.11e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.05 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQET---PALP 77
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLyldTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 78 QAALEYVidgdreyrqleaQLHDANERNDgqaiatihgKLDAIDawsiRSRAASLLhglgfsneqlERPVSDFSGGWRMR 157
Cdd:PRK09544 84 LTVNRFL------------RLRPGTKKED---------ILPALK----RVQAGHLI----------DAPMQKLSGGETQR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTL----ILISHDRDFLDPIVDKII----HIEQQSMFEYTG 229
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcavLMVSHDLHLVMAKTDEVLclnhHICCSGTPEVVS 208
|
250 260 270
....*....|....*....|....*....|....
gi 446557484 230 NYSSFEVQRATRLAQQQAMYESQQERVAHLQSYI 263
Cdd:PRK09544 209 LHPEFISMFGPRGAEQLGIYRHHHNHRHDLQGRI 242
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
325-462 |
7.30e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.02 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQleylRAdespiQHLARL--- 401
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID-GKDVTKLPEYK----RA-----KYIGRVfqd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 402 -----AP-------------------------QELEQKLRDYLGGFGfQG--DKVTEETRRFSGGEkaRLVLALI--VWQ 447
Cdd:COG1101 89 pmmgtAPsmtieenlalayrrgkrrglrrgltKKRRELFRELLATLG-LGleNRLDTKVGLLSGGQ--RQALSLLmaTLT 165
|
170
....*....|....*
gi 446557484 448 RPNLLLLDEPTNHLD 462
Cdd:COG1101 166 KPKLLLLDEHTAALD 180
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
313-486 |
8.10e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 57.78 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEYLRADE 392
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI---------LIGGRDVTDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 SPI----Q------HL------------ARLAPQELEQK---------LRDYLGgfgfqgdkvteetRR---FSGGEKAR 438
Cdd:COG3839 75 RNIamvfQsyalypHMtvyeniafplklRKVPKAEIDRRvreaaellgLEDLLD-------------RKpkqLSGGQRQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446557484 439 lVlAL---IVwQRPNLLLLDEPTNHLD----LDMRQALTEALIEFEGALVVVSHD 486
Cdd:COG3839 142 -V-ALgraLV-REPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-207 |
8.16e-09 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 56.32 E-value: 8.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKN-------EISADGGSYTFPGSWQLAwVNQETPALPQAALEYVIdgdr 89
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlaqptsgGVILEGKQITEPGPDRMV-VFQNYSLLPWLTVRENI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 90 eYRQLEAQLHDANeRNDGQAIATIHgkldaIDawsirsraaslLHGLGfsnEQLERPVSDFSGGWRMRLNLAQALICRSD 169
Cdd:TIGR01184 76 -ALAVDRVLPDLS-KSERRAIVEEH-----IA-----------LVGLT---EAADKRPGQLSGGMKQRVAIARALSIRPK 134
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446557484 170 LLLLDEPTNHLD-LDAVIWLEKWLKSYQG---TLILISHDRD 207
Cdd:TIGR01184 135 VLLLDEPFGALDaLTRGNLQEELMQIWEEhrvTVLMVTHDVD 176
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-207 |
9.06e-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: 57.80 E-value: 9.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpgswqlawvnqetpalpqaa 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL-------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 leyvidGDREYRQLEAqlhdaNERNdgqaIATI--------H---------G-KLDAIDAWSIRSRAASLLH--GLGfsn 140
Cdd:COG3842 65 ------DGRDVTGLPP-----EKRN----VGMVfqdyalfpHltvaenvafGlRMRGVPKAEIRARVAELLElvGLE--- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 141 EQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQ----GTLILISHDRD 207
Cdd:COG3842 127 GLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQrelgITFIYVTHDQE 197
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
291-503 |
1.07e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.87 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 291 PAHVDNPFrFSFRAPESLPNPLLK-MEKVSAGYGdRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
Cdd:TIGR01257 910 PEGINDSF-FERELPGLVPGVCVKnLVKIFEPSG-RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTV 987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 370 GLA-KGIK---------LGYFAQHQL--EYLRADESpIQHLARL-------APQELEQKLRDYlggfGFQgDKVTEETRR 430
Cdd:TIGR01257 988 LVGgKDIEtnldavrqsLGMCPQHNIlfHHLTVAEH-ILFYAQLkgrsweeAQLEMEAMLEDT----GLH-HKRNEEAQD 1061
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 431 FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVVVSHDRHLlrsttDDLYLVHDR 503
Cdd:TIGR01257 1062 LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHM-----DEADLLGDR 1129
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
308-458 |
1.11e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.04 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 308 LPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKLGYFAQHQLE 386
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFdGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 387 YLRADESPIQHLARLAPQE-------------LEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLL 453
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEEnlamggffaerdqFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
....*
gi 446557484 454 LDEPT 458
Cdd:PRK11614 161 LDEPS 165
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
12-216 |
1.16e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.02 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLALLkneisadGGSYTFpGSWQlawvnqetpalpqaaLEYVIDGDrey 91
Cdd:PRK13549 17 GVKAL-DNVSLKVRAGEIVSLCGENGAGKSTLMKVL-------SGVYPH-GTYE---------------GEIIFEGE--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 92 rqleaQLHDANERNDGQA-IATIHGKL---------------------DAIDAWSIRSRAASLLHGLGFsNEQLERPVSD 149
Cdd:PRK13549 70 -----ELQASNIRDTERAgIAIIHQELalvkelsvleniflgneitpgGIMDYDAMYLRAQKLLAQLKL-DINPATPVGN 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHL-DLDAVIWLE--KWLKSYQGTLILISHDRDFLDPIVDKI 216
Cdd:PRK13549 144 LGLGQQQLVEIAKALNKQARLLILDEPTASLtESETAVLLDiiRDLKAHGIACIYISHKLNEVKAISDTI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-221 |
1.21e-08 |
|
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: 56.05 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQAALeyvidgdR 89
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDG--------TDLTLLSGKEL-------R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 90 EYRQ----LEAQLHDANERNDGQAIA---TIHGKLDAidawSIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQ 162
Cdd:cd03258 79 KARRrigmIFQHFNLLSSRTVFENVAlplEIAGVPKA----EIEERVLELLELVGLEDKADAYP-AQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 163 ALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQG-TLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03258 154 ALANNPKVLLCDEATSALDpetTQSILALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
304-473 |
1.31e-08 |
|
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: 55.94 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 304 APESLPNpLLKMEKVSAGY---GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIklgy 379
Cdd:cd03248 4 APDHLKG-IVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdGKPI---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 380 fAQHQLEYLRADESPIQHlarlAPQELEQKLRDYLgGFGFQG---DKVTEETRR------------------------FS 432
Cdd:cd03248 79 -SQYEHKYLHSKVSLVGQ----EPVLFARSLQDNI-AYGLQScsfECVKEAAQKahahsfiselasgydtevgekgsqLS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446557484 433 GGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
Cdd:cd03248 153 GGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQAL 193
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-221 |
1.34e-08 |
|
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: 55.69 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSY-TFPGSW---QLAWVNQETPALPQAALEYVI 85
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLmrfydpqKGQILIDGIDIrDISRKSlrsMIGVVLQDTFLFSGTIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 86 DGDREyrqleaqlhdaNERNDGQAIATIHGKLDAIDawsirsraaSLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQALI 165
Cdd:cd03254 99 LGRPN-----------ATDEEVIEAAKEAGAHDFIM---------KLPNGY---DTVLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557484 166 CRSDLLLLDEPTNHLD--LDAVIW--LEKWLKsyQGTLILISHDrdfLDPIV--DKIIHIEQ 221
Cdd:cd03254 156 RDPKILILDEATSNIDteTEKLIQeaLEKLMK--GRTSIIIAHR---LSTIKnaDKILVLDD 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
311-371 |
1.37e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.49 E-value: 1.37e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI 64
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-225 |
1.42e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 55.92 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLldNATATINPGQKVGLVGKNGCGKSTLLALLkneisadgGSYTFPGSWQLAWVNQETPALPQAA 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLI--------AGFLPPDSGRILWNGQDLTALPPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 leyvidgdreyRQL-----EAQL--HDANERNDGQAIATiHGKLDAIDawsiRSRAASLLHGLGFSnEQLERPVSDFSGG 153
Cdd:COG3840 71 -----------RPVsmlfqENNLfpHLTVAQNIGLGLRP-GLKLTAEQ----RAQVEQALERVGLA-GLLDRLPGQLSGG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 154 WRMRLNLAQALICRSDLLLLDEPTNHLD-------LDaviWLEKWLKSYQGTLILISHDrdfldpiVDKIIHIEQQSMF 225
Cdd:COG3840 134 QRQRVALARCLVRKRPILLLDEPFSALDpalrqemLD---LVDELCRERGLTVLMVTHD-------PEDAARIADRVLL 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
306-369 |
1.57e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 1.57e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557484 306 ESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
Cdd:PRK15439 5 DTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL 68
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
323-462 |
1.71e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGY----FAQhQLEYL------RADE 392
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV-LWQGEPIRRqrdeYHQ-DLLYLghqpgiKTEL 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446557484 393 SPIQHL---ARLAPQELEQKLRDYLGGFGFQGdkvTEE--TRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:PRK13538 90 TALENLrfyQRLHGPGDDEALWEALAQVGLAG---FEDvpVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
327-489 |
1.72e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.56 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEYLRADESP--------IQHL 398
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLV-GQPLHQMDEEARAKLRAKHVGfvfqsfmlIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 399 ARLAPQELEQKLR------------DYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
Cdd:PRK10584 104 NALENVELPALLRgessrqsrngakALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180
....*....|....*....|....*..
gi 446557484 467 QALTEALI----EFEGALVVVSHDRHL 489
Cdd:PRK10584 183 DKIADLLFslnrEHGTTLILVTHDLQL 209
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-205 |
1.84e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 56.63 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgswqlawVNQETPALPQAALEY---VIDGDREyrqleaQLH 99
Cdd:COG4586 44 TIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR---------VLGYVPFKRRKEFARrigVVFGQRS------QLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 100 ------DANErndgqaiatIHGKLDAIDAWSIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLL 173
Cdd:COG4586 109 wdlpaiDSFR---------LLKAIYRIPDAEYKKRLDELVELLDLG-ELLDTPVRQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 446557484 174 DEPTnhLDLDAVI------WLEKWLKSYQGTLILISHD 205
Cdd:COG4586 179 DEPT--IGLDVVSkeaireFLKEYNRERGTTILLTSHD 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-221 |
1.84e-08 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 55.19 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQAaleyvidgDREYRQL--EAQL-- 98
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--------VDVTAAPPA--------DRPVSMLfqENNLfa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 99 HDANERNDGQAIATiHGKLDAIDawsiRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTN 178
Cdd:cd03298 84 HLTVEQNVGLGLSP-GLKLTAED----RQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446557484 179 HLD-------LDAVIWLEkwlKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03298 158 ALDpalraemLDLVLDLH---AETKMTVLMVTHQPEDAKRLAQRVVFLDN 204
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
315-485 |
2.08e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.42 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 315 MEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLAKGIKL--- 377
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldgrplsslshsVLRQGVAMvqq 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 378 -------GYFAQHQLEYLRADESPIQHLARLAPQELEQKLRDYLGG-FGFQGDkvteetrRFSGGEKARLVLALIVWQRP 449
Cdd:PRK10790 423 dpvvladTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTpLGEQGN-------NLSVGQKQLLALARVLVQTP 495
|
170 180 190
....*....|....*....|....*....|....*...
gi 446557484 450 NLLLLDEPTNHLDLDMRQALTEAL--IEFEGALVVVSH 485
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALaaVREHTTLVVIAH 533
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
328-485 |
2.10e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.91 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA----------KGIK--------LGYFAQHQLeylr 389
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtlitstsknKDIKqirkkvglVFQFPESQL---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 390 ADESPIQHLArLAPQ-------ELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:PRK13649 99 FEETVLKDVA-FGPQnfgvsqeEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180
....*....|....*....|....*.
gi 446557484 463 LDMRQALTEALIEFEGA---LVVVSH 485
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSgmtIVLVTH 203
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
323-486 |
2.17e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.27 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPvSGEI-GLAK--GIKLGYFAQHQLEYLRADE------S 393
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAA-NGRIgGSATfnGREILNLPEKELNKLRAEQismifqD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 394 PIQHL---ARLAPQELE-QKLRDYLGGF-GFQGD-------KVTEETRR-------FSGGEKARLVLALIVWQRPNLLLL 454
Cdd:PRK09473 106 PMTSLnpyMRVGEQLMEvLMLHKGMSKAeAFEESvrmldavKMPEARKRmkmypheFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 446557484 455 DEPTNHLDLDMrQA-----LTEALIEFEGALVVVSHD 486
Cdd:PRK09473 186 DEPTTALDVTV-QAqimtlLNELKREFNTAIIMITHD 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-277 |
2.24e-08 |
|
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: 57.65 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 11 RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSwqLAWVNQetpalpQAALEYviDGDRE 90
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQ------QAWIQN--DSLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 91 YRQLEAQLHDANERNDGQAIATIhGKLDAIDAwsirsraasllhglGFSNEQLERPVsDFSGGWRMRLNLAQALICRSDL 170
Cdd:TIGR00957 718 NILFGKALNEKYYQQVLEACALL-PDLEILPS--------------GDRTEIGEKGV-NLSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 171 LLLDEPTNHLD-------LDAVIWLEKWLKSyqGTLILISHDRDFLdPIVDKIIHIEQQSMFEyTGNYSSFeVQRATRLA 243
Cdd:TIGR00957 782 YLFDDPLSAVDahvgkhiFEHVIGPEGVLKN--KTRILVTHGISYL-PQVDVIIVMSGGKISE-MGSYQEL-LQRDGAFA 856
|
250 260 270
....*....|....*....|....*....|....
gi 446557484 244 QQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQ 277
Cdd:TIGR00957 857 EFLRTYAPDEQQGHLEDSWTALVSGEGKEAKLIE 890
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-221 |
3.13e-08 |
|
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: 54.46 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLL---ALLKN----EISADGGSYTFPGSwQLAWVNQETP 74
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLrciNLLEEpdsgTIIIDGLKLTDDKK-NINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 75 ALPQ--------AALEYVIDGDREYRqleaqlhdanerndgqaiatihgKLDAIDAwsiRSRAASLLHGLGFSNEQLERP 146
Cdd:cd03262 80 MVFQqfnlfphlTVLENITLAPIKVK-----------------------GMSKAEA---EERALELLEKVGLADKADAYP 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 147 vSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03262 134 -AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-220 |
3.14e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 54.41 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADggsYTFPGSWQLAwvNQETPALPQaa 80
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPA---FSASGEVLLN--GRRLTALPA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 leyvidgdrEYRQL-----EAQLHD------------ANERNDGQAIATIHGKLDAIDawsirsraaslLHGLGfsneql 143
Cdd:COG4136 74 ---------EQRRIgilfqDDLLFPhlsvgenlafalPPTIGRAQRRARVEQALEEAG-----------LAGFA------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 144 ERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKW----LKSYQGTLILISHDRDflD-PIVDKIIH 218
Cdd:COG4136 128 DRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDEE--DaPAAGRVLD 205
|
..
gi 446557484 219 IE 220
Cdd:COG4136 206 LG 207
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
324-473 |
3.15e-08 |
|
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: 54.85 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-------------------------------A 372
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdgvdirdlnlrwlrsqiglvsqepvlfdgtiA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 373 KGIKLGYFAQHQLEYLRAdespiqhlARLAP-----QELEQKLRDYLGGFGFQgdkvteetrrFSGGEKARLVLALIVWQ 447
Cdd:cd03249 95 ENIRYGKPDATDEEVEEA--------AKKANihdfiMSLPDGYDTLVGERGSQ----------LSGGQKQRIAIARALLR 156
|
170 180
....*....|....*....|....*.
gi 446557484 448 RPNLLLLDEPTNHLDLDMRQALTEAL 473
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEAL 182
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
316-506 |
3.32e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.51 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 316 EKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLAKGIKL---- 377
Cdd:PRK13657 338 DDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIlidgtdirtvtraSLRRNIAVvfqd 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 378 -GYFAQHQLEYLR---ADESPIQ-HLARLAPQELEQKLRDyLGGFGFQgdkVTEETRRFSGGEKARLVLALIVWQRPNLL 452
Cdd:PRK13657 418 aGLFNRSIEDNIRvgrPDATDEEmRAAAERAQAHDFIERK-PDGYDTV---VGERGRQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 453 LLDEPTNHLDldmrqALTEALIefEGALVVVSHDR------HLL---RSTTDDLYLVHDRKVE 506
Cdd:PRK13657 494 ILDEATSALD-----VETEAKV--KAALDELMKGRttfiiaHRLstvRNADRILVFDNGRVVE 549
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-207 |
3.35e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.48 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpgsWQLAWVNQETPALPQAALEYVIDGDREYRQL-- 94
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW---IFKDEKNKKKTKEKEKVLEKLVIQKTRFKKIkk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 95 ---------------EAQLHDANERNDgqaiaTIHGKLD-AIDAWSIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRL 158
Cdd:PRK13651 100 ikeirrrvgvvfqfaEYQLFEQTIEKD-----IIFGPVSmGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446557484 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY--QG-TLILISHDRD 207
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnkQGkTIILVTHDLD 226
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
338-501 |
3.56e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 53.73 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYfaqhqleylradespiqhlarlAPQELEqklrdylggf 417
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVY----------------------KPQYID---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 418 gfqgdkvteetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEF----EGALVVVSHDRHLLRST 493
Cdd:cd03222 72 -------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYL 138
|
....*...
gi 446557484 494 TDDLYLVH 501
Cdd:cd03222 139 SDRIHVFE 146
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
313-487 |
3.75e-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: 56.37 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQL------ 385
Cdd:COG5265 358 VRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRI-LIDGQDIRDVTQASLraaigi 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 386 ----------------EYLRADESP--IQHLARLApqeleqklrdYLGGF------GFQgDKVTEETRRFSGGEKARLVL 441
Cdd:COG5265 437 vpqdtvlfndtiayniAYGRPDASEeeVEAAARAA----------QIHDFieslpdGYD-TRVGERGLKLSGGEKQRVAI 505
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446557484 442 ALIVWQRPNLLLLDEPTNHLDldmrqALTEALIefEGALVVVSHDR 487
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALD-----SRTERAI--QAALREVARGR 544
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
328-486 |
3.90e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.13 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGI------------KLGYFAQH---QLEYLRADE 392
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVM-GRevnaenekwvrsKVGLVFQDpddQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 S----PIQhlARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQA 468
Cdd:PRK13647 100 DvafgPVN--MGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180
....*....|....*....|.
gi 446557484 469 LTEALIEF--EGALVVVS-HD 486
Cdd:PRK13647 177 LMEILDRLhnQGKTVIVAtHD 197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
323-487 |
4.01e-08 |
|
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: 56.84 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAgELAPVSGEIGLaKGIK------------LGYFAQHQLEYLRA 390
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQI-DGVSwnsvtlqtwrkaFGVIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 DESPIQHLARLAPQEL-----EQKLRDYLGGFGFQGDKVTEETRR-FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
Cdd:TIGR01271 1308 FRKNLDPYEQWSDEEIwkvaeEVGLKSVIEQFPDKLDFVLVDGGYvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPV 1387
|
170 180
....*....|....*....|....
gi 446557484 465 MRQALTEALIE-FEGALVVVSHDR 487
Cdd:TIGR01271 1388 TLQIIRKTLKQsFSNCTVILSEHR 1411
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
331-456 |
4.22e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 56.34 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 331 IKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGyfaQHQLEYLRADESPI-------QHLARLAP 403
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI-LLDGQPVT---ADNREAYRQLFSAVfsdfhlfDRLLGLDG 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 404 QELEQKLRDYLGGFGFQgDKVTEETRRF-----SGGEKARlvLALIV-W--QRPnLLLLDE 456
Cdd:COG4615 427 EADPARARELLERLELD-HKVSVEDGRFsttdlSQGQRKR--LALLVaLleDRP-ILVFDE 483
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
313-486 |
4.28e-08 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 54.61 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 313 LKMEKVSAGYGD-RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI------------KLGY 379
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEI-FIDGEdireqdpvelrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 380 FAQ------H-----------QLEYL-------RADEspIQHLARLAPQELEQKLRDYLggfgfqgdkvteetrrfSGGE 435
Cdd:cd03295 80 VIQqiglfpHmtveenialvpKLLKWpkekireRADE--LLALVGLDPAEFADRYPHEL-----------------SGGQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446557484 436 KARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGAL----VVVSHD 486
Cdd:cd03295 141 QQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgktiVFVTHD 195
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-217 |
4.47e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.05 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLL----ALLK---NEISADGGSYTfPGSWQLAWVNQETPAL---PQAAL-E 82
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIqhlnGLLKptsGKIIIDGVDIT-DKKVKLSDIRKKVGLVfqyPEYQLfE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 83 YVIDGDREYrqleaqlhdaNERNDGQAIATIHgkldaidawsIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQ 162
Cdd:PRK13637 99 ETIEKDIAF----------GPINLGLSEEEIE----------NRVKRAMNIVGLDY-EDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 163 ALICRSDLLLLDEPTNHLD---LDAVIWLEKWL-KSYQGTLILISHDRDFLDPIVDKII 217
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDpkgRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRII 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-181 |
7.63e-08 |
|
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: 53.77 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnqetpalpQAALEYVIDGDREYRQLEA 96
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG---------------HDVRDYTLASLRRQIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 97 Q---LHDANERNDgqaIAtiHGKLDAIDAwSIRsRAASLLHGLGF---SNEQLERPVSD----FSGGWRMRLNLAQALIC 166
Cdd:cd03251 83 QdvfLFNDTVAEN---IA--YGRPGATRE-EVE-EAARAANAHEFimeLPEGYDTVIGErgvkLSGGQRQRIAIARALLK 155
|
170
....*....|....*
gi 446557484 167 RSDLLLLDEPTNHLD 181
Cdd:cd03251 156 DPPILILDEATSALD 170
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
297-512 |
7.66e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.36 E-value: 7.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 297 PFRFSFRAPESLPN-PLLKMEKVSAGYGDR-IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKG 374
Cdd:PRK10522 306 PYKAEFPRPQAFPDwQTLELRNVTFAYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI-LLDG 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 375 IKLGyfAQHQLEYLR------ADESPIQHLarLAPQ---ELEQKLRDYLGGFGFQgDKVTEE-----TRRFSGGEKARLV 440
Cdd:PRK10522 385 KPVT--AEQPEDYRKlfsavfTDFHLFDQL--LGPEgkpANPALVEKWLERLKMA-HKLELEdgrisNLKLSKGQKKRLA 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 441 LALIVWQRPNLLLLDEPTNHLDLDMR----QALTEALIEFEGALVVVSHdrhllrsttDDLYLVH-DRKVEPFDGDL 512
Cdd:PRK10522 460 LLLALAEERDILLLDEWAADQDPHFRrefyQVLLPLLQEMGKTIFAISH---------DDHYFIHaDRLLEMRNGQL 527
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
312-502 |
7.71e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.22 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAP---VSGEIGL------AKGIK----LG 378
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPhgtWDGEIYWsgsplkASNIRdterAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 379 YFAQHQLEYLRADESPIQHL----------ARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQR 448
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIflgneitlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 449 PNLLLLDEPTNHLDLDMRQALTEALIEFEG---ALVVVSHDRHLLRSTTDDLYLVHD 502
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRD 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
327-502 |
9.18e-08 |
|
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: 55.69 E-value: 9.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKL---------GYFAQHQLEYLRADEspIQH 397
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFspqtswimpGTIKDNIIFGLSYDE--YRY 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 398 LARLAPQELEQKLRDYLggfgfQGDKVT--EETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA--- 472
Cdd:TIGR01271 519 TSVIKACQLEEDIALFP-----EKDKTVlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESclc 593
|
170 180 190
....*....|....*....|....*....|.
gi 446557484 473 -LIEFEGALVVVSHDRHLLRSttDDLYLVHD 502
Cdd:TIGR01271 594 kLMSNKTRILVTSKLEHLKKA--DKILLLHE 622
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
323-462 |
9.48e-08 |
|
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: 52.88 E-value: 9.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE---------------------IGLAKGIKLGYFA 381
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRvllnggpldfqrdsiargllyLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 382 QHQLEYLRADESPIQHLARLApqeleqklRDYLGGFGfqgdkvTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
Cdd:cd03231 91 LENLRFWHADHSDEQVEEALA--------RVGLNGFE------DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
.
gi 446557484 462 D 462
Cdd:cd03231 157 D 157
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-227 |
9.65e-08 |
|
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: 52.80 E-value: 9.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQAALeyvidgdREYRQLEA 96
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG--------IDISTIPLEDL-------RSSLTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 97 QlhdanernDGQAIA-TIHGKLDAIDAWSIRSRAASLLHGLGFSNeqlerpvsdFSGGWRMRLNLAQALICRSDLLLLDE 175
Cdd:cd03369 89 Q--------DPTLFSgTIRSNLDPFDEYSDEEIYGALRVSEGGLN---------LSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 176 PTNHLDL--DAVIWlEKWLKSYQG-TLILISHD-RDFLDpiVDKIIHIEQQSMFEY 227
Cdd:cd03369 152 ATASIDYatDALIQ-KTIREEFTNsTILTIAHRlRTIID--YDKILVMDAGEVKEY 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
17-221 |
9.66e-08 |
|
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: 53.05 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETPALPQAALEYvidgdREYRQLE- 95
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERGLY-----PKMKVIDq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 96 ----AQLHDANERNdgqaiatihgkldaidawsIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
Cdd:cd03269 91 lvylAQLKGLKKEE-------------------ARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446557484 172 LLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLNK 203
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-230 |
1.02e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.86 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSyTFPGSWQLawvnqetPALPQAALEyVIDGDRE----YR 92
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDYAI-------PANLKKIKE-VKRLRKEiglvFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 93 QLEAQLHDANERNDgQAIATIHGKLDAIDAWSirsRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLL 172
Cdd:PRK13645 98 FPEYQLFQETIEKD-IAFGPVNLGENKQEAYK---KVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 173 LDEPTNHLD----LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII--H----IEQQSMFEYTGN 230
Cdd:PRK13645 174 LDEPTGGLDpkgeEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIvmHegkvISIGSPFEIFSN 241
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
310-486 |
1.10e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 53.65 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 310 NPLLKMEKVSAGYGD--RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP---------VSGEIGLAKGI--- 375
Cdd:PRK13640 3 DNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskitVDGITLTAKTVwdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 376 --KLG-YFAQHQLEYLRA---DESPIQHLARLAP-QELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQR 448
Cdd:PRK13640 83 reKVGiVFQNPDNQFVGAtvgDDVAFGLENRAVPrPEMIKIVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446557484 449 PNLLLLDEPTNHLDLDMRQALTEALIEF--EGALVVVS--HD 486
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLkkKNNLTVISitHD 203
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
311-495 |
1.25e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.50 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLaGELAPVSGEIGLAKgiKLGYFAQH------Q 384
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEG--RVEFFNQNiyerrvN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 385 LEYLRADESPIQHLARLAPQELEQKLRDYLGGFGFQ----------------------GDKVTEETRRFSGGEKARLVLA 442
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRpkleiddivesalkdadlwdeiKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 443 LIVWQRPNLLLLDEPTNHLD----LDMRQALTEALIEFEGALVVVSHDRHLLRSTTD 495
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-194 |
1.48e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 52.26 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQI------RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADG---GSYTFPGswqlaWVNQ 71
Cdd:cd03233 1 ASTLSWRNIsfttgkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNG-----IPYK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 72 ETPALPQAALEYVIDGDreyrqleaqLHDANerndgqaiATIHGKLDAidawSIRSRAASLLHGlgfsneqlerpvsdFS 151
Cdd:cd03233 76 EFAEKYPGEIIYVSEED---------VHFPT--------LTVRETLDF----ALRCKGNEFVRG--------------IS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446557484 152 GGWRMRLNLAQALICRSDLLLLDEPTNhlDLDAVIWLEkWLKS 194
Cdd:cd03233 121 GGERKRVSIAEALVSRASVLCWDNSTR--GLDSSTALE-ILKC 160
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
139-486 |
1.49e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 139 SNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTL----ILISHDRDFLDPIVD 214
Cdd:PRK10261 158 AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMsmgvIFITHDMGVVAEIAD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 215 KIIHIEQQSMFEyTGnySSFEVQRATRLAQQQAMYESQQERVAHLQSYIDRfRAKATKAKQAQSRIKMLERMELIAPAHV 294
Cdd:PRK10261 238 RVLVMYQGEAVE-TG--SVEQIFHAPQHPYTRALLAAVPQLGAMKGLDYPR-RFPLISLEHPAKQEPPIEQDTVVDGEPI 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 295 ----DNPFRFSFRApeSLPNPLLKmeKVSAgygdriiLDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG 370
Cdd:PRK10261 314 lqvrNLVTRFPLRS--GLLNRVTR--EVHA-------VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEII 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 371 LaKGIKLGYFAQHQLEYLRADespIQHL-----ARLAPQE-----LEQKLRDY---------------LGGFGFQGDKVT 425
Cdd:PRK10261 383 F-NGQRIDTLSPGKLQALRRD---IQFIfqdpyASLDPRQtvgdsIMEPLRVHgllpgkaaaarvawlLERVGLLPEHAW 458
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446557484 426 EETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI----EFEGALVVVSHD 486
Cdd:PRK10261 459 RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLdlqrDFGIAYLFISHD 523
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-181 |
1.61e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 52.78 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG------SWQLAWVNQETP 74
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpvegpGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 75 ALP-QAALEYVIDGdreyrqLEAQLHDANERndgqaiatihgkldaidawsiRSRAASLLHGLGFSNEQlERPVSDFSGG 153
Cdd:PRK11248 81 LLPwRNVQDNVAFG------LQLAGVEKMQR---------------------LEIAHQMLKKVGLEGAE-KRYIWQLSGG 132
|
170 180
....*....|....*....|....*...
gi 446557484 154 WRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-181 |
1.82e-07 |
|
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: 52.49 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGV--RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG--------SW---QLAW 68
Cdd:cd03252 1 ITFEHVRFRYKPdgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpAWlrrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 69 VNQETPALPQAALEYVIDGD----REYRQLEAQLHDANE--RNDGQAIATIHGKldaidawsirsRAASLlhglgfsneq 142
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADpgmsMERVIEAAKLAGAHDfiSELPEGYDTIVGE-----------QGAGL---------- 139
|
170 180 190
....*....|....*....|....*....|....*....
gi 446557484 143 lerpvsdfSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:cd03252 140 --------SGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
324-486 |
1.87e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.81 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLG----YFAQHQL---------EYLRA 390
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI-IIDGDLLTeenvWDIRHKIgmvfqnpdnQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 ----------DESPIQHlarlapQELEQKLRDYLGGFGFQGDKvTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
Cdd:PRK13650 98 tveddvafglENKGIPH------EEMKERVNEALELVGMQDFK-EREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190
....*....|....*....|....*....|
gi 446557484 461 LDLDMRQALTEAL--IEFEGALVVVS--HD 486
Cdd:PRK13650 171 LDPEGRLELIKTIkgIRDDYQMTVISitHD 200
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
328-523 |
2.02e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.09 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE--IG----------------LAKGIKLGY-FAQHQL--E 386
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtiVGdyaipanlkkikevkrLRKEIGLVFqFPEYQLfqE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 387 YLRADES--PIqHLARlAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
Cdd:PRK13645 107 TIEKDIAfgPV-NLGE-NKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 465 MRQALTEALI----EFEGALVVVSHDRHLLRSTTDDLYLVHDRKV----EPFdgDLEDYQQWLSDVQ 523
Cdd:PRK13645 185 GEEDFINLFErlnkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVisigSPF--EIFSNQELLTKIE 249
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
343-517 |
2.06e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 343 LLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIklGYFAQHQ-----------LEYLRADESPIQHLARLApqELEQKLR 411
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEISEGRVWAERSI--AYVPQQAwimnatvrgniLFFDEEDAARLADAVRVS--QLEADLA 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 412 DYLGGFGFQgdkVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALieFEGAL-----VVVSHD 486
Cdd:PTZ00243 767 QLGGGLETE---IGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEC--FLGALagktrVLATHQ 841
|
170 180 190
....*....|....*....|....*....|.
gi 446557484 487 RHLLrSTTDDLYLVHDRKVEpFDGDLEDYQQ 517
Cdd:PTZ00243 842 VHVV-PRADYVVALGDGRVE-FSGSSADFMR 870
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
315-495 |
2.12e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.44 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 315 MEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL------------AGELA-----PVSGEIGLAKGIK- 376
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITidtarSLSQQKGLIRQLRq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 377 -LGYFAQ------HQLEYLRADESPIQhLARLAPQELEQKLRDYLGGFGFQGdKVTEETRRFSGGEKARLVLALIVWQRP 449
Cdd:PRK11264 86 hVGFVFQnfnlfpHRTVLENIIEGPVI-VKGEPKEEATARARELLAKVGLAG-KETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446557484 450 NLLLLDEPTNHLDLDM-RQALT--EALIEFEGALVVVSHDRHLLRSTTD 495
Cdd:PRK11264 164 EVILFDEPTSALDPELvGEVLNtiRQLAQEKRTMVIVTHEMSFARDVAD 212
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-218 |
2.34e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 26 PGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQAALEYVidgdreYRQLEAQLHDANERN 105
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG--------QRIDTLSPGKLQAL------RRDIQFIFQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 106 D-----GQAIAT---IHGKLDAIDAwsiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPT 177
Cdd:PRK10261 415 DprqtvGDSIMEplrVHGLLPGKAA---AARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446557484 178 NHLDLD---AVIWLEKWLKSYQG-TLILISHDRdfldPIVDKIIH 218
Cdd:PRK10261 492 SALDVSirgQIINLLLDLQRDFGiAYLFISHDM----AVVERISH 532
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-205 |
2.34e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETPA----LPQAAl 81
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARriglLAQNA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 eyVIDGDREYRQLEAQlhdanERNDGQAIATIHGKLDAiDAWSIRSRAASLLHGLGFSneqlerpVSDFSGGWRMRLNLA 161
Cdd:PRK10253 91 --TTPGDITVQELVAR-----GRYPHQPLFTRWRKEDE-EAVTKAMQATGITHLADQS-------VDTLSGGQRQRAWIA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446557484 162 QALICRSDLLLLDEPTNHLDLDAVIWLEKWL------KSYqgTLILISHD 205
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLselnreKGY--TLAAVLHD 203
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
324-484 |
2.38e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.73 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGEL--APVSGEIgLAKGIKL--------GYFAQHQLEY--LRAD 391
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgNNFTGTI-LANNRKPtkqilkrtGFVTQDDILYphLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 392 ESPI-QHLARLaPQELEQKLRDYLG-------GFGFQGDKVTEET--RRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
Cdd:PLN03211 159 ETLVfCSLLRL-PKSLTKQEKILVAesviselGLTKCENTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180
....*....|....*....|....*
gi 446557484 462 DLD--MRQALTEALIEFEGALVVVS 484
Cdd:PLN03211 238 DATaaYRLVLTLGSLAQKGKTIVTS 262
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-204 |
2.43e-07 |
|
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: 52.09 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGS-----------WQLAWVNQEtPALPQ 78
Cdd:cd03248 23 TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhSKVSLVGQE-PVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 79 AALEyvidgdreyrqleaqlhdanernDGQAIATIHGKLDAIDAWSIRSRAASLLHGL--GFSNEQLERPvSDFSGGWRM 156
Cdd:cd03248 102 RSLQ-----------------------DNIAYGLQSCSFECVKEAAQKAHAHSFISELasGYDTEVGEKG-SQLSGGQKQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446557484 157 RLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLksYQG----TLILISH 204
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQAL--YDWperrTVLVIAH 207
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
327-502 |
2.50e-07 |
|
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: 52.55 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKL---------GYFAQHQLEYLRADEspIQH 397
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFssqfswimpGTIKENIIFGVSYDE--YRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 398 LARLAPQELEQKLRDYLggfgfQGDKVT--EETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA--- 472
Cdd:cd03291 130 KSVVKACQLEEDITKFP-----EKDNTVlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEScvc 204
|
170 180 190
....*....|....*....|....*....|.
gi 446557484 473 -LIEFEGALVVVSHDRHLLRSttDDLYLVHD 502
Cdd:cd03291 205 kLMANKTRILVTSKMEHLKKA--DKILILHE 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
326-473 |
2.51e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 53.70 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELaPVSGEIgLAKGIKLgyfAQHQLEYLRadespiQHLARLA--P 403
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSL-KINGIEL---RELDPESWR------KHLSWVGqnP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 404 QELEQKLRD---------------------YLGGFGFQGDK-----VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
Cdd:PRK11174 433 QLPHGTLRDnvllgnpdasdeqlqqalenaWVSEFLPLLPQgldtpIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170
....*....|....*.
gi 446557484 458 TNHLDLDMRQALTEAL 473
Cdd:PRK11174 513 TASLDAHSEQLVMQAL 528
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-485 |
2.59e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.22 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--ELAP---VSGEIGL-AKGIklgyFAQHQLEYLRADE--- 392
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPearVSGEVYLdGQDI----FKMDVIELRRRVQmvf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 ---SPIQHLA------------RLAP--QELEQKLRDYLggfgfQGDKVTEETR--------RFSGGEKARLVLALIVWQ 447
Cdd:PRK14247 89 qipNPIPNLSifenvalglklnRLVKskKELQERVRWAL-----EKAQLWDEVKdrldapagKLSGGQQQRLCIARALAF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446557484 448 RPNLLLLDEPTNHLDLDMRQALTEALIEF--EGALVVVSH 485
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELkkDMTIVLVTH 203
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-221 |
2.59e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.45 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 26 PGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgswqlawvnqetpalpqaaleYVIDGDREYRQLEAQLHdanern 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV------------------------IYIDGEDILEEVLDQLL------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 106 dgqaiatihgkldaidawsirsraasllhglgfsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---- 181
Cdd:smart00382 51 ----------------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDaeqe 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446557484 182 -----LDAVIWLEKWLKSYQGTLILISHDRDFLDP-----IVDKIIHIEQ 221
Cdd:smart00382 97 allllLEELRLLLLLKSEKNLTVILTTNDEKDLGPallrrRFDRRIVLLL 146
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
560-625 |
2.67e-07 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 47.85 E-value: 2.67e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 560 LRKEIARLEKEMEKLNAQLAQAEEKLGDSELYdqSRKAELTACLQQQASAKSGLEECEMAWLEAQE 625
Cdd:pfam16326 6 EQRELEELEAEIEKLEEEIAELEAQLADPELY--SDYEKLQELSAELEELEAELEELYERWEELEE 69
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
345-500 |
2.90e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.45 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 345 GRNGAGKSTLIKL----LAGELAPVSgeiglakgiklgYFAQHqleylraDESPIQHLARLAPQELEqkLRDYLGG---- 416
Cdd:cd03240 29 GQNGAGKTTIIEAlkyaLTGELPPNS------------KGGAH-------DPKLIREGEVRAQVKLA--FENANGKkyti 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 417 -----------FGFQGD--KVTEETR-RFSGGEKA------RLVLALIVWQRPNLLLLDEPTNHLDLD-MRQALTEALIE 475
Cdd:cd03240 88 trslailenviFCHQGEsnWPLLDMRgRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLAEIIEE 167
|
170 180
....*....|....*....|....*....
gi 446557484 476 FEGA----LVVVSHDRHLLRStTDDLYLV 500
Cdd:cd03240 168 RKSQknfqLIVITHDEELVDA-ADHIYRV 195
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-177 |
3.33e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.59 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALlkneisadggsytfpgswqLAWVNqetpALPQAALEyVIDGDr 89
Cdd:NF033858 10 RYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSL-------------------IAGAR----KIQQGRVE-VLGGD- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 90 eyrqleaqLHDANERND-GQAIA------------TI--------HGKLDAIDAWSIRSRAASLLHGLG---FsneqLER 145
Cdd:NF033858 65 --------MADARHRRAvCPRIAympqglgknlypTLsvfenldfFGRLFGQDAAERRRRIDELLRATGlapF----ADR 132
|
170 180 190
....*....|....*....|....*....|..
gi 446557484 146 PVSDFSGGWRMRLNLAQALICRSDLLLLDEPT 177
Cdd:NF033858 133 PAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-223 |
4.15e-07 |
|
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: 51.18 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGsytfpgswQLAWVNQETPALPQAALEYVIDGDREYRQLEA 96
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG--------KVHWSNKNESEPSFEATRSRNRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 97 QLHDAN-ERND--GQAIATIHGKLdAIDAWSIRSRAASLLHGlgFSNEQLERPVsDFSGGWRMRLNLAQALICRSDLLLL 173
Cdd:cd03290 89 WLLNATvEENItfGSPFNKQRYKA-VTDACSLQPDIDLLPFG--DQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446557484 174 DEPTNHLDL---DAVIW--LEKWLKSYQGTLILISHDRDFLdPIVDKIIHIEQQS 223
Cdd:cd03290 165 DDPFSALDIhlsDHLMQegILKFLQDDKRTLVLVTHKLQYL-PHADWIIAMKDGS 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-181 |
4.29e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.85 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---PGSWqlawvnQETPALPQAALEYVID 86
Cdd:PRK11701 15 LYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQL------RDLYALSEAERRRLLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 87 GDREY-RQLEAQlhdaNERNDGQAIATIHGKLDAIDA---WSIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQ 162
Cdd:PRK11701 89 TEWGFvHQHPRD----GLRMQVSAGGNIGERLMAVGArhyGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIAR 164
|
170
....*....|....*....
gi 446557484 163 ALICRSDLLLLDEPTNHLD 181
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLD 183
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-205 |
4.85e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.71 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----SW-------QLAWVNQETPALPQAAL- 81
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpleSWsskafarKVAYLPQQLPAAEGMTVr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 EYVIDGDREYRQLEAQLHDANERNDGQAIATIHGKLDAidawsirsraasllhglgfsneqlERPVSDFSGGWRMRLNLA 161
Cdd:PRK10575 104 ELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLA------------------------HRLVDSLSGGERQRAWIA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446557484 162 QALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQG-TLILISHD 205
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAhqvDVLALVHRLSQERGlTVIAVLHD 207
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-232 |
5.35e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.33 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL--KNEISADGGSYTFPGSWQLAWVNQ------- 71
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEdragegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 72 --------ETPALP-QAALEYVIDGDREYRQLEAqlhdanerndgqaiatihgkLDAIDAWSIRSRAASLLHglgFSNEQ 142
Cdd:PRK09580 81 fmafqypvEIPGVSnQFFLQTALNAVRSYRGQEP--------------------LDRFDFQDLMEEKIALLK---MPEDL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 143 LERPVS-DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIH 218
Cdd:PRK09580 138 LTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDgkrSFIIVTHYQRILDYIKPDYVH 217
|
250
....*....|....
gi 446557484 219 IEQQSMFEYTGNYS 232
Cdd:PRK09580 218 VLYQGRIVKSGDFT 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
322-517 |
5.51e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 51.17 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA------------KGI-----KLGY-FAQH 383
Cdd:COG4161 12 YGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAghqfdfsqkpseKAIrllrqKVGMvFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 384 QL-------EYLRadESPIQHL------ARLAPQELEQKLR--DYLGGFGFQgdkvteetrrFSGGEKARLVLALIVWQR 448
Cdd:COG4161 92 NLwphltvmENLI--EAPCKVLglskeqAREKAMKLLARLRltDKADRFPLH----------LSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 449 PNLLLLDEPTNHLDLDMRQALTEALIEFEG---ALVVVSHDRHLLRST-TDDLYLVHDRKVEpfDGDLEDYQQ 517
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIVTHEVEFARKVaSQVVYMEKGRIIE--QGDASHFTQ 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
316-467 |
5.57e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.82 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 316 EKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGelapvsgeiglAKGIKLGyfaqhQLEYLRADESPI 395
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG-----------ARKIQQG-----RVEVLGGDMADA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 396 QHLARLA------PQELEQKL------RDYLGGFG--FqGDKVTEETRR------------F--------SGGEKARLVL 441
Cdd:NF033858 69 RHRRAVCpriaymPQGLGKNLyptlsvFENLDFFGrlF-GQDAAERRRRidellratglapFadrpagklSGGMKQKLGL 147
|
170 180
....*....|....*....|....*....
gi 446557484 442 --ALIvwQRPNLLLLDEPTNHLD-LDMRQ 467
Cdd:NF033858 148 ccALI--HDPDLLILDEPTTGVDpLSRRQ 174
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
310-471 |
5.72e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.29 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 310 NPLLKMEKVSAGY-GDR-IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYF-----AQ 382
Cdd:PRK13648 5 NSIIVFKNVSFQYqSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI---------FYnnqaiTD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 383 HQLEYLRAD----------------------------ESPIQHLARLAPQELEQKlrDYLggfgfqgDKVTEETRRFSGG 434
Cdd:PRK13648 76 DNFEKLRKHigivfqnpdnqfvgsivkydvafglenhAVPYDEMHRRVSEALKQV--DML-------ERADYEPNALSGG 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 446557484 435 EKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTE 471
Cdd:PRK13648 147 QKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
322-369 |
5.76e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.33 E-value: 5.76e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446557484 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEI 58
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-205 |
5.76e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.89 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTL---LALLKNeisadggsytfPGSWQLAWVNQETPALPQAAleyvidgDREYRQ 93
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIET-----------PTGGELYYQGQDLLKADPEA-------QKLLRQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 94 lEAQL------HDANERNDGQAIAT----IHGKLDAIDAwsiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQA 163
Cdd:PRK11308 93 -KIQIvfqnpyGSLNPRKKVGQILEepllINTSLSAAER---REKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446557484 164 LICRSDLLLLDEPTNHLD-------LDAVIWLEKWLK-SYqgtlILISHD 205
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDvsvqaqvLNLMMDLQQELGlSY----VFISHD 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-176 |
7.21e-07 |
|
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: 50.62 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALP-----QAAL 81
Cdd:cd03218 6 LSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG--------QDITKLPmhkraRLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 EYVIDGDREYRQLEAqlhdanERNDGqAIATIHGKLDAIdawsIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLA 161
Cdd:cd03218 78 GYLPQEASIFRKLTV------EENIL-AVLEIRGLSKKE----REEKLEELLEEFHIT-HLRKSKASSLSGGERRRVEIA 145
|
170
....*....|....*
gi 446557484 162 QALICRSDLLLLDEP 176
Cdd:cd03218 146 RALATNPKFLLLDEP 160
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
323-462 |
8.20e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.93 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--ELAPVSGEIgLAKGIKLGYFAQHQLEYlradespIQHLAR 400
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEI-LINGRPLDKNFQRSTGY-------VEQQDV 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 401 LAPqelEQKLRdylggfgfqgdkvteETRRFSG-------GEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:cd03232 90 HSP---NLTVR---------------EALRFSAllrglsvEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
143-205 |
8.43e-07 |
|
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: 50.41 E-value: 8.43e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 143 LERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL----DAVIWLEKWLKSYQGTLILISHD 205
Cdd:cd03299 123 LNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVrtkeKLREELKKIRKEFGVTVLHVTHD 189
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
10-216 |
8.73e-07 |
|
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: 49.95 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSytfpgswqlawvnqetpalpqaaleyVIDGDR 89
Cdd:cd03301 9 RFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGR--------------------------IYIGGR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 90 EYRQLEAqlhdaNERNDG---------------QAIAtiHG-KLDAIDAWSIRSRAASLLHGLGFSNEqLERPVSDFSGG 153
Cdd:cd03301 63 DVTDLPP-----KDRDIAmvfqnyalyphmtvyDNIA--FGlKLRKVPKDEIDERVREVAELLQIEHL-LDRKPKQLSGG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 154 WRMRLNLAQALICRSDLLLLDEPTNHLD----LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKI 216
Cdd:cd03301 135 QRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRI 201
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-181 |
9.33e-07 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 49.86 E-value: 9.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 11 RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL--KNEISADGGSYTFPGSwqlawvnQETPALPQAALEYVidgd 88
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGR-------PLDKRSFRKIIGYV---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 89 reyRQleaqlHDanerndgqaiaTIHGKLDAIDAWSIrsraASLLHGLgfsneqlerpvsdfSGGWRMRLNLAQALICRS 168
Cdd:cd03213 88 ---PQ-----DD-----------ILHPTLTVRETLMF----AAKLRGL--------------SGGERKRVSIALELVSNP 130
|
170
....*....|...
gi 446557484 169 DLLLLDEPTNHLD 181
Cdd:cd03213 131 SLLFLDEPTSGLD 143
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-216 |
9.67e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.71 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnqetpalpqaaleyvidgdREYRQLEA 96
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN--------------------------INYNKLDH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 97 QLHDANerndgqAIATIHGKLDAIDAWSI-------------------------RSRAASLLHGLGFSNEqLERPVSDFS 151
Cdd:PRK09700 75 KLAAQL------GIGIIYQELSVIDELTVlenlyigrhltkkvcgvniidwremRVRAAMMLLRVGLKVD-LDEKVANLS 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 152 GGWRMRLNLAQALICRSDLLLLDEPTNHL---DLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKI 216
Cdd:PRK09700 148 ISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRY 215
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
323-563 |
9.76e-07 |
|
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: 50.62 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAgELAPVSGEIglakgiklgyfaqhQLEYLRADESPIQHLAR-- 400
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDI--------------QIDGVSWNSVPLQKWRKaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 401 -LAPQEL---EQKLRDYLGGFGFQGD----KVTEET------RRFSG---------------GEKARLVLALIVWQRPNL 451
Cdd:cd03289 80 gVIPQKVfifSGTFRKNLDPYGKWSDeeiwKVAEEVglksviEQFPGqldfvlvdggcvlshGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 452 LLLDEPTNHLDLDMRQALTEALIE-FEGALVVVSHDRHLLRSTTDDLYLVHDRKVEPFDgdleDYQQWLSdvQKQENQAD 530
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQaFADCTVILSEHRIEAMLECQRFLVIEENKVRQYD----SIQKLLN--EKSHFKQA 233
|
250 260 270
....*....|....*....|....*....|...
gi 446557484 531 EAPKENANSAQARKDQKRREaELRAQTQPLRKE 563
Cdd:cd03289 234 ISPSDRLKLFPRRNSSKSKR-KPRPQIQALQEE 265
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-220 |
9.79e-07 |
|
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: 49.07 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIRRGV-RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLkNEI-SADGGSYTFPGSWQLAWvnqetpaLPQA 79
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLwPWGSGRIGMPEGEDLLF-------LPQR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 80 AleYVIDGdreyrqleaqlhdanerndgqaiatihgkldaidawSIRsraasllhglgfsnEQLERPVSD-FSGGWRMRL 158
Cdd:cd03223 73 P--YLPLG------------------------------------TLR--------------EQLIYPWDDvLSGGEQQRL 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557484 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHdRDFLDPIVDKIIHIE 220
Cdd:cd03223 101 AFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
328-369 |
1.02e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 1.02e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI 61
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-181 |
1.10e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 8 QIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEIsaDGGSYT-------FPG---SWQ--LAWVNQETPA 75
Cdd:TIGR00956 770 KIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITggdrlvnGRPldsSFQrsIGYVQQQDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 76 LPQAALeyvidgdREYRQLEAQLHDANErndgqaiATIHGKLD----AIDAWSIRSRAASL--LHGLGFSNEQlerpvsd 149
Cdd:TIGR00956 848 LPTSTV-------RESLRFSAYLRQPKS-------VSKSEKMEyveeVIKLLEMESYADAVvgVPGEGLNVEQ------- 906
|
170 180 190
....*....|....*....|....*....|...
gi 446557484 150 fsggwRMRLNLAQALICRSDLLL-LDEPTNHLD 181
Cdd:TIGR00956 907 -----RKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
337-473 |
1.17e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.59 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 337 PGSRIGLLGRNGAGKSTLIKLLAGELAP---VSGEIGL------AKGIKL--GYFAQHQL--------EYL------RAD 391
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLngmpidAKEMRAisAYVQQDDLfiptltvrEHLmfqahlRMP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 392 ESPIQHLARLAPQELEQKL-----RDYLGGfgfQGDKVteetRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
Cdd:TIGR00955 130 RRVTKKEKRERVDEVLQALglrkcANTRIG---VPGRV----KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMA 202
|
....*..
gi 446557484 467 QALTEAL 473
Cdd:TIGR00955 203 YSVVQVL 209
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
328-620 |
1.17e-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: 51.87 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGiKLGYFAQH---QLEYLRAD------------E 392
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-KG-SVAYVPQQawiQNDSLRENilfgkalnekyyQ 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 393 SPIQHLARLAPQELeqklrdyLGGfgfqGDK--VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470
Cdd:TIGR00957 732 QVLEACALLPDLEI-------LPS----GDRteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 471 EALIEFEGAL-----VVVSHDRHLLrSTTDDLYLVHDRKVEPF---------DGDLEDY-QQWLSDVQKQENQADEAPKE 535
Cdd:TIGR00957 801 EHVIGPEGVLknktrILVTHGISYL-PQVDVIIVMSGGKISEMgsyqellqrDGAFAEFlRTYAPDEQQGHLEDSWTALV 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 536 NANSAQARKDQKRREAELRAQTQplrkeiarLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEE 615
Cdd:TIGR00957 880 SGEGKEAKLIENGMLVTDVVGKQ--------LQRQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQTGQVE 951
|
....*
gi 446557484 616 CEMAW 620
Cdd:TIGR00957 952 LSVYW 956
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
328-486 |
1.22e-06 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 50.87 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDsIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL--------AKGI-------KLGY-FAQHQL------ 385
Cdd:COG4148 16 LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdsARGIflpphrrRIGYvFQEARLfphlsv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 386 ----EY----LRADESP-----------IQHLARLAPQELeqklrdylggfgfqgdkvteetrrfSGGEKARLVL--ALI 444
Cdd:COG4148 95 rgnlLYgrkrAPRAERRisfdevvellgIGHLLDRRPATL-------------------------SGGERQRVAIgrALL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446557484 445 VwqRPNLLLLDEPTNHLDLDMRQALT---EALI-EFEGALVVVSHD 486
Cdd:COG4148 150 S--SPRLLLMDEPLAALDLARKAEILpylERLRdELDIPILYVSHS 193
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
325-485 |
1.25e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 50.40 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGI---------------KLGY---FAQHQLE 386
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkplrkKVGIvfqFPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 387 ylradESPIQHLARLAPQ-------ELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
Cdd:PRK13634 100 -----EETVEKDICFGPMnfgvseeDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190
....*....|....*....|....*....|
gi 446557484 460 HLDLDMRQALTEALIEF--EGAL--VVVSH 485
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLhkEKGLttVLVTH 204
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
328-493 |
1.29e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 50.47 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------------------------------AKG 374
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkekekvleklviqktrfkkikkIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 375 IK--LGY---FAQHQLeYLRADESPIQHLAR---LAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVW 446
Cdd:PRK13651 103 IRrrVGVvfqFAEYQL-FEQTIEKDIIFGPVsmgVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446557484 447 QRPNLLLLDEPTNHLD----LDMRQALTEaLIEFEGALVVVSHD-RHLLRST 493
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDpqgvKEILEIFDN-LNKQGKTIILVTHDlDNVLEWT 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-181 |
1.36e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 50.08 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPqaaleyvidgdrEYR- 92
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG--------KDVTKLP------------EYKr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 93 -------------------QLEAQLhdanerndgqAIATIHGK-------LDAIDAWSIRSRAASLlhGLGFSNeQLERP 146
Cdd:COG1101 79 akyigrvfqdpmmgtapsmTIEENL----------ALAYRRGKrrglrrgLTKKRRELFRELLATL--GLGLEN-RLDTK 145
|
170 180 190
....*....|....*....|....*....|....*
gi 446557484 147 VSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:COG1101 146 VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-205 |
1.50e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.15 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALPQAAL----- 81
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG--------ENIPAMSRSRLytvrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 82 ------------------EYVIDGDREYRQL-EAQLHdanerndgqaiATIHGKLDAIdawSIRSrAASLLhglgfsneq 142
Cdd:PRK11831 85 rmsmlfqsgalftdmnvfDNVAYPLREHTQLpAPLLH-----------STVMMKLEAV---GLRG-AAKLM--------- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 143 lerPvSDFSGGWRMRLNLAQALICRSDLLLLDEP---TNHLDLDAVIWLEKWLKSYQG-TLILISHD 205
Cdd:PRK11831 141 ---P-SELSGGMARRAALARAIALEPDLIMFDEPfvgQDPITMGVLVKLISELNSALGvTCVVVSHD 203
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
322-520 |
1.66e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 49.63 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA------------KGI-----KLGY-FAQH 383
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAgnhfdfsktpsdKAIrelrrNVGMvFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 384 QL-------EYL-------------RADESPIQHLARLapqeleqKLRDYLGGFGFQgdkvteetrrFSGGEKARLVLAL 443
Cdd:PRK11124 92 NLwphltvqQNLieapcrvlglskdQALARAEKLLERL-------RLKPYADRFPLH----------LSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 444 IVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEG---ALVVVSHDRHLLRST-TDDLYLVHDRKVEPFDGD------LE 513
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtgiTQVIVTHEVEVARKTaSRVVYMENGHIVEQGDAScftqpqTE 234
|
....*..
gi 446557484 514 DYQQWLS 520
Cdd:PRK11124 235 AFKNYLS 241
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-181 |
1.70e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 50.49 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLAL---LKN----EISADGGSYTFPGSWQ--LAWVNQETPALPQAA 80
Cdd:PRK11432 15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLvagLEKptegQIFIDGEDVTHRSIQQrdICMVFQSYALFPHMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 LeyvidGDreyrqleaqlhdanerNDGQAIatihgKLDAIDAWSIRSR---AASLLHGLGFSneqlERPVSDFSGGWRMR 157
Cdd:PRK11432 95 L-----GE----------------NVGYGL-----KMLGVPKEERKQRvkeALELVDLAGFE----DRYVDQISGGQQQR 144
|
170 180
....*....|....*....|....
gi 446557484 158 LNLAQALICRSDLLLLDEPTNHLD 181
Cdd:PRK11432 145 VALARALILKPKVLLFDEPLSNLD 168
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
311-360 |
1.83e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 1.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG 360
Cdd:PRK13549 4 YLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-226 |
2.04e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 49.78 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlAWVNQETPalpqaaleyvidgDREYRQL-- 94
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDD----ITITHKTK-------------DKYIRPVrk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 95 ---------EAQL-HDANERNdgqaiaTIHG-KLDAIDAWSIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQA 163
Cdd:PRK13646 86 rigmvfqfpESQLfEDTVERE------IIFGpKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQ----GTLILISHDRDFLDPIVDKIIHIEQQSMFE 226
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-205 |
2.07e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.65 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLkNEISADGGSYTFPGSWQLawvnqetpaLPQAALEYVIDGDREYRQLE 95
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEF---------FNQNIYERRVNLNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 96 AQLHDAN--------ERNDGQAIATIHGKLDAIDAWSIRSRAASLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQALICR 167
Cdd:PRK14258 92 MVHPKPNlfpmsvydNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEI---KHKIHKSALDLSGGQQQRLCIARALAVK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446557484 168 SDLLLLDEPTNHLDLDAVIWLEKWLKSY----QGTLILISHD 205
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHN 210
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
5-221 |
2.20e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 49.60 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 5 SSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnQETPALP--QAALE 82
Cdd:PRK11300 9 SGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG--------QHIEGLPghQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 83 YVI---DGDREYRQLEA--QLHDANERNDGQAIatIHGKL----------DAIDawsirsRAASLLHGLG---FSNeqle 144
Cdd:PRK11300 81 GVVrtfQHVRLFREMTVieNLLVAQHQQLKTGL--FSGLLktpafrraesEALD------RAATWLERVGlleHAN---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 145 RPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHL------DLDAVIwlEKWLKSYQGTLILISHDRDFLDPIVDKIIH 218
Cdd:PRK11300 149 RQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLnpketkELDELI--AELRNEHNVTVLLIEHDMKLVMGISDRIYV 226
|
...
gi 446557484 219 IEQ 221
Cdd:PRK11300 227 VNQ 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
310-462 |
2.29e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 49.70 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 310 NPLLKMEKVSAGYGD------RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI-------- 375
Cdd:PRK13633 2 NEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-YVDGLdtsdeenl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 376 -----KLGYFAQ---HQLEYLRADES----PiQHLArLAPQELEQKLRDYLGGFGFQgdkvteETRRF-----SGGEKAR 438
Cdd:PRK13633 81 wdirnKAGMVFQnpdNQIVATIVEEDvafgP-ENLG-IPPEEIRERVDESLKKVGMY------EYRRHaphllSGGQKQR 152
|
170 180
....*....|....*....|....
gi 446557484 439 LVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLD 176
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
16-221 |
2.36e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.08 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnqetpalpqaaleyvidgdreyrQLE 95
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG------------------------------TDV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 96 AQLHdANERNDG---QAIA---------------TIHGKLDAIDAWSIRSRAASLLHGLgfsneQL----ERPVSDFSGG 153
Cdd:PRK10851 67 SRLH-ARDRKVGfvfQHYAlfrhmtvfdniafglTVLPRRERPNAAAIKAKVTQLLEMV-----QLahlaDRYPAQLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKS----YQGTLILISHDRDFLDPIVDKII-----HIEQ 221
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQlheeLKFTSVFVTHDQEEAMEVADRVVvmsqgNIEQ 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
310-500 |
2.48e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 49.71 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 310 NPLLKMEKVSAGY---GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG------ELAPVSGEIGLAKGI----- 375
Cdd:PRK13642 2 NKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGlfeefeGKVKIDGELLTAENVwnlrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 376 KLGY-FAQHQLEYLRA---DESPIQHLARLAP-QELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPN 450
Cdd:PRK13642 82 KIGMvFQNPDNQFVGAtveDDVAFGMENQGIPrEEMIKRVDEALLAVNML-DFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446557484 451 LLLLDEPTNHLDLDMRQALTEALIEFEGA--LVVVSHDRHLLRSTTDDLYLV 500
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILV 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
126-244 |
2.59e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.20 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 126 RSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILI 202
Cdd:PRK10619 129 RERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVV 208
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446557484 203 SHDRDFLDPIVDKIIHIEQQSMFEYTGNYSSFEVQRATRLAQ 244
Cdd:PRK10619 209 THEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQ 250
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
328-486 |
2.65e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 49.39 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA----------KGI-----KLGY---FAQHQLEylr 389
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDditithktkdKYIrpvrkRIGMvfqFPESQLF--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 390 adESPIQHLARLAPQ-------ELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:PRK13646 100 --EDTVEREIIFGPKnfkmnldEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180
....*....|....*....|....*...
gi 446557484 463 LDMRQALTEALIEFE----GALVVVSHD 486
Cdd:PRK13646 178 PQSKRQVMRLLKSLQtdenKTIILVSHD 205
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
324-462 |
2.74e-06 |
|
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: 48.81 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG---ELAPVSGEI---GLAKGIKL-----GYFAQHQ--LEYLRA 390
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQIlfnGQPRKPDQfqkcvAYVRQDDilLPGLTV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 391 DES----PIQHLARLAPQELEQKlRDYLGGFGFQGDKVTEETRR--FSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:cd03234 99 RETltytAILRLPRKSSDAIRKK-RVEDVLLRDLALTRIGGNLVkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
312-462 |
3.00e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.12 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL--------------AKGIkl 377
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 378 GYFAQHQLEY--------------LRADESPIQHLARlAPQELEQ----KLRDYLGgfgfqgdkvteetRRFSGGEKARL 439
Cdd:PRK10895 81 GYLPQEASIFrrlsvydnlmavlqIRDDLSAEQREDR-ANELMEEfhieHLRDSMG-------------QSLSGGERRRV 146
|
170 180
....*....|....*....|...
gi 446557484 440 VLALIVWQRPNLLLLDEPTNHLD 462
Cdd:PRK10895 147 EIARALAANPKFILLDEPFAGVD 169
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
328-486 |
3.22e-06 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 49.28 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP---VSGEIgLAKGIKLGYFAQHQLEYLRADE----------S- 393
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEI-LFDGEDLLKLSEKELRKIRGREiqmifqdpmtSl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 394 ------------PIQHLARLAPQELEQKLRDYLggfgfqgDKV--TEETRR-------FSGGEKARLVLA--LIVwqRPN 450
Cdd:COG0444 100 npvmtvgdqiaePLRIHGGLSKAEARERAIELL-------ERVglPDPERRldrypheLSGGMRQRVMIAraLAL--EPK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446557484 451 LLLLDEPTNHLD-------LDMRQALTEaliEFEGALVVVSHD 486
Cdd:COG0444 171 LLIADEPTTALDvtiqaqiLNLLKDLQR---ELGLAILFITHD 210
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-204 |
3.83e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.88 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgSWQLAWVNQETPALpQAA 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV----LWQGEPIRRQRDEY-HQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 LEYV-----IDGDreyrqLEAqlhDANERndgqAIATIHGKLDAIDAWSIRSRAasllhGL-GFsnEQLerPVSDFSGGW 154
Cdd:PRK13538 76 LLYLghqpgIKTE-----LTA---LENLR----FYQRLHGPGDDEALWEALAQV-----GLaGF--EDV--PVRQLSAGQ 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446557484 155 RMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQ---GTLILISH 204
Cdd:PRK13538 135 QRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAeqgGMVILTTH 187
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
7-204 |
4.08e-06 |
|
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: 47.87 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgSWQLAWVNQETPALPQAALeYV-- 84
Cdd:cd03231 6 LTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV----LLNGGPLDFQRDSIARGLL-YLgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 85 IDGDREYRQLEAQLHDANERNDGQAIATihgKLDAIDawsirsraaslLHGLGfsneqlERPVSDFSGGWRMRLNLAQAL 164
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQVEE---ALARVG-----------LNGFE------DRPVAQLSAGQQRRVALARLL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446557484 165 ICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY---QGTLILISH 204
Cdd:cd03231 141 LSGRPLWILDEPTTALDKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-181 |
4.09e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.33 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETPALpqaaleyvidgDREY 91
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL-----------RRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 92 RQLEAQLHDANERN--DGQAIATIHGKLDAIDawsIRSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALICRSD 169
Cdd:PRK10908 82 GMIFQDHHLLMDRTvyDNVAIPLIIAGASGDD---IRRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPA 157
|
170
....*....|..
gi 446557484 170 LLLLDEPTNHLD 181
Cdd:PRK10908 158 VLLADEPTGNLD 169
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-230 |
4.69e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 49.80 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 23 TINPGQKVGLVGKNGCGKSTLLALLKneisadgGSYTfPGSWQLaWVNQETpalpqaaleyVIDGDRE-YRQLeaqlhda 101
Cdd:COG4615 354 TIRRGELVFIVGGNGSGKSTLAKLLT-------GLYR-PESGEI-LLDGQP----------VTADNREaYRQL------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 102 nerndgqaIATIHG------KLDAIDAWSIRSRAASLLHGLgfsneQLERPVS---------DFSGGWRMRLNLAQALIC 166
Cdd:COG4615 408 --------FSAVFSdfhlfdRLLGLDGEADPARARELLERL-----ELDHKVSvedgrfsttDLSQGQRKRLALLVALLE 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 167 RSDLLLLDEptnhldldaviW---------------LEKWLKSyQG-TLILISHDRDFLDpIVDKIIHIEQQSMFEYTGN 230
Cdd:COG4615 475 DRPILVFDE-----------WaadqdpefrrvfyteLLPELKA-RGkTVIAISHDDRYFD-LADRVLKMDYGKLVELTGP 541
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
328-499 |
4.86e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.81 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQLEYLRAD---------------- 391
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYY-QGQDLLKADPEAQKLLRQKiqivfqnpygslnprk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 392 ------ESPIQHLARLAPQELEQKLRDYLGGFGFQgdkvTEETRR----FSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
Cdd:PRK11308 110 kvgqilEEPLLINTSLSAAERREKALAMMAKVGLR----PEHYDRyphmFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446557484 462 DLDMR-QALTeaLI-----EFEGALVVVSHDRHLLRSTTDDL---YL 499
Cdd:PRK11308 186 DVSVQaQVLN--LMmdlqqELGLSYVFISHDLSVVEHIADEVmvmYL 230
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
16-227 |
4.87e-06 |
|
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: 48.70 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 16 LLDNATATINPGQKVGLVGKNGCGKSTLL-ALLK-----NEISADGgsytfpGSWQLAWVNQETPA---LPQAAleYVID 86
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLsAFLRllnteGDIQIDG------VSWNSVPLQKWRKAfgvIPQKV--FIFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 87 GdreyrQLEAQLhDANERNDGQAIatihgkLDAIDAWSIRSRAASLLHGLGFsneQLERPVSDFSGGWRMRLNLAQALIC 166
Cdd:cd03289 91 G-----TFRKNL-DPYGKWSDEEI------WKVAEEVGLKSVIEQFPGQLDF---VLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557484 167 RSDLLLLDEPTNHLDLDAVIWLEKWLK-SYQGTLILISHDRdfLDPIVD--KIIHIEQQSMFEY 227
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKqAFADCTVILSEHR--IEAMLEcqRFLVIEENKVRQY 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
311-512 |
6.21e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.17 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGeIGLAKGIKLG----YFAQHQLE 386
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGgrsiFNYRDVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 387 Y--------LRADESPIQHL---------ARLAPQE----LEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIV 445
Cdd:PRK14271 99 FrrrvgmlfQRPNPFPMSIMdnvlagvraHKLVPRKefrgVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 446 WQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVVVSHDRHLLRSTTddlylVHDRKVEPFDGDL 512
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAAR-----ISDRAALFFDGRL 240
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-181 |
7.94e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 48.80 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGS-----------WQLAWVNQEtPALPQAALEYVI 85
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtraslrRNIAVVFQD-AGLFNRSIEDNI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 86 DGDREyRQLEAQLHDANERndGQAIATIHGKLDAIDAwSIRSRAASLlhglgfsneqlerpvsdfSGGWRMRLNLAQALI 165
Cdd:PRK13657 430 RVGRP-DATDEEMRAAAER--AQAHDFIERKPDGYDT-VVGERGRQL------------------SGGERQRLAIARALL 487
|
170
....*....|....*.
gi 446557484 166 CRSDLLLLDEPTNHLD 181
Cdd:PRK13657 488 KDPPILILDEATSALD 503
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-177 |
8.08e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.57 E-value: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGS----WQLAWVNQEtpal 76
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdWQTAKIMRE---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 77 pqaALEYVIDGDREYRQLEAQLH------DANERNDGQAIATIHGKLDAIDAWSIRsRAASLlhglgfsneqlerpvsdf 150
Cdd:PRK11614 81 ---AVAIVPEGRRVFSRMTVEENlamggfFAERDQFQERIKWVYELFPRLHERRIQ-RAGTM------------------ 138
|
170 180
....*....|....*....|....*..
gi 446557484 151 SGGWRMRLNLAQALICRSDLLLLDEPT 177
Cdd:PRK11614 139 SGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
311-462 |
8.80e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 47.46 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL--AGELAP---VSGEIG--------------- 370
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVynghniysprtdtvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 371 LAKGIKLgYFAQHQLEYLRADESPIQHLaRLA----PQELEQKLRDYLGGFGFQG---DKVTEETRRFSGGEKARLVLAL 443
Cdd:PRK14239 84 LRKEIGM-VFQQPNPFPMSIYENVVYGL-RLKgikdKQVLDEAVEKSLKGASIWDevkDRLHDSALGLSGGQQQRVCIAR 161
|
170
....*....|....*....
gi 446557484 444 IVWQRPNLLLLDEPTNHLD 462
Cdd:PRK14239 162 VLATSPKIILLDEPTSALD 180
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-230 |
8.81e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.71 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISAD--GGSYTFPGSWqlawVNQETP-ALPQA----ALEYVID-- 86
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGES----ILDLEPeERAHLgiflAFQYPIEip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 87 GDREYRQLEAQLhdaNERNDGQAIAtihgKLDAIDAWSIRSRAASLLhglGFSNEQLERPVSD-FSGGWRMRLNLAQALI 165
Cdd:CHL00131 98 GVSNADFLRLAY---NSKRKFQGLP----ELDPLEFLEIINEKLKLV---GMDPSFLSRNVNEgFSGGEKKRNEILQMAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 166 CRSDLLLLDEPTNHLDLDAVIWLEK---WLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMFEYTGN 230
Cdd:CHL00131 168 LDSELAILDETDSGLDIDALKIIAEginKLMTSENSIILITHYQRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-485 |
8.94e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.53 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIK-----LLAGELAPVSGEIGL------------------------- 371
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLfgrniyspdvdpievrrevgmvfqy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 372 -------------AKGIKLGYFAQHQLEYlraDESPIQHLARLAP-QELEQKLRDYLGgfgfqgdkvteetrRFSGGEKA 437
Cdd:PRK14267 94 pnpfphltiydnvAIGVKLNGLVKSKKEL---DERVEWALKKAALwDEVKDRLNDYPS--------------NLSGGQRQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446557484 438 RLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEF--EGALVVVSH 485
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTH 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-234 |
1.05e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 47.35 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLK-------NEISADGGSYTFPGSW----------QLAWVNQETPAL 76
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGKDIfqidaiklrkEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 77 PQAALeyvidgdreYRQLEAQLHDANERNDGQAIATIHGKLDAIDAWSIrsraasllhglgfSNEQLERPVSDFSGGWRM 156
Cdd:PRK14246 103 PHLSI---------YDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKE-------------VYDRLNSPASQLSGGQQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 157 RLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG--TLILISHDRDFLDPIVDKIIHIEQQSMFEYTGNYSSF 234
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
116-219 |
1.07e-05 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 47.37 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 116 KLDAIDAWSIRSRAASLLHGLGFSNEQLERPV-SDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAV------Iwl 188
Cdd:COG0396 106 RGEELSAREFLKLLKEKMKELGLDEDFLDRYVnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALrivaegV-- 183
|
90 100 110
....*....|....*....|....*....|.
gi 446557484 189 eKWLKSYQGTLILISHDRDFLDPIVDKIIHI 219
Cdd:COG0396 184 -NKLRSPDRGILIITHYQRILDYIKPDFVHV 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-183 |
1.11e-05 |
|
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: 48.79 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTL-LALL------KNEISADGGSYTFPG----SWQLAWVNQEtP 74
Cdd:TIGR00957 1291 CLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFrinesaEGEIIIDGLNIAKIGlhdlRFKITIIPQD-P 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 75 ALPQAALEYVIDGDREYRQLEAQLhdanerndgqaiatihgkldAIDAWSIRSRAASLLHGLGFsneQLERPVSDFSGGW 154
Cdd:TIGR00957 1370 VLFSGSLRMNLDPFSQYSDEEVWW--------------------ALELAHLKTFVSALPDKLDH---ECAEGGENLSVGQ 1426
|
170 180
....*....|....*....|....*....
gi 446557484 155 RMRLNLAQALICRSDLLLLDEPTNHLDLD 183
Cdd:TIGR00957 1427 RQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
331-522 |
1.67e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.56 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 331 IKLNLvPGSRI-GLLGRNGAGKSTLIKLLAGELAPVSGEIGL--------AKGI-------KLGYFAQHqleylradesp 394
Cdd:PRK11144 17 VNLTL-PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfdaEKGIclppekrRIGYVFQD----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 395 iqhlARLAPQ-ELEQKLRdylggFGF------QGDKVTE----ET--RRF----SGGEKARLVLALIVWQRPNLLLLDEP 457
Cdd:PRK11144 85 ----ARLFPHyKVRGNLR-----YGMaksmvaQFDKIVAllgiEPllDRYpgslSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 458 TNHLDLDMRQALT---EALI-EFEGALVVVSHD-RHLLRsTTDDLYLVHDRKVEPFdGDLEDYqqWLSDV 522
Cdd:PRK11144 156 LASLDLPRKRELLpylERLArEINIPILYVSHSlDEILR-LADRVVVLEQGKVKAF-GPLEEV--WASSA 221
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
328-584 |
1.86e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---GLAKGIKLGYFAQHQLEYLRADE--SPIQHLARLA 402
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVdikGSAALIAISSGLNGQLTGIENIElkGLMMGLTKEK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 403 PQELEQKLRDylggFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFE---GA 479
Cdd:PRK13545 120 IKEIIPEIIE----FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKeqgKT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 480 LVVVSHDRHLLRS-TTDDLYLVHdrkvepfdGDLEDYqqwlSDVQKQENQADEAPKENANSAQARKDQKRREAELRAQTQ 558
Cdd:PRK13545 196 IFFISHSLSQVKSfCTKALWLHY--------GQVKEY----GDIKEVVDHYDEFLKKYNQMSVEERKDFREEQISQFQHG 263
|
250 260
....*....|....*....|....*.
gi 446557484 559 PLRKEIARLEKEMEKLNAQLAQAEEK 584
Cdd:PRK13545 264 LLQEDQTGRERKRKKGKKTSRKFKKK 289
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-232 |
1.88e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 47.71 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawVNQEtpalpqaalEYVIDGDREYRQLEA 96
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG------HDLR---------DYTLASLRNQVALVS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 97 Q-LHDANE---------RNDGQAIATIhgkldaidawsirSRAASLLHGLGFSNEQL--------ERPVSdFSGGWRMRL 158
Cdd:PRK11176 424 QnVHLFNDtianniayaRTEQYSREQI-------------EEAARMAYAMDFINKMDngldtvigENGVL-LSGGQRQRI 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG--TLILISHDrdfLDPI--VDKIIHIEQQSMFEYtGNYS 232
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAHR---LSTIekADEILVVEDGEIVER-GTHA 563
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
14-217 |
1.96e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 46.62 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLL----ALLkneisadggsytfpgswqlawvnqetpaLPQAALEYVIDGDR 89
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAkhmnALL----------------------------IPSEGKVYVDGLDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 90 EyrqLEAQLHDANERN-------DGQAIATIHGKLDA-------IDAWSIRSRAASLLHGLGFSnEQLERPVSDFSGGWR 155
Cdd:PRK13633 75 S---DEENLWDIRNKAgmvfqnpDNQIVATIVEEDVAfgpenlgIPPEEIRERVDESLKKVGMY-EYRRHAPHLLSGGQK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 156 MRLNLAQALICRSDLLLLDEPTNHLD----LDAVIWLEKWLKSYQGTLILISHdrdFLDPIV--DKII 217
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH---YMEEAVeaDRII 215
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-221 |
2.12e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 46.65 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpGSWQLAWVNQETPALPQAALEYVIdgdreYRQLEAQLHDANE 103
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEIKPVRKKVGVV-----FQFPESQLFEETV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 104 RNDgQAIATIHGKLDAIDAWSIrsrAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD 183
Cdd:PRK13643 103 LKD-VAFGPQNFGIPKEKAEKI---AAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446557484 184 AVIWLEKWLKSYQ---GTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:PRK13643 179 ARIEMMQLFESIHqsgQTVVLVTHLMDDVADYADYVYLLEK 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
310-486 |
2.14e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 47.34 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 310 NPLLKMEKVSAGYGDRIILDSIKLNL---------VPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYF 380
Cdd:PRK10070 17 HPQRAFKYIEQGLSKEQILEKTGLSLgvkdaslaiEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQV-LIDGVDIAKI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 381 AQHQLEYLRADESPI--------------------QHLARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLV 440
Cdd:PRK10070 96 SDAELREVRRKKIAMvfqsfalmphmtvldntafgMELAGINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446557484 441 LALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEG----ALVVVSHD 486
Cdd:PRK10070 175 LARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAkhqrTIVFISHD 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-207 |
2.21e-05 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 46.48 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG---------------SWQLAWVNQETP 74
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrRKKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 75 ALPQ-AALEYVIDGdreyrqLEAQLHDANERndgqaiatihgkldaidawsiRSRAASLLHGLGFSNeQLERPVSDFSGG 153
Cdd:cd03294 113 LLPHrTVLENVAFG------LEVQGVPRAER---------------------EERAAEALELVGLEG-WEHKYPDELSGG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 154 WRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLEKWLksyQGTLILISHDRD 207
Cdd:cd03294 165 MQQRVGLARALAVDPDILLMDEAFSALDplirremQDELLRLQAEL---QKTIVFITHDLD 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-226 |
2.23e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 46.28 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPgswqlawvnqetpalpqaa 80
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 lEYVIDGDREY-------RQLEAQL-----------HDANERN--DGQAIATIHGKLDAIdawsirSRAASLLHGLGFSN 140
Cdd:PRK11264 64 -DITIDTARSLsqqkgliRQLRQHVgfvfqnfnlfpHRTVLENiiEGPVIVKGEPKEEAT------ARARELLAKVGLAG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 141 EQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
Cdd:PRK11264 137 KETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAI 215
|
....*....
gi 446557484 218 HIEQQSMFE 226
Cdd:PRK11264 216 FMDQGRIVE 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
126-217 |
2.43e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.77 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 126 RSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQGTLILI 202
Cdd:PRK13631 153 KKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGeheMMQLILDAKANNKTVFVI 232
|
90
....*....|....*
gi 446557484 203 SHDRDFLDPIVDKII 217
Cdd:PRK13631 233 THTMEHVLEVADEVI 247
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-207 |
2.52e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 46.26 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGsytfpgswqlawvnqetpalpqaalEYVIDGDR------- 89
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESG-------------------------QIIIDGDLlteenvw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 90 EYRQleaQLHDANERNDGQAI-ATIHGKL------DAIDAWSIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQ 162
Cdd:PRK13650 78 DIRH---KIGMVFQNPDNQFVgATVEDDVafglenKGIPHEEMKERVNEALELVGMQDFKEREP-ARLSGGQKQRVAIAG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446557484 163 ALICRSDLLLLDEPTNHLD----LDAVIWLEKWLKSYQGTLILISHDRD 207
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLD 202
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
323-462 |
2.59e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP--VSGEIGLAKGIKL--------GYFAQH--QLEYLRA 390
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgvITGGDRLVNGRPLdssfqrsiGYVQQQdlHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 DESpIQHLARL-APQELEQK--------------LRDYLGGF-GFQGDKVTEETRRfsggekaRLVLALIVWQRPNLLL- 453
Cdd:TIGR00956 854 RES-LRFSAYLrQPKSVSKSekmeyveeviklleMESYADAVvGVPGEGLNVEQRK-------RLTIGVELVAKPKLLLf 925
|
....*....
gi 446557484 454 LDEPTNHLD 462
Cdd:TIGR00956 926 LDEPTSGLD 934
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-252 |
2.65e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 46.23 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKS-TLLALLKneisadggsyTFPgswqlawvnqetPALPQAALEYVIDGDReyr 92
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALG----------ILP------------AGVRQTAGRVLLDGKP--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 93 qleaqLHDANERndGQAIATI----------------HGK--LDAIDAWSIRSRAASLLHGLGFSNEQ--LERPVSDFSG 152
Cdd:PRK10418 71 -----VAPCALR--GRKIATImqnprsafnplhtmhtHARetCLALGKPADDATLTAALEAVGLENAArvLKLYPFEMSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 153 GWRMRLNLAQALICRSDLLLLDEPTNhlDLDAVI------WLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMFE 226
Cdd:PRK10418 144 GMLQRMMIALALLCEAPFIIADEPTT--DLDVVAqarildLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
250 260 270
....*....|....*....|....*....|
gi 446557484 227 YTGNYSSFEVQR--ATR--LAQQQAMYESQ 252
Cdd:PRK10418 222 QGDVETLFNAPKhaVTRslVSAHLALYGME 251
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
126-293 |
3.00e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.65 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 126 RSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHldldaviwlekwlksyqgtlilishd 205
Cdd:NF000106 122 RARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTG-------------------------- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 206 rdfLDPIVDKIIHIEQQSMFEytgnyssfevQRATRLAQQQAMYESQQerVAHLQSYIDRFRAKAtKAKQAQSRIKMLER 285
Cdd:NF000106 175 ---LDPRTRNEVWDEVRSMVR----------DGATVLLTTQYMEEAEQ--LAHELTVIDRGRVIA-DGKVDELKTKVGGR 238
|
....*...
gi 446557484 286 MELIAPAH 293
Cdd:NF000106 239 TLQIRPAH 246
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-186 |
3.11e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.47 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 2 IVFSSLQIR--RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----SWQLAWVNQETPA 75
Cdd:PTZ00243 1309 LVFEGVQMRyrEGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGreigAYGLRELRRQFSM 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 76 LPQAALEYvidgDREYRQ-----LEAqlhdanerndgqAIATIHGKLDAIdawSIRSRAASllhglgfSNEQLERPV--- 147
Cdd:PTZ00243 1389 IPQDPVLF----DGTVRQnvdpfLEA------------SSAEVWAALELV---GLRERVAS-------ESEGIDSRVleg 1442
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446557484 148 -SDFSGGWRMRLNLAQALICR-SDLLLLDEPTNHLD--LDAVI 186
Cdd:PTZ00243 1443 gSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDpaLDRQI 1485
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-217 |
3.20e-05 |
|
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: 45.72 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADG---GSYTFPGSwqlawvnQETPALPQAALEYVIDGD-- 88
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQ-------PRKPDQFQKCVAYVRQDDil 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 89 ------REYRQLEAQLHDANERNDGQaiatihgkLDAIDAwSIRSRAASLLHgLGFSNeqlerpVSDFSGGWRMRLNLAQ 162
Cdd:cd03234 93 lpgltvRETLTYTAILRLPRKSSDAI--------RKKRVE-DVLLRDLALTR-IGGNL------VKGISGGERRRVSIAV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 163 ALICRSDLLLLDEPTNHLD----LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDsftaLNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRIL 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
312-484 |
3.66e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 45.77 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIK----LLAGELAP----------VSGEIGLAKGIK- 376
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAgshiellgrtVQREGRLARDIRk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 377 ----LGYFAQ-----HQLEYLR------ADESP-----IQHLARLAPQELEQKL-RDYLGGFGFQgdkvteETRRFSGGE 435
Cdd:PRK09984 84 sranTGYIFQqfnlvNRLSVLEnvligaLGSTPfwrtcFSWFTREQKQRALQALtRVGMVHFAHQ------RVSTLSGGQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446557484 436 KARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEF---EGALVVVS 484
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqnDGITVVVT 209
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
512-630 |
3.85e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 512 LEDYQQWLSDVQKQENQADEAPKENANSAQARKDQKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGdsely 591
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG----- 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446557484 592 dQSRKA-ELTACLQQQASAKSGLEECEMAWLEAQEQLEQM 630
Cdd:COG1579 84 -NVRNNkEYEALQKEIESLKRRISDLEDEILELMERIEEL 122
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-225 |
3.97e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 46.93 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG---SWQLAWVNQETPALPQAALEYVIDGDRE 90
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdiETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 91 YRQLEAQLhdanernDGQAIATIHGKLDAidawsirsraasLLHGLGFSNEQLERpVSDFSGGWRMRLNLAQALICRSDL 170
Cdd:TIGR01257 1023 HILFYAQL-------KGRSWEEAQLEMEA------------MLEDTGLHHKRNEE-AQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 171 LLLDEPTNHLDLDA--VIWlEKWLKSYQG-TLILISHDRDFLDPIVDKIIHIEQQSMF 225
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSrrSIW-DLLLKYRSGrTIIMSTHHMDEADLLGDRIAIISQGRLY 1139
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
512-633 |
4.03e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 512 LEDYQQWLSDVQKQENQADEApKENANSAQARKDQKRREAELRAQTqpLRKEIARLEKEMEKLNAQLAQAEEKLGDSELY 591
Cdd:COG1196 276 LEELELELEEAQAEEYELLAE-LARLEQDIARLEERRRELEERLEE--LEEELAELEEELEELEEELEELEEELEEAEEE 352
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446557484 592 DQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQMLLE 633
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
311-500 |
4.72e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 45.37 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI--------GLA------KGIK 376
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIllrgqhieGLPghqiarMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 377 LGY----------------FAQH-QLE------------YLRADESPIQHlarlAPQELEQ-KLRDYlggfgfqgdkVTE 426
Cdd:PRK11300 84 RTFqhvrlfremtvienllVAQHqQLKtglfsgllktpaFRRAESEALDR----AATWLERvGLLEH----------ANR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 427 ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALtEALI-----EFEGALVVVSHDRHLLRSTTDDLYLV 500
Cdd:PRK11300 150 QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKEL-DELIaelrnEHNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-220 |
4.76e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.84 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnqetpalpqaalEYVIDGDREyRQLEAQLHDANE 103
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG-------------------KTATRGDRS-RFMAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 104 RNDGQAIATIHgKLDAIDAWSIRSRAASLLHGLGFSNEQlERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD 183
Cdd:PRK13543 94 KADLSTLENLH-FLCGLHGRRAKQMPGSALAIVGLAGYE-DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446557484 184 AVIWLEKWLKSY---QGTLILISHDRDFLDPIVDKIIHIE 220
Cdd:PRK13543 172 GITLVNRMISAHlrgGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
10-216 |
4.85e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 46.18 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETPALPQAALEYVidgdr 89
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMV----- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 90 eYRQLEAQLHDANERNDGQAIatihgKLDAIDAWSIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSD 169
Cdd:PRK10070 112 -FQSFALMPHMTVLDNTAFGM-----ELAGINAEERREKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446557484 170 LLLLDEPTNHLD----LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKI 216
Cdd:PRK10070 185 ILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRI 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
315-369 |
4.95e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 4.95e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446557484 315 MEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 55
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-221 |
5.07e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 45.59 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLL----ALLKneisADGGSYTFPGSwqlawvnQETPALPQAALEYVidgdREYR 92
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMqhfnALLK----PSSGTITIAGY-------HITPETGNKNLKKL----RKKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 93 QL-----EAQLHDANERNDgqaiaTIHGKLD-AIDAWSIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALIC 166
Cdd:PRK13641 88 SLvfqfpEAQLFENTVLKD-----VEFGPKNfGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 167 RSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEH 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
151-244 |
5.41e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 45.01 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLI---LISHDRDFLDPIVDKIIHIEQQSMFEy 227
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVEVARKTASRVVYMENGHIVE- 221
|
90
....*....|....*..
gi 446557484 228 TGNYSSFEVQRATRLAQ 244
Cdd:PRK11124 222 QGDASCFTQPQTEAFKN 238
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
8-181 |
5.44e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 44.54 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 8 QIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKN---------EISADG--GSYTFPGSwqLAWVNQETPAL 76
Cdd:cd03232 14 PVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrktagvitgEILINGrpLDKNFQRS--TGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 77 PQAALEyvidgdreyrqlEAQLHDANERndgqaiatihgkldaidawsirsraasllhglGFSNEQlerpvsdfsggwRM 156
Cdd:cd03232 92 PNLTVR------------EALRFSALLR--------------------------------GLSVEQ------------RK 115
|
170 180
....*....|....*....|....*
gi 446557484 157 RLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:cd03232 116 RLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
512-637 |
5.94e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 512 LEDYQQWLSDVQKQENQADEAPKENANSAQARKDQKRREAELRAQTQPLRKEIARLEKEMEKLN------------AQLA 579
Cdd:TIGR00618 224 LEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaaplaahiKAVT 303
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 580 QAEEKLGDSELYDQSRKAELTACLQQ-QASAKSGLEECEMAWLEAQEQLEQMLLEGQSN 637
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKrAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHE 362
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
310-462 |
6.57e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.87 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 310 NPLLKMEKVSAGY--GDRII--LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA------------- 372
Cdd:PRK10535 2 TALLELKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAgqdvatldadala 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 373 --KGIKLGYFAQ--HQLEYLRAD---ESPIQHlARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIV 445
Cdd:PRK10535 82 qlRREHFGFIFQryHLLSHLTAAqnvEVPAVY-AGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARAL 159
|
170
....*....|....*..
gi 446557484 446 WQRPNLLLLDEPTNHLD 462
Cdd:PRK10535 160 MNGGQVILADEPTGALD 176
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-181 |
6.92e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 45.86 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG---------SW--QLAWVNQeTPALPQAALEYVI 85
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDipltklqldSWrsRLAVVSQ-TPFLFSDTVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 86 DGDREyrqleaqlhDANERNDGQA--IATIHgklDAIdawsirsraasLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQA 163
Cdd:PRK10789 410 ALGRP---------DATQQEIEHVarLASVH---DDI-----------LRLPQGYDTEVGERGVM-LSGGQKQRISIARA 465
|
170
....*....|....*...
gi 446557484 164 LICRSDLLLLDEPTNHLD 181
Cdd:PRK10789 466 LLLNAEILILDDALSAVD 483
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
311-369 |
7.84e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 7.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSI 61
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
334-486 |
8.81e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.50 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 334 NLVPGSRIGLL---GRNGAGKSTL---IKLLAGELAPVsgeIGLAKGIKLGYFaqhqleylRADESPIQHLARLapqele 407
Cdd:cd03227 14 NDVTFGEGSLTiitGPNGSGKSTIldaIGLALGGAQSA---TRRRSGVKAGCI--------VAAVSAELIFTRL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 408 qklrdylggfgfqgdkvteetrRFSGGEKARLVLALIV----WQRPNLLLLDEPTNHLDLDMRQALTEALIEF--EGALV 481
Cdd:cd03227 77 ----------------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvKGAQV 134
|
....*.
gi 446557484 482 -VVSHD 486
Cdd:cd03227 135 iVITHL 140
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-57 |
8.99e-05 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 44.69 E-value: 8.99e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGS 57
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGE 57
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
466-629 |
9.07e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 466 RQALTEALIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKVEPFDGDLEDYQQWLSDVQKQENQADEAPKENANSAQARKD 545
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 546 QKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQE 625
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
....
gi 446557484 626 QLEQ 629
Cdd:COG1196 401 QLEE 404
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
126-235 |
9.09e-05 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 44.23 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 126 RSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLI---LI 202
Cdd:COG4161 119 REKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGItqvIV 197
|
90 100 110
....*....|....*....|....*....|...
gi 446557484 203 SHDRDFLDPIVDKIIHIEQQSMFEYtGNYSSFE 235
Cdd:COG4161 198 THEVEFARKVASQVVYMEKGRIIEQ-GDASHFT 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-177 |
1.08e-04 |
|
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: 43.96 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLL----ALLK---NEISADGGSYTfpgswqlawvNQETPALPQAALEYVIDGdr 89
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLktimGLLPprsGSIRFDGRDIT----------GLPPHERARAGIGYVPEG-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 90 eyRQLEAQLhdanerndgqaiaTIHGKLD-AIDAWSIRSRAASL---------LHglgfsnEQLERPVSDFSGGWRMRLN 159
Cdd:cd03224 84 --RRIFPEL-------------TVEENLLlGAYARRRAKRKARLervyelfprLK------ERRKQLAGTLSGGEQQMLA 142
|
170
....*....|....*...
gi 446557484 160 LAQALICRSDLLLLDEPT 177
Cdd:cd03224 143 IARALMSRPKLLLLDEPS 160
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-181 |
1.28e-04 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 44.68 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLkneisadggsytfpgswqlawvnqetpalpqAA 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMI-------------------------------AG 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 81 LEYV------IDGdREYRQLEAQlhdanERNdgqaIA------------TIHG------KLDAIDAWSIRSR---AASLL 133
Cdd:COG3839 52 LEDPtsgeilIGG-RDVTDLPPK-----DRN----IAmvfqsyalyphmTVYEniafplKLRKVPKAEIDRRvreAAELL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446557484 134 hGLGfsnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:COG3839 122 -GLE---DLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
23-273 |
1.44e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 43.85 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADggsyTFPGSwQLAWVNQETPALPQAAleyvidgdREYRQLEAQ----L 98
Cdd:PRK09984 26 NIHHGEMVALLGPSGSGKSTLLRHLSGLITGD----KSAGS-HIELLGRTVQREGRLA--------RDIRKSRANtgyiF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 99 HDANERNDGQAIATIH-GKLDAIDAWSI---------RSRAASLLHGLGFSNEQLERpVSDFSGGWRMRLNLAQALICRS 168
Cdd:PRK09984 93 QQFNLVNRLSVLENVLiGALGSTPFWRTcfswftreqKQRALQALTRVGMVHFAHQR-VSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 169 DLLLLDEPTNHLDLD-AVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIHIEQQSMFeYTGNYSSFEvqratrlaq 244
Cdd:PRK09984 172 KVILADEPIASLDPEsARIVMDTLRDINQNdgiTVVVTLHQVDYALRYCERIVALRQGHVF-YDGSSQQFD--------- 241
|
250 260
....*....|....*....|....*....
gi 446557484 245 qqamyesqQERVAHLQSYIDRFRAKATKA 273
Cdd:PRK09984 242 --------NERFDHLYRSINRVEENAKAA 262
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
466-628 |
1.59e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 466 RQALTEALIEFEGALVVVSHDRHLLRSTTD----DLYLVHDRKvEPFDGDLEDYQQWLSDV----QKQENQADEApKENA 537
Cdd:PRK02224 274 REELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARR-EELEDRDEELRDRLEECrvaaQAHNEEAESL-REDA 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 538 NSAQARKDQKRREA--------ELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASA 609
Cdd:PRK02224 352 DDLEERAEELREEAaeleseleEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL 431
|
170
....*....|....*....
gi 446557484 610 KSGLEECEMAWLEAQEQLE 628
Cdd:PRK02224 432 EATLRTARERVEEAEALLE 450
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
430-486 |
1.85e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.96 E-value: 1.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 430 RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEG----ALVVVSHD 486
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkenmALVLITHD 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
312-462 |
1.89e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 44.02 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 312 LLKMEKVSAGYGDRII-LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEYLRA 390
Cdd:PRK11153 4 LKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV-LVDGQDLTALSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 391 DESPI-QH------------------LARLAPQELEQKLRDYLggfgfqgDKV--TEETRRF----SGGEKARLVLALIV 445
Cdd:PRK11153 83 QIGMIfQHfnllssrtvfdnvalpleLAGTPKAEIKARVTELL-------ELVglSDKADRYpaqlSGGQKQRVAIARAL 155
|
170
....*....|....*..
gi 446557484 446 WQRPNLLLLDEPTNHLD 462
Cdd:PRK11153 156 ASNPKVLLCDEATSALD 172
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
12-54 |
1.93e-04 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 43.70 E-value: 1.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 446557484 12 GVRVLldNATATINPGQKVGLVGKNGCGKSTLLALLKNEISAD 54
Cdd:cd01136 54 GVRAI--DGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDAD 94
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-238 |
1.99e-04 |
|
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: 43.69 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----SWQLAWVnqetpaLPQAALEYVIDGDR-- 89
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGrisfSSQFSWI------MPGTIKENIIFGVSyd 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 90 EYR--------QLEAQLHDANERNDgqaiaTIHGKldaidawsirsraasllHGLgfsneqlerpvsDFSGGWRMRLNLA 161
Cdd:cd03291 126 EYRyksvvkacQLEEDITKFPEKDN-----TVLGE-----------------GGI------------TLSGGQRARISLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 162 QALICRSDLLLLDEPTNHLDldavIWLEKWLKSY-------QGTLILISHDRDFLDpIVDKIIHIEQQSMFEYtGNYSSF 234
Cdd:cd03291 172 RAVYKDADLYLLDSPFGYLD----VFTEKEIFEScvcklmaNKTRILVTSKMEHLK-KADKILILHEGSSYFY-GTFSEL 245
|
....
gi 446557484 235 EVQR 238
Cdd:cd03291 246 QSLR 249
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
24-217 |
2.04e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 43.86 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 24 INPGQKVGLVGKNGCGKSTLLALLkneisadggsytfpgswqlawvnqetpalpqAALEYVIDGDreyrqleaqLHDANE 103
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLLRMI-------------------------------AGLEDITSGD---------LFIGEK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 104 R-ND--------G---QAIA-----------TIHGKLDAIDAWSIRSR---AASLLHgLGfsnEQLERPVSDFSGGWRMR 157
Cdd:PRK11000 66 RmNDvppaergvGmvfQSYAlyphlsvaenmSFGLKLAGAKKEEINQRvnqVAEVLQ-LA---HLLDRKPKALSGGQRQR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557484 158 LNLAQALICRSDLLLLDEPTNHLD----LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
Cdd:PRK11000 142 VAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIV 205
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-217 |
2.19e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.96 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKS-TLLALLkneisadgGSYTFPG---SWQLAWVNQETPALPqaaleyvidgDREYR 92
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSvSSLAIM--------GLIDYPGrvmAEKLEFNGQDLQRIS----------EKERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 93 QLEA----------------------QLHDANERNDGQAIATIhgkldaidawsiRSRAASLLHGLGFSN--EQLERPVS 148
Cdd:PRK11022 85 NLVGaevamifqdpmtslnpcytvgfQIMEAIKVHQGGNKKTR------------RQRAIDLLNQVGIPDpaSRLDVYPH 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 149 DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD--LDAVI--WLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtIQAQIieLLLELQQKENMALVLITHDLALVAEAAHKII 225
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
151-228 |
2.34e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.96 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 151 SGGWR----MRLNLAQALICRSDLLLLDEPTNHLDL-DAVIWLEKWLKSYQG--TLILISHDRDFLDPIvDKIIHIEQQS 223
Cdd:cd03227 79 SGGEKelsaLALILALASLKPRPLYILDEIDRGLDPrDGQALAEAILEHLVKgaQVIVITHLPELAELA-DKLIHIKKVI 157
|
....*
gi 446557484 224 MFEYT 228
Cdd:cd03227 158 TGVYK 162
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
311-506 |
2.77e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.93 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 311 PLLKMEKVSAGY----GDRIILDSIKLNLVPGSRIGLLGRNGAGKS----TLIKLLAGelAPV---SGEIGLAkGIKLGY 379
Cdd:PRK15134 4 PLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPS--PPVvypSGDIRFH-GESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 380 FAQHQLEYLRAD------ESPIQHLARLapQELEQKLRDYLG---------------------GFGFQGDKVTEETRRFS 432
Cdd:PRK15134 81 ASEQTLRGVRGNkiamifQEPMVSLNPL--HTLEKQLYEVLSlhrgmrreaargeilncldrvGIRQAAKRLTDYPHQLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 433 GGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR----QALTEALIEFEGALVVVSHDRHLLRSTTDDLYLV-HDRKVE 506
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQaqilQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMqNGRCVE 237
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-207 |
2.79e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 42.65 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 21 TATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGS---------YTFPGSWQLAWVNQETPALPQAALEyvidgdrey 91
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSltlngqdhtTTPPSRRPVSMLFQENNLFSHLTVA--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 92 RQLEAQLHDANERNDGQaiatiHGKLDAIdawsirsraaslLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
Cdd:PRK10771 90 QNIGLGLNPGLKLNAAQ-----REKLHAI------------ARQMGIED-LLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446557484 172 LLDEPTNHLD----LDAVIWLEKWLKSYQGTLILISHDRD 207
Cdd:PRK10771 152 LLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHSLE 191
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
328-501 |
3.36e-04 |
|
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: 42.32 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEYLRADESPIQHLARLAPQELE 407
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 408 -----------QKLRDYLGGFGFQGD----------KVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
Cdd:cd03290 97 enitfgspfnkQRYKAVTDACSLQPDidllpfgdqtEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 446557484 467 QALTEaliefEGALVVVSHDRHLLRSTTDDL-YLVH 501
Cdd:cd03290 177 DHLMQ-----EGILKFLQDDKRTLVLVTHKLqYLPH 207
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
120-216 |
3.87e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 42.87 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 120 IDAWSIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD----LDAVIWLEKWLKSY 195
Cdd:PRK13652 109 LDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETY 187
|
90 100
....*....|....*....|.
gi 446557484 196 QGTLILISHDRDFLDPIVDKI 216
Cdd:PRK13652 188 GMTVIFSTHQLDLVPEMADYI 208
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
16-182 |
4.07e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.59 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 16 LLDNATATINPGQKVGLVGKNGCGKSTL-LALLK------NEISADGGS------YTFPGswQLAWVNQEtPALPQAALE 82
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRmvdifdGKIVIDGIDisklplHTLRS--RLSIILQD-PILFSGSIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 83 YVID------GDREYRQLE-AQLHDanerndgqAIATIHGKLDAIdawsirsraasllhglgfsneqLERPVSDFSGGWR 155
Cdd:cd03288 113 FNLDpeckctDDRLWEALEiAQLKN--------MVKSLPGGLDAV----------------------VTEGGENFSVGQR 162
|
170 180
....*....|....*....|....*..
gi 446557484 156 MRLNLAQALICRSDLLLLDEPTNHLDL 182
Cdd:cd03288 163 QLFCLARAFVRKSSILIMDEATASIDM 189
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
522-637 |
4.18e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 522 VQKQENQADEAPKE--NANSAQARKDQ-----KRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQS 594
Cdd:TIGR02168 276 VSELEEEIEELQKElyALANEISRLEQqkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446557484 595 RKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQMLLEGQSN 637
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-287 |
4.56e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEIS-ADGGSYTFPGSwqLAWVNQeTPALPQAALEYVIDGDREYRqle 95
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShAETSSVVIRGS--VAYVPQ-VSWIFNATVRENILFGSDFE--- 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 96 aqlhdaNERndgqaiatiHGKldAIDAWSIRsRAASLLHGLGFSnEQLERPVsDFSGGWRMRLNLAQALICRSDLLLLDE 175
Cdd:PLN03232 707 ------SER---------YWR--AIDVTALQ-HDLDLLPGRDLT-EIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 176 PTNHLD-------LDAVIWLEkwlksYQG-TLILISHDRDFLdPIVDKIIHIeQQSMFEYTGNYSSFE---------VQR 238
Cdd:PLN03232 767 PLSALDahvahqvFDSCMKDE-----LKGkTRVLVTNQLHFL-PLMDRIILV-SEGMIKEEGTFAELSksgslfkklMEN 839
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446557484 239 ATRLAQQQAMYEsQQERVAHLQSY--IDRFRAKATKAKQAQSRIKMLERME 287
Cdd:PLN03232 840 AGKMDATQEVNT-NDENILKLGPTvtIDVSERNLGSTKQGKRGRSVLVKQE 889
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
343-462 |
4.68e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 42.92 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 343 LLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQLEYLRADESPIQHLARL--------------------- 401
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQV-GDIYIGDKKNNHELITNPYSKKIKNFKELrrrvsmvfqfpeyqlfkdtie 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 402 ------------APQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:PRK13631 136 kdimfgpvalgvKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
518-609 |
6.10e-04 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 42.89 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 518 WLSDVQKQENQADEAPKENA-------NSAQARKDQKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLgdsel 590
Cdd:PRK13729 32 YLSDVDMSGNGEAVAEQEPVpdmtgvvDTTFDDKVRQHATTEMQVTAAQMQKQYEEIRRELDVLNKQRGDDQRRI----- 106
|
90
....*....|....*....
gi 446557484 591 ydQSRKAELTAcLQQQASA 609
Cdd:PRK13729 107 --EKLGQDNAA-LAEQVKA 122
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
527-629 |
6.23e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 527 NQADEAPKENA--NSAQARKDQKRREAELRA------QTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAE 598
Cdd:PRK11281 30 ASNGDLPTEADvqAQLDALNKQKLLEAEDKLvqqdleQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD 109
|
90 100 110
....*....|....*....|....*....|.
gi 446557484 599 LTACLQQQASAKSgLEECEMAWLEAQEQLEQ 629
Cdd:PRK11281 110 NDEETRETLSTLS-LRQLESRLAQTLDQLQN 139
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-216 |
6.42e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 41.99 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGswqlawvnqetpalpqAALEYVIDGDREYRQ--- 93
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG----------------EPIKYDKKSLLEVRKtvg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 94 LEAQLHDanerndgqaiatihgklDAIDAWSIRSRAASLLHGLGFSNEQLERPVSD-----------------FSGGWRM 156
Cdd:PRK13639 82 IVFQNPD-----------------DQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEalkavgmegfenkpphhLSGGQKK 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557484 157 RLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY--QGTLILIS-HDRDFLDPIVDKI 216
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGITIIIStHDVDLVPVYADKV 207
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
148-204 |
6.78e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 41.75 E-value: 6.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 148 SDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWL----KSYqgTLILISH 204
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLfelkKEY--TIVLVTH 206
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
340-366 |
8.23e-04 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 39.52 E-value: 8.23e-04
10 20
....*....|....*....|....*..
gi 446557484 340 RIGLLGRNGAGKSTLIKLLAGELAPVS 366
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVS 27
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
521-637 |
8.64e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 521 DVQKQENQADE-------APKENANSAQARKDQKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSElydq 593
Cdd:TIGR02168 685 KIEELEEKIAElekalaeLRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE---- 760
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446557484 594 srkAELTACLQQQASAKSGLEECEMAWLEAQEQLEQMLLEGQSN 637
Cdd:TIGR02168 761 ---AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
402-492 |
1.04e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 402 APQELEQKLRDYLGGFGFQGDKVT---------------EETRRFSGGEKARLVLAL--IVWQRPN----LLLLDEPTNH 460
Cdd:PRK01156 758 ASQAMTSLTRKYLFEFNLDFDDIDvdqdfnitvsrggmvEGIDSLSGGEKTAVAFALrvAVAQFLNndksLLIMDEPTAF 837
|
90 100 110
....*....|....*....|....*....|....*....
gi 446557484 461 LDLDMRQALTEaLIEFE-------GALVVVSHDRHLLRS 492
Cdd:PRK01156 838 LDEDRRTNLKD-IIEYSlkdssdiPQVIMISHHRELLSV 875
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
511-633 |
1.07e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 511 DLEDYQQWLSDVQKQENQAD---EAPKENANSAQARKDQ-KRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLG 586
Cdd:COG1196 254 ELEELEAELAELEAELEELRlelEELELELEEAQAEEYElLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446557484 587 DSELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQMLLE 633
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-182 |
1.16e-03 |
|
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: 42.20 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----SWQLAWVnqetpaLPQAALEYVIDGDR-- 89
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGrisfSPQTSWI------MPGTIKDNIIFGLSyd 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 90 EYRqleaqlhdanerndgqaiatihgkldaidaWSIRSRAASLLHGLGFSNEQLERPVSD----FSGGWRMRLNLAQALI 165
Cdd:TIGR01271 515 EYR------------------------------YTSVIKACQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVY 564
|
170
....*....|....*..
gi 446557484 166 CRSDLLLLDEPTNHLDL 182
Cdd:TIGR01271 565 KDADLYLLDSPFTHLDV 581
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
321-603 |
1.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 321 GYGdriILDSIKLNLVPGSRIgLLGRNGAGKSTLIK----LLAGELAPVSGEIGLAKGiKLGYFAQHQLEYLRAdespiq 396
Cdd:COG4717 10 GFG---KFRDRTIEFSPGLNV-IYGPNEAGKSTLLAfiraMLLERLEKEADELFKPQG-RKPELNLKELKELEE------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 397 hlarlAPQELEQKLRDYlggfgfqgdKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEF 476
Cdd:COG4717 79 -----ELKEAEEKEEEY---------AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 477 EGALvvvshdRHLLrsttddlylvhdRKVEPFDGDLEDYQQWLSDVQKQENQADEAPKENANSAQAR-KDQKRREAELRA 555
Cdd:COG4717 145 PERL------EELE------------ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQ 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446557484 556 QTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACL 603
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLI 254
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
511-636 |
1.17e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 511 DLEDYQQWLSDVQKQENQADEAPKENANSAQARKDQKRREAELRAQTQPLRkeiaRLEKEMEKLNAQLAQAEEKLGD--- 587
Cdd:PRK11281 74 KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLR----QLESRLAQTLDQLQNAQNDLAEyns 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 588 -------------SELY-DQSRKAELTACLQQQASAKSGLE-------ECEMAWLEAQEQLEQMLLEGQS 636
Cdd:PRK11281 150 qlvslqtqperaqAALYaNSQRLQQIRNLLKGGKVGGKALRpsqrvllQAEQALLNAQNDLQRKSLEGNT 219
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
467-629 |
1.22e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 467 QALTEALIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKVEPFDGDLEDYQQWLSDVQKQENQADEAPKENANSAQARKDQ 546
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 547 KRREAELRAqtqplrkEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQ 626
Cdd:TIGR02168 767 EERLEEAEE-------ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
...
gi 446557484 627 LEQ 629
Cdd:TIGR02168 840 LED 842
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-57 |
1.27e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.82 E-value: 1.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446557484 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGS 57
Cdd:PRK11288 16 GVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGS 60
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
125-214 |
1.29e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.70 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 125 IRSRAASLLH-GLGFSNeqLERPVSDFSGGWRMRLNLAQALICRSD--LLLLDEPTNHL---DLDAVIWLEKWLKSYQGT 198
Cdd:cd03270 114 IRERLGFLVDvGLGYLT--LSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLhprDNDRLIETLKRLRDLGNT 191
|
90
....*....|....*....
gi 446557484 199 LILISHDRDFL---DPIVD 214
Cdd:cd03270 192 VLVVEHDEDTIraaDHVID 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
141-204 |
1.48e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 40.67 E-value: 1.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446557484 141 EQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG--TLILISH 204
Cdd:PRK14247 138 DRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
323-462 |
1.64e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 41.22 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEYLRADESPI-QH---- 397
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSV-LVDGVDLTALSERELRAARRKIGMIfQHfnll 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 398 --------------LARLAPQELEQKLRDYLggfgfqgDKV--TEETRRF----SGGEKARlV-----LALivwqRPNLL 452
Cdd:COG1135 95 ssrtvaenvalpleIAGVPKAEIRKRVAELL-------ELVglSDKADAYpsqlSGGQKQR-VgiaraLAN----NPKVL 162
|
170
....*....|
gi 446557484 453 LLDEPTNHLD 462
Cdd:COG1135 163 LCDEATSALD 172
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
113-205 |
1.68e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 113 IHGKLDAidawsirsraaslLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSD---LLLLDEPTNHL---DLDAVI 186
Cdd:PRK00635 786 IHEKIHA-------------LCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLhthDIKALI 852
|
90 100
....*....|....*....|
gi 446557484 187 WLEKWLkSYQG-TLILISHD 205
Cdd:PRK00635 853 YVLQSL-THQGhTVVIIEHN 871
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
513-611 |
1.69e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 513 EDYQQWLSDVQKQENQADEAPKENANSAQARKDQKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGD--SEL 590
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllRAL 113
|
90 100
....*....|....*....|.
gi 446557484 591 YDQSRKAELTACLQQQASAKS 611
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLDA 134
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
135-214 |
1.92e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.61 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 135 GLGFSneQLERPVSDFSGGWRMRLNLAQALICRSD--LLLLDEPT---NHLDLDAVIWLEKWLKSYQGTLILISHDRDFL 209
Cdd:cd03238 75 GLGYL--TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPStglHQQDINQLLEVIKGLIDLGNTVILIEHNLDVL 152
|
....*...
gi 446557484 210 ---DPIVD 214
Cdd:cd03238 153 ssaDWIID 160
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
520-606 |
2.07e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 520 SDVQKQENQADEAPKENANSAQARKDQKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSelydQSRKAEL 599
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL----EKEIAEL 95
|
....*..
gi 446557484 600 TACLQQQ 606
Cdd:COG4942 96 RAELEAQ 102
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
143-207 |
2.54e-03 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 40.47 E-value: 2.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446557484 143 LERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL---DAVI-WLEKWLKSYQGTLILISHDRD 207
Cdd:COG4148 127 LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkAEILpYLERLRDELDIPILYVSHSLD 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
142-222 |
2.58e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 40.70 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 142 QLE----RPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD--LDAVIWLEkwLKSYQGTL----ILISHDRDFLDP 211
Cdd:PRK09452 133 QLEefaqRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDykLRKQMQNE--LKALQRKLgitfVFVTHDQEEALT 210
|
90
....*....|....*.
gi 446557484 212 IVDKII-----HIEQQ 222
Cdd:PRK09452 211 MSDRIVvmrdgRIEQD 226
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
520-637 |
2.64e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 520 SDVQKQENQADEAPKENANSAQARKDQKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAEL 599
Cdd:COG4372 73 SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446557484 600 TACLQQQASAKSGLEECE-----MAWLEAQEQLEQMLLEGQSN 637
Cdd:COG4372 153 KELEEQLESLQEELAALEqelqaLSEAEAEQALDELLKEANRN 195
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
516-637 |
2.72e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 516 QQWLSDVQKQENQADEAPKENANSAQARKdQKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELY---D 592
Cdd:COG3096 498 RELLRRYRSQQALAQRLQQLRAQLAELEQ-RLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQaaeA 576
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446557484 593 QSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQmlLEGQSN 637
Cdd:COG3096 577 VEQRSELRQQLEQLRARIKELAARAPAWLAAQDALER--LREQSG 619
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
540-630 |
2.73e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.63 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 540 AQARKDQKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKlgdselydQSRKAELTACLQQQASAKSGLEECEMA 619
Cdd:COG2268 215 AIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAET--------ARAEAEAAYEIAEANAEREVQRQLEIA 286
|
90
....*....|.
gi 446557484 620 WLEAQEQLEQM 630
Cdd:COG2268 287 EREREIELQEK 297
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
324-462 |
2.95e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 40.47 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLgyfAQHQLEYLR-------------- 389
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI-RFHDIPL---TKLQLDSWRsrlavvsqtpflfs 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 390 -------------ADESPIQHLARLA---------PQeleqklrdylggfGFQgDKVTEETRRFSGGEKARLVLALIVWQ 447
Cdd:PRK10789 403 dtvannialgrpdATQQEIEHVARLAsvhddilrlPQ-------------GYD-TEVGERGVMLSGGQKQRISIARALLL 468
|
170
....*....|....*
gi 446557484 448 RPNLLLLDEPTNHLD 462
Cdd:PRK10789 469 NAEILILDDALSAVD 483
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
539-631 |
3.03e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 539 SAQARKDQKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEECEM 618
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|...
gi 446557484 619 AWLEAQEQLEQML 631
Cdd:COG4942 98 ELEAQKEELAELL 110
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
109-214 |
3.56e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.52 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 109 AIATIHGKLDAidawsirsraaslLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSD---LLLLDEPTNHLDLDAV 185
Cdd:cd03271 142 NIPKIARKLQT-------------LCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDV 208
|
90 100 110
....*....|....*....|....*....|....*
gi 446557484 186 IWLEKWLKS--YQG-TLILISHDRDFL---DPIVD 214
Cdd:cd03271 209 KKLLEVLQRlvDKGnTVVVIEHNLDVIkcaDWIID 243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
513-629 |
4.00e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 513 EDYQQWLSDVQKQENQADEAPKENANSAQARKD-------QKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKL 585
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEEleeqletLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446557484 586 gdSELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQ 629
Cdd:TIGR02168 424 --EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
149-222 |
4.07e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 38.71 E-value: 4.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 149 DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD----LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQ 222
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
512-624 |
4.09e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 512 LEDYQQWLSDVQKQENQADEAPKENANSAQARKdqkrrEAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLgdSELY 591
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEELLEALD-----EEELEEELEELEEELEELEEELEELREELAELEAEL--EQLE 466
|
90 100 110
....*....|....*....|....*....|...
gi 446557484 592 DQSRKAELtacLQQQASAKSGLEECEMAWLEAQ 624
Cdd:COG4717 467 EDGELAEL---LQELEELKAELRELAEEWAALK 496
|
|
| Mod_r |
pfam07200 |
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region ... |
512-631 |
4.18e-03 |
|
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region approximately 150 residues long within a number of eukaryotic proteins that show homology with Drosophila melanogaster Modifier of rudimentary (Mod(r)) proteins. The N-terminal half of Mod(r) proteins is acidic, whereas the C-terminal half is basic, and both of these regions are represented in this family. Members of this family include the Vps37 subunit of the endosomal sorting complex ESCRT-I, a complex involved in recruiting transport machinery for protein sorting at the multivesicular body (MVB). The yeast ESCRT-I complex consists of three proteins (Vps23, Vps28 and Vps37). The mammalian homolog of Vps37 interacts with Tsg101 (Pfam: PF05743) through its mod(r) domain and its function is essential for lysosomal sorting of EGF receptors.
Pssm-ID: 462117 [Multi-domain] Cd Length: 146 Bit Score: 37.98 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 512 LEDYQQWLSDVQKQENQADEAPKENANSAQARKDQKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELY 591
Cdd:pfam07200 18 LDAFVHSLPQVKALQAEKEELLAENESLAEENLSLEPELEELRSQLQELLEELKALKSEYEEKEQELDELLSKFSPDALL 97
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446557484 592 dqsrkaeltACLQQQASAKsgLEECEM---AWLEAQEQLEQML 631
Cdd:pfam07200 98 ---------ARLQAAAAEA--EEESEAlaeSFLEGEIDLDEFL 129
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
108-214 |
4.21e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 108 QAIATIHGKLDaidawsirsraasLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSD---LLLLDEPTNHLDLDA 184
Cdd:TIGR00630 801 EAVPSISRKLQ-------------TLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDD 867
|
90 100 110
....*....|....*....|....*....|....*.
gi 446557484 185 VIWLEKWLKSY--QG-TLILISHDRDFL---DPIVD 214
Cdd:TIGR00630 868 IKKLLEVLQRLvdKGnTVVVIEHNLDVIktaDYIID 903
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
304-369 |
4.93e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 39.25 E-value: 4.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557484 304 APESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--ELAP---VSGEI 369
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPgarVEGEI 73
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
562-586 |
6.50e-03 |
|
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 39.65 E-value: 6.50e-03
10 20
....*....|....*....|....*
gi 446557484 562 KEIARLEKEMEKLNAQLAQAEEKLG 586
Cdd:COG0525 815 AERARLEKELAKLEKEIARVEKKLS 839
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
515-624 |
7.28e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 515 YQQWLSDVQKQENQADEAPKENANSAQARKDQKRREAELRAQ--------TQPLRKEIARLEKEMEKLNAQLAQAEEKLG 586
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERERRRARLEALLA 369
|
90 100 110
....*....|....*....|....*....|....*...
gi 446557484 587 DSELYDQSRKAELTAcLQQQASAKSGLEECEMAWLEAQ 624
Cdd:COG4913 370 ALGLPLPASAEEFAA-LRAEAAALLEALEEELEALEEA 406
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-62 |
7.29e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.33 E-value: 7.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446557484 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG 62
Cdd:PRK10982 10 GVKAL-DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG 59
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
497-633 |
7.36e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 497 LYLVHDRKVEpfdgdlEDYQQWLSDVQKQENQADEApKENANSAQARKDQKRRE-AELRAQTQPLRKEIARLEKEMEKLN 575
Cdd:COG1196 229 LLLLKLRELE------AELEELEAELEELEAELEEL-EAELAELEAELEELRLElEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446557484 576 AQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQMLLE 633
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
534-628 |
7.71e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 534 KENANSAQARKDQKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGL 613
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARI 767
|
90
....*....|....*
gi 446557484 614 EECEMAWLEAQEQLE 628
Cdd:TIGR02169 768 EELEEDLHKLEEALN 782
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
502-629 |
8.78e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557484 502 DRKVEPFDgDLEDYQQWLSDVQKQENQADEAPKENANSAQARKD---------------QKRREAELRAQTQPLRKEIAR 566
Cdd:COG4913 228 DALVEHFD-DLERAHEALEDAREQIELLEPIRELAERYAAARERlaeleylraalrlwfAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557484 567 LEKEMEKLNAQLAQAEEKLGD-SELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQ 629
Cdd:COG4913 307 LEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
|
| |
