|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-633 |
0e+00 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 1330.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQLAWVNQETPALPQPA 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 IDYVIDGDREYRQLEAALQQANERNDGHAIATVHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNL 160
Cdd:PRK10636 81 LEYVIDGDREYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIEQQTMFEYTGNYSSFEVQRAT 240
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 241 RLAQQQAMYESQQQRVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHFSFRQPESLPNPLLKMEKVSA 320
Cdd:PRK10636 241 RLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 321 GYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLAR 400
Cdd:PRK10636 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLAR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 401 LAPQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL 480
Cdd:PRK10636 401 LAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 481 VVVSHDRHLIRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDSQKQESQSGEAPKE-SGNSAQARKDQKRREAELRSQTQP 559
Cdd:PRK10636 481 VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQENQTDEAPKEnNANSAQARKDQKRREAELRTQTQP 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 560 LRKEIARLEKEMDKLNAQLASAEEKLGDSELYDASRKAELTECLQQQASAKSGLEECEMAWLEAQEQLERMLQE 633
Cdd:PRK10636 561 LRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQMLLE 634
|
|
| 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: 755.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 4 FSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQLAWVNQETPALP-QPAID 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDdLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 83 YVIDGDREYRQLEAALQQANER-----NDGHAIATVHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMR 157
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKlaepdEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIEQQTMFEYTGNYSSFEVQ 237
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 238 RATRLAQQQAMYESQQQRVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHFSFRQPESLPNPLLKMEK 317
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKVLELEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 318 VSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKLGYFAQHQlEFLRADESPLQH 397
Cdd:COG0488 321 LSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDPDKTVLDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 398 LARLAPQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFE 477
Cdd:COG0488 400 LRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 490290321 478 GALVVVSHDRHLIRSTTDDLYLVHDGKVEPFDGDLEDYQQW 518
Cdd:COG0488 480 GTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-519 |
2.28e-133 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 407.71 E-value: 2.28e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEiSADGgsmtFPGNWQLAWVNQETPALPQPAI 81
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMH-AIDG----IPKNCQILHVEQEVVGDDTTAL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 82 DYVIDGDREYRQL---EAALQQANERND---------------------GHAIATVHGKLDAIDAWTIRSRAASLLHGLG 137
Cdd:PLN03073 253 QCVLNTDIERTQLleeEAQLVAQQRELEfetetgkgkgankdgvdkdavSQRLEEIYKRLELIDAYTAEARAASILAGLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 138 FSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKII 217
Cdd:PLN03073 333 FTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDIL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 218 HIEQQTMFEYTGNYSSFEVQRATRLAQQQAMYESQQQRVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNP 297
Cdd:PLN03073 413 HLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLGHVDAVVNDPD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 298 FHFSFRQPESLPN-PLLKMEKVSAGY-GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGI 375
Cdd:PLN03073 493 YKFEFPTPDDRPGpPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 376 KLGYFAQHQLEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
Cdd:PLN03073 573 RMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLD 652
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 456 EPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKVEPFDGDLEDYQQWL 519
Cdd:PLN03073 653 EPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKTL 716
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-515 |
2.42e-106 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 331.47 E-value: 2.42e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQLAWVNQETPALPQ-P 79
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEfT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 80 AIDYVIDGDREYRQLEA------ALQQANErNDGHAIATVHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGG 153
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQerdriyALPEMSE-EDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIEQQTMFEYTGNYSS 233
Cdd:PRK15064 160 WKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 234 FEVQRATRLAQQQAMYESQQQRVAHLQSYIDRFRAKATKAKQAQSRIKMLERMEL--IAPAHVDNPFhFSFRQPESLPNP 311
Cdd:PRK15064 240 YMTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLeeVKPSSRQNPF-IRFEQDKKLHRN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKLGYFAQ-HQLEFlRA 390
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQdHAYDF-EN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 DESPLQHLARLA-PQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
Cdd:PRK15064 398 DLTLFDWMSQWRqEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESL 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 490290321 470 TEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKVEPFDGDLEDY 515
Cdd:PRK15064 478 NMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-626 |
1.20e-85 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 280.68 E-value: 1.20e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 16 LLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQLAWVNQETPALPQPAI-DYVIDGDRE---- 90
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGTVyDFVAEGIEEqaey 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 91 ---YRQLEAAL-QQANERNDGHaIATVHGKLDAIDAWTIRSRAASLLHGLGFSNEQlerPVSDFSGGWRMRLNLAQALIC 166
Cdd:PRK11147 98 lkrYHDISHLVeTDPSEKNLNE-LAKLQEQLDHHNLWQLENRINEVLAQLGLDPDA---ALSSLSGGWLRKAALGRALVS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 167 RSDLLLLDEPTNHLDLDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIEQQTMFEYTGNYSSFEVQRATRL---A 243
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALrveE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 244 QQQAMYEsqqQRVAHLQSYI----------DRFRAKATKAKQaQSRIKMLERMElIAPAHVDNpfhfSFRQPESlpnpLL 313
Cdd:PRK11147 254 LQNAEFD---RKLAQEEVWIrqgikarrtrNEGRVRALKALR-RERSERREVMG-TAKMQVEE----ASRSGKI----VF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 314 KMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKLGYFAQHQLEfLRADES 393
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAE-LDPEKT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 394 PLQHLARlAPQELEQKLRD-----YLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQA 468
Cdd:PRK11147 400 VMDNLAE-GKQEVMVNGRPrhvlgYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLEL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 469 LTEALIDFEGALVVVSHDRHLIRSTTDDLYLVH-DGKVEPFDGDLEDYQQWLSDSQKQESQSGEAPKEsgNSAQARKDQK 547
Cdd:PRK11147 479 LEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIGRYVGGYHDARQQQAQYLALKQPAVKKKEE--AAAPKAETVK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 548 RREAELRSQtqpLRKEIARLEKEMDKLNAQLASAEEKLGDSELYdaSRKAELTE-CLQQQASAKSGLEECEMAW--LEAQ 624
Cdd:PRK11147 557 RSSKKLSYK---LQRELEQLPQLLEDLEAEIEALQAQVADADFF--SQPHEQTQkVLADLADAEQELEVAFERWeeLEAL 631
|
..
gi 490290321 625 EQ 626
Cdd:PRK11147 632 KN 633
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-518 |
2.11e-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: 277.59 E-value: 2.11e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSL---LKNEIsaDGGSMTFPGnWQLAWVNQEtPALpQPAIDY---VIDG 87
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRImagVDKDF--NGEARPQPG-IKVGYLPQE-PQL-DPTKTVrenVEEG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 88 DREYRQL-----EAALQQANERNDGHAIATVHGKL----DAIDAWTIRSRAASLLHGLGFSNEqlERPVSDFSGGWRMRL 158
Cdd:TIGR03719 93 VAEIKDAldrfnEISAKYAEPDADFDKLAAEQAELqeiiDAADAWDLDSQLEIAMDALRCPPW--DADVTKLSGGERRRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIEQQTMFEYTGNYSSFEVQR 238
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 239 ATRLAQQQAMYESQQQRVAHLQSYIdRFRAKATKAKQaQSRIKMLERMELIAPAHVDNPFHFSFRQPESLPNPLLKMEKV 318
Cdd:TIGR03719 251 QKRLEQEEKEESARQKTLKRELEWV-RQSPKGRQAKS-KARLARYEELLSQEFQKRNETAEIYIPPGPRLGDKVIEAENL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 319 SAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKLGYFAQHQlEFLRADESPLQHL 398
Cdd:TIGR03719 329 TKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSR-DALDPNKTVWEEI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 399 A------RLAPQELEQklRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
Cdd:TIGR03719 408 SggldiiKLGKREIPS--RAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEA 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 490290321 473 LIDFEGALVVVSHDR-HLIRSTTDDLYLVHDGKVEPFDGDLEDYQQW 518
Cdd:TIGR03719 486 LLNFAGCAVVISHDRwFLDRIATHILAFEGDSHVEWFEGNFSEYEED 532
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-518 |
1.04e-78 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 260.05 E-value: 1.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLkneisadggsmtfpgnwqlAWVNQE-----TPA-------LPQ-PA 80
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------------AGVDKEfegeaRPApgikvgyLPQePQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 ID-------YVIDGDREYRQL-----EAALQQANERNDGHAIATVHGKL----DAIDAWTIRSraasllhglgfsneQLE 144
Cdd:PRK11819 81 LDpektvreNVEEGVAEVKAAldrfnEIYAAYAEPDADFDALAAEQGELqeiiDAADAWDLDS--------------QLE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 145 R------------PVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTGTLILISHDRDFLDPI 212
Cdd:PRK11819 147 IamdalrcppwdaKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 213 VDKIIHIEQQTMFEYTGNYSSFEVQRATRLAQQQAMYESQQQRVAHLQSYIdRFRAKATKAK-----------QAQSRIK 281
Cdd:PRK11819 227 AGWILELDRGRGIPWEGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWV-RQSPKARQAKskarlaryeelLSEEYQK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 282 MLERMELIAPAhvdnpfhfsfrqPESLPNPLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGE 361
Cdd:PRK11819 306 RNETNEIFIPP------------GPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 362 LQPVSGEIGLAKGIKLGYFAQHqleflRADESP-----------LQHLaRLAPQELEQklRDYLGGFGF----QGDKVSE 426
Cdd:PRK11819 374 EQPDSGTIKIGETVKLAYVDQS-----RDALDPnktvweeisggLDII-KVGNREIPS--RAYVGRFNFkggdQQKKVGV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 427 etrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDR-HLIRSTTDDLYLVHDGKV 505
Cdd:PRK11819 446 ----LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRwFLDRIATHILAFEGDSQV 521
|
570
....*....|...
gi 490290321 506 EPFDGDLEDYQQW 518
Cdd:PRK11819 522 EWFEGNFQEYEED 534
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
313-504 |
5.55e-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: 188.81 E-value: 5.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKLGYFAQhqleflrade 392
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 393 splqhlarlapqeleqklrdylggfgfqgdkvseetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
Cdd:cd03221 71 --------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEA 112
|
170 180 190
....*....|....*....|....*....|..
gi 490290321 473 LIDFEGALVVVSHDRHLIRSTTDDLYLVHDGK 504
Cdd:cd03221 113 LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-235 |
2.96e-49 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 179.49 E-value: 2.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQLAWVNQETPALP--Q 78
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDpdK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 79 PAIDYVIDGDREYRQLEaalqqanerndghaiatvhgkldaidawtirsrAASLLHGLGFSNEQLERPVSDFSGGWRMRL 158
Cdd:COG0488 395 TVLDELRDGAPGGTEQE---------------------------------VRGYLGRFLFSGDDAFKPVGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIEQQTMFEYTGNYSSFE 235
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYL 518
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-223 |
1.82e-47 |
|
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: 163.39 E-value: 1.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQLAWVNQetpalpqpai 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 82 dyvidgdreyrqleaalqqanerndghaiatvhgkldaidawtirsraasllhglgfsneqlerpvsdFSGGWRMRLNLA 161
Cdd:cd03221 71 --------------------------------------------------------------------LSGGEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490290321 162 QALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIEQQT 223
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-505 |
5.30e-42 |
|
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: 159.30 E-value: 5.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADG---GSMTFPGNWQLAWvnqeTPALPQPAID 82
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLEL----SEALRGRRIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 83 YVidgdreyrqLEAALQQANERNDGHAIATVhGKLDAIDAWTIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQ 162
Cdd:COG1123 87 MV---------FQDPMTQLNPVTVGDQIAEA-LENLGLSRAEARARVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 163 ALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKGYTG-TLILISHDRDFLDPIVDKIIHIEQQTMFEytgnyssfevqr 238
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRIVE------------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 239 atrlaqqqamyesqqqrvahlqsyidrfrakATKAKQAQSRIKMLERMELIAPAHVDNPfhfsfrQPESLPNPLLKMEKV 318
Cdd:COG1123 224 -------------------------------DGPPEEILAAPQALAAVPRLGAARGRAA------PAAAAAEPLLEVRNL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 319 SAGY-----GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYFAQHQLEFLRAD-- 391
Cdd:COG1123 267 SKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI-LFDGKDLTKLSRRSLRELRRRvq 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 392 --------------------ESPLQHLARLAPQELEQKLRDYLggfgfqgDKV--SEETRR-----FSGGEKARLVLA-- 442
Cdd:COG1123 346 mvfqdpysslnprmtvgdiiAEPLRLHGLLSRAERRERVAELL-------ERVglPPDLADrypheLSGGQRQRVAIAra 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 443 LIVwqRPNLLLLDEPTNHLDLDMRQALTEALID----FEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:COG1123 419 LAL--EPKLLILDEPTSALDVSVQAQILNLLRDlqreLGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
217-300 |
4.83e-35 |
|
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: 127.30 E-value: 4.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 217 IHIEQQTMFEYTGNYSSFEVQRATRLAQQQAMYESQQQRVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDN 296
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK 80
|
....*
gi 490290321 297 P-FHF 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 |
1.61e-31 |
|
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: 129.28 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 315 MEKVSAGY-GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKLGYFAQH-QL------- 385
Cdd:TIGR03719 7 MNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEpQLdptktvr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 386 EFLRADESPLQHL-------------------ARLAPQ-ELEQKLrDYLGGFGF--QGDKVSEETR---------RFSGG 434
Cdd:TIGR03719 87 ENVEEGVAEIKDAldrfneisakyaepdadfdKLAAEQaELQEII-DAADAWDLdsQLEIAMDALRcppwdadvtKLSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 435 EKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKVEPFDGdleD 514
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEG---N 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 515 YQQWLsdSQKQESQSGEAPKESgnsaqARKDQKRREAELRSQTQPLR--KEIARLEKeMDKLNAQlaSAEEKLGDSELY 591
Cdd:TIGR03719 243 YSSWL--EQKQKRLEQEEKEES-----ARQKTLKRELEWVRQSPKGRqaKSKARLAR-YEELLSQ--EFQKRNETAEIY 311
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
313-505 |
1.74e-31 |
|
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: 120.20 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIglakgIKLGYfaqhqlEFLRADE 392
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEI-----KVLGK------DIKKEPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 393 SPLQHLArLAPQEleqklrdylggFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
Cdd:cd03230 70 EVKRRIG-YLPEE-----------PSLYENLTVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWEL 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 490290321 473 LIDF--EGALVVV-SHDRHLIRSTTDDLYLVHDGKV 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 |
1.03e-30 |
|
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: 118.31 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 314 KMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGIKLGYFAQHQLeflrades 393
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD-GKDLASLSPKEL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 394 pLQHLArLAPQELEQklrdyLGGFGFQGDKVSEetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
Cdd:cd03214 72 -ARKIA-YVPQALEL-----LGLAHLADRPFNE----LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELL 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 490290321 474 IDF---EGALVV-VSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:cd03214 141 RRLareRGKTVVmVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
314-504 |
2.31e-30 |
|
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: 116.58 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 314 KMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIglakgiklgyfaqhqlEFLrades 393
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI----------------LID----- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 394 pLQHLARLAPQELEQKLrdylgGFGFQgdkvseetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
Cdd:cd00267 60 -GKDIAKLPLEELRRRI-----GYVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELL 123
|
170 180 190
....*....|....*....|....*....|....
gi 490290321 474 IDF--EG-ALVVVSHDRHLIRSTTDDLYLVHDGK 504
Cdd:cd00267 124 RELaeEGrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
309-515 |
5.04e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 118.65 E-value: 5.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 309 PNPLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL------AKGIKLGYFAQ 382
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 383 HQ----------LEFLRADESPLQHLARLAPQELEQKLRDYL---GGFGFQGDKVSEetrrFSGGEKARLVLA--LIvwQ 447
Cdd:COG1121 83 RAevdwdfpitvRDVVLMGRYGRRGLFRRPSRADREAVDEALervGLEDLADRPIGE----LSGGQQQRVLLAraLA--Q 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 448 RPNLLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLIRSTTDDLYLVHDGKVepFDGDLEDY 515
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELrrEGkTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPPEEV 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
314-504 |
6.67e-30 |
|
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: 117.18 E-value: 6.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 314 KMEKVSAGY--GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGY------------ 379
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEV-LVDGKDLTKlslkelrrkvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 380 ---FAQHQLEFLRADE---SPLQHLArLAPQELEQKLRDYLGGFGFQGDKvSEETRRFSGGEKARLVLALIVWQRPNLLL 453
Cdd:cd03225 80 vfqNPDDQFFGPTVEEevaFGLENLG-LPEEEIEERVEEALELVGLEGLR-DRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490290321 454 LDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLIRSTTDDLYLVHDGK 504
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
322-514 |
7.96e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 117.86 E-value: 7.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 322 YGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI---GL-----AKGIK--LGYFAQHQ--LEFLR 389
Cdd:COG1131 10 YGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlGEdvardPAEVRrrIGYVPQEPalYPDLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 390 ADESpLQHLARLAP---QELEQKLRDYLGGFGFqGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
Cdd:COG1131 90 VREN-LRFFARLYGlprKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEAR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490290321 467 QALTEALIDF--EGALVVVS-HDRHLIRSTTDDLYLVHDGKVEpFDGDLED 514
Cdd:COG1131 168 RELWELLRELaaEGKTVLLStHYLEEAERLCDRVAIIDKGRIV-ADGTPDE 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
312-523 |
8.44e-30 |
|
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: 118.04 E-value: 8.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGI---KLGYFAQHQLEFL 388
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSI-LIDGEdvrKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 389 rADESPL----------QHLARLAP---QELEQKLRDYLGGFGFQGD---KVSEetrrFSGGEKARLVLALIVWQRPNLL 452
Cdd:COG4555 80 -PDERGLydrltvreniRYFAELYGlfdEELKKRIEELIELLGLEEFldrRVGE----LSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 453 LLDEPTNHLDLDMRQALTEALIDF--EGALVVVS-HDRHLIRSTTDDLYLVHDGKVePFDGDLEDYQQWLSDSQ 523
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALkkEGKTVLFSsHIMQEVEALCDRVVILHKGKV-VAQGSLDELREEIGEEN 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
313-514 |
8.72e-30 |
|
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: 117.43 E-value: 8.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGY-GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGI------------KLGY 379
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEV-LVDGKditkknlrelrrKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 380 ---FAQHQLeFLR--ADE---SPLQHlaRLAPQELEQKLRDYLGGFGFQG--DKvseETRRFSGGEKARLVLALIVWQRP 449
Cdd:COG1122 80 vfqNPDDQL-FAPtvEEDvafGPENL--GLPREEIRERVEEALELVGLEHlaDR---PPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 450 NLLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLIRSTTDDLYLVHDGKVEpFDGDLED 514
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADRVIVLDDGRIV-ADGTPRE 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
312-505 |
2.69e-29 |
|
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: 116.68 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI---G----------LAKgiKLG 378
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldGrdlaslsrreLAR--RIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 379 YFAQ-HQLEF-LRADESPLqhLARLApqeleqklrdYLGGFGFQGDK----VSE----------ETRRF---SGGEKARL 439
Cdd:COG1120 79 YVPQePPAPFgLTVRELVA--LGRYP----------HLGLFGRPSAEdreaVEEalertglehlADRPVdelSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 440 VLALIVWQRPNLLLLDEPTNHLDLDMRQALTE---ALIDFEG-ALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLEllrRLARERGrTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-221 |
2.90e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 115.30 E-value: 2.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNW-----------QLAWVN 70
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 71 QEtPALPqpaidyvidGDREYRQLEAALQQANERNDghaiatvhgkldaidawtiRSRAASLLHGLGFSNEQLERPVSDF 150
Cdd:COG4619 81 QE-PALW---------GGTVRDNLPFPFQLRERKFD-------------------RERALELLERLGLPPDILDKPVERL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVI-WLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:COG4619 132 SGGERQRLALIRALLLQPDVLLLDEPTSALDPEntrRVEeLLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
315-591 |
3.26e-28 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 119.45 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 315 MEKVSAGYG-ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKLGYFAQH-QLeflraDE 392
Cdd:PRK11819 9 MNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEpQL-----DP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 393 SP-------------LQHLARL------------------APQ-ELEQKLrDYLGGFGFQ--------------GD-KVS 425
Cdd:PRK11819 84 EKtvrenveegvaevKAALDRFneiyaayaepdadfdalaAEQgELQEII-DAADAWDLDsqleiamdalrcppWDaKVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 426 eetrRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK11819 163 ----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 506 EPFDGdleDYQQWLsdSQKQESQSGEAPKESgnsaqARkdQKRREAEL---RS-----QTqplrKEIARLEKeMDKLNAQ 577
Cdd:PRK11819 239 IPWEG---NYSSWL--EQKAKRLAQEEKQEA-----AR--QKALKRELewvRQspkarQA----KSKARLAR-YEELLSE 301
|
330
....*....|....
gi 490290321 578 laSAEEKLGDSELY 591
Cdd:PRK11819 302 --EYQKRNETNEIF 313
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-288 |
8.83e-28 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 118.51 E-value: 8.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQLAWVNQETPAL--PQPAIDYVIDGDREy 91
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELdpEKTVMDNLAEGKQE- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 92 rqleaalqqanerndghaiATVHGkldaidawtiRSRaasllHGLG------FSNEQLERPVSDFSGGWRMRLNLAQALI 165
Cdd:PRK11147 411 -------------------VMVNG----------RPR-----HVLGylqdflFHPKRAMTPVKALSGGERNRLLLARLFL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 166 CRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKII------HIEqqtmfEYTGNYSSFEVQRA 239
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWifegngKIG-----RYVGGYHDARQQQA 531
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490290321 240 TRLAQQQAMYESQQQRVAhlqsyidrfrAKATKAKQAQSRIKMLERMEL 288
Cdd:PRK11147 532 QYLALKQPAVKKKEEAAA----------PKAETVKRSSKKLSYKLQREL 570
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
313-505 |
1.17e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 110.68 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLaKGI------------KLGYF 380
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYL-DGKplsampppewrrQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 381 AQhqlEFLRADESPLQHLA---RLAPQEL-EQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDE 456
Cdd:COG4619 80 PQ---EPALWGGTVRDNLPfpfQLRERKFdRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490290321 457 PTNHLDLDMRQALTEALIDF----EGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:COG4619 157 PTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
328-459 |
1.29e-27 |
|
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: 108.50 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAK-----------GIKLGYFAQHQLEFLR------- 389
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslRKEIGYVFQDPQLFPRltvrenl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 390 ADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-221 |
1.69e-27 |
|
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: 109.02 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqlawVNQETPALPQPAI 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK-----DIKKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 82 DYVIDGDREYRQLeaalqqanerndghaiaTVHgkldaidawtirsraasllhglgfsnEQLerpvsDFSGGWRMRLNLA 161
Cdd:cd03230 76 GYLPEEPSLYENL-----------------TVR--------------------------ENL-----KLSGGMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490290321 162 QALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYT---GTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNN 170
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-242 |
7.61e-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: 115.03 E-value: 7.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQLAWVNQETPALpqpaidyviDGDREY 91
Cdd:TIGR03719 333 GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDAL---------DPNKTV 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 92 RQleaalqqanERNDGHAIATVHGKldaidawTIRSRAasLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
Cdd:TIGR03719 404 WE---------EISGGLDIIKLGKR-------EIPSRA--YVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 172 LLDEPTNHLDLDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIE---QQTMFEytGNYSSFEVQRATRL 242
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgdsHVEWFE--GNFSEYEEDKKRRL 537
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-221 |
3.61e-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: 106.41 E-value: 3.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQlawvnQETPALPQPA 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-----RDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 IDYVIDGDREYRQLEAA--LQqanerndghAIATVHGKLDAidawtiRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRL 158
Cdd:COG4133 77 LAYLGHADGLKPELTVRenLR---------FWAALYGLRAD------REAIDEALEAVGLA-GLADLPVRQLSAGQKRRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYT---GTLILISHDRDFLDPivDKIIHIEQ 221
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAA--ARVLDLGD 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-221 |
3.88e-26 |
|
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: 107.25 E-value: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqetpalpqpa 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 IDYVIDgDREYRQLEAALQQANErndGHAIATV------HGKLDAIDAWTIRSRAASLLHGLGFSnEQLERPVSDFSGGW 154
Cdd:COG4555 63 EDVRKE-PREARRQIGVLPDERG---LYDRLTVreniryFAELYGLFDEELKKRIEELIELLGLE-EFLDRRVGELSTGM 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 155 RMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGY--TGTLILIS-HDRDFLDPIVDKIIHIEQ 221
Cdd:COG4555 138 KKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkEGKTVLFSsHIMQEVEALCDRVVILHK 207
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-217 |
4.03e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 107.07 E-value: 4.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSmtfpgnwqlAWVNQETPALPQPA- 80
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGE---------VRVLGEDVARDPAEv 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 ---IDYVIDGDREYRQLeaalqqanernDGHAIATVHGKLDAIDAWTIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMR 157
Cdd:COG1131 72 rrrIGYVPQEPALYPDL-----------TVRENLRFFARLYGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490290321 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYT--GTLILIS-HDRDFLDPIVDKII 217
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAaeGKTVLLStHYLEEAERLCDRVA 202
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
313-504 |
4.80e-26 |
|
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: 104.77 E-value: 4.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERI--ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLgyfAQHQLEFLRa 390
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI-LIDGVDL---RDLDLESLR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 desplQHLArLAPQEleqklrDYLggfgFQGdkvseeTRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
Cdd:cd03228 76 -----KNIA-YVPQD------PFL----FSG------TIReniLSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 490290321 468 ALTEALIDFEG--ALVVVSHDRHLIRStTDDLYLVHDGK 504
Cdd:cd03228 134 LILEALRALAKgkTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-504 |
2.15e-25 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 111.05 E-value: 2.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 23 TINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNW-----------------QLAwVNQETPAL-PQpAIDY- 83
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWdevlkrfrgtelqnyfkKLY-NGEIKVVHkPQ-YVDLi 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 84 --VIDGdrEYRQLeaaLQQANERndghaiatvhGKLDaidawtirsraaSLLHGLGFSNeQLERPVSDFSGGWRMRLNLA 161
Cdd:PRK13409 173 pkVFKG--KVREL---LKKVDER----------GKLD------------EVVERLGLEN-ILDRDISELSGGELQRVAIA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 162 QALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTG--TLILISHDRDFLDPIVDkIIHIeqqtMFEYTGNYSSFEVQRA 239
Cdd:PRK13409 225 AALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEgkYVLVVEHDLAVLDYLAD-NVHI----AYGEPGAYGVVSKPKG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 240 TRLAQQQamyesqqqrvaHLQSYID----RFRakatkakqaqsrikmlermeliapahvDNPFHFSFRQPESLPN--PLL 313
Cdd:PRK13409 300 VRVGINE-----------YLKGYLPeenmRIR---------------------------PEPIEFEERPPRDESEreTLV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 314 KMEKVSAGYGEriildsIKLNLVPGSR-----IGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkgIKLGYFAQHQL--- 385
Cdd:PRK13409 342 EYPDLTKKLGD------FSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--LKISYKPQYIKpdy 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 386 -----EFLRA-----DESPLQH-------LARLapqeLEQKLRDylggfgfqgdkvseetrrFSGGEKARLVLALIVWQR 448
Cdd:PRK13409 414 dgtveDLLRSitddlGSSYYKSeiikplqLERL----LDKNVKD------------------LSGGELQRVAIAACLSRD 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 449 PNLLLLDEPTNHLDLDMRQALTEA---LID-FEGALVVVSHDRHLIRSTTDDLyLVHDGK 504
Cdd:PRK13409 472 ADLYLLDEPSAHLDVEQRLAVAKAirrIAEeREATALVVDHDIYMIDYISDRL-MVFEGE 530
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-221 |
2.77e-25 |
|
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: 104.09 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPQpaidyvi 85
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDG--------KDLTKLSL------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 86 dgdREYRQLEA-ALQQANerndgHAI--ATV---------HGKLDAIDawtIRSRAASLLHGLGFSnEQLERPVSDFSGG 153
Cdd:cd03225 71 ---KELRRKVGlVFQNPD-----DQFfgPTVeeevafgleNLGLPEEE---IEERVEEALELVGLE-GLRDRSPFTLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTG---TLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03225 139 QKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
4.44e-25 |
|
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: 109.85 E-value: 4.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGV-RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTF---------PGNW--QLAWV 69
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIngvdlsdldPASWrrQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 70 NQeTPALPQPAI-----DYVIDGDREyrQLEAALQQANerndghaiatvhgkldaIDAWtirsrAASLLHGlgfsneqLE 144
Cdd:COG4988 417 PQ-NPYLFAGTIrenlrLGRPDASDE--ELEAALEAAG-----------------LDEF-----VAALPDG-------LD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 145 RPVSD----FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD--AVIW--LEKWLKGYtgTLILISHDRDFLDpIVDKI 216
Cdd:COG4988 465 TPLGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAEteAEILqaLRRLAKGR--TVILITHRLALLA-QADRI 541
|
....*
gi 490290321 217 IHIEQ 221
Cdd:COG4988 542 LVLDD 546
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
311-486 |
5.15e-25 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 102.94 E-value: 5.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLG-----YFAQ--- 382
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEV-LWNGEPIRdaredYRRRlay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 383 --HQLEfLRADESPLQHL---ARLAPQEL-EQKLRDYLGGFGFQG--DKvseETRRFSGGEKARLVLA-LIVWQRPnLLL 453
Cdd:COG4133 80 lgHADG-LKPELTVRENLrfwAALYGLRAdREAIDEALEAVGLAGlaDL---PVRQLSAGQKRRVALArLLLSPAP-LWL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 490290321 454 LDEPTNHLDLDMRQALTEALIDF---EGALVVVSHD 486
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQ 190
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
283-490 |
7.34e-25 |
|
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: 109.09 E-value: 7.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 283 LERMELIAPAHVDNPFHfsfRQPESLPNPL-LKMEKVSAGY--GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLA 359
Cdd:COG4987 306 ARRLNELLDAPPAVTEP---AEPAPAPGGPsLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 360 GELQPVSGEIGLAkGIKLGYFAQHQLeflRADESPL-QH-------------LAR--LAPQELEQKLRD-YLGGFGFQGD 422
Cdd:COG4987 383 RFLDPQSGSITLG-GVDLRDLDEDDL---RRRIAVVpQRphlfdttlrenlrLARpdATDEELWAALERvGLGDWLAALP 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 423 K-----VSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVVVSHDRHLI 490
Cdd:COG4987 459 DgldtwLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAGL 533
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-221 |
1.14e-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: 100.40 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 4 FSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqetpalpqpaIDY 83
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG------------------KDI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 84 VIDGDREYRQLeaalqqanerndghaIATVHgkldaidawtirsraasllhglgfsneQLerpvsdfSGGWRMRLNLAQA 163
Cdd:cd00267 64 AKLPLEELRRR---------------IGYVP---------------------------QL-------SGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTG---TLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
312-519 |
1.17e-24 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 108.88 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKLG------------- 378
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVArlqqdpprnvegt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 379 ---YFA---QHQLEFLRA------------DESPLQHLARLAPQ-------ELEQKLRDYLGGFGFQGD-KVSEetrrFS 432
Cdd:PRK11147 83 vydFVAegiEEQAEYLKRyhdishlvetdpSEKNLNELAKLQEQldhhnlwQLENRINEVLAQLGLDPDaALSS----LS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 433 GG--EKARLVLALIVwqRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKVEPFDG 510
Cdd:PRK11147 159 GGwlRKAALGRALVS--NPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPG 236
|
250
....*....|...
gi 490290321 511 DLEDY----QQWL 519
Cdd:PRK11147 237 NYDQYllekEEAL 249
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
314-500 |
1.55e-24 |
|
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: 101.84 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 314 KMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLA------KGIKLGYFAQHQ--- 384
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgkplekERKRIGYVPQRRsid 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 385 -------LEF----LRADESPLQHLARLAPQELEQKLrDYLGGFGFqgdkvseETRRF---SGGEKARLVLALIVWQRPN 450
Cdd:cd03235 81 rdfpisvRDVvlmgLYGHKGLFRRLSKADKAKVDEAL-ERVGLSEL-------ADRQIgelSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490290321 451 LLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLIRSTTDDLYLV 500
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELrrEGmTILVVTHDLGLVLEYFDRVLLL 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
260-505 |
4.61e-24 |
|
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: 107.23 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 260 QSYIDRFRAKATKAKQAQSRIKM----LERMELIAPAHVDNPFHFSFRQPESLpNPLLKMEKVSAGYG--ERIILDSIKL 333
Cdd:COG2274 418 NILSGRFLAPVAQLIGLLQRFQDakiaLERLDDILDLPPEREEGRSKLSLPRL-KGDIELENVSFRYPgdSPPVLDNISL 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 334 NLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGI------------KLGYFAQHQLEF---LR--------- 389
Cdd:COG2274 497 TIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI-LIDGIdlrqidpaslrrQIGVVLQDVFLFsgtIRenitlgdpd 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 390 ADESPLQHLARLApqELEQKLRDYLGGFGFQgdkVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
Cdd:COG2274 576 ATDEEIIEAARLA--GLHDFIEALPMGYDTV---VGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAII 650
|
250 260 270
....*....|....*....|....*....|....*...
gi 490290321 470 TEALIDFEG--ALVVVSHDRHLIRStTDDLYLVHDGKV 505
Cdd:COG2274 651 LENLRRLLKgrTVIIIAHRLSTIRL-ADRIIVLDKGRI 687
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
310-514 |
5.12e-24 |
|
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: 101.31 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 310 NPLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGE----IGLAKG------IK--L 377
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlFGERRGgedvweLRkrI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 378 GYFAQHQLEFLRADESPLQ----------HLARLAPQELEQKLRDYLGGFGFQGDKvseeTRRF---SGGEKaRLVL--- 441
Cdd:COG1119 81 GLVSPALQLRFPRDETVLDvvlsgffdsiGLYREPTDEQRERARELLELLGLAHLA----DRPFgtlSQGEQ-RRVLiar 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 442 ALIvwQRPNLLLLDEPTNHLDLDMRQALTEAL--IDFEG--ALVVVSHDRHLIRSTTDDLYLVHDGKVePFDGDLED 514
Cdd:COG1119 156 ALV--KDPELLILDEPTAGLDLGARELLLALLdkLAAEGapTLVLVTHHVEEIPPGITHVLLLKDGRV-VAAGPKEE 229
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-178 |
5.81e-24 |
|
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: 98.10 E-value: 5.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqlaWVNQETPALPQPAIDYVIDGDREYRQLEA 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQ----DLTDDERKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 97 alqqanERNdghaIATVhGKLDAIDAWTIRSRAASLLHGLG---FSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLL 173
Cdd:pfam00005 77 ------REN----LRLG-LLLKGLSKREKDARAEEALEKLGlgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLL 145
|
....*
gi 490290321 174 DEPTN 178
Cdd:pfam00005 146 DEPTA 150
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
321-499 |
7.85e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.23 E-value: 7.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 321 GYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKLGYFAQHqlefLRADES------- 393
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQR----SEVPDSlpltvrd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 394 -----------PLQHLARLAPQELEQKLrDYLGGFGFQGDKVSEetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:NF040873 77 lvamgrwarrgLWRRLTRDDRAAVDDAL-ERVGLADLAGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490290321 463 LDMRQALTEALIDF--EGALVV-VSHDRHLIRSTTDDLYL 499
Cdd:NF040873 152 AESRERIIALLAEEhaRGATVVvVTHDLELVRRADPCVLL 191
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-242 |
1.55e-23 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 104.82 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQLAWVNQETPALpqpaidyviDGDREY 91
Cdd:PRK11819 335 GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDAL---------DPNKTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 92 RQleaalqqanERNDGHAIATVHGKldaidawTIRSRAasLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
Cdd:PRK11819 406 WE---------EISGGLDIIKVGNR-------EIPSRA--YVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 172 LLDEPTNHLDLDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIE---QQTMFEytGNYSSFEVQRATRL 242
Cdd:PRK11819 468 LLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEgdsQVEWFE--GNFQEYEEDKKRRL 539
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
313-505 |
3.09e-23 |
|
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: 99.50 E-value: 3.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKLGYFAQHQ------LE 386
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARarrvalVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 387 FLRADESPLQ-----------HLARLA--PQELEQKLRDYLGGFGFQgDKVSEETRRFSGGEKARLVLALIVWQRPNLLL 453
Cdd:TIGR03873 82 QDSDTAVPLTvrdvvalgripHRSLWAgdSPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 454 LDEPTNHLDLDMRQALTEALIDF--EGALVVVS-HDRHLIRSTTDDLYLVHDGKV 505
Cdd:TIGR03873 161 LDEPTNHLDVRAQLETLALVRELaaTGVTVVAAlHDLNLAASYCDHVVVLDGGRV 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
305-486 |
3.11e-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: 103.98 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 305 PESLPNPLLKMEKVSAGY-GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL-----------A 372
Cdd:TIGR02868 327 AVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdgvpvssldqdE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 373 KGIKLGYFAQ--H--------QLEFLRADESPLQHLARLAPQELEQKLRDYLGGFGfqgDKVSEETRRFSGGEKARLVLA 442
Cdd:TIGR02868 407 VRRRVSVCAQdaHlfdttvreNLRLARPDATDEELWAALERVGLADWLRALPDGLD---TVLGEGGARLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490290321 443 LIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVVVSHD 486
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLAAlsGRTVVLITHH 529
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
5-205 |
6.31e-23 |
|
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: 98.35 E-value: 6.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 5 SSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG----NW-------QLAWVNQET 73
Cdd:TIGR03873 5 SRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGvdlhGLsrrararRVALVEQDS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 74 P-ALPQPAIDYVIDGDREYRQLEAAlqqanERNDGHAIAtvhgkldaiDAWTIRSRAASLLhglgfsneqlERPVSDFSG 152
Cdd:TIGR03873 85 DtAVPLTVRDVVALGRIPHRSLWAG-----DSPHDAAVV---------DRALARTELSHLA----------DRDMSTLSG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 153 GWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKGYTGTLILISHD 205
Cdd:TIGR03873 141 GERQRVHVARALAQEPKLLLLDEPTNHLDVRAqleTLALVRELAATGVTVVAALHD 196
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
1.20e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 97.47 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqETPALPQPA 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG---------KPPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 IDYVIdgdreyrqleaalQQANerNDGHAIATVH--------------GKLDAIDawtiRSRAASLLHGLGFSnEQLERP 146
Cdd:COG1121 77 IGYVP-------------QRAE--VDWDFPITVRdvvlmgrygrrglfRRPSRAD----REAVDEALERVGLE-DLADRP 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 147 VSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTG---TLILISHDRDFLDPIVDKIIHIEQQ 222
Cdd:COG1121 137 IGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
312-505 |
1.42e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 97.49 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIG-------------LAKgiKLG 378
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlngrplaawspweLAR--RRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 379 YFAQH-QLEF-LRADE------SPLQHLARLAPQELEQKL----------RDYlggfgfqgdkvseetRRFSGGEKARLV 440
Cdd:COG4559 79 VLPQHsSLAFpFTVEEvvalgrAPHGSSAAQDRQIVREALalvglahlagRSY---------------QTLSGGEQQRVQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 441 LA--LI-VWQ----RPNLLLLDEPTNHLDLDMRQALTEALIDF---EGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:COG4559 144 LArvLAqLWEpvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
313-505 |
1.52e-22 |
|
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: 94.98 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYG--ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIglakgiklgyfaqhqleflra 390
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 desplqhlaRLAPQELEQKLRDYLGGF-GF--QGDKVSEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
Cdd:cd03246 60 ---------RLDGADISQWDPNELGDHvGYlpQDDELFSGSIAeniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490290321 465 MRQALTEALIDFEGA---LVVVSHDRHLIRStTDDLYLVHDGKV 505
Cdd:cd03246 131 GERALNQAIAALKAAgatRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
311-497 |
1.57e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 97.11 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKLGYFAQHqlefLRA 390
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK----LYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 DES-PL--QHLARLAPQELEQKLRDYLGGFGfQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
Cdd:PRK09544 79 DTTlPLtvNRFLRLRPGTKKEDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190
....*....|....*....|....*....|....*
gi 490290321 468 ALTEaLID-----FEGALVVVSHDRHLIRSTTDDL 497
Cdd:PRK09544 158 ALYD-LIDqlrreLDCAVLMVSHDLHLVMAKTDEV 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-505 |
2.01e-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: 101.42 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLSLLK--NEISADGGSMTFpgnwQLAW------------VNQETP--- 74
Cdd:TIGR03269 12 GKEVL-KNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmDQYEPTSGRIIY----HVALcekcgyverpskVGEPCPvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 75 -ALPQPAIDYVIDGDREYRQLEAALQQANERN-----DGHAIATVHGKLDAI--DAWTIRSRAASLLHGLGFSNeQLERP 146
Cdd:TIGR03269 87 gTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTfalygDDTVLDNVLEALEEIgyEGKEAVGRAVDLIEMVQLSH-RITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 147 VSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD-LDAVI---WLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIEQQ 222
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKLvhnALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 223 TMFEyTGNysSFEVqratrlaqqqamyesqqqrvahlqsyIDRFrakatkakqaQSRIKMLERMELIapahvdnpfhfsf 302
Cdd:TIGR03269 246 EIKE-EGT--PDEV--------------------------VAVF----------MEGVSEVEKECEV------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 303 rqpeSLPNPLLKMEKVSAGY-----GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKG--- 374
Cdd:TIGR03269 274 ----EVGEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdew 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 375 ---IKLGYFAQ----------HQLEFLRADESPLQHLARLA----PQELEQKLRDY-LGGFGFQGDKVSEETRRF----S 432
Cdd:TIGR03269 350 vdmTKPGPDGRgrakryigilHQEYDLYPHRTVLDNLTEAIglelPDELARMKAVItLKMVGFDEEKAEEILDKYpdelS 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 433 GGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTE----ALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsilkAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
313-505 |
2.25e-22 |
|
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: 95.72 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSrIGLLGRNGAGKSTLIKLLAGELQPVSGEI------GLAKGIK----LGYFAQ 382
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIridgqdVLKQPQKlrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 383 hqlEF-----LRADESpLQHLARL-------APQELEQKLRDyLGGFGFQGDKVSEetrrFSGGEKARLVLALIVWQRPN 450
Cdd:cd03264 80 ---EFgvypnFTVREF-LDYIAWLkgipskeVKARVDEVLEL-VNLGDRAKKKIGS----LSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 451 LLLLDEPTNHLDLDMRQALTEALIDF-EGALVVVS-HDRHLIRSTTDDLYLVHDGKV 505
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELgEDRIVILStHIVEDVESLCNQVAVLNKGKL 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-205 |
2.31e-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: 96.65 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG----NW-------QLAWV 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaSLsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 70 NQETPA-LPQPAIDYVIDGDREYRqleAALQQANERnDGHAIATVhgkLDAIDAWTIRsraasllhglgfsneqlERPVS 148
Cdd:COG1120 81 PQEPPApFGLTVRELVALGRYPHL---GLFGRPSAE-DREAVEEA---LERTGLEHLA-----------------DRPVD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 149 DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTG----TLILISHD 205
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARergrTVVMVLHD 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-205 |
5.39e-22 |
|
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: 93.65 E-value: 5.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 5 SSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPQpaidyv 84
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG--------KDLASLSP------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 85 idgdREYRQLEAALQQANERNDghaiatvhgkldaidawtirsrAASLLHglgfsneqleRPVSDFSGGWRMRLNLAQAL 164
Cdd:cd03214 69 ----KELARKIAYVPQALELLG----------------------LAHLAD----------RPFNELSGGERQRVLLARAL 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490290321 165 ICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTG----TLILISHD 205
Cdd:cd03214 113 AQEPPILLLDEPTSHLDIAHQIELLELLRRLARergkTVVMVLHD 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
303-505 |
8.91e-22 |
|
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: 99.45 E-value: 8.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 303 RQPESLPNPLLKMEKVSAGY-GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYFA 381
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI-LINGVDLSDLD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 382 QHQL-------------------EFLR-----ADESPLQHLARLA-----PQELEQKLRDYLGgfgfqgdkvsEETRRFS 432
Cdd:COG4988 406 PASWrrqiawvpqnpylfagtirENLRlgrpdASDEELEAALEAAgldefVAALPDGLDTPLG----------EGGRGLS 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 433 GGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID-FEGALV-VVSHDRHLIRStTDDLYLVHDGKV 505
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlAKGRTViLITHRLALLAQ-ADRILVLDDGRI 549
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-224 |
1.46e-21 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 93.05 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFpgnWQLAWVNQEtPALPQpaI 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF---DGKSYQKNI-EALRR--I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 82 DYVIDGDREYRQLEAalqqaneRNDGHAIATVHGKLDaidawtirSRAASLLHGLGFSNEQlERPVSDFSGGWRMRLNLA 161
Cdd:cd03268 75 GALIEAPGFYPNLTA-------RENLRLLARLLGIRK--------KRIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 162 QALICRSDLLLLDEPTNHLDLDAVIWLEKW---LKGYTGTLILISHDRDFLDPIVDKIIHIEQQTM 224
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
313-504 |
1.47e-21 |
|
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: 92.25 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIglakgiklgyfaqhqleflRADE 392
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI-------------------LIDG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 393 SPLQHLARLAPqELEQKLrdylgGFGFQ----------GDKVSEetrRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:cd03229 62 EDLTDLEDELP-PLRRRI-----GMVFQdfalfphltvLENIAL---GLSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490290321 463 LDMR---QALTEALIDFEG-ALVVVSHDRHLIRSTTDDLYLVHDGK 504
Cdd:cd03229 133 PITRrevRALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-504 |
1.48e-21 |
|
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: 99.09 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 26 PGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNW-----------------QLAwvNQE-TPAL-PQpAIDY--- 83
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWdevlkrfrgtelqdyfkKLA--NGEiKVAHkPQ-YVDLipk 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 84 VIDGdrEYRQLeaaLQQANERndghaiatvhGKLDAIdawtirsraASLLhGLgfsNEQLERPVSDFSGGWRMRLNLAQA 163
Cdd:COG1245 175 VFKG--TVREL---LEKVDER----------GKLDEL---------AEKL-GL---ENILDRDISELSGGELQRVAIAAA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTG---TLILISHDRDFLDPIVDkIIHIeqqtMFEYTGNYSSFEVQRAT 240
Cdd:COG1245 227 LLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEegkYVLVVEHDLAILDYLAD-YVHI----LYGEPGVYGVVSKPKSV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 241 RLAQQQamyesqqqrvaHLQSYID----RFRakatkakqaqsrikmlermeliapahvDNPFHFSFRQPESLPN--PLLK 314
Cdd:COG1245 302 RVGINQ-----------YLDGYLPeenvRIR---------------------------DEPIEFEVHAPRREKEeeTLVE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 315 MEKVSAGYGEriildsIKLNLVPGS-----RIGLLGRNGAGKSTLIKLLAGELQPVSGEIGlaKGIKLGYFAQHQL---- 385
Cdd:COG1245 344 YPDLTKSYGG------FSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKISYKPQYISpdyd 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 386 ----EFLRA------DESPLQH-------LARLapqeLEQKLRDylggfgfqgdkvseetrrFSGGEKARLVLALIVWQR 448
Cdd:COG1245 416 gtveEFLRSantddfGSSYYKTeiikplgLEKL----LDKNVKD------------------LSGGELQRVAIAACLSRD 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 449 PNLLLLDEPTNHLDLDMRQALTEALIDF----EGALVVVSHDRHLIRSTTDDLyLVHDGK 504
Cdd:COG1245 474 ADLYLLDEPSAHLDVEQRLAVAKAIRRFaenrGKTAMVVDHDIYLIDYISDRL-MVFEGE 532
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
313-505 |
1.81e-21 |
|
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: 93.11 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYFAQHQLEFLRADE 392
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV-LFDGKPLDIAARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 393 ---------SPLQHLARLA---PQELEQKLRDYLGGFGFqGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
Cdd:cd03269 80 glypkmkviDQLVYLAQLKglkKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490290321 461 LDLDMRQALTEALIDFEGA---LVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:cd03269 159 LDPVNVELLKDVIRELARAgktVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-221 |
2.28e-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: 98.30 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 16 LLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG----NW-------QLAWVNQETP---------- 74
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrDLdeddlrrRIAVVPQRPHlfdttlrenl 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 75 --ALPQpAIDyvidgdreyRQLEAALQQAnerndghaiatvhgkldAIDAWtirsrAASLLHGlgfsneqLERPVSD--- 149
Cdd:COG4987 430 rlARPD-ATD---------EELWAALERV-----------------GLGDW-----LAALPDG-------LDTWLGEggr 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 150 -FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD--AVIW--LEKWLKGytGTLILISHDRDFLDpIVDKIIHIEQ 221
Cdd:COG4987 471 rLSGGERRRLALARALLRDAPILLLDEPTEGLDAAteQALLadLLEALAG--RTVLLITHRLAGLE-RMDRILVLED 544
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
313-492 |
2.60e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 92.81 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGY-GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGIKLGYFAQHQLEFLR-- 389
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-GQDLSRLKRREIPYLRrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 390 -----------ADES-------PLQhLARLAPQELEQKLRDYLggfgfqgDKVSEETRRF------SGGEKARLVL--AL 443
Cdd:COG2884 81 igvvfqdfrllPDRTvyenvalPLR-VTGKSRKEIRRRVREVL-------DLVGLSDKAKalphelSGGEQQRVAIarAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490290321 444 IVwqRPNLLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLIRS 492
Cdd:COG2884 153 VN--RPELLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELVDR 202
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
313-506 |
3.09e-21 |
|
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: 91.22 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGE--RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLakgiklgyfaqhqleflra 390
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 DESPlqhlarlaPQELEQKLRDYLG-----GFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
Cdd:cd03247 62 DGVP--------VSDLEKALSSLISvlnqrPYLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490290321 466 RQALTEALIDF--EGALVVVSHdrHLIR-STTDDLYLVHDGKVE 506
Cdd:cd03247 134 ERQLLSLIFEVlkDKTLIWITH--HLTGiEHMDKILFLENGKII 175
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
315-517 |
5.81e-21 |
|
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: 92.18 E-value: 5.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 315 MEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYFAQHQLEFLRADES- 393
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEV-LIDGEDISGLSEAELYRLRRRMGm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 394 -------------------PLQHLARLAPQELEQKLRDYLGGFGFQG--DKVSEEtrrFSGGEKARLVLALIVWQRPNLL 452
Cdd:cd03261 82 lfqsgalfdsltvfenvafPLREHTRLSEEEIREIVLEKLEAVGLRGaeDLYPAE---LSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490290321 453 LLDEPTNHLD-------LDMRQALTEALidfEGALVVVSHDRHLIRSTTDDLYLVHDGKVEpFDGDLEDYQQ 517
Cdd:cd03261 159 LYDEPTAGLDpiasgviDDLIRSLKKEL---GLTSIMVTHDLDTAFAIADRIAVLYDGKIV-AEGTPEELRA 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
311-505 |
6.27e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.53 E-value: 6.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLA-------KGIKL----GY 379
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNgrpladwSPAELarrrAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 380 FAQH-QLEF-LRADE------SPLQHLARLAPQELEQKL----------RDYlggfgfqgdkvseetRRFSGGEKARLVL 441
Cdd:PRK13548 81 LPQHsSLSFpFTVEEvvamgrAPHGLSRAEDDALVAAALaqvdlahlagRDY---------------PQLSGGEQQRVQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 442 ALI---VWQ---RPNLLLLDEPTNHLDLDMRQALTEALIDF----EGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK13548 146 ARVlaqLWEpdgPPRWLLLDEPTSALDLAHQHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
313-505 |
6.54e-21 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 91.12 E-value: 6.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIG-LAKGIKLGYFAQHQL------ 385
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfDGKSYQKNIEALRRIgaliea 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 386 ----------EFLRAdespLQHLARLAPQELEQKLRdyLGGFGFQGDKvseETRRFSGGEKARLVLALIVWQRPNLLLLD 455
Cdd:cd03268 81 pgfypnltarENLRL----LARLLGIRKKRIDEVLD--VVGLKDSAKK---KVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490290321 456 EPTNHLD----LDMRQaLTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:cd03268 152 EPTNGLDpdgiKELRE-LILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
307-491 |
1.27e-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: 95.82 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 307 SLPNPLLKMEKVSAGY-GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGIKL-------- 377
Cdd:TIGR02857 316 AAPASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN-GVPLadadadsw 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 378 ----GYFAQH----------QLEFLRADESPL---QHLARLAPQELEQKLRDYLggfgfqGDKVSEETRRFSGGEKARLV 440
Cdd:TIGR02857 395 rdqiAWVPQHpflfagtiaeNIRLARPDASDAeirEALERAGLDEFVAALPQGL------DTPIGEGGAGLSGGQAQRLA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490290321 441 LALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF-EGALV-VVSHDRHLIR 491
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaQGRTVlLVTHRLALAA 521
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-217 |
1.99e-20 |
|
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: 90.26 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqlawvnqetpalpqpAIDYVI 85
Cdd:cd03257 10 SFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGK----------------DLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 86 DGDREYRQLEAAL--QQANERND-----GHAIA---TVHGKLDaiDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWR 155
Cdd:cd03257 74 RRLRKIRRKEIQMvfQDPMSSLNprmtiGEQIAeplRIHGKLS--KKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 156 MRLNLAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKGYTG-TLILISHDRDFLDPIVDKII 217
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVsvqAQILDLLKKLQEELGlTLLFITHDLGVVAKIADRVA 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-221 |
2.03e-20 |
|
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: 90.47 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqetpalpqpaIDYVIDGDREYRQ 93
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDG------------------KDITKKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 94 lEAAL--QQANerndgHAI--ATV----------HGkldaIDAWTIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLN 159
Cdd:COG1122 76 -KVGLvfQNPD-----DQLfaPTVeedvafgpenLG----LPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 160 LAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTG---TLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
316-505 |
2.75e-20 |
|
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: 89.24 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 316 EKVSAGYGERI-ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL-AKGIKL-------GYFAQ---H 383
Cdd:cd03226 3 ENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLnGKPIKAkerrksiGYVMQdvdY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 384 QLEF--------LRADESPlqhlarLAPQELEQKLRDyLGGFGFQgdkvSEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
Cdd:cd03226 83 QLFTdsvreellLGLKELD------AGNEQAETVLKD-LDLYALK----ERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490290321 456 EPTNHLDLDMRQALTEALIDFEG---ALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
313-568 |
8.35e-20 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 93.77 E-value: 8.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAgeLQPVSGeigLAKGIKLGYFAQhqlEFLRADE 392
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDG---IPKNCQILHVEQ---EVVGDDT 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 393 SPLQHL--------------ARLAPQELEQKLRDY-------------------------------------------LG 415
Cdd:PLN03073 250 TALQCVlntdiertqlleeeAQLVAQQRELEFETEtgkgkgankdgvdkdavsqrleeiykrlelidaytaearaasiLA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 416 GFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLIRSTTD 495
Cdd:PLN03073 330 GLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVT 409
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490290321 496 DLYLVHDGKVEPFDGDLEDYQQWLSDSQKQESQSGEAPKESGNSAQARKDQKRREAELRSQTQPLRKEIARLE 568
Cdd:PLN03073 410 DILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLG 482
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-220 |
9.95e-20 |
|
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: 87.70 E-value: 9.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 6 SLQIRRGVRVLlDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQLAWVNQETPALPQPAIDYVI 85
Cdd:cd03226 6 SFSYKKGTEIL-DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDVDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 86 DGDREYRQLEAALQQANERNdghaiatvhgkldaidawtirSRAASLLHGLGFSNEQLERPVsDFSGGWRMRLNLAQALI 165
Cdd:cd03226 85 FTDSVREELLLGLKELDAGN---------------------EQAETVLKDLDLYALKERHPL-SLSGGQKQRLAIAAALL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 166 CRSDLLLLDEPTNHLDLDAVIWLEKW---LKGYTGTLILISHDRDFLDPIVDKIIHIE 220
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELireLAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
324-505 |
1.52e-19 |
|
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: 87.65 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 324 ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGI------------KLGYFAQHQLEF---L 388
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV-LLDGTdirqldpadlrrNIGYVPQDVTLFygtL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 389 R---------ADESPLQHLARLApqELEQKLRDYLGGFGFQgdkVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
Cdd:cd03245 95 RdnitlgaplADDERILRAAELA--GVTDFVNKHPNGLDLQ---IGERGRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490290321 460 HLDLDMRQALTEALIDFEG--ALVVVSHdRHLIRSTTDDLYLVHDGKV 505
Cdd:cd03245 170 AMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
313-505 |
1.59e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.53 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLaKGIKLGYFAQHQL----EFL 388
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFL-GDKPISMLSSRQLarrlALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 389 radesPLQHLAR--LAPQELEQKLRD-YLGGFGFQGDK-------VSEET-------RR---FSGGEKARLVLALIVWQR 448
Cdd:PRK11231 82 -----PQHHLTPegITVRELVAYGRSpWLSLWGRLSAEdnarvnqAMEQTrinhladRRltdLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 449 PNLLLLDEPTNHLDLD--------MRQALTEAlidfeGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK11231 157 TPVVLLDEPTTYLDINhqvelmrlMRELNTQG-----KTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
320-510 |
1.68e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 87.59 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 320 AGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIK----LGYFAQHQLE-----FLRA 390
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSsllgLGGGFNPELTgreniYLNG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 desplqHLARLAPQELEQKLRDYLgGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT----NHLDLDMR 466
Cdd:cd03220 110 ------RLLGLSRKEIDEKIDEII-EFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLavgdAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490290321 467 QALTEaLIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKVEpFDG 510
Cdd:cd03220 183 RRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR-FDG 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
313-505 |
2.20e-19 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 85.56 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIglakgiklgYFAQHQLEFLRADE 392
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI---------LVDGKEVSFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 393 SpLQHLARLAPQeleqklrdylggfgfqgdkvseetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDldmrQALTEA 472
Cdd:cd03216 72 A-RRAGIAMVYQ--------------------------LSVGERQMVEIARALARNARLLILDEPTAALT----PAEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490290321 473 LIDF------EG-ALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:cd03216 121 LFKVirrlraQGvAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
321-486 |
2.43e-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: 87.18 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 321 GYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAK----------GIKLGYFAQH--QLEFL 388
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaaRQSLGYCPQFdaLFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 389 radeSPLQHL---ARL-------APQELEQKLRdylgGFGFQgDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
Cdd:cd03263 91 ----TVREHLrfyARLkglpkseIKEEVELLLR----VLGLT-DKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190
....*....|....*....|....*....|
gi 490290321 459 NHLDLDMRQALTEALIDFEG--ALVVVSHD 486
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-221 |
2.91e-19 |
|
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: 85.51 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqetpaLPQPAIDyvidgDREYRQ 93
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG-------------VDLRDLD-----LESLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 94 LEAALQQanerndghaiatvhgkldaiDAW----TIRSraaSLLhglgfsneqlerpvsdfSGGWRMRLNLAQALICRSD 169
Cdd:cd03228 77 NIAYVPQ--------------------DPFlfsgTIRE---NIL-----------------SGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 170 LLLLDEPTNHLDLD--AVIW--LEKWLKGYtgTLILISHdRDFLDPIVDKIIHIEQ 221
Cdd:cd03228 117 ILILDEATSALDPEteALILeaLRALAKGK--TVIVIAH-RLSTIRDADRIIVLDD 169
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-220 |
3.67e-19 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 86.72 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLL-SLLKNEIsADGGSMTF--PGNW-----------------QLAWVNQETPAL 76
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLkCIYGNYL-PDSGSILVrhDGGWvdlaqaspreilalrrrTIGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 77 P-QPAIDYVIdgdreyrqlEAALqqanERNDGHAIAtvhgkldaidawtiRSRAASLLHGLGFSNEQLERPVSDFSGGWR 155
Cdd:COG4778 106 PrVSALDVVA---------EPLL----ERGVDREEA--------------RARARELLARLNLPERLWDLPPATFSGGEQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 156 MRLNLAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIE 220
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAanrAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
313-509 |
4.99e-19 |
|
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: 86.03 E-value: 4.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLA-----------KGIklGYFA 381
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvtgvpperRNI--GMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 382 QHQLEF------------LRADESPLQHLARLAPQELEQ-KLRDYLGgfgfqgdkvsEETRRFSGGEKARLVLA--LIVw 446
Cdd:cd03259 79 QDYALFphltvaeniafgLKLRGVPKAEIRARVRELLELvGLEGLLN----------RYPHELSGGQQQRVALAraLAR- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 447 qRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLIRSTTDDLYLVHDGKVEPFD 509
Cdd:cd03259 148 -EPSLLLLDEPLSALDAKLREELREELKELQRELgittIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-221 |
5.23e-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: 86.78 E-value: 5.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 8 QIRRGVRVLlDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqlawvnqetpALPQPAidyvidg 87
Cdd:COG1124 13 QGGRRVPVL-KDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR-----------PVTRRR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 88 DREYRQLEAALQQ-----ANERndgHAIATV-------HGKLDaidawtIRSRAASLLHGLGFSNEQLERPVSDFSGGWR 155
Cdd:COG1124 74 RKAFRRRVQMVFQdpyasLHPR---HTVDRIlaeplriHGLPD------REERIAELLEQVGLPPSFLDRYPHQLSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 156 MRLNLAQALICRSDLLLLDEPTNHLDL--DAVIW--LEKwLKGYTG-TLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVsvQAEILnlLKD-LREERGlTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
301-523 |
6.49e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.29 E-value: 6.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 301 SFRQPESLPNPLLKM--EKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI--------- 369
Cdd:COG1134 13 SYRLYHEPSRSLKELllRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVevngrvsal 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 370 -GLAKGIklgyfaQHQL---E--FLRAdesplqHLARLAPQELEQKLRDY-----LGGFGFQgdKVseetRRFSGGEKAR 438
Cdd:COG1134 93 lELGAGF------HPELtgrEniYLNG------RLLGLSRKEIDEKFDEIvefaeLGDFIDQ--PV----KTYSSGMRAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 439 LVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF---EGALVVVSHDRHLIRSTTDDLYLVHDGKVEpFDGDLED- 514
Cdd:COG1134 155 LAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELresGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV-MDGDPEEv 233
|
250
....*....|..
gi 490290321 515 ---YQQWLSDSQ 523
Cdd:COG1134 234 iaaYEALLAGRE 245
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-221 |
7.46e-19 |
|
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: 85.66 E-value: 7.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 4 FSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqETPALPQPAIDY 83
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG---------KPLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 84 V-----IDGDREYRQLEAALQqaneRNDGHAIAtvHGKLDAIDawtiRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRL 158
Cdd:cd03235 73 VpqrrsIDRDFPISVRDVVLM----GLYGHKGL--FRRLSKAD----KAKVDEALERVGLS-ELADRQIGELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 159 NLAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPktqEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNR 207
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
312-505 |
7.76e-19 |
|
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: 85.64 E-value: 7.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGERI----ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYFAQHQLEF 387
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSI-IFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 388 LRAD----------------------ESPLQHLARLAPQELEQKLRDYLggfgfqGDKVSEETRR-------FSGGEKAR 438
Cdd:cd03257 80 RRKEiqmvfqdpmsslnprmtigeqiAEPLRIHGKLSKKEARKEAVLLL------LVGVGLPEEVlnrypheLSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 439 LVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID----FEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-221 |
8.70e-19 |
|
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: 90.66 E-value: 8.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 16 LLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTF---------PGNW--QLAWVNQETP---------- 74
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidlrqidPASLrrQIGVVLQDVFlfsgtireni 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 75 ALPQPAIDYvidgdreyRQLEAALQQANerndghaiatVHgklDAIDAwtirsraasllHGLGfsneqLERPVSD----F 150
Cdd:COG2274 570 TLGDPDATD--------EEIIEAARLAG----------LH---DFIEA-----------LPMG-----YDTVVGEggsnL 612
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD--AVIW--LEKWLKGytGTLILISHDRDFLDpIVDKIIHIEQ 221
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAEteAIILenLRRLLKG--RTVIIIAHRLSTIR-LADRIIVLDK 684
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-219 |
2.13e-18 |
|
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: 88.88 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIR-RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGN---------W--QLAWV 69
Cdd:TIGR02857 322 LEFSGVSVAyPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVpladadadsWrdQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 70 NQeTPALPQPAI-DYVIDGDREyrQLEAALQQANERNDghaiatvhgkldaidawtirsrAASLLHGLGfsnEQLERPVS 148
Cdd:TIGR02857 402 PQ-HPFLFAGTIaENIRLARPD--ASDAEIREALERAG----------------------LDEFVAALP---QGLDTPIG 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 149 D----FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD-AVIWLEKWLKGYTG-TLILISHDRDFLdPIVDKIIHI 219
Cdd:TIGR02857 454 EggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAEtEAEVLEALRALAQGrTVLLVTHRLALA-ALADRIVVL 529
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
304-505 |
4.60e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 84.34 E-value: 4.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 304 QPESLPN--PLLkMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEiglakgiklgyfa 381
Cdd:PRK11247 3 NTARLNQgtPLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 382 qhqlefLRADESPLQHL----------ARLAPQeleQKLRDYLgGFGFQG----------------DKVSEETRRFSGGE 435
Cdd:PRK11247 69 ------LLAGTAPLAEAredtrlmfqdARLLPW---KKVIDNV-GLGLKGqwrdaalqalaavglaDRANEWPAALSGGQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 436 KARLVLALIVWQRPNLLLLDEPTNHLD----LDMrQALTEALIDFEGALVV-VSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK11247 139 KQRVALARALIHRPGLLLLDEPLGALDaltrIEM-QDLIESLWQQHGFTVLlVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-207 |
5.09e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.28 E-value: 5.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQLAWVNQET---PALPQPAIDYVIDGDRE 90
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSevpDSLPLTVRDLVAMGRWA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 91 YRQLEaalqqanERNDGHAIATVHGKLDAIDawtirsraaslLHGLgfsneqLERPVSDFSGGWRMRLNLAQALICRSDL 170
Cdd:NF040873 85 RRGLW-------RRLTRDDRAAVDDALERVG-----------LADL------AGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490290321 171 LLLDEPTNHLDLDAVIWLEKWLKGYTG---TLILISHDRD 207
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLE 180
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
313-505 |
5.82e-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: 82.92 E-value: 5.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERI----ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGIKLGYFAQHQLEFL 388
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD-GTDISKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 389 RAD---------------------ESPLqHLARLAPQELEQKLRDYLGGFGFQGD---KVSEetrrFSGGEKARLVLA-- 442
Cdd:cd03255 80 RRRhigfvfqsfnllpdltalenvELPL-LLAGVPKKERRERAEELLERVGLGDRlnhYPSE----LSGGQQQRVAIAra 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 443 LIvwQRPNLLLLDEPTNHLDLDMRQALTEALIDF---EG-ALVVVSHDRHLIrSTTDDLYLVHDGKV 505
Cdd:cd03255 155 LA--NDPKIILADEPTGNLDSETGKEVMELLRELnkeAGtTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
17-221 |
8.21e-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: 82.54 E-value: 8.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG---------------NWQLAWVNQETPALP-QPA 80
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdisklsekelaafrRRHIGFVFQSFNLLPdLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 IDYVidgdreyrqlEAALQqanerndghaIATVHGKldaidawTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNL 160
Cdd:cd03255 100 LENV----------ELPLL----------LAGVPKK-------ERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 161 AQALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKGYTG-TLILISHDRDfLDPIVDKIIHIEQ 221
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSEtgkEVMELLRELNKEAGtTIVVVTHDPE-LAEYADRIIELRD 215
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
309-505 |
8.27e-18 |
|
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: 83.55 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 309 PNPLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI--------GLA------KG 374
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlfdgrditGLPphriarLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 375 I-------------------KLGYFAQHQLEFLRADESPLQHLARLApqELEQKLRDYLGGFGFqGDKVSEETRRFSGGE 435
Cdd:COG0411 81 IartfqnprlfpeltvlenvLVAAHARLGRGLLAALLRLPRARREER--EARERAEELLERVGL-ADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 436 KARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI---DFEG-ALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRrlrDERGiTILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
313-505 |
9.96e-18 |
|
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: 82.46 E-value: 9.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERII-LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYFAQHQLEFLR-- 389
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTI-RVNGQDVSDLRGRAIPYLRrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 390 -----ADESPLQHL------------ARLAPQELEQKLRDYLGGFGFQgDKVSEETRRFSGGEKARLVLALIVWQRPNLL 452
Cdd:cd03292 80 igvvfQDFRLLPDRnvyenvafalevTGVPPREIRKRVPAALELVGLS-HKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 453 LLDEPTNHLDLDMRQALTEALIDFE--GALVVVS-HDRHLIRSTTDDLYLVHDGKV 505
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINkaGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-203 |
1.03e-17 |
|
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: 82.42 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 8 QIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlAWVNQEtPALPQPAIDYVIDG 87
Cdd:cd03266 12 RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG----FDVVKE-PAEARRRLGFVSDS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 88 DREYRQLEAalqqaneRNDGHAIATVHG-KLDAIDAwtirsRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALIC 166
Cdd:cd03266 87 TGLYDRLTA-------RENLEYFAGLYGlKGDELTA-----RLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 490290321 167 RSDLLLLDEPTNHLDLDAVIWLEKWLKGY--TGTLILIS 203
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLraLGKCILFS 192
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
310-506 |
1.11e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 82.40 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 310 NPLLKMEKVS----AGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI-------------GLA 372
Cdd:COG1136 2 SPLLELRNLTksygTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlidgqdisslserELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 373 K--GIKLGY-FAQHQL-EFLRADES---PLQhLARLAPQELEQKLRDYLGGFGFqGDKVSEETRRFSGGEK-----ARlv 440
Cdd:COG1136 82 RlrRRHIGFvFQFFNLlPELTALENvalPLL-LAGVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQQqrvaiAR-- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 441 lALIvwQRPNLLLLDEPTNHLDLDMRQALTEALIDF---EG-ALVVVSHDRHLIrSTTDDLYLVHDGKVE 506
Cdd:COG1136 158 -ALV--NRPKLILADEPTGNLDSKTGEEVLELLRELnreLGtTIVMVTHDPELA-ARADRVIRLRDGRIV 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
328-505 |
1.13e-17 |
|
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: 82.03 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGI-----------KLGYFAQHQ--LEFLRADESp 394
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD-GFdvvkepaearrRLGFVSDSTglYDRLTAREN- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 395 LQHLARL---APQELEQKLRDYLGGFGFqGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTE 471
Cdd:cd03266 99 LEYFAGLyglKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALRE 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 490290321 472 ---ALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:cd03266 178 firQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
273-508 |
1.17e-17 |
|
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: 86.73 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 273 AKQAQSRIKMLerMELIAPAhvdnpfhfsfRQPESLPNP--LLKMEKVSAGY--GERIILDSIKLNLVPGSRIGLLGRNG 348
Cdd:COG4618 301 ARQAYRRLNEL--LAAVPAE----------PERMPLPRPkgRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 349 AGKSTLIKLLAGELQPVSGEIGL-----------AKGIKLGYFAQhQLEFLR------------ADESPLQHLARLAP-Q 404
Cdd:COG4618 369 SGKSTLARLLVGVWPPTAGSVRLdgadlsqwdreELGRHIGYLPQ-DVELFDgtiaeniarfgdADPEKVVAAAKLAGvH 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 405 ELEQKLRDylgGFGFQgdkVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGA-LV 481
Cdd:COG4618 448 EMILRLPD---GYDTR---IGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkaRGAtVV 521
|
250 260
....*....|....*....|....*..
gi 490290321 482 VVSHDRHLIRStTDDLYLVHDGKVEPF 508
Cdd:COG4618 522 VITHRPSLLAA-VDKLLVLRDGRVQAF 547
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-221 |
1.31e-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: 81.87 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqetpalpqpaidyvIDgdreYRQLEA 96
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG----------------------TD----IRQLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 97 ALQQaneRNDGHAIATVH------------GKLDAIDAWTIRsraASLLHGLG-FSNEQ---LERPVSD----FSGGWRM 156
Cdd:cd03245 74 ADLR---RNIGYVPQDVTlfygtlrdnitlGAPLADDERILR---AAELAGVTdFVNKHpngLDLQIGErgrgLSGGQRQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 157 RLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTG--TLILISHDRDFLDpIVDKIIHIEQ 221
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLD-LVDRIIVMDS 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-205 |
1.52e-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: 81.75 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqETPALPQPAIDYVidgdr 89
Cdd:cd03293 13 GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG---------EPVTGPGPDRGYV----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 eyrqleaaLQQAN-------ERNdghaIA---TVHGKLDAIdawtIRSRAASLLH--GL-GFSN---EQLerpvsdfSGG 153
Cdd:cd03293 79 --------FQQDAllpwltvLDN----VAlglELQGVPKAE----ARERAEELLElvGLsGFENaypHQL-------SGG 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 154 WRMRLNLAQALICRSDLLLLDEPTNHLD----LDAVIWLEKWLKGYTGTLILISHD 205
Cdd:cd03293 136 MRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHD 191
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
312-506 |
2.10e-17 |
|
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: 82.16 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGE----RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI-----GLAKGIKLGYFAQ 382
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 383 HQLEF----------LRADES---PLQHLARLAPQELEQKLRDYLGgfgfqgdkVSEETR-RF----SGGEKARLVL--A 442
Cdd:COG1124 81 VQMVFqdpyaslhprHTVDRIlaePLRIHGLPDREERIAELLEQVG--------LPPSFLdRYphqlSGGQRQRVAIarA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 443 LIVwqRPNLLLLDEPTNHLDLDMrQALTEALI-----DFEGALVVVSHDRHLIRSTTDDLYLVHDGKVE 506
Cdd:COG1124 153 LIL--EPELLLLDEPTSALDVSV-QAEILNLLkdlreERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-505 |
2.31e-17 |
|
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: 85.51 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 12 GVRVLLDNATATINPGQKVGLVGKNGCGKS----TLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPQPAIdyvidg 87
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDG--------QDLLGLSEREL------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 88 dREYRqleaalqqanerndGHAIA------------------------TVHGKLDAIDAwtiRSRAASLLHGLGFSNEql 143
Cdd:COG4172 87 -RRIR--------------GNRIAmifqepmtslnplhtigkqiaevlRLHRGLSGAAA---RARALELLERVGIPDP-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 144 ERPVSDF----SGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDaviwLEKWLKGYTGT-LILISHD----RD 207
Cdd:COG4172 147 ERRLDAYphqlSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqaqiLD----LLKDLQRELGMaLLLITHDlgvvRR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 208 FLDPIV----DKIihIEQQTmfeytgnyssfevqRATRLAQQQAMYesqqqrvahlqsyidrfrakaTKAkqaqsrikml 283
Cdd:COG4172 223 FADRVAvmrqGEI--VEQGP--------------TAELFAAPQHPY---------------------TRK---------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 284 ermeLIA--PAHVDNPfhfsfrQPESLPnPLLKMEKVSAGY-----------GERIILDSIKLNLVPGSRIGLLGRNGAG 350
Cdd:COG4172 256 ----LLAaePRGDPRP------VPPDAP-PLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 351 KSTLIKLLAGeLQPVSGEIGLAkGIKLGYFAQHQLEFLRAD----------------------ESPLQ-HLARLAPQELE 407
Cdd:COG4172 325 KSTLGLALLR-LIPSEGEIRFD-GQDLDGLSRRALRPLRRRmqvvfqdpfgslsprmtvgqiiAEGLRvHGPGLSAAERR 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 408 QKLRDYLggfgfqgDKV--SEETR-R----FSGGEKARLVLA--LIVwqRPNLLLLDEPTNHLDLDMRQALTEALID--- 475
Cdd:COG4172 403 ARVAEAL-------EEVglDPAARhRypheFSGGQRQRIAIAraLIL--EPKLLVLDEPTSALDVSVQAQILDLLRDlqr 473
|
570 580 590
....*....|....*....|....*....|.
gi 490290321 476 -FEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:COG4172 474 eHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
328-507 |
2.66e-17 |
|
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: 81.19 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNL---VPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL--------AKGI-------KLGY-FAQHQLeF- 387
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdsRKKInlppqqrKIGLvFQQYAL-Fp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 388 -LRADESPLQHLARLAPQELEQKLRDYLGGFGFQGdKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
Cdd:cd03297 89 hLNVRENLAFGLKRKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490290321 467 QA----LTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKVEP 507
Cdd:cd03297 168 LQllpeLKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-219 |
4.02e-17 |
|
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: 81.28 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLlkneISAD-----GGSMTFPGN-------WQL-- 66
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSL----ITGDlpptyGNDVRLFGErrggedvWELrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 67 --AWVnqeTPALPQpaidyvidgdrEYRQLEAALQqanerndghAIATvhGKLDAIDAW-----TIRSRAASLLHGLGFS 139
Cdd:COG1119 79 riGLV---SPALQL-----------RFPRDETVLD---------VVLS--GFFDSIGLYreptdEQRERARELLELLGLA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 140 nEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA----VIWLEKWLKGYTGTLILISHdrdFLDPIVDK 215
Cdd:COG1119 134 -HLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH---HVEEIPPG 209
|
....
gi 490290321 216 IIHI 219
Cdd:COG1119 210 ITHV 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
313-505 |
4.04e-17 |
|
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: 80.94 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYFAQHQ-------- 384
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV-LFDGEDITGLPPHEiarlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 385 -------------LE------FLRADESPLQHLARLAPQELEQKLRDYLGGFGFqGDKVSEETRRFSGGEKARLVLALIV 445
Cdd:cd03219 80 tfqiprlfpeltvLEnvmvaaQARTGSGLLLARARREEREARERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490290321 446 WQRPNLLLLDEPTNHLDLDMRQALTE---ALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAElirELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
313-514 |
4.12e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 82.46 E-value: 4.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI-------GLAKGIKLGYF----- 380
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlwdgeplDPEDRRRIGYLpeerg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 381 ------AQHQLEFlradesplqhLARL---APQELEQKLRDYLGGFG---FQGDKVSEetrrFSGGE--KARLVLALIvw 446
Cdd:COG4152 82 lypkmkVGEQLVY----------LARLkglSKAEAKRRADEWLERLGlgdRANKKVEE----LSKGNqqKVQLIAALL-- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 447 QRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVVVS-HDRHLIRSTTDDLYLVHDGKVePFDGDLED 514
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELaaKGTTVIFSsHQMELVEELCDRIVIINKGRK-VLSGSVDE 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-228 |
4.24e-17 |
|
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: 81.01 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALpQPAI 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDG--------EDISGL-SEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 82 DYVIDgdreyRQLEAALQQAnerndghaiA-----TV----------HGKLDAidaWTIRSRAASLLHGLGFSNEQLERP 146
Cdd:cd03261 72 LYRLR-----RRMGMLFQSG---------AlfdslTVfenvafplreHTRLSE---EEIREIVLEKLEAVGLRGAEDLYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 147 vSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKGYTG-TLILISHDRDFLDPIVDKIIHI-EQ 221
Cdd:cd03261 135 -AELSGGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGlTSIMVTHDLDTAFAIADRIAVLyDG 213
|
....*..
gi 490290321 222 QTMFEYT 228
Cdd:cd03261 214 KIVAEGT 220
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
328-504 |
5.44e-17 |
|
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: 80.92 E-value: 5.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGS-----RIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGIKLGYFAQhqleFLRADEsplqhlarla 402
Cdd:cd03237 10 LGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQ----YIKADY---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 403 PQELEQKLRDYLGGFG------------FQGDKVSE-ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
Cdd:cd03237 75 EGTVRDLLSSITKDFYthpyfkteiakpLQIEQILDrEVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 490290321 470 TEALIDF----EGALVVVSHDRHLIRSTTDDLyLVHDGK 504
Cdd:cd03237 155 SKVIRRFaennEKTAFVVEHDIIMIDYLADRL-IVFEGE 192
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
17-217 |
6.12e-17 |
|
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: 80.13 E-value: 6.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFpgNWQLAWVN------QETPALPQPAIDYVIDGDR- 89
Cdd:TIGR02324 24 LKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILV--RHEGAWVDlaqaspREVLEVRRKTIGYVSQFLRv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 --EYRQLEAALQQANERNDGHAIAtvhgkldaidawtiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICR 167
Cdd:TIGR02324 102 ipRVSALEVVAEPLLERGVPREAA--------------RARARELLARLNIPERLWHLPPATFSGGEQQRVNIARGFIAD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490290321 168 SDLLLLDEPTNHLDL---DAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKII 217
Cdd:TIGR02324 168 YPILLLDEPTASLDAanrQVVVELIAEAKARGAALIGIFHDEEVRELVADRVM 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
313-510 |
6.20e-17 |
|
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: 80.69 E-value: 6.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGE-RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI-------GLAKGIKL------- 377
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdiNKLKGKALrqlrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 378 GY-FAQHQL-EFLRADE----------SPLQHLARLAPQELEQKLRDYLGGFGFQgDKVSEETRRFSGGEKARLVLALIV 445
Cdd:cd03256 81 GMiFQQFNLiERLSVLEnvlsgrlgrrSTWRSLFGLFPKEEKQRALAALERVGLL-DKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 446 WQRPNLLLLDEPTNHLDLDMRQALTEALIDF---EGALVVVS-HDRHLIRSTTDDLYLVHDGKVePFDG 510
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQVDLAREYADRIVGLKDGRI-VFDG 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
322-471 |
7.63e-17 |
|
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: 79.72 E-value: 7.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 322 YGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLA--------KGIK--LGYFAQHQL--EFLR 389
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghdvvrepREVRrrIGIVFQDLSvdDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 390 ADESPLQHlARLA---PQELEQKLRDYLGGFGFqGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
Cdd:cd03265 90 GWENLYIH-ARLYgvpGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
....*
gi 490290321 467 QALTE 471
Cdd:cd03265 168 AHVWE 172
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
327-505 |
1.00e-16 |
|
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: 80.62 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGIKLGYFAQHQLEFLRAD--------------- 391
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFR-GQDLYQLDRKQRRAFRRDvqlvfqdspsavnpr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 392 -------ESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
Cdd:TIGR02769 105 mtvrqiiGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490290321 465 MR----QALTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:TIGR02769 185 LQavilELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
328-514 |
1.15e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 81.29 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLakgikLGYF-AQHQLEFLR----------------- 389
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV-----LGYVpFKRRKEFARrigvvfgqrsqlwwdlp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 390 ADES--PLQHLARLAPQELEQKLRDYLGGFGfQGDKVSEETRRFSGGE--KARLVLALIvwQRPNLLLLDEPTNHLDLDM 465
Cdd:COG4586 113 AIDSfrLLKAIYRIPDAEYKKRLDELVELLD-LGELLDTPVRQLSLGQrmRCELAAALL--HRPKILFLDEPTIGLDVVS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490290321 466 RQALTEALIDF---EGALVVV-SHDRHLIRSTTDDLYLVHDGKVEpFDGDLED 514
Cdd:COG4586 190 KEAIREFLKEYnreRGTTILLtSHDMDDIEALCDRVIVIDHGRII-YDGSLEE 241
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-216 |
1.21e-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: 79.09 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGN---WQLAWVNQETPALPQpaiDYVID 86
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirTDRKAARQSLGYCPQ---FDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 87 GD---REYRQLeaalqqanerndghaiatvHGKLDAIDAWTIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQA 163
Cdd:cd03263 88 DEltvREHLRF-------------------YARLKGLPKSEIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 164 LICRSDLLLLDEPTnhLDLDAV----IW--LEKWLKGYtgTLILISHDRDFLDPIVDKI 216
Cdd:cd03263 148 LIGGPSVLLLDEPT--SGLDPAsrraIWdlILEVRKGR--SIILTTHSMDEAEALCDRI 202
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
328-505 |
2.15e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 79.74 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYFAQHQLE--------FLRADE-----SP 394
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEV-LIKGEPIKYDKKSLLEvrktvgivFQNPDDqlfapTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 395 LQHLA------RLAPQELEQKLRDYLGGFGFQGdkvSEET--RRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
Cdd:PRK13639 97 EEDVAfgplnlGLSKEEVEKRVKEALKAVGMEG---FENKppHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490290321 467 QALTEALIDF--EGALVVVS-HDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK13639 174 SQIMKLLYDLnkEGITIIIStHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
313-517 |
2.41e-16 |
|
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: 78.82 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL-AKGI--------KLGYFAQH 383
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLdGKDItnlpphkrPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 384 QLEF--LRADES---PLQhLARLAPQELEQKLRDYL---GGFGFQGDKVSEetrrFSGGEKARLVLALIVWQRPNLLLLD 455
Cdd:cd03300 81 YALFphLTVFENiafGLR-LKKLPKAEIKERVAEALdlvQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 456 EPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLIRSTTDDLYLVHDGKVEPFDGDLEDYQQ 517
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELgitfVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-216 |
2.48e-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: 78.18 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSmtfpgnwqlAWVNqetpalpqpAI 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGR---------ATVA---------GH 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 82 DYVIDGDREYRQLEAALQQANERND--GHAIATVHGKLDAIDAWTIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLN 159
Cdd:cd03265 63 DVVREPREVRRRIGIVFQDLSVDDEltGWENLYIHARLYGVPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLE 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 160 LAQALICRSDLLLLDEPTNHLDLDAV--IW--LEKWLKGYTGTLILISHDRDFLDPIVDKI 216
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQTRahVWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRV 202
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
311-505 |
8.84e-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: 76.94 E-value: 8.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIglakgiklgYFAQHQLEFLRA 390
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSI---------RFDGEDITGLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 DEsplqhLARL----APQE--------LEQKLRdyLGGFGFQGDKVSEETR-----RF--------------SGGEK--- 436
Cdd:COG0410 73 HR-----IARLgigyVPEGrrifpsltVEENLL--LGAYARRDRAEVRADLervyeLFprlkerrrqragtlSGGEQqml 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 437 --ARlvlALIvwQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:COG0410 146 aiGR---ALM--SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLnrEGvTILLVEQNARFALEIADRAYVLERGRI 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
322-510 |
1.06e-15 |
|
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: 76.99 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 322 YGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGI----KLGYFAQHQLEF-----LRADE 392
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrRKKFLRRIGVVFgqktqLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 393 SP------LQHLARLAPQELEQKLrDYLGGFGFQGDKVSEETRRFSGGE--KARLVLALIvwQRPNLLLLDEPTNHLDL- 463
Cdd:cd03267 111 PVidsfylLAAIYDLPPARFKKRL-DELSELLDLEELLDTPVRQLSLGQrmRAEIAAALL--HEPEILFLDEPTIGLDVv 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490290321 464 ---DMRQALTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKVEpFDG 510
Cdd:cd03267 188 aqeNIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL-YDG 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
313-505 |
1.38e-15 |
|
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: 75.64 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--ELQPVSGEIgLAKGiklgyfaqhqleflra 390
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEI-LFKG---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 desplQHLARLAPQEleqklRDYLGGF-GFQ------GDKVSEETRR----FSGGEKARLVLALIVWQRPNLLLLDEPTN 459
Cdd:cd03217 64 -----EDITDLPPEE-----RARLGIFlAFQyppeipGVKNADFLRYvnegFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490290321 460 HLDLDMRQALTEA---LIDFEGALVVVSHDRHLIRS-TTDDLYLVHDGKV 505
Cdd:cd03217 134 GLDIDALRLVAEVinkLREEGKSVLIITHYQRLLDYiKPDRVHVLYDGRI 183
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
317-505 |
1.58e-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: 75.28 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 317 KVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQP--VSGEIgLAKGIKL---------GYFAQHql 385
Cdd:cd03213 14 KSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEV-LINGRPLdkrsfrkiiGYVPQD-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 386 eflradespLQHLARLAPQEleqklrdYLggfgfqgdKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
Cdd:cd03213 91 ---------DILHPTLTVRE-------TL--------MFAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490290321 466 RQALTEALIDF--EGALVVVS-HD-RHLIRSTTDDLYLVHDGKV 505
Cdd:cd03213 147 ALQVMSLLRRLadTGRTIICSiHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-181 |
1.62e-15 |
|
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: 75.69 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQkVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPQpai 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG--------QDVLKQPQ--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 82 dyvidgdrEYRQLEAALQQaneRNDGHAIATVHGKLDAIdAW-------TIRSRAASLLHGLGFsNEQLERPVSDFSGGW 154
Cdd:cd03264 69 --------KLRRRIGYLPQ---EFGVYPNFTVREFLDYI-AWlkgipskEVKARVDEVLELVNL-GDRAKKKIGSLSGGM 135
|
170 180
....*....|....*....|....*..
gi 490290321 155 RMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:cd03264 136 RRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
307-486 |
1.77e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 76.67 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 307 SLPNPLLKMEKVSAGY----GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL------AKGIK 376
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 377 LGY-FAQHQL----------EFlradesPLQhLARLAPQELEQKLRDYLGGFGFQGDKvseetRRF----SGGEKARLVL 441
Cdd:COG1116 82 RGVvFQEPALlpwltvldnvAL------GLE-LRGVPKAERRERARELLELVGLAGFE-----DAYphqlSGGMRQRVAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490290321 442 A--LIVwqRPNLLLLDEPTNHLD----LDMRQALTEALIDFEGALVVVSHD 486
Cdd:COG1116 150 AraLAN--DPEVLLMDEPFGALDaltrERLQDELLRLWQETGKTVLFVTHD 198
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
309-487 |
1.92e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 78.22 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 309 PNPLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIglakgiklgYFAQHQLEFL 388
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRI---------LLDGRDVTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 389 RADESPL----QHLA------------------RLAPQELEQKLRDYL-----GGFGfqgdkvseetRRF----SGGEKA 437
Cdd:COG3842 73 PPEKRNVgmvfQDYAlfphltvaenvafglrmrGVPKAEIRARVAELLelvglEGLA----------DRYphqlSGGQQQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 438 RLVLA--LIVwqRPNLLLLDEPTNHLDL----DMRQALTEALIDFEGALVVVSHDR 487
Cdd:COG3842 143 RVALAraLAP--EPRVLLLDEPLSALDAklreEMREELRRLQRELGITFIYVTHDQ 196
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
300-505 |
2.99e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.10 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 300 FSFRQPESLPNPLLKMEKVSAGY--GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGIKL 377
Cdd:PRK11160 326 FPTTSTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLN-GQPI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 378 GYFAQHQlefLRADESPL------------QHLARLAPQELEQKLRDYLGGFGF----QGDK-----VSEETRRFSGGEK 436
Cdd:PRK11160 405 ADYSEAA---LRQAISVVsqrvhlfsatlrDNLLLAAPNASDEALIEVLQQVGLekllEDDKglnawLGEGGRQLSGGEQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 437 ARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVVVSHDRHLIRStTDDLYLVHDGKV 505
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHRLTGLEQ-FDRICVMDNGQI 551
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
313-513 |
3.71e-15 |
|
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: 75.37 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGE--LQPVSGEIGLA--------------KGIK 376
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsYEVTSGTILFKgqdllelepderarAGLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 377 LGYfaQHQLE--------FLRA---------DESPLQHLARLapQELEQKLRDYLGGFGFQGDKVSEEtrrFSGGEKAR- 438
Cdd:TIGR01978 81 LAF--QYPEEipgvsnleFLRSalnarrsarGEEPLDLLDFE--KLLKEKLALLDMDEEFLNRSVNEG---FSGGEKKRn 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 439 --LVLALIvwqRPNLLLLDEPTNHLDLDMRQALTEALIDF---EGALVVVSHDRHLIRSTTDD-LYLVHDGKVePFDGDL 512
Cdd:TIGR01978 154 eiLQMALL---EPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLNYIKPDyVHVLLDGRI-VKSGDV 229
|
.
gi 490290321 513 E 513
Cdd:TIGR01978 230 E 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
313-514 |
3.99e-15 |
|
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: 74.78 E-value: 3.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIglakgiklgYFAQHQLEFLRADE 392
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSI---------RFDGRDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 393 splqhLAR----LAPQE--------LEQKLRdyLGGFGFQGDKVSE------------ETRR------FSGGEK-----A 437
Cdd:cd03224 72 -----RARagigYVPEGrrifpeltVEENLL--LGAYARRRAKRKArlervyelfprlKERRkqlagtLSGGEQqmlaiA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 438 RlvlALIvwQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLIRSTTDDLYLVHDGKVEpFDGDLED 514
Cdd:cd03224 145 R---ALM--SRPKLLLLDEPSEGLAPKIVEEIFEAIRELrdEGvTILLVEQNARFALEIADRAYVLERGRVV-LEGTAAE 218
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
307-505 |
4.00e-15 |
|
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: 79.01 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 307 SLPNPLLKMEKVSAGYG-ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLaKGIKLGYFAQHQL 385
Cdd:TIGR01193 468 NNLNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILL-NGFSLKDIDRHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 386 ---------EFLRADESPLQHLARLAPQELEQ----------KLRDYLGGF--GFQGDkVSEETRRFSGGEKARLVLALI 444
Cdd:TIGR01193 547 rqfinylpqEPYIFSGSILENLLLGAKENVSQdeiwaaceiaEIKDDIENMplGYQTE-LSEEGSSISGGQKQRIALARA 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490290321 445 VWQRPNLLLLDEPTNHLDLDMRQALTEALIDF-EGALVVVSHdRHLIRSTTDDLYLVHDGKV 505
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLqDKTIIFVAH-RLSVAKQSDKIIVLDHGKI 686
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
311-505 |
9.16e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.58 E-value: 9.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI-------------GLAKGIK- 376
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqlrdlyALSEAERr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 377 ------LGYFAQHQLEFLRADES-------PLQHLARLAPQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLAL 443
Cdd:PRK11701 85 rllrteWGFVHQHPRDGLRMQVSaggnigeRLMAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 444 IVWQRPNLLLLDEPTNHLD-------LDMRQALTEaliDFEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDvsvqarlLDLLRGLVR---ELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
328-505 |
9.45e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.49 E-value: 9.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLQPVSGEIGLAkGIKLGYFAQHQLEFLRA----DESPLQ------- 396
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLN-GRPLSDWSAAELARHRAylsqQQSPPFampvfqy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 397 ---HLARLAPQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLA---LIVWQRPN----LLLLDEPTNHLDLdMR 466
Cdd:COG4138 90 lalHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAavlLQVWPTINpegqLLLLDEPMNSLDV-AQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490290321 467 QALTEALI----DFEGALVVVSHD-----RHlirstTDDLYLVHDGKV 505
Cdd:COG4138 169 QAALDRLLrelcQQGITVVMSSHDlnhtlRH-----ADRVWLLKQGKL 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
10-207 |
9.48e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 74.74 E-value: 9.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqETPALPQPAIDYVidgdr 89
Cdd:COG1116 20 GGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG---------KPVTGPGPDRGVV----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 eyrqleaaLQQAN-------ERNdghaiATVHGKLDAIDAWTIRSRAASLLH--GL-GFSNE---QLerpvsdfSGGWRM 156
Cdd:COG1116 86 --------FQEPAllpwltvLDN-----VALGLELRGVPKAERRERARELLElvGLaGFEDAyphQL-------SGGMRQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490290321 157 RLNLAQALICRSDLLLLDEPTNHLD-----------LDavIWLEkwlkgyTG-TLILISHDRD 207
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDaltrerlqdelLR--LWQE------TGkTVLFVTHDVD 200
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
313-505 |
1.02e-14 |
|
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: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGY-GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLgyfAQHQLEFLR-- 389
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI-LIDGVDI---RDLTLESLRrq 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 390 -------------------------ADESPLQHLARLApqELEQKLRDYLGGFGFQgdkVSEETRRFSGGEKARLVLALI 444
Cdd:COG1132 416 igvvpqdtflfsgtirenirygrpdATDEEVEEAAKAA--QAHEFIEALPDGYDTV---VGERGVNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 445 VWQRPNLLLLDEPTNHLDldmrqALTEALIdfEGAL---------VVVSHDRHLIRStTDDLYLVHDGKV 505
Cdd:COG1132 491 LLKDPPILILDEATSALD-----TETEALI--QEALerlmkgrttIVIAHRLSTIRN-ADRILVLDDGRI 552
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
311-487 |
1.04e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.03 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLaKGIKLGYFAQHQleflRA 390
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLSHVPPYQ----RP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 DESPLQHLARLAPQELEQKLrdylgGFGFQGDKVS--EETRR--------------------FSGGEKARLVLALIVWQR 448
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNI-----AFGLKQDKLPkaEIASRvnemlglvhmqefakrkphqLSGGQRQRVALARSLAKR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490290321 449 PNLLLLDEPTNHLDLDMRQALTEALIDF---EGAL-VVVSHDR 487
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEVVDIlerVGVTcVMVTHDQ 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
312-506 |
1.16e-14 |
|
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: 73.77 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGER----IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGIKLGYFAQHQLEF 387
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVD-GTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 388 LRAD--------------------ESPLQhLARLAPQELEQKLRDYLGGFGFqGDKVSEETRRFSGGEKARLVLALIVWQ 447
Cdd:cd03258 80 ARRRigmifqhfnllssrtvfenvALPLE-IAGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490290321 448 RPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLIRSTTDDLYLVHDGKVE 506
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELgltiVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
303-473 |
1.53e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.25 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 303 RQPESLPNPLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL----------A 372
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvpararL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 373 KGIKLGYFAQH---QLEF-LRADESPLQHLARLAPQELEQKLRDYLGgFGFQGDKVSEETRRFSGGEKARLVLALIVWQR 448
Cdd:PRK13536 112 ARARIGVVPQFdnlDLEFtVRENLLVFGRYFGMSTREIEAVIPSLLE-FARLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180
....*....|....*....|....*
gi 490290321 449 PNLLLLDEPTNHLDLDMRQALTEAL 473
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERL 215
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
12-217 |
1.65e-14 |
|
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: 73.92 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPQPAIdyvidgdreY 91
Cdd:COG0411 16 GLVAV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG--------RDITGLPPHRI---------A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 92 RQ-----------------LE----AALQQANERNDGHAIATVHGKLDAIDAwtiRSRAASLLHGLGFSnEQLERPVSDF 150
Cdd:COG0411 78 RLgiartfqnprlfpeltvLEnvlvAAHARLGRGLLAALLRLPRARREEREA---RERAEELLERVGLA-DRADEPAGNL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 151 SGGWRMRLNLAQALICRSDLLLLDEPT---NHLDLDAVIWLEKWLKGYTG-TLILISHDRDFLDPIVDKII 217
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIV 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
310-505 |
1.67e-14 |
|
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: 76.48 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 310 NPLLKMEKVSAGY--GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQP---VSGEIGLA-----------K 373
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDgrdllelsealR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 374 GIKLGYFAQ------------HQLEF-LRADESPLQHLARLAPQELEQ-KLRDYLGGFGFQgdkvseetrrFSGGEKARL 439
Cdd:COG1123 82 GRRIGMVFQdpmtqlnpvtvgDQIAEaLENLGLSRAEARARVLELLEAvGLERRLDRYPHQ----------LSGGQRQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 440 VLALIVWQRPNLLLLDEPTNHLDLDMRQ---ALTEALIDFEG-ALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAeilDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
318-505 |
2.07e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.57 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 318 VSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGIKLGYFAQHQLEFLRAD------ 391
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-GEPLAKLNRAQRKAFRRDiqmvfq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 392 ----------------ESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
Cdd:PRK10419 97 dsisavnprktvreiiREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490290321 456 EPTNHLDL----DMRQALTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK10419 177 EAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
311-505 |
2.65e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.26 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLA------------------ 372
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsaraasrrvas 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 373 --KGIKLGY-FAQHQLefLRADESPlqHLARLAPQE------LEQKLrDYLGGFGFQGDKVSEetrrFSGGEKARLVLAL 443
Cdd:PRK09536 82 vpQDTSLSFeFDVRQV--VEMGRTP--HRSRFDTWTetdraaVERAM-ERTGVAQFADRPVTS----LSGGERQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 444 IVWQRPNLLLLDEPTNHLDLDmRQ----ALTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDIN-HQvrtlELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-207 |
2.79e-14 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 72.17 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALP--QPAIDYV 84
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG--------RDVTGVPpeRRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 85 IDGDREYRQLEAAlqqanernDGHAIATVHGKLDAIDawtIRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQAL 164
Cdd:cd03259 78 FQDYALFPHLTVA--------ENIAFGLKLRGVPKAE---IRARVRELLELVGLEG-LLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490290321 165 ICRSDLLLLDEPTNHLDLDAVIWLEKWLKGY---TG-TLILISHDRD 207
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELqreLGiTTIYVTHDQE 192
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
308-473 |
2.99e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.07 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 308 LPNPLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGIKLGYFAQH---- 383
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLC-GEPVPSRARHarqr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 384 -----QLEFLRADESPLQHL---AR---LAPQELEQKLRDYLGgFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLL 452
Cdd:PRK13537 82 vgvvpQFDNLDPDFTVRENLlvfGRyfgLSAAAARALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180
....*....|....*....|.
gi 490290321 453 LLDEPTNHLDLDMRQALTEAL 473
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERL 181
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
313-486 |
3.26e-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: 72.12 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYG----ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL------AKGIKLGY-FA 381
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYvFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 382 QHQL-EFLRADES---PLQhLARLAPQELEQKLRDYLGGFGFQG--DKVSEEtrrFSGGEKARLVLA--LIVwqRPNLLL 453
Cdd:cd03293 81 QDALlPWLTVLDNvalGLE-LQGVPKAEARERAEELLELVGLSGfeNAYPHQ---LSGGMRQRVALAraLAV--DPDVLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 490290321 454 LDEPTNHLDLDMRQALTEALIDF---EGALVV-VSHD 486
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIwreTGKTVLlVTHD 191
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
322-524 |
3.66e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 72.69 E-value: 3.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 322 YGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLA---------KGIKLGYFAQHQLEFLRAD- 391
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvrdKDGQLKVADKNQLRLLRTRl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 392 --------------------ESPLQHLArLAPQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNL 451
Cdd:PRK10619 95 tmvfqhfnlwshmtvlenvmEAPIQVLG-LSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 452 LLLDEPTNHLD-------LDMRQALTEalidfEG-ALVVVSHDRHLIRSTTDDLYLVHDGKVEPfDGDLED--------- 514
Cdd:PRK10619 174 LLFDEPTSALDpelvgevLRIMQQLAE-----EGkTMVVVTHEMGFARHVSSHVIFLHQGKIEE-EGAPEQlfgnpqspr 247
|
250
....*....|
gi 490290321 515 YQQWLSDSQK 524
Cdd:PRK10619 248 LQQFLKGSLK 257
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-187 |
4.36e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.30 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqlawvnqetpALPQPAi 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGE-----------PVPSRA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 82 dyvidgdREYRQLEAALQQANERNDGHAIAT---VHGKLDAIDAWTIRSRAASLLHGLGFSNEQlERPVSDFSGGWRMRL 158
Cdd:PRK13537 76 -------RHARQRVGVVPQFDNLDPDFTVREnllVFGRYFGLSAAAARALVPPLLEFAKLENKA-DAKVGELSGGMKRRL 147
|
170 180 190
....*....|....*....|....*....|.
gi 490290321 159 NLAQALICRSDLLLLDEPTNHLDLDA--VIW 187
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQArhLMW 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
313-505 |
5.05e-14 |
|
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: 71.41 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLgYFAQHQLEFLRAD- 391
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI-IIDGLKL-TDDKKNINELRQKv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 392 ------------ESPLQHLArLAP--------QELEQKLRDYLGGFGFQgDKVSEETRRFSGGEKARLVLALIVWQRPNL 451
Cdd:cd03262 79 gmvfqqfnlfphLTVLENIT-LAPikvkgmskAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 452 LLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLaeEGmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
313-514 |
5.10e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 71.71 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIIldSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI----------------------- 369
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqdltalppaerpvsmlfqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 370 ---------------GLAKGIKLGYFAQHQLEflradesplQHLARLAPQELEQKLRDYLggfgfqgdkvseetrrfSGG 434
Cdd:COG3840 80 nnlfphltvaqniglGLRPGLKLTAEQRAQVE---------QALERVGLAGLLDRLPGQL-----------------SGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 435 EKARLVLA-LIVWQRPnLLLLDEPTNHLDLDMRQ---ALTEALIDFEGA-LVVVSHDRHLIRSTTDDLYLVHDGKVEPfD 509
Cdd:COG3840 134 QRQRVALArCLVRKRP-ILLLDEPFSALDPALRQemlDLVDELCRERGLtVLMVTHDPEDAARIADRVLLVADGRIAA-D 211
|
....*
gi 490290321 510 GDLED 514
Cdd:COG3840 212 GPTAA 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
313-505 |
7.02e-14 |
|
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: 71.42 E-value: 7.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL--------------AKGIklG 378
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLdgqditklpmhkraRLGI--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 379 YFAQHQLEF--LRADESPLQHL--ARLAPQELEQKLRDYLGGFGFQgdKVSEET-RRFSGGEKARLVLALIVWQRPNLLL 453
Cdd:cd03218 79 YLPQEASIFrkLTVEENILAVLeiRGLSKKEREEKLEELLEEFHIT--HLRKSKaSSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 454 LDEPTNHLD----LDMrQALTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:cd03218 157 LDEPFAGVDpiavQDI-QKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-183 |
7.83e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.72 E-value: 7.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG----NWQLAWVNQETPAL 76
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddveALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 77 PQpaiDYVIDGDREYRQL-------------------EAALQQANERNDGHAIAtvhgkldaidawtirsraasllhglg 137
Cdd:PRK09536 83 PQ---DTSLSFEFDVRQVvemgrtphrsrfdtwtetdRAAVERAMERTGVAQFA-------------------------- 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490290321 138 fsneqlERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD 183
Cdd:PRK09536 134 ------DRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
309-491 |
9.39e-14 |
|
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: 70.93 E-value: 9.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 309 PNPLLKMEKVS----AGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGIKLGYFAQHQ 384
Cdd:COG4181 5 SAPIIELRGLTktvgTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLA-GQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 385 LEFLRAD-------ESPL-QHLARLA----PQEL------EQKLRDYLGGFGFqGDKVSEETRRFSGGEKARLVLALIVW 446
Cdd:COG4181 84 RARLRARhvgfvfqSFQLlPTLTALEnvmlPLELagrrdaRARARALLERVGL-GHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490290321 447 QRPNLLLLDEPTNHLDLDMRQALTEALidFE-----GA-LVVVSHDRHLIR 491
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLL--FElnrerGTtLVLVTHDPALAA 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
312-505 |
1.15e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 70.67 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGY-GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIglakgiklgYFAQHQLEFLRA 390
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKI---------WFSGHDITRLKN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 DESPL-----------QHL----------------ARLAPQELEQKLRDYLGGFGFQgDKVSEETRRFSGGEKARLVLAL 443
Cdd:PRK10908 72 REVPFlrrqigmifqdHHLlmdrtvydnvaipliiAGASGDDIRRRVSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 444 IVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVV---SHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVlmaTHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
313-509 |
1.23e-13 |
|
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: 70.13 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERI--ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLaKGIKLGYFaqhqleflra 390
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDISTI---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 desPLQHLAR---LAPQE---LEQKLRDYLGGFGFQGD-------KVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
Cdd:cd03369 76 ---PLEDLRSsltIIPQDptlFSGTIRSNLDPFDEYSDeeiygalRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 458 TNHLDLDmrqalTEALI------DFEGALVVVShdRHLIRSTTD-DLYLVHD-GKVEPFD 509
Cdd:cd03369 153 TASIDYA-----TDALIqktireEFTNSTILTI--AHRLRTIIDyDKILVMDaGEVKEYD 205
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
316-487 |
1.40e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 72.49 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 316 EKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAK---GIKL-------GYFAQHQL 385
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlFTNLpprerrvGFVFQHYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 386 EFlradesplQHL------------ARLAPQELEQKLRDYLGGFGFQGdkvsEETRR---FSGGEKARLVLA--LIVwqR 448
Cdd:COG1118 86 LF--------PHMtvaeniafglrvRPPSKAEIRARVEELLELVQLEG----LADRYpsqLSGGQRQRVALAraLAV--E 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490290321 449 PNLLLLDEPTNHLD----LDMRQALTEALIDFEGALVVVSHDR 487
Cdd:COG1118 152 PEVLLLDEPFGALDakvrKELRRWLRRLHDELGGTTVFVTHDQ 194
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-221 |
1.61e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.86 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMtFPGNWQLAWVNQETPALPQPA- 80
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTRLMFQDAr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 -------IDYVIDGDReyrqleaalqqanerndGHaiatvhgkldaidaWtiRSRAASLLHGLGFSNEQLERPVSdFSGG 153
Cdd:PRK11247 92 llpwkkvIDNVGLGLK-----------------GQ--------------W--RDAALQALAAVGLADRANEWPAA-LSGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 154 WRMRLNLAQALICRSDLLLLDEPTNHLD---------LDAVIWLEkwlkgYTGTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:PRK11247 138 QKQRVALARALIHRPGLLLLDEPLGALDaltriemqdLIESLWQQ-----HGFTVLLVTHDVSEAVAMADRVLLIEE 209
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
325-504 |
2.01e-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: 68.33 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLQPV-SGEIGLAkgiklgyfAQHQLEFLradesplqhlarlaP 403
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWgSGRIGMP--------EGEDLLFL--------------P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 404 QeleqklRDYLGgfgfQG----------DKVseetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
Cdd:cd03223 71 Q------RPYLP----LGtlreqliypwDDV------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
170 180 190
....*....|....*....|....*....|.
gi 490290321 474 IDFEGALVVVSHDRHLIRSTTDDLYLVHDGK 504
Cdd:cd03223 135 KELGITVISVGHRPSLWKFHDRVLDLDGEGG 165
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
324-510 |
2.75e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 70.85 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 324 ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL------AKGIKLGY----------FAQHQL-- 385
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditDKKVKLSDirkkvglvfqYPEYQLfe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 386 EFLRAD-ESPLQHLArLAPQELEQKLRDYLGGFGFQGDKVSEETR-RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
Cdd:PRK13637 99 ETIEKDiAFGPINLG-LSEEEIENRVKRAMNIVGLDYEDYKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490290321 464 DMRQALTEALID----FEGALVVVSHDRHLIRSTTDDLYLVHDGKVEpFDG 510
Cdd:PRK13637 178 KGRDEILNKIKElhkeYNMTIILVSHSMEDVAKLADRIIVMNKGKCE-LQG 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
313-514 |
3.21e-13 |
|
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: 69.67 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGErIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL-AKGIKLGYFAQHQLEFLRAD 391
Cdd:cd03299 1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 392 ESPLQHLA-----------RLAPQ-ELEQKLRDYLGGFGFqGDKVSEETRRFSGGEKARLVLA--LIVwqRPNLLLLDEP 457
Cdd:cd03299 80 YALFPHMTvykniayglkkRKVDKkEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIAraLVV--NPKILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 458 TNHLDLDMRQALTEALID----FEGALVVVSHDRHLIRSTTDDLYLVHDGKVEPFdGDLED 514
Cdd:cd03299 157 FSALDVRTKEKLREELKKirkeFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV-GKPEE 216
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
325-498 |
3.26e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.53 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLQP-VSGEIGLAKGIKLGYFAQH---QLEFLRADESPLQHLAR 400
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPyGSGRIARPAGARVLFLPQRpylPLGTLREALLYPATAEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 401 LAPQELEQKLRDY-LGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID--FE 477
Cdd:COG4178 455 FSDAELREALEAVgLGHLAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPG 534
|
170 180
....*....|....*....|.
gi 490290321 478 GALVVVSHdrhliRSTTDDLY 498
Cdd:COG4178 535 TTVISVGH-----RSTLAAFH 550
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
10-217 |
3.60e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSmtfpGNWQLaWVNQETPALPqpaidyVIDgdr 89
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA----GCVDV-PDNQFGREAS------LID--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 eyrqleaalqqanerndghAIATVHGKLDAIDawtirsraasLLHGLGFSNEQL-ERPVSDFSGGWRMRLNLAQALICRS 168
Cdd:COG2401 105 -------------------AIGRKGDFKDAVE----------LLNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 169 DLLLLDEPTNHLDLD-----AVIWLEKWLKGYTgTLILISHDRDFLDPIV-DKII 217
Cdd:COG2401 156 KLLVIDEFCSHLDRQtakrvARNLQKLARRAGI-TLVVATHHYDVIDDLQpDLLI 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-182 |
3.64e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.80 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGN-------WQLAwvnQET 73
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspAELA---RRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 74 PALPQ--------PAIDYV----IDGDREYRQLEAALQQAnerndghaiatvhgkLDAIDAWTIRSRaasLLHGLgfsne 141
Cdd:PRK13548 79 AVLPQhsslsfpfTVEEVVamgrAPHGLSRAEDDALVAAA---------------LAQVDLAHLAGR---DYPQL----- 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490290321 142 qlerpvsdfSGGWRMRLNLAQALI---CRSD---LLLLDEPTNHLDL 182
Cdd:PRK13548 136 ---------SGGEQQRVQLARVLAqlwEPDGpprWLLLDEPTSALDL 173
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-204 |
3.74e-13 |
|
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: 67.45 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqlawvnqetpalpqpaiDYVIDGDREY 91
Cdd:cd03216 12 GVKAL-DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK------------------EVSFASPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 92 RQleaalqqanerndgHAIATVHgkldaidawtirsraasllhglgfsneQLerpvsdfSGGWRMRLNLAQALICRSDLL 171
Cdd:cd03216 73 RR--------------AGIAMVY---------------------------QL-------SVGERQMVEIARALARNARLL 104
|
170 180 190
....*....|....*....|....*....|....*.
gi 490290321 172 LLDEPTNHLDLDAVIWLEKWLKGYTG---TLILISH 204
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-205 |
4.12e-13 |
|
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: 72.01 E-value: 4.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPQPAIDYVIDGDREYRQLEA 96
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG--------VPVSSLDQDEVRRRVSVCAQDAHLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 97 ALQQANERndghaiatvHGKLDAIDA--WTIRSRA------ASLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQALICRS 168
Cdd:TIGR02868 423 TTVRENLR---------LARPDATDEelWAALERVgladwlRALPDGL---DTVLGEGGARLSGGERQRLALARALLADA 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 490290321 169 DLLLLDEPTNHLDLD-AVIWLEKWLKGYTG-TLILISHD 205
Cdd:TIGR02868 491 PILLLDEPTEHLDAEtADELLEDLLAALSGrTVVLITHH 529
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-181 |
4.14e-13 |
|
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: 67.72 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFpgnwqlawvNQETPALPQPAIdyvidgdreyRQL 94
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL---------DGVPVSDLEKAL----------SSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 95 EAALQQAnerndGHAIATvhgkldaidawTIRsraasllhglgfsnEQLERPvsdFSGGWRMRLNLAQALICRSDLLLLD 174
Cdd:cd03247 77 ISVLNQR-----PYLFDT-----------TLR--------------NNLGRR---FSGGERQRLALARILLQDAPIVLLD 123
|
....*..
gi 490290321 175 EPTNHLD 181
Cdd:cd03247 124 EPTVGLD 130
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
325-505 |
4.81e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.86 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQ--------PVSGEIGLaKGIKLGYFAQHQLEFLRA------ 390
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTL-NGEPLAAIDAPRLARLRAvlpqaa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 --------DESPL----QHLAR----------LAPQELEQKLRDYLggfgfqgdkVSEETRRFSGGEKARLVLALIVWQ- 447
Cdd:PRK13547 93 qpafafsaREIVLlgryPHARRagalthrdgeIAWQALALAGATAL---------VGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 448 --------RPNLLLLDEPTNHLDLDMRQALTEALIDFE-----GALVVVsHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwnlGVLAIV-HDPNLAARHADRIAMLADGAI 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
313-505 |
5.12e-13 |
|
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: 71.76 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--ELQPVSGEI--GLAKGIKLGY--------- 379
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyHVALCEKCGYverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 380 --------FAQHQLEFLRADESPLQHLARLAPQELEQKLRDY------------LGGFGFQGDK---------------- 423
Cdd:TIGR03269 81 pcpvcggtLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFALYgddtvldnvleaLEEIGYEGKEavgravdliemvqlsh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 424 -VSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD----MRQALTEALIDFEGALVVVSHDRHLIRSTTDDLY 498
Cdd:TIGR03269 161 rITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtaklVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
....*..
gi 490290321 499 LVHDGKV 505
Cdd:TIGR03269 241 WLENGEI 247
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-221 |
5.48e-13 |
|
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: 67.60 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwQLAWVNQETPALPQPaI 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE-DLTDLEDELPPLRRR-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 82 DYVIdgdreyrqleaalQQANerndghaiatvhgkldaidAWTIRSRAASLLHGLgfsneqlerpvsdfSGGWRMRLNLA 161
Cdd:cd03229 79 GMVF-------------QDFA-------------------LFPHLTVLENIALGL--------------SGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 162 QALICRSDLLLLDEPTNHLDLDAVIWLEKWLK------GYtgTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKslqaqlGI--TVVLVTHDLDEAARLADRVVVLRD 176
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
17-220 |
6.52e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 68.53 E-value: 6.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPQpaidyvidgdreyRQLeA 96
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDG--------QDISSLSE-------------REL-A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 97 AL---------QQAN-------ERNdghaIATVHgKLDAIDAWTIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNL 160
Cdd:COG1136 82 RLrrrhigfvfQFFNllpeltaLEN----VALPL-LLAGVSRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 161 AQALICRSDLLLLDEPTNHLD-------LDAviwLEKWLKGYTGTLILISHDRDFLDpIVDKIIHIE 220
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDsktgeevLEL---LRELNRELGTTIVMVTHDPELAA-RADRVIRLR 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-224 |
7.28e-13 |
|
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: 68.47 E-value: 7.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPqpa 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDG--------QDITGLS--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 idyvidgDREYRQLEA----ALQQAnerndghaiA-----TV----------HGKLdaiDAWTIRSRAASLLH--GLGFS 139
Cdd:COG1127 74 -------EKELYELRRrigmLFQGG---------AlfdslTVfenvafplreHTDL---SEAEIRELVLEKLElvGLPGA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 140 NEQLerPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD------LDAVIwLEkwLKGYTG-TLILISHDRDFLDPI 212
Cdd:COG1127 135 ADKM--P-SELSGGMRKRVALARALALDPEILLYDEPTAGLDpitsavIDELI-RE--LRDELGlTSVVVTHDLDSAFAI 208
|
250
....*....|..
gi 490290321 213 VDKIIHIEQQTM 224
Cdd:COG1127 209 ADRVAVLADGKI 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
313-485 |
7.69e-13 |
|
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: 67.77 E-value: 7.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI---------------------GL 371
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrwngtplaeqrdephenilylGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 372 AKGIKLGYFAQHQLEFLR-----ADESPLQHLARLAPQELEQKLRDYLggfgfqgdkvseetrrfSGGEKARLVLA-LIV 445
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAaihggAQRTIEDALAAVGLTGFEDLPAAQL-----------------SAGQQRRLALArLWL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490290321 446 WQRPnLLLLDEPTNHLD---LDMRQALTEALIDFEGALVVVSH 485
Cdd:TIGR01189 144 SRRP-LWILDEPTTALDkagVALLAGLLRAHLARGGIVLLTTH 185
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-205 |
8.86e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.95 E-value: 8.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 5 SSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwQLAWVNQETPALPQPAIDYV 84
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE-PLAKLNRAQRKAFRRDIQMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 85 idgdreyrqLEAALQQANERND-GHAIATVHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQA 163
Cdd:PRK10419 95 ---------FQDSISAVNPRKTvREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490290321 164 LICRSDLLLLDEPTNHLDL---DAVIWLEKWLKGYTGT-LILISHD 205
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLvlqAGVIRLLKKLQQQFGTaCLFITHD 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-205 |
9.81e-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: 69.31 E-value: 9.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTL-LSLLK--NEISADGGSMTFPGnwqlawvnQETPALPQPAId 82
Cdd:COG0444 10 YFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaRAILGllPPPGITSGEILFDG--------EDLLKLSEKEL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 83 yvidgdREYRQLEAAL--QqanernD-----------GHAIA---TVHGKLDAIDAwtiRSRAASLLH--GLGFSNEQLE 144
Cdd:COG0444 81 ------RKIRGREIQMifQ------DpmtslnpvmtvGDQIAeplRIHGGLSKAEA---RERAIELLErvGLPDPERRLD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 145 R-PvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKGYTG-TLILISHD 205
Cdd:COG0444 146 RyP-HELSGGMRQRVMIARALALEPKLLIADEPTTALDVtiqAQILNLLKDLQRELGlAILFITHD 210
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
337-505 |
1.00e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 337 PGSRIGLLGRNGAGKSTLIKLLAGeLQPVSGEIGLAkGIKLGYFAQHQLEFLRA----DESPL----------QHLARLA 402
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFA-GQPLEAWSAAELARHRAylsqQQTPPfampvfqyltLHQPDKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 403 PQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLA---LIVWQRPN----LLLLDEPTNHLDLDMRQALTEALID 475
Cdd:PRK03695 99 RTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvLQVWPDINpagqLLLLDEPMNSLDVAQQAALDRLLSE 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 490290321 476 FE---GALVVVSHD-----RHlirstTDDLYLVHDGKV 505
Cdd:PRK03695 179 LCqqgIAVVMSSHDlnhtlRH-----ADRVWLLKQGKL 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
330-516 |
1.06e-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: 69.76 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 330 SIKLNL-VPGS-RIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL--------AKGI-------KLGYFAQHQLEF--LRA 390
Cdd:TIGR02142 13 SLDADFtLPGQgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfdsRKGIflppekrRIGYVFQEARLFphLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 DESPLQHLARLAPQEL---EQKLRDYLGgfgfQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
Cdd:TIGR02142 93 RGNLRYGMKRARPSERrisFERVIELLG----IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490290321 468 ALT---EALID-FEGALVVVSHDRHLIRSTTDDLYLVHDGKVEPFdGDLEDYQ 516
Cdd:TIGR02142 169 EILpylERLHAeFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA-GPIAEVW 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
308-505 |
1.13e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 68.72 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 308 LPNPLLKMEKVSAGYGERI-ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYFAQHQLE 386
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 387 FLRAD----ESPLQHL---------------ARLAPQELEQKLRDYLGGFGFQGDKvSEETRRFSGGEKARLVLALIVWQ 447
Cdd:PRK13636 80 LRESVgmvfQDPDNQLfsasvyqdvsfgavnLKLPEDEVRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490290321 448 RPNLLLLDEPTNHLD----LDMRQALTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK13636 159 EPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
142-505 |
1.33e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 142 QLERPVSDF----SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKGYTG-TLILISHDRDfldpIV 213
Cdd:PRK15134 145 QAAKRLTDYphqlSGGERQRVMIAMALLTRPELLIADEPTTALDVSVqaqILQLLRELQQELNmGLLFITHNLS----IV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 214 DKIIHieqqtmfeytgnysSFEVQRATRLAQQQamyesqqqrvahlqsyidrfRAKATKAKQAQSRIKMLERMEliaPAH 293
Cdd:PRK15134 221 RKLAD--------------RVAVMQNGRCVEQN--------------------RAATLFSAPTHPYTQKLLNSE---PSG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 294 vdnpfhfsfrQPESLPN---PLLKMEKVSAGY-----------GERIILDSIKLNLVPGSRIGLLGRNGAGKST----LI 355
Cdd:PRK15134 264 ----------DPVPLPEpasPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 356 KLLAGElqpvsGEIGLaKGIKLGYFAQHQLEFLRAD----------------------ESPLQ-HLARLAPQELEQKLRD 412
Cdd:PRK15134 334 RLINSQ-----GEIWF-DGQPLHNLNRRQLLPVRHRiqvvfqdpnsslnprlnvlqiiEEGLRvHQPTLSAAQREQQVIA 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 413 YLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMrQALTEALI-----DFEGALVVVSHDR 487
Cdd:PRK15134 408 VMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTV-QAQILALLkslqqKHQLAYLFISHDL 486
|
410
....*....|....*...
gi 490290321 488 HLIRSTTDDLYLVHDGKV 505
Cdd:PRK15134 487 HVVRALCHQVIVLRQGEV 504
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
316-474 |
1.49e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 316 EKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKG--IKLGYFAQ-----HQ---- 384
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiDDPDVAEAchylgHRnamk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 385 --------LEFLRA-----DESPLQHLARLAPQELEQKLRDYLggfgfqgdkvseetrrfSGGEKARLVLA-LIVWQRPn 450
Cdd:PRK13539 86 paltvaenLEFWAAflggeELDIAAALEAVGLAPLAHLPFGYL-----------------SAGQKRRVALArLLVSNRP- 147
|
170 180
....*....|....*....|....
gi 490290321 451 LLLLDEPTNHLDLDMrQALTEALI 474
Cdd:PRK13539 148 IWILDEPTAALDAAA-VALFAELI 170
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-181 |
1.61e-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: 67.59 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqlawvnqETPALPQPAIdyvidgdREY 91
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGT--------DINKLKGKAL-------RQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 92 RQLEAAL-QQAN--ERNDghAIATV-HGKLDAIDAWtiRS-----------RAASLLHGLGFSnEQLERPVSDFSGGWRM 156
Cdd:cd03256 77 RRQIGMIfQQFNliERLS--VLENVlSGRLGRRSTW--RSlfglfpkeekqRALAALERVGLL-DKAYQRADQLSGGQQQ 151
|
170 180
....*....|....*....|....*
gi 490290321 157 RLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLD 176
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
313-485 |
1.66e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.78 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--ELQPVSGEIGL--------------AKGIK 376
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLdgedilelspderaRAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 377 LGYfaQHQLE--------FLRADESPlQHLARLAPQELEQKLRDYLGGFGFqgdkvSEE-TRR-----FSGGEKARL-VL 441
Cdd:COG0396 81 LAF--QYPVEipgvsvsnFLRTALNA-RRGEELSAREFLKLLKEKMKELGL-----DEDfLDRyvnegFSGGEKKRNeIL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490290321 442 ALIVwQRPNLLLLDEPTNHLDLDMRQALTE---ALIDFEGALVVVSH 485
Cdd:COG0396 153 QMLL-LEPKLAILDETDSGLDIDALRIVAEgvnKLRSPDRGILIITH 198
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
313-505 |
1.71e-12 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 67.68 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL-------------AKgIKLGY 379
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIdgqdithlpmherAR-LGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 380 FAQHQLEFLR---AD--ESPLQHLARLAPQELEQKLRDYLGGFGFQGDKvSEETRRFSGGEKARLVLALIVWQRPNLLLL 454
Cdd:TIGR04406 81 LPQEASIFRKltvEEniMAVLEIRKDLDRAEREERLEALLEEFQISHLR-DNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 455 DEPTNHLD----LDMRQaLTEALIDFEGALVVVSHDrhlIRST---TDDLYLVHDGKV 505
Cdd:TIGR04406 160 DEPFAGVDpiavGDIKK-IIKHLKERGIGVLITDHN---VRETldiCDRAYIISDGKV 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-224 |
1.74e-12 |
|
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: 66.09 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlAWVNQETPAlpqpaidyvidgdrEYRQ 93
Cdd:cd03246 15 PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG----ADISQWDPN--------------ELGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 94 LEAALQQANERNDGhAIAtvhgklDAIdawtirsraasllhglgfsneqlerpvsdFSGGWRMRLNLAQALICRSDLLLL 173
Cdd:cd03246 77 HVGYLPQDDELFSG-SIA------ENI-----------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490290321 174 DEPTNHLDLDAVIWLE---KWLKGYTGTLILISHDRDFLDpIVDKIIHIEQQTM 224
Cdd:cd03246 121 DEPNSHLDVEGERALNqaiAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
313-505 |
2.03e-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: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG-----ELQPVSGEIGL-AKGIklgYFAQHQLE 386
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLdGKDI---YDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 387 FLR-----------------AD--ESPLQHLARLAPQELEQKLRDYLGGFGFqGDKVSEET--RRFSGGEKARLVLA--L 443
Cdd:cd03260 78 ELRrrvgmvfqkpnpfpgsiYDnvAYGLRLHGIKLKEELDERVEEALRKAAL-WDEVKDRLhaLGLSGGQQQRLCLAraL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 444 IVwqRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:cd03260 157 AN--EPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
314-505 |
2.43e-12 |
|
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: 66.87 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 314 KMEKVSAGYGE-RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGI------------KLGYF 380
Cdd:cd03254 4 EFENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQI-LIDGIdirdisrkslrsMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 381 AQHQLEFLRADESPLQHLARLAPQELEQKLRDYLGGFGF-----QG--DKVSEETRRFSGGEKARLVLALIVWQRPNLLL 453
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFimklpNGydTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 454 LDEPTNHLDLDMRQALTEALID-FEG-ALVVVSHdrHLirSTT---DDLYLVHDGKV 505
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKlMKGrTSIIIAH--RL--STIknaDKILVLDDGKI 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
316-505 |
2.43e-12 |
|
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: 66.87 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 316 EKVSAGYG-ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGI------------KLGYFAQ 382
Cdd:cd03253 4 ENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSI-LIDGQdirevtldslrrAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 383 ----------HQLEFLRADESPLQ--HLARLApqeleqKLRDYLGGFGFQGD-KVSEETRRFSGGEKARLVLALIVWQRP 449
Cdd:cd03253 83 dtvlfndtigYNIRYGRPDATDEEviEAAKAA------QIHDKIMRFPDGYDtIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 450 NLLLLDEPTNHLDLDMRQALTEALID-FEG-ALVVVSHDRHLIrSTTDDLYLVHDGKV 505
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDvSKGrTTIVIAHRLSTI-VNADKIIVLKDGRI 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
12-217 |
2.48e-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: 67.08 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPQPAIdyvidgdreY 91
Cdd:cd03219 12 GLVAL-DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG--------EDITGLPPHEI---------A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 92 RQ-----------------LEAALQQANERNDGHAIATVHGKLDAidawTIRSRAASLLHGLGFSnEQLERPVSDFSGGW 154
Cdd:cd03219 74 RLgigrtfqiprlfpeltvLENVMVAAQARTGSGLLLARARREER----EARERAEELLERVGLA-DLADRPAGELSYGQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 155 RMRLNLAQALICRSDLLLLDEPT---NHLDLDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKII 217
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-182 |
2.62e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.35 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGN--WQLawvnqetpalpq 78
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpiSML------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 79 paidyvidGDREYRQLEAALQQANERNDGhaiATVH--------------GKLDAIDawtiRSRAASLLHGLGFsNEQLE 144
Cdd:PRK11231 70 --------SSRQLARRLALLPQHHLTPEG---ITVRelvaygrspwlslwGRLSAED----NARVNQAMEQTRI-NHLAD 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 490290321 145 RPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL 182
Cdd:PRK11231 134 RRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-181 |
2.65e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 68.22 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVL--LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPQpaidyvidg 87
Cdd:COG4608 25 GRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG--------QDITGLSG--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 88 dREYRQLEAALQ------QA--NERND-GHAIA---TVHGKLDAIDawtIRSRAASLLHGLGFSNEQLERPVSDFSGGWR 155
Cdd:COG4608 88 -RELRPLRRRMQmvfqdpYAslNPRMTvGDIIAeplRIHGLASKAE---RRERVAELLELVGLRPEHADRYPHEFSGGQR 163
|
170 180
....*....|....*....|....*.
gi 490290321 156 MRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALD 189
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-221 |
2.81e-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: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqLAWVNQetpalpqpaidyvidgDREYRQLEA 96
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL--VPWKRR----------------KKFLRRIGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 97 ALQQANE------RNDGHA-IATVHGkLDAIDAWTIRSRAASLLHgLGfsnEQLERPVSDFSGGWRMRLNLAQALICRSD 169
Cdd:cd03267 99 VFGQKTQlwwdlpVIDSFYlLAAIYD-LPPARFKKRLDELSELLD-LE---ELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 170 LLLLDEPTNHLDLDAVIWLEKWLKGYT----GTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNrergTTVLLTSHYMKDIEALARRVLVIDK 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
311-489 |
2.90e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.76 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGE----RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYFAQ---- 382
Cdd:PRK11629 4 ILLQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV-IFNGQPMSKLSSaaka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 383 ----------HQLEFLRADESPLQHLA------RLAPQELEQKLRDYLGGFGFQgDKVSEETRRFSGGEKARLVLALIVW 446
Cdd:PRK11629 83 elrnqklgfiYQFHHLLPDFTALENVAmplligKKKPAEINSRALEMLAAVGLE-HRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490290321 447 QRPNLLLLDEPTNHLDLDMRQALTEALIDFE----GALVVVSHDRHL 489
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHDLQL 208
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-506 |
2.91e-12 |
|
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: 69.47 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLkneisadggSMTFP-GNW--QLAWVNQETPAlpqpaidyvidgdREYRQ 93
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKIL---------SGVYPhGTWdgEIYWSGSPLKA-------------SNIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 94 LEAA--------------LQQANERNDGHAIaTVHGKLDAIDAWTIRSRAasLLHGLGFSNEQLERPVSDFSGGWRMRLN 159
Cdd:TIGR02633 75 TERAgiviihqeltlvpeLSVAENIFLGNEI-TLPGGRMAYNAMYLRAKN--LLRELQLDADNVTRPVGDYGGGQQQLVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 160 LAQALICRSDLLLLDEPTNHL---DLDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIEQqtmfeytGNYSSFEV 236
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLtekETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRD-------GQHVATKD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 237 QRATRLAQQQAMYESQQQRvahlqsyidrfrakATKAKQAQSRIKMLERMELIAPAHVDNPfhfsfrqpeslpnpllKME 316
Cdd:TIGR02633 225 MSTMSEDDIITMMVGREIT--------------SLYPHEPHEIGDVILEARNLTCWDVINP----------------HRK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 317 KVsagygeriilDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQ-PVSGEIglakgiklgYFAQHQLEfLRADESPL 395
Cdd:TIGR02633 275 RV----------DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNV---------FINGKPVD-IRNPAQAI 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 396 QHLARLAPqelEQKLRD---------------YLGGFGFQG--DKVSEE--------------------TRRFSGGEKAR 438
Cdd:TIGR02633 335 RAGIAMVP---EDRKRHgivpilgvgknitlsVLKSFCFKMriDAAAELqiigsaiqrlkvktaspflpIGRLSGGNQQK 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 439 LVLALIVWQRPNLLLLDEPTNHLDLDMRQA---LTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKVE 506
Cdd:TIGR02633 412 AVLAKMLLTNPRVLILDEPTRGVDVGAKYEiykLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-221 |
2.99e-12 |
|
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: 66.87 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqetpalpQPAIDYVIDGDReyRQ 93
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG---------------QDIREVTLDSLR--RA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 94 LEAALQQANERND--GHAIAtvHGKLDAIDAWTIRSRAASLLHGL------GFSNEQLERPVSdFSGGWRMRLNLAQALI 165
Cdd:cd03253 77 IGVVPQDTVLFNDtiGYNIR--YGRPDATDEEVIEAAKAAQIHDKimrfpdGYDTIVGERGLK-LSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 166 CRSDLLLLDEPTNHLD-------LDAviwLEKWLKGYtgTLILISHDrdfLDPIV--DKIIHIEQ 221
Cdd:cd03253 154 KNPPILLLDEATSALDthtereiQAA---LRDVSKGR--TTIVIAHR---LSTIVnaDKIIVLKD 210
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-247 |
3.06e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.49 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADgGSMTF---------PGNW--QLAWVNQEtPALPQPAI-D 82
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKIngielreldPESWrkHLSWVGQN-PQLPHGTLrD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 83 YVIDGDREYR--QLEAALQQANerndghaiatvhgkldaidawtIRSRAASLLHGlgfsneqLERPVSD----FSGGWRM 156
Cdd:PRK11174 442 NVLLGNPDASdeQLQQALENAW----------------------VSEFLPLLPQG-------LDTPIGDqaagLSVGQAQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 157 RLNLAQALICRSDLLLLDEPTNHLDLD---AVIwleKWLKGYTG--TLILISHDRDFLDPiVDKIIHIEQQTMFEyTGNY 231
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHseqLVM---QALNAASRrqTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQ-QGDY 567
|
250
....*....|....*....
gi 490290321 232 SSFEVQR---ATRLAQQQA 247
Cdd:PRK11174 568 AELSQAGglfATLLAHRQE 586
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
310-490 |
3.33e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.28 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 310 NPLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLA-KGI----------KLG 378
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEgEDIstlkpeiyrqQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 379 YFAQHQLEFlraDES-------PLQhLARLAPQelEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNL 451
Cdd:PRK10247 85 YCAQTPTLF---GDTvydnlifPWQ-IRNQQPD--PAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490290321 452 LLLDEPTNHLDLDMRQALTEaLI-----DFEGALVVVSHDRHLI 490
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNE-IIhryvrEQNIAVLWVTHDKDEI 201
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
313-506 |
4.11e-12 |
|
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: 66.21 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL---------AKGIKLGYFAQH 383
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggedatdvpVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 384 QLEF------------LRAdesplQHLARLAP-QELEQKLRDYLGGFGFQG--DKVSEEtrrFSGGEKARLVLALIVWQR 448
Cdd:cd03296 83 YALFrhmtvfdnvafgLRV-----KPRSERPPeAEIRAKVHELLKLVQLDWlaDRYPAQ---LSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490290321 449 PNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLIRSTTDDLYLVHDGKVE 506
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHDQEEALEVADRVVVMNKGRIE 216
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-221 |
4.44e-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: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIR-RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG-------NWQLAW---- 68
Cdd:COG2884 1 MIRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkRREIPYlrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 69 ---VNQETPALPqpaidyvidgDRE-YRQLEAALQqanerndghaiatVHGKLDAidawTIRSRAASLLH--GLGfsnEQ 142
Cdd:COG2884 81 igvVFQDFRLLP----------DRTvYENVALPLR-------------VTGKSRK----EIRRRVREVLDlvGLS---DK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 143 LERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGY--TGTLILI-SHDRDFLDPIVDKIIHI 219
Cdd:COG2884 131 AKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRMPKRVLEL 210
|
..
gi 490290321 220 EQ 221
Cdd:COG2884 211 ED 212
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
313-505 |
4.78e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.55 E-value: 4.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL---------AKGI--KLGYFA 381
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdgehiqhyaSKEVarRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 382 QHQL--------EFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQgDKVSEETRRFSGGEKARLVLALIVWQRPNLLL 453
Cdd:PRK10253 88 QNATtpgditvqELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 454 LDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNRekgyTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
312-505 |
5.26e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.07 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGY------GERIILDsIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKLGYFAQHQL 385
Cdd:PRK13643 1 MIKFEKVNYTYqpnspfASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 386 EFLRA--------------DESPLQHLArLAPQ-------ELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALI 444
Cdd:PRK13643 80 KPVRKkvgvvfqfpesqlfEETVLKDVA-FGPQnfgipkeKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 445 VWQRPNLLLLDEPTNHLDLDMR---QALTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARiemMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
10-204 |
5.50e-12 |
|
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: 66.02 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLlDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG--------NW---QLAWVNQEtPALPQ 78
Cdd:cd03249 13 RPDVPIL-KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirdlnlRWlrsQIGLVSQE-PVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 79 PAIDYVI---DGDREYRQLEAALQQANerndghaiatvhgkldaidawtIRSRAASLLHG----LGFSNEQLerpvsdfS 151
Cdd:cd03249 91 GTIAENIrygKPDATDEEVEEAAKKAN----------------------IHDFIMSLPDGydtlVGERGSQL-------S 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 152 GGWRMRLNLAQALICRSDLLLLDEPTNHLDLD--AVIW--LEKWLKGYtgTLILISH 204
Cdd:cd03249 142 GGQKQRIAIARALLRNPKILLLDEATSALDAEseKLVQeaLDRAMKGR--TTIVIAH 196
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-256 |
6.46e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.31 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG----NW-------QLAWVNQ----------ETPA 75
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiaDYseaalrqAISVVSQrvhlfsatlrDNLL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 76 LPQPAIDyviDgdreyRQLEAALQQAN-----ERNDGhaiatvhgkldaIDAWtirsraasllhgLGFSNEQLerpvsdf 150
Cdd:PRK11160 436 LAAPNAS---D-----EALIEVLQQVGlekllEDDKG------------LNAW------------LGEGGRQL------- 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAviwLEKWLKGytGTLILISHDRDFLDPIvDKIIHIEQQT 223
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDaeterqiLEL---LAEHAQN--KTVLMITHRLTGLEQF-DRICVMDNGQ 550
|
250 260 270
....*....|....*....|....*....|...
gi 490290321 224 MFEyTGNYSSfevqratrLAQQQAMYESQQQRV 256
Cdd:PRK11160 551 IIE-QGTHQE--------LLAQQGRYYQLKQRL 574
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-220 |
7.04e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.16 E-value: 7.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTF-----PGNWQLAwvNQETPAL 76
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvPARARLA--RARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 77 PQpaIDYVidgDREYRQLEAALqqanerndghaiatVHGKLDAIDAWTIRSRAASLLHglgFSneQLER----PVSDFSG 152
Cdd:PRK13536 120 PQ--FDNL---DLEFTVRENLL--------------VFGRYFGMSTREIEAVIPSLLE---FA--RLESkadaRVSDLSG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 153 GWRMRLNLAQALICRSDLLLLDEPTNHLDLDA--VIWLE-KWLKGYTGTLILISHDRDFLDPIVDKIIHIE 220
Cdd:PRK13536 176 GMKRRLTLARALINDPQLLILDEPTTGLDPHArhLIWERlRSLLARGKTILLTTHFMEEAERLCDRLCVLE 246
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
343-584 |
7.53e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 68.65 E-value: 7.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 343 LLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIklGYFAQHQ-----------LEFLRADESPLQHLARLApqELEQKLR 411
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEISEGRVWAERSI--AYVPQQAwimnatvrgniLFFDEEDAARLADAVRVS--QLEADLA 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 412 DYLGGFGFQgdkVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALidFEGAL-----VVVSHD 486
Cdd:PTZ00243 767 QLGGGLETE---IGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEC--FLGALagktrVLATHQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 487 RHLIrSTTDDLYLVHDGKVEpFDGDLEDYQQwLSDSQKQESQSGEAPKESGNSAQARKDQKRREAELRSQTQPLRKEIAR 566
Cdd:PTZ00243 842 VHVV-PRADYVVALGDGRVE-FSGSSADFMR-TSLYATLAAELKENKDSKEGDADAEVAEVDAAPGGAVDHEPPVAKQEG 918
|
250 260
....*....|....*....|...
gi 490290321 567 LEKEMDKLN-----AQLASAEEK 584
Cdd:PTZ00243 919 NAEGGDGAAldaaaGRLMTREEK 941
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-217 |
7.78e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 68.27 E-value: 7.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 23 TINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMtfPGNWQLAWVnqetpalPQpaidYV-IDGDREYRQLeaaLQQA 101
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYK-------PQ----YIsPDYDGTVEEF---LRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 102 NErndghaiatvhgklDAIDAWTIRSRaasLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:COG1245 426 NT--------------DDFGSSYYKTE---IIKPLGL-EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490290321 182 LDAVIWLEKWLKGYT----GTLILISHDRDFLDPIVDKII 217
Cdd:COG1245 488 VEQRLAVAKAIRRFAenrgKTAMVVDHDIYLIDYISDRLM 527
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
312-474 |
7.78e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.88 E-value: 7.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLA------KGIKLGYFAQHQ- 384
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegPGAERGVVFQNEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 385 ----LEFLRADESPLQhLARLAPQELEQKLRDYLGGFGFQGdkvsEETRR---FSGGEKARLVLALIVWQRPNLLLLDEP 457
Cdd:PRK11248 81 llpwRNVQDNVAFGLQ-LAGVEKMQRLEIAHQMLKKVGLEG----AEKRYiwqLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170
....*....|....*..
gi 490290321 458 TNHLDLDMRQALTEALI 474
Cdd:PRK11248 156 FGALDAFTREQMQTLLL 172
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
313-519 |
8.01e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.39 E-value: 8.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYG-----ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLA----------KGIK- 376
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhitpetgnKNLKk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 377 -------LGYFAQHQLeflrADESPLQHLaRLAP-------QELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLA 442
Cdd:PRK13641 83 lrkkvslVFQFPEAQL----FENTVLKDV-EFGPknfgfseDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 443 LIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA---LVVVSHDRHLIRSTTDDLYLVHDGKVEPFDGDLEDY--QQ 517
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFsdKE 237
|
..
gi 490290321 518 WL 519
Cdd:PRK13641 238 WL 239
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
328-503 |
8.16e-12 |
|
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: 65.15 E-value: 8.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKG--------------IKL-----GYFAQhqleFL 388
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdlaqaspreiLALrrrtiGYVSQ----FL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 389 RA-------D--ESPLQHLArLAPQELEQKLRDYLGGFGfqgdkVSEE-------TrrFSGGEKARLVLA--LIVwqRPN 450
Cdd:COG4778 103 RViprvsalDvvAEPLLERG-VDREEARARARELLARLN-----LPERlwdlppaT--FSGGEQQRVNIArgFIA--DPP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 451 LLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLIRSTTDDLYLVHDG 503
Cdd:COG4778 173 LLLLDEPTASLDAANRAVVVELIEEAkaRGtAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-220 |
8.48e-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: 65.01 E-value: 8.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 26 PGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGN-WQLAWVNQETPalPQP-AIDYVIdgdREY--------RQ-L 94
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvLFDSRKKINLP--PQQrKIGLVF---QQYalfphlnvREnL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 95 EAALQQANERNDghaiatvhgkldaidawtiRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLD 174
Cdd:cd03297 97 AFGLKRKRNRED-------------------RISVDELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490290321 175 EPTNHLD----LDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIE 220
Cdd:cd03297 157 EPFSALDralrLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVME 206
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
312-505 |
8.65e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.94 E-value: 8.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYFAQHQLEFLRAD 391
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LFDGENIPAMSRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 392 ES--------------------PLQHLARLAPQELEQKLRDYLGGFGFQGD---KVSEetrrFSGGEKARLVLALIVWQR 448
Cdd:PRK11831 86 MSmlfqsgalftdmnvfdnvayPLREHTQLPAPLLHSTVMMKLEAVGLRGAaklMPSE----LSGGMARRAALARAIALE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 449 PNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALgvtcVVVSHDVPEVLSIADHAYIVADKKI 222
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-226 |
9.18e-12 |
|
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: 67.82 E-value: 9.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqlawvnqetpalpqPAIDYVIDGDReyRQ 93
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGH---------------DLADYTLASLR--RQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 94 LEAALQQANERNDGHAIATVHGKLDAIDAWTIRS--RAASLLHGLGFSNEQLERPVSD----FSGGWRMRLNLAQALICR 167
Cdd:TIGR02203 408 VALVSQDVVLFNDTIANNIAYGRTEQADRAEIERalAAAYAQDFVDKLPLGLDTPIGEngvlLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 168 SDLLLLDEPTNHLD-------LDAviwLEKWLKGYTGtlILISHDrdfLDPI--VDKIIHIEQQTMFE 226
Cdd:TIGR02203 488 APILILDEATSALDneserlvQAA---LERLMQGRTT--LVIAHR---LSTIekADRIVVMDDGRIVE 547
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-205 |
9.20e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 65.63 E-value: 9.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISAdGGSMTFPG----NWQL-------AWVNQETPALPQ-PAIDYV 84
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGrplsDWSAaelarhrAYLSQQQSPPFAmPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 85 idgdreyrqleaALQQANERNDGHAIATVhgkldaidawtirsraASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQAL 164
Cdd:COG4138 91 ------------ALHQPAGASSEAVEQLL----------------AQLAEALGLED-KLSRPLTQLSGGEWQRVRLAAVL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490290321 165 --ICRSD-----LLLLDEPTNHLDLDAVIWLEKWLKGYT---GTLILISHD 205
Cdd:COG4138 142 lqVWPTInpegqLLLLDEPMNSLDVAQQAALDRLLRELCqqgITVVMSSHD 192
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
17-204 |
1.06e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 67.88 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG---------NW--QLAWVNQETP----------A 75
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdirdltleSLrrQIGVVPQDTFlfsgtireniR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 76 LPQPaidyviDGDREyrQLEAALQQANerndghaiatVHgklDAIDAwtirsraasLLHGLgfsNEQL-ERPVSdFSGGW 154
Cdd:COG1132 436 YGRP------DATDE--EVEEAAKAAQ----------AH---EFIEA---------LPDGY---DTVVgERGVN-LSGGQ 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490290321 155 RMRLNLAQALICRSDLLLLDEPTNHLDL--DAVIW--LEKWLKGYtgTLILISH 204
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTetEALIQeaLERLMKGR--TTIVIAH 533
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-220 |
1.15e-11 |
|
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: 64.74 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPQPAIDYVidgdreYRQLEA 96
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNG--------QDVSDLRGRAIPYL------RRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 97 ALQQANERNDGHAIATVHGKLDAIDA--WTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLD 174
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVppREIRKRVPAALELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490290321 175 EPTNHLDLDAVIWLEKWLKGYT--GTLILIS-HDRDFLDPIVDKIIHIE 220
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINkaGTTVVVAtHAKELVDTTRHRVIALE 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
314-486 |
1.38e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 65.10 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 314 KMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLA----KGIKLGYFAQHqLEFLR 389
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDgldvATTPSRELAKR-LAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 390 ADesplQHL-ARLapqeleqKLRDyLGGFG-F---QG-------DKVSEETRRF-------------SGGEKARLVLALI 444
Cdd:COG4604 82 QE----NHInSRL-------TVRE-LVAFGrFpysKGrltaedrEIIDEAIAYLdledladryldelSGGQRQRAFIAMV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490290321 445 VWQRPNLLLLDEPTNHLDL----DMRQALTEALIDFEGALVVVSHD 486
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
309-458 |
1.45e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.97 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 309 PNPLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIglakgiklgYFAQHQLEFL 388
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEI---------LLDGEPVRFR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 389 radeSPL-----------QHLArLAPQ----------------------ELEQKLRDYLGGFGFQGDkVSEETRRFSGGE 435
Cdd:COG1129 72 ----SPRdaqaagiaiihQELN-LVPNlsvaeniflgreprrgglidwrAMRRRARELLARLGLDID-PDTPVGDLSVAQ 145
|
170 180
....*....|....*....|....*...
gi 490290321 436 K-----ARlvlALIvwQRPNLLLLDEPT 458
Cdd:COG1129 146 QqlveiAR---ALS--RDARVLILDEPT 168
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-204 |
1.70e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 67.44 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG-----------NWQLAWVNQEtPAL----PQPAI 81
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylHRQVALVGQE-PVLfsgsVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 82 DYVIDgDREYRQLEAALQQANERN----DGHAIATVHGKldaidawtirsraasllHGlgfsneqlerpvSDFSGGWRMR 157
Cdd:TIGR00958 576 AYGLT-DTPDEEIMAAAKAANAHDfimeFPNGYDTEVGE-----------------KG------------SQLSGGQKQR 625
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490290321 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTGTLILISH 204
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
310-457 |
2.16e-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: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 310 NPLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLA--------------KGI 375
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDgedithlpmhkrarLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 376 klGYFAQH-----QL---EFLRAdesPLQhLARLAPQELEQKLRDYLGGFGFqgdkvsEETRR-----FSGGEKARLVLA 442
Cdd:COG1137 81 --GYLPQEasifrKLtveDNILA---VLE-LRKLSKKEREERLEELLEEFGI------THLRKskaysLSGGERRRVEIA 148
|
170
....*....|....*..
gi 490290321 443 --LIVwqRPNLLLLDEP 457
Cdd:COG1137 149 raLAT--NPKFILLDEP 163
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-220 |
2.19e-11 |
|
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: 63.64 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 16 LLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqLAWVNQEtPALPQPAI------DYVIDGDR 89
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQE-PWIQNGTIrenilfGKPFDEER 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 eYR------QLEAALQQanerndghaiatvhgkLDAIDAWTIRSRAASLlhglgfsneqlerpvsdfSGGWRMRLNLAQA 163
Cdd:cd03250 97 -YEkvikacALEPDLEI----------------LPDGDLTEIGEKGINL------------------SGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 164 LICRSDLLLLDEPtnhldLDAV-------IW----LEKWLKGytGTLILISHDRDFLdPIVDKIIHIE 220
Cdd:cd03250 142 VYSDADIYLLDDP-----LSAVdahvgrhIFenciLGLLLNN--KTRILVTHQLQLL-PHADQIVVLD 201
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
311-475 |
2.40e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 64.50 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYG----ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL------AKGIKLGYF 380
Cdd:COG4525 2 SMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdgvpvtGPGADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 381 AQHQ--LEFLRADES---PLQhLARLAPQELEQKLRDYL---GGFGFQGDKVSEetrrFSGGEKARLVLALIVWQRPNLL 452
Cdd:COG4525 82 FQKDalLPWLNVLDNvafGLR-LRGVPKAERRARAEELLalvGLADFARRRIWQ----LSGGMRQRVGIARALAADPRFL 156
|
170 180
....*....|....*....|...
gi 490290321 453 LLDEPTNHLDLDMRQALTEALID 475
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLD 179
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
313-474 |
2.44e-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: 63.67 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGY--GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLgyfAQHQLEFLRa 390
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSI-LIDGVDI---SKIGLHDLR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 desplQHLArLAPQE--------------------------LEQ-KLRDYLGGFGFQGD-KVSEETRRFSGGEKARLVLA 442
Cdd:cd03244 78 -----SRIS-IIPQDpvlfsgtirsnldpfgeysdeelwqaLERvGLKEFVESLPGGLDtVVEEGGENLSVGQRQLLCLA 151
|
170 180 190
....*....|....*....|....*....|..
gi 490290321 443 LIVWQRPNLLLLDEPTNHLDLDmrqalTEALI 474
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPE-----TDALI 178
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-205 |
2.50e-11 |
|
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: 64.44 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 5 SSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqetpalpQPAIDYV 84
Cdd:TIGR02769 15 GGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRG---------------QDLYQLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 85 IDGDREY-RQLEAALQQA----NERND-GHAIATVHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRL 158
Cdd:TIGR02769 80 RKQRRAFrRDVQLVFQDSpsavNPRMTvRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490290321 159 NLAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKGYTGT-LILISHD 205
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMvlqAVILELLRKLQQAFGTaYLFITHD 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-207 |
2.51e-11 |
|
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: 64.24 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqlaWVNQETPALPQPAIDYVIdgdr 89
Cdd:cd03295 10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE----DIREQDPVELRRKIGYVI---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 eyrqleaalQQAN-------ERNdghaIATVHgKLDAIDAWTIRSRAASLLHGLGFSNEQL-ERPVSDFSGGWRMRLNLA 161
Cdd:cd03295 82 ---------QQIGlfphmtvEEN----IALVP-KLLKWPKEKIRERADELLALVGLDPAEFaDRYPHELSGGQQQRVGVA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490290321 162 QALICRSDLLLLDEPTNHLD-------LDAVIWLEKWLKgytGTLILISHDRD 207
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDpitrdqlQEEFKRLQQELG---KTIVFVTHDID 197
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
312-505 |
2.58e-11 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 63.86 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGyFAQHQLEFLRAD 391
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI-TVDGEDLT-DSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 392 ---------------------ESPLQHLaRLAPQELEQKLRDYLGGFGFqGDKVSEETRRFSGGEK-----ARlVLALiv 445
Cdd:COG1126 79 vgmvfqqfnlfphltvlenvtLAPIKVK-KMSKAEAEERAMELLERVGL-ADKADAYPAQLSGGQQqrvaiAR-ALAM-- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 446 wqRPNLLLLDEPTNHLD-------LD-MRQaLTEalidfEG-ALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:COG1126 154 --EPKVMLFDEPTSALDpelvgevLDvMRD-LAK-----EGmTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
313-505 |
2.59e-11 |
|
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: 63.67 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIIldSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYF--AQHQLEFLRA 390
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV-LINGVDVTAAppADRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 DESPLQHLA-------------RLAPQElEQKLRDYLGGFGFQGdKVSEETRRFSGGEKARLVLA-LIVWQRPnLLLLDE 456
Cdd:cd03298 78 ENNLFAHLTveqnvglglspglKLTAED-RQAIEVALARVGLAG-LEKRLPGELSGGERQRVALArVLVRDKP-VLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490290321 457 PTNHLDLDMRQALTEALIDF----EGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLhaetKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
328-541 |
2.62e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 64.45 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI---GLAKGIKLGYFAQHQLEFLRADESPL-------QH 397
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdrnGEVSVIAISAGLSGQLTGIENIEFKMlcmgfkrKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 398 LARLAPQELEqklrdylggFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFE 477
Cdd:PRK13546 120 IKAMTPKIIE---------FSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 478 GA---LVVVSHDRHLIRSTTDDLYLVHDGKVEPFdGDLED----YQQWLSDSQKQESQSGEAPKESGNSAQ 541
Cdd:PRK13546 191 EQnktIFFVSHNLGQVRQFCTKIAWIEGGKLKDY-GELDDvlpkYEAFLNDFKKKSKAEQKEFRNKLDESR 260
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-227 |
2.73e-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: 63.67 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIR--RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG-NW----------QLAW 68
Cdd:cd03244 3 IEFKNVSLRyrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvDIskiglhdlrsRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 69 VNQEtPALPQPAIDYVIDGDREY--RQLEAALQQANERNdghAIATVHGKLDAIDAwtirsraasllhgLGFSNeqlerp 146
Cdd:cd03244 83 IPQD-PVLFSGTIRSNLDPFGEYsdEELWQALERVGLKE---FVESLPGGLDTVVE-------------EGGEN------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 147 vsdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL--DAVIW--LEKWLKGYtgTLILISHdRdfLDPIV--DKIIHIE 220
Cdd:cd03244 140 ---LSVGQRQLLCLARALLRKSKILVLDEATASVDPetDALIQktIREAFKDC--TVLTIAH-R--LDTIIdsDRILVLD 211
|
....*..
gi 490290321 221 QQTMFEY 227
Cdd:cd03244 212 KGRVVEF 218
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
327-495 |
2.76e-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: 63.56 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIG---LAKGIKLGYFAQHQL------------EFLRA- 390
Cdd:TIGR02324 23 VLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILvrhEGAWVDLAQASPREVlevrrktigyvsQFLRVi 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 --------DESPLQHLArLAPQELEQKLRDYLGGFgfqgdKVSEE-----TRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
Cdd:TIGR02324 103 prvsalevVAEPLLERG-VPREAARARARELLARL-----NIPERlwhlpPATFSGGEQQRVNIARGFIADYPILLLDEP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490290321 458 TNHLDLDMRQALTEAL--IDFEG-ALVVVSHDRHLIRSTTD 495
Cdd:TIGR02324 177 TASLDAANRQVVVELIaeAKARGaALIGIFHDEEVRELVAD 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
311-458 |
2.90e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.20 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI---G-----------LAKGIk 376
Cdd:COG3845 4 PALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEIlidGkpvrirsprdaIALGI- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 377 lGYFAQHqleF-------------LRADESPlqhLARLAPQELEQKLRDYLGGFGFQGD---KVSEetrrFSGGEKARL- 439
Cdd:COG3845 83 -GMVHQH---FmlvpnltvaenivLGLEPTK---GGRLDRKAARARIRELSERYGLDVDpdaKVED----LSVGEQQRVe 151
|
170 180
....*....|....*....|
gi 490290321 440 -VLALivWQRPNLLLLDEPT 458
Cdd:COG3845 152 iLKAL--YRGARILILDEPT 169
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
328-486 |
3.06e-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: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL-AKGI------KLGYFAQHQL-EFLRADESPLQHLA 399
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQItepgpdRMVVFQNYSLlPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 400 RLAPQ----ELEQKLRDYLG--GFGFQGDKVSEEtrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
Cdd:TIGR01184 81 RVLPDlsksERRAIVEEHIAlvGLTEAADKRPGQ---LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170
....*....|....*..
gi 490290321 474 I----DFEGALVVVSHD 486
Cdd:TIGR01184 158 MqiweEHRVTVLMVTHD 174
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-220 |
3.45e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.98 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRR-GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLkNEISADG-GSMTFPGNWQLAWVNQ------- 71
Cdd:COG4178 362 ALALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI-AGLWPYGsGRIARPAGARVLFLPQrpylplg 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 72 ---ETPALPQPAIDYvidgDREyrQLEAALQQANerndghaIATVHGKLDAIDAWTIRsraasllhglgfsneqlerpvs 148
Cdd:COG4178 441 tlrEALLYPATAEAF----SDA--ELREALEAVG-------LGHLAERLDEEADWDQV---------------------- 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 149 dFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKG--YTGTLILISHdRDFLDPIVDKIIHIE 220
Cdd:COG4178 486 -LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELT 557
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
324-505 |
3.52e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 324 ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGEL--QPVSGEIGLAkgiklgyfaqhQLEFLRaDESPLQHLARL 401
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVP-----------DNQFGR-EASLIDAIGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 402 APqeLEQKLRdYLGGFGFqGDKVSEeTRRF---SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF-- 476
Cdd:COG2401 110 GD--FKDAVE-LLNAVGL-SDAVLW-LRRFkelSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLar 184
|
170 180 190
....*....|....*....|....*....|..
gi 490290321 477 --EGALVVVSHDRHLIRSTTDDLYL-VHDGKV 505
Cdd:COG2401 185 raGITLVVATHHYDVIDDLQPDLLIfVGYGGV 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
316-505 |
4.39e-11 |
|
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: 63.27 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 316 EKVSAGYG--ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGI------------KLGYFA 381
Cdd:cd03252 4 EHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-LVDGHdlaladpawlrrQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 382 QHQLEFLR--------ADESPLQH----LARLA-PQELEQKLRDylgGFgfqGDKVSEETRRFSGGEKARLVLALIVWQR 448
Cdd:cd03252 83 QENVLFNRsirdnialADPGMSMErvieAAKLAgAHDFISELPE---GY---DTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 449 PNLLLLDEPTNHLDLDMRQALTEALIDFEG--ALVVVSHDRHLIRsTTDDLYLVHDGKV 505
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAHRLSTVK-NADRIIVMEKGRI 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
310-486 |
4.50e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 63.88 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 310 NPLLKMEKVSAGY--GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGIKL---------- 377
Cdd:PRK13635 3 EEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG-GMVLseetvwdvrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 378 --------------GYFAQHQLEF-LRADESPLQHLARLAPQELEQ-KLRDYLggfgfqgdkvSEETRRFSGGEKARLVL 441
Cdd:PRK13635 82 qvgmvfqnpdnqfvGATVQDDVAFgLENIGVPREEMVERVDQALRQvGMEDFL----------NREPHRLSGGQKQRVAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490290321 442 ALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVVVS--HD 486
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSitHD 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-181 |
5.04e-11 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 65.48 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVL--LDNATATINPGQKVGLVGKNGCGKSTL-LSLLKneISADGGSMTFPGnwqlawvnQETPALPQpaidyvid 86
Cdd:COG4172 293 RRTVGHVkaVDGVSLTLRRGETLGLVGESGSGKSTLgLALLR--LIPSEGEIRFDG--------QDLDGLSR-------- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 87 gdREYRQLEAALQ---QanernD-----------GHAIA---TVHGklDAIDAWTIRSRAASLLHGLGFSNEQLERPVSD 149
Cdd:COG4172 355 --RALRPLRRRMQvvfQ-----DpfgslsprmtvGQIIAeglRVHG--PGLSAAERRARVAEALEEVGLDPAARHRYPHE 425
|
170 180 190
....*....|....*....|....*....|..
gi 490290321 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
311-506 |
5.23e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.58 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKLGYFAQHqleflRA 390
Cdd:PRK09452 13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-----RH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 DESPLQHLArLAPQeleQKLRDYLgGFGFQGDKVSEE-------------------TRR---FSGGEKARLVLALIVWQR 448
Cdd:PRK09452 88 VNTVFQSYA-LFPH---MTVFENV-AFGLRMQKTPAAeitprvmealrmvqleefaQRKphqLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 449 PNLLLLDEPTNHLDLDMRQALTEAL--------IDFegalVVVSHDRHLIRSTTDDLYLVHDGKVE 506
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELkalqrklgITF----VFVTHDQEEALTMSDRIVVMRDGRIE 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
322-505 |
5.83e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.49 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 322 YGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYfAQHQLEFLRAD-----ESPLQ 396
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLDY-SKRGLLALRQQvatvfQDPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 397 HL---------------ARLAPQELEQKLRDYLGGFGFQGDKvSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
Cdd:PRK13638 89 QIfytdidsdiafslrnLGVPEAEITRRVDEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490290321 462 DLDMRQ---ALTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK13638 168 DPAGRTqmiAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-227 |
6.80e-11 |
|
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: 62.55 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwQLAWVnqetpalpqPAIDYVIDGD- 88
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--RVSSL---------LGLGGGFNPEl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 89 --REYRQLEAALQqanerndGHAIATVHGKLDAIdawtirsraasllhgLGFS--NEQLERPVSDFSGGWRMRLNLAQAL 164
Cdd:cd03220 100 tgRENIYLNGRLL-------GLSRKEIDEKIDEI---------------IEFSelGDFIDLPVKTYSSGMKARLAFAIAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 165 ICRSDLLLLDEPT----NHLDLDAVIWLEKWLKGyTGTLILISHDRDFLDPIVDKIIHIEQQTMFEY 227
Cdd:cd03220 158 ALEPDILLIDEVLavgdAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
7-185 |
6.97e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqlawvNQETPALPqPAIDYVID 86
Cdd:PRK13539 8 LACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG------DIDDPDVA-EACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 87 GD--------REYRQLEAALQQANERNDGHAIATVhgKLDAIdawtirsraasllhglgfsneqLERPVSDFSGGWRMRL 158
Cdd:PRK13539 81 RNamkpaltvAENLEFWAAFLGGEELDIAAALEAV--GLAPL----------------------AHLPFGYLSAGQKRRV 136
|
170 180
....*....|....*....|....*..
gi 490290321 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 ... |
2-181 |
7.85e-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: 62.20 E-value: 7.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLL-----KNEISADGGSMTFPGnwQLAWVNQETP-A 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDG--KDIYDLDVDVlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 76 LPqpaidyvidgdreyRQLEAALQQAN------ERNdghaIA---TVHGKLDAIDawtIRSRAASLLHGLGFSNEQLERP 146
Cdd:cd03260 79 LR--------------RRVGMVFQKPNpfpgsiYDN----VAyglRLHGIKLKEE---LDERVEEALRKAALWDEVKDRL 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 490290321 147 -VSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:cd03260 138 hALGLSGGQQQRLCLARALANEPEVLLLDEPTSALD 173
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
337-496 |
1.19e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 60.08 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 337 PGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIglakgiklgyfaqhqleflradesplqhlARLAPQELEQKLRDYLGG 416
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-----------------------------IYIDGEDILEEVLDQLLL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 417 FGFQGDKVSeetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLIRSTTDD 496
Cdd:smart00382 52 IIVGGKKAS-----GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDE 126
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
323-505 |
1.23e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 62.51 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 323 GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYFAQHQ------LEFLRADE---S 393
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV-LIRGEPITKENIREvrkfvgLVFQNPDDqifS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 394 PL--QHLA------RLAPQELEQKLRDYLGGFGFQgDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
Cdd:PRK13652 94 PTveQDIAfgpinlGLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490290321 466 RQALTEALIDFE---GALVVVS-HDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK13652 173 VKELIDFLNDLPetyGMTVIFStHQLDLVPEMADYIYVMDKGRI 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
313-506 |
1.31e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.18 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL---------AKGIKLGYFAQH 383
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtdvsrlhARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 384 Q---------------LEFLRADESP-----------------LQHLARLAPQELeqklrdylggfgfqgdkvseetrrf 431
Cdd:PRK10851 83 YalfrhmtvfdniafgLTVLPRRERPnaaaikakvtqllemvqLAHLADRYPAQL------------------------- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 432 SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLIRSTTDDLYLVHDGKVE 506
Cdd:PRK10851 138 SGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkftsVFVTHDQEEAMEVADRVVVMSQGNIE 216
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
330-505 |
1.42e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.11 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 330 SIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGY----FAQHQLEFLRADES------------ 393
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL-LIDDHPLHFgdysYRSQRIRMIFQDPStslnprqrisqi 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 394 ---PLQHLARLAPQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470
Cdd:PRK15112 110 ldfPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 490290321 471 EALIDFEG----ALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK15112 190 NLMLELQEkqgiSYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
311-505 |
1.47e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.97 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGE--LQPVSGEIgLAKGI-----------KL 377
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDI-LFKGEsildlepeeraHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 378 GYFA--QHQLE--------FLRA---DESPLQHLARLAPQELEQKLRDYLGGFG----FQGDKVSEEtrrFSGGEKAR-- 438
Cdd:CHL00131 85 GIFLafQYPIEipgvsnadFLRLaynSKRKFQGLPELDPLEFLEIINEKLKLVGmdpsFLSRNVNEG---FSGGEKKRne 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 439 -LVLALIvwqRPNLLLLDEPTNHLDLDMRQALTEA---LIDFEGALVVVSHDRHLIRSTTDDlyLVH---DGKV 505
Cdd:CHL00131 162 iLQMALL---DSELAILDETDSGLDIDALKIIAEGinkLMTSENSIILITHYQRLLDYIKPD--YVHvmqNGKI 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-219 |
1.49e-10 |
|
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: 61.00 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLkneisadggsMTFPgnwqlawvnqetpalpqpaiDY-VI 85
Cdd:cd03217 6 LHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI----------MGHP--------------------KYeVT 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 86 DGDREYrqleaalqqanernDGHAIatvhgkLDAidawTIRSRAASLLhGLGF---------SNEQLERPVSD-FSGGWR 155
Cdd:cd03217 56 EGEILF--------------KGEDI------TDL----PPEERARLGI-FLAFqyppeipgvKNADFLRYVNEgFSGGEK 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 156 MRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEK---WLKGYTGTLILISHDRDFLDPIVDKIIHI 219
Cdd:cd03217 111 KRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEvinKLREEGKSVLIITHYQRLLDYIKPDRVHV 177
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-221 |
1.69e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 61.64 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTfpgnwqlawVNQETPALpqpaI 81
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE---------VNGRVSAL----L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 82 DY--VIDGD---REYRQLEAALQqanerndGHAIATVHGKLDAIDAWTirsraasllhGLGfsnEQLERPVSDFSGGWRM 156
Cdd:COG1134 94 ELgaGFHPEltgRENIYLNGRLL-------GLSRKEIDEKFDEIVEFA----------ELG---DFIDQPVKTYSSGMRA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 157 RLNLAQALICRSDLLLLDEptnhldldaviWL----------------EKWLKGytGTLILISHDRDFLDPIVDKIIHIE 220
Cdd:COG1134 154 RLAFAVATAVDPDILLVDE-----------VLavgdaafqkkclarirELRESG--RTVIFVSHSMGAVRRLCDRAIWLE 220
|
.
gi 490290321 221 Q 221
Cdd:COG1134 221 K 221
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
303-485 |
1.72e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.02 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 303 RQPESLPnPLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL-AKGIKLGYFA 381
Cdd:PRK13543 3 EPLHTAP-PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATRGDRS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 382 QH-----QLEFLRADESPLQHLARLA------PQELEQKLRDYLGGFGFQGDKVseetRRFSGGEKARLVLALIvWQRPN 450
Cdd:PRK13543 82 RFmaylgHLPGLKADLSTLENLHFLCglhgrrAKQMPGSALAIVGLAGYEDTLV----RQLSAGQKKRLALARL-WLSPA 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 490290321 451 -LLLLDEPTNHLDLD---MRQALTEALIDFEGALVVVSH 485
Cdd:PRK13543 157 pLWLLDEPYANLDLEgitLVNRMISAHLRGGGAALVTTH 195
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-221 |
1.92e-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: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG---------NWQLAWVNQE 72
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 73 TPALPQPAI-DYVIDGDREyrqleaalQQANERNDghaiatvhgkldaidAWTIRSRAASLLHGLGFSNEQlERPVSDFS 151
Cdd:cd03296 83 YALFRHMTVfDNVAFGLRV--------KPRSERPP---------------EAEIRAKVHELLKLVQLDWLA-DRYPAQLS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 152 GGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTG----TLILISHDRDFLDPIVDKII-----HIEQ 221
Cdd:cd03296 139 GGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelhvTTVFVTHDQEEALEVADRVVvmnkgRIEQ 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-181 |
2.06e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 61.80 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqlawvnqetpALPQPAIDyvidgdr 89
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV-----------PVTGPGAD------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 eyR----QLEAALQQANERnDGHAIATvhgKLDAIDAWTIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALI 165
Cdd:COG4525 78 --RgvvfQKDALLPWLNVL-DNVAFGL---RLRGVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALA 150
|
170
....*....|....*.
gi 490290321 166 CRSDLLLLDEPTNHLD 181
Cdd:COG4525 151 ADPRFLLMDEPFGALD 166
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
337-486 |
2.07e-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: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 337 PGSRIGLLGRNGAGKSTLIKLLAGELQPVSGE----------IGLAKGIKL-GYFAQHQLEFLRADESPlQHLARLaPQE 405
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeiLDEFRGSELqNYFTKLLEGDVKVIVKP-QYVDLI-PKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 406 LEQKLRDYL------GGFGFQGDK------VSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLdmRQALTEA- 472
Cdd:cd03236 103 VKGKVGELLkkkderGKLDELVDQlelrhvLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI--KQRLNAAr 180
|
170
....*....|....*...
gi 490290321 473 ----LIDFEGALVVVSHD 486
Cdd:cd03236 181 lireLAEDDNYVLVVEHD 198
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-216 |
2.08e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.95 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwQLAWVNQETPALPQPA 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK-PLDYSKRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 IDYVIDGDRE--YRQLEAALQqANERNDGHAIATVHGKLDaidawtirsRAASLLHGLGFSNEqlerPVSDFSGGWRMRL 158
Cdd:PRK13638 80 ATVFQDPEQQifYTDIDSDIA-FSLRNLGVPEAEITRRVD---------EALTLVDAQHFRHQ----PIQCLSHGQKKRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 159 NLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKI 216
Cdd:PRK13638 146 AIAGALVLQARYLLLDEPTAGLDpagRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAV 206
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
312-471 |
2.10e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.93 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGERI-ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYFAQHQ------ 384
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV-LVSGIDTGDFSKLQgirklv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 385 --------LEFL-RADESPL----QHLArLAPQELEQKLRDYLGGFGFQGDKvSEETRRFSGGEKARLVLALIVWQRPNL 451
Cdd:PRK13644 80 givfqnpeTQFVgRTVEEDLafgpENLC-LPPIEIRKRVDRALAEIGLEKYR-HRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180
....*....|....*....|
gi 490290321 452 LLLDEPTNHLDLDMRQALTE 471
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLE 177
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-485 |
2.24e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 5 SSLQIRRGVRVLLDNATA-----TINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMT--FPGNWQLAWVNQetpalp 77
Cdd:PRK10938 2 SSLQISQGTFRLSDTKTLqlpslTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQsqFSHITRLSFEQL------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 78 QPAIDyvidgdREYRQLEAALQQANERNDGHAIATVhgKLDAIDAwtiRSRAASLLHGLGFSNeQLERPVSDFSGGWRMR 157
Cdd:PRK10938 76 QKLVS------DEWQRNNTDMLSPGEDDTGRTTAEI--IQDEVKD---PARCEQLAQQFGITA-LLDRRFKYLSTGETRK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWL-----KGYTGTLILISHDR--DFldpivdkiihieqqtmfeytgn 230
Cdd:PRK10938 144 TLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLaslhqSGITLVLVLNRFDEipDF---------------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 231 yssfeVQRATRLAQQQAMYESQQQRVahlqsyidrfrakatkakQAQSRIKMLERMELIAPAHVDNPFHFSFRQPESLPN 310
Cdd:PRK10938 202 -----VQFAGVLADCTLAETGEREEI------------------LQQALVAQLAHSEQLEGVQLPEPDEPSARHALPANE 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGEL-QPVSGEI---GLAKG-------IK--L 377
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpQGYSNDLtlfGRRRGsgetiwdIKkhI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 378 GYFA-QHQLEFlRADESPLQ----------HLARLAPQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKaRLVL---AL 443
Cdd:PRK10938 339 GYVSsSLHLDY-RVSTSVRNvilsgffdsiGIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQ-RLALivrAL 416
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 490290321 444 IvwQRPNLLLLDEPTNHLDLDMRQaLTEALIDF-----EGALVVVSH 485
Cdd:PRK10938 417 V--KHPTLLILDEPLQGLDPLNRQ-LVRRFVDVlisegETQLLFVSH 460
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-282 |
2.37e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.59 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLkneisadgGSMTFP--GNWQLAWVNQETpalpqpaidyvIDGDreyrql 94
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNIL--------GCLDKPtsGTYRVAGQDVAT-----------LDAD------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 95 eaALQQANERNDG----------HAIATVHGKLDAIDAWTIRS----RAASLLHGLGFSnEQLERPVSDFSGGWRMRLNL 160
Cdd:PRK10535 79 --ALAQLRREHFGfifqryhllsHLTAAQNVEVPAVYAGLERKqrllRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 161 AQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKGYTGTLILISHdrdflDPIV----DKIIHIEQQTMFEYTGNYSS 233
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDShsgEEVMAILHQLRDRGHTVIIVTH-----DPQVaaqaERVIEIRDGEIVRNPPAQEK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490290321 234 FEVQRATrlaqqqamyESQQQRVAHLQSYIDRFRAKATKAKQAQSRIKM 282
Cdd:PRK10535 231 VNVAGGT---------EPVVNTASGWRQFVSGFREALTMAWRAMAANKM 270
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-458 |
2.38e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.11 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlAWVNQETPAlpqpaidyvidgdrey 91
Cdd:COG1129 16 GVKAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG----EPVRFRSPR---------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 92 rqleAALQqanerndgHAIATVH---------------------GKLDAIDAWTIRSRAASLLHGLGFsNEQLERPVSDF 150
Cdd:COG1129 75 ----DAQA--------AGIAIIHqelnlvpnlsvaeniflgrepRRGGLIDWRAMRRRARELLARLGL-DIDPDTPVGDL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWL----EKwLKGYTGTLILISHdrdFLDpivdkiihieqqtmfe 226
Cdd:COG1129 142 SVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLfriiRR-LKAQGVAIIYISH---RLD---------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 227 ytgnyssfEVQratRLAqqqamyesqqQRVAHLQ--SYIDRFRAKATkakqaqSRIKMLERMeliAPAHVDNPFHfsfRQ 304
Cdd:COG1129 202 --------EVF---EIA----------DRVTVLRdgRLVGTGPVAEL------TEDELVRLM---VGRELEDLFP---KR 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 305 PESLPNPLLKMEKVSAGYGeriiLDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI--------------G 370
Cdd:COG1129 249 AAAPGEVVLEVEGLSVGGV----VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIrldgkpvrirsprdA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 371 LAKGI--------KLGYFAQHQLeflrADESPLQHLARLA------PQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEK 436
Cdd:COG1129 325 IRAGIayvpedrkGEGLVLDLSI----RENITLASLDRLSrgglldRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQ 400
|
490 500
....*....|....*....|....
gi 490290321 437 ARLVLA--LIvwQRPNLLLLDEPT 458
Cdd:COG1129 401 QKVVLAkwLA--TDPKVLILDEPT 422
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-253 |
2.45e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.42 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 18 DNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGsmtfpgnwQLAWVNQETPALpqpaidyvidGDREYRQLEAA 97
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDG--------EVAWLGKDLLGM----------KDDEWRAVRSD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 98 LQ--------QANER-NDGHAIA----TVHGKLDAIDawtIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQAL 164
Cdd:PRK15079 100 IQmifqdplaSLNPRmTIGEIIAeplrTYHPKLSRQE---VKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 165 ICRSDLLLLDEPTNHLDLD---AVIWLEKWLKGYTG-TLILISHDRDfldpiVDKiiHIEQQTMFEYTGNyssfevqrAT 240
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSiqaQVVNLLQQLQREMGlSLIFIAHDLA-----VVK--HISDRVLVMYLGH--------AV 241
|
250
....*....|...
gi 490290321 241 RLAQQQAMYESQQ 253
Cdd:PRK15079 242 ELGTYDEVYHNPL 254
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
313-504 |
2.47e-10 |
|
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: 60.56 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGER-----IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIklGYFAQhqlef 387
Cdd:cd03250 1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--AYVSQ----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 388 lradESPLQH---------LARLAPQELEQKLR--------DYLGGfgfqGDK--VSEETRRFSGGEKARLVLALIVWQR 448
Cdd:cd03250 74 ----EPWIQNgtirenilfGKPFDEERYEKVIKacalepdlEILPD----GDLteIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490290321 449 PNLLLLDEPTNHLDLDMRQALTEALIdfEGAL------VVVSHDRHLIRStTDDLYLVHDGK 504
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFENCI--LGLLlnnktrILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
317-514 |
2.61e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 61.26 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 317 KVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL-------AGEL----QPVSG------EIGLAKGIklgY 379
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLivdgLKVNDpkvderLIRQEAGM---V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 380 FAQHQLeF--LRADES----PLqHLARLAPQELEQKLRDYLGGFGFqGDKVSEETRRFSGGEKARLVLALIVWQRPNLLL 453
Cdd:PRK09493 83 FQQFYL-FphLTALENvmfgPL-RVRGASKEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 454 LDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLIRSTTDDLYLVHDGKVEPfDGDLED 514
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLaeEGmTMVIVTHEIGFAEKVASRLIFIDKGRIAE-DGDPQV 222
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
17-219 |
2.70e-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: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLL----KNEISadGGSMTFPGnwqlawvnQETPALPqpaidyvIDgDREYR 92
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghpSYEVT--SGTILFKG--------QDLLELE-------PD-ERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 93 QLEAALQQANE----------RNDGHAIATVHGKlDAIDAWTIRSRAASLLHGLGFSNEQLERPVSD-FSGGWRMRLNLA 161
Cdd:TIGR01978 78 GLFLAFQYPEEipgvsnleflRSALNARRSARGE-EPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEIL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490290321 162 QALICRSDLLLLDEPTNHLDLDAVI----WLEKWlKGYTGTLILISHDRDFLDPIVDKIIHI 219
Cdd:TIGR01978 157 QMALLEPKLAILDEIDSGLDIDALKivaeGINRL-REPDRSFLIITHYQRLLNYIKPDYVHV 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
306-462 |
2.85e-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: 60.35 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 306 ESLPNPLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQP---VSGEIgLAKGIKLGYFA- 381
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDI-HYNGIPYKEFAe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 382 --QHQLEFLRADESplqHLARLAPQE-LEQKLRdylggfgFQGDKVSeetRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
Cdd:cd03233 80 kyPGEIIYVSEEDV---HFPTLTVREtLDFALR-------CKGNEFV---RGISGGERKRVSIAEALVSRASVLCWDNST 146
|
....
gi 490290321 459 NHLD 462
Cdd:cd03233 147 RGLD 150
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
326-504 |
3.11e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 63.23 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLaGELQPVSGeiGL----AKGiKLGYFAQH---QLEFLRAD----ESP 394
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYG--GRltkpAKG-KLFYVPQRpymTLGTLRDQiiypDSS 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 395 LQHLAR-LAPQELEQ-----KLRDYL---GGFgfqgDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
Cdd:TIGR00954 542 EDMKRRgLSDKDLEQildnvQLTHILereGGW----SAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
|
170 180 190
....*....|....*....|....*....|....*....
gi 490290321 466 RQALTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGK 504
Cdd:TIGR00954 618 EGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGG 656
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
312-485 |
3.13e-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: 63.49 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGERIIlDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLA-KGI---------KLGYFA 381
Cdd:TIGR01257 1940 LNELTKVYSGTSSPAV-DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAgKSIltnisdvhqNMGYCP 2018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 382 QHQ-LEFLRADESPLQHLARL--APQELEQKLRDY---LGGFGFQGDKVSEEtrrFSGGEKARLVLALIVWQRPNLLLLD 455
Cdd:TIGR01257 2019 QFDaIDDLLTGREHLYLYARLrgVPAEEIEKVANWsiqSLGLSLYADRLAGT---YSGGNKRKLSTAIALIGCPPLVLLD 2095
|
170 180 190
....*....|....*....|....*....|...
gi 490290321 456 EPTNHLDLDMRQALTEALIDF---EGALVVVSH 485
Cdd:TIGR01257 2096 EPTTGMDPQARRMLWNTIVSIireGRAVVLTSH 2128
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
313-506 |
3.53e-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: 60.35 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIglakgiklgYFAQHQLEFLRADE 392
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI---------YIGGRDVTDLPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 393 -----------------------SPLQhLARLAPQELEQKLRDYLGGFGFqGDKVSEETRRFSGGEKARLVLALIVWQRP 449
Cdd:cd03301 72 rdiamvfqnyalyphmtvydniaFGLK-LRKVPKDEIDERVREVAELLQI-EHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 450 NLLLLDEPTNHLD----LDMRQALTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKVE 506
Cdd:cd03301 150 KVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-221 |
4.23e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.49 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlAWVNQetpalpqPA 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG----LKVND-------PK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 IDyvidgDREYRQlEAAL--QQANERNDGHAIATV---------HGKLDAidawtiRSRAASLLHGLGFSNEQLERPvSD 149
Cdd:PRK09493 70 VD-----ERLIRQ-EAGMvfQQFYLFPHLTALENVmfgplrvrgASKEEA------EKQARELLAKVGLAERAHHYP-SE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPElrhEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDK 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
306-524 |
4.60e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.38 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 306 ESLPNPLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL----------AKGI 375
Cdd:PRK15439 5 DTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIggnpcarltpAKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 376 KLGYFAQHQLEFLRADESPLQH-LARLA-PQELEQKLRDYLGGFGFQGD-KVSEETRRFSGGEKARLVLALIvwQRPNLL 452
Cdd:PRK15439 85 QLGIYLVPQEPLLFPNLSVKENiLFGLPkRQASMQKMKQLLAALGCQLDlDSSAGSLEVADRQIVEILRGLM--RDSRIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 453 LLDEPTNHLDLDMRQAL---TEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKVePFDGDLEDY-------------- 515
Cdd:PRK15439 163 ILDEPTASLTPAETERLfsrIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI-ALSGKTADLstddiiqaitpaar 241
|
....*....
gi 490290321 516 QQWLSDSQK 524
Cdd:PRK15439 242 EKSLSASQK 250
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-215 |
4.94e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.13 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 9 IRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFP-GNwqlAWVNQETPAlpqpaidyvIDG 87
Cdd:TIGR03269 292 VDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGD---EWVDMTKPG---------PDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 88 DREYRQLEAALQQaneRNDGHAIATVHGKL-DAI-----DAWTIRsRAASLLHGLGFSNEQ----LERPVSDFSGGWRMR 157
Cdd:TIGR03269 360 RGRAKRYIGILHQ---EYDLYPHRTVLDNLtEAIglelpDELARM-KAVITLKMVGFDEEKaeeiLDKYPDELSEGERHR 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 158 LNLAQALICRSDLLLLDEPTNHLD-----------LDAVIWLEKwlkgytgTLILISHDRDFLDPIVDK 215
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDpitkvdvthsiLKAREEMEQ-------TFIIVSHDMDFVLDVCDR 497
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-231 |
5.24e-10 |
|
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: 62.45 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGV-RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG----NWQLAWVNQETPAL 76
Cdd:TIGR01193 474 IVINDVSYSYGYgSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 77 PQPAidYVIDGDreyrQLEAALQQANERndghaiATVHGKLDAIDAWTIRSRAASLLHGLGFSneqLERPVSDFSGGWRM 156
Cdd:TIGR01193 554 PQEP--YIFSGS----ILENLLLGAKEN------VSQDEIWAACEIAEIKDDIENMPLGYQTE---LSEEGSSISGGQKQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 157 RLNLAQALICRSDLLLLDEPTNHLDL--DAVIwLEKWLKGYTGTLILISHdRDFLDPIVDKIIHIEQQTMFEyTGNY 231
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDTitEKKI-VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIE-QGSH 692
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-227 |
6.71e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLL-------KNEISADGGSMTFPGNWQLAWVNQ---ETPAL 76
Cdd:PLN03232 1242 LRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALfriveleKGRIMIDDCDVAKFGLTDLRRVLSiipQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 77 PQPAIDYVIDGDREYRqlEAALQQANERndghaiatVHGKlDAIDAwtirsraasllHGLGFSNEQLERPvSDFSGGWRM 156
Cdd:PLN03232 1322 FSGTVRFNIDPFSEHN--DADLWEALER--------AHIK-DVIDR-----------NPFGLDAEVSEGG-ENFSVGQRQ 1378
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 157 RLNLAQALICRSDLLLLDEPTNHLDL--DAVIWLEKWLKGYTGTLILISHDrdfLDPIV--DKIIHIEQQTMFEY 227
Cdd:PLN03232 1379 LLSLARALLRRSKILVLDEATASVDVrtDSLIQRTIREEFKSCTMLVIAHR---LNTIIdcDKILVLSSGQVLEY 1450
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-187 |
7.99e-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: 62.34 E-value: 7.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGN---WQLAWVNQETPALPQ-PAIDYVIDGdREYR 92
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsilTNISDVHQNMGYCPQfDAIDDLLTG-REHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 93 QLEAALQQANERndghaiatvhgKLDAIDAWTIRSRAASLLhglgfsneqLERPVSDFSGGWRMRLNLAQALICRSDLLL 172
Cdd:TIGR01257 2034 YLYARLRGVPAE-----------EIEKVANWSIQSLGLSLY---------ADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170
....*....|....*..
gi 490290321 173 LDEPTNHLDLDA--VIW 187
Cdd:TIGR01257 2094 LDEPTTGMDPQArrMLW 2110
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-505 |
8.24e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.06 E-value: 8.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 324 ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKgiKLGYFAQHQLEF----LRAD-------E 392
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKDIFQIdaikLRKEvgmvfqqP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 393 SPLQHLA-----------------RLAPQELEQKLRDyLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
Cdd:PRK14246 100 NPFPHLSiydniayplkshgikekREIKKIVEECLRK-VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490290321 456 EPTNHLDLDMRQALTEALIDF--EGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELknEIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-207 |
9.69e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 60.50 E-value: 9.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFpgnwqlawvnqetpalpqpa 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL-------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 idyvidGDREYRQLEAalqqaNERNdghaIATV--------H---------G-KLDAIDAWTIRSRAASLLH--GLGfsn 140
Cdd:COG3842 65 ------DGRDVTGLPP-----EKRN----VGMVfqdyalfpHltvaenvafGlRMRGVPKAEIRARVAELLElvGLE--- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 141 EQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGY---TG-TLILISHDRD 207
Cdd:COG3842 127 GLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqreLGiTFIYVTHDQE 197
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
323-462 |
9.78e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 58.66 E-value: 9.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 323 GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGE---------------------IGLAKGIKLGYFA 381
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRvllnggpldfqrdsiargllyLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 382 QHQLEFLRADESPLQHLARLApqeleqklRDYLGGFGfqgdkvSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
Cdd:cd03231 91 LENLRFWHADHSDEQVEEALA--------RVGLNGFE------DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
.
gi 490290321 462 D 462
Cdd:cd03231 157 D 157
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
323-462 |
9.89e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.66 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 323 GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLG-----YFAQ-----HQL---EFLR 389
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV-LWQGEPIRrqrdeYHQDllylgHQPgikTELT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 390 ADESpLQHLARLAPQELEQKLRDYLGGFGFQGdkvSEE--TRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:PRK13538 91 ALEN-LRFYQRLHGPGDDEALWEALAQVGLAG---FEDvpVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
310-462 |
1.01e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 59.62 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 310 NPLLKMEKVSAGYG--ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLaKGIKLgyfAQHQLEF 387
Cdd:PRK13632 5 SVMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI-DGITI---SKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 388 LRAD-----ESP----------------LQHlARLAPQELEQKLRDYLGGFGFQgDKVSEETRRFSGGEKARLVLALIVW 446
Cdd:PRK13632 81 IRKKigiifQNPdnqfigatveddiafgLEN-KKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLA 158
|
170
....*....|....*.
gi 490290321 447 QRPNLLLLDEPTNHLD 462
Cdd:PRK13632 159 LNPEIIIFDESTSMLD 174
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
23-217 |
1.08e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.51 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 23 TINPGQKVGLVGKNGCGKS----TLLSLL-KNEISadGGSMTFPGN-------WQLAWVNQETPAL----PQPAID-YVI 85
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSqtafALMGLLaANGRI--GGSATFNGReilnlpeKELNKLRAEQISMifqdPMTSLNpYMR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 86 DGDreyrQLEAALQQANERNDGHAIATVHGKLDAIDAWTIRSRAASLLHglgfsneqlerpvsDFSGGWRMRLNLAQALI 165
Cdd:PRK09473 116 VGE----QLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPH--------------EFSGGMRQRVMIAMALL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 166 CRSDLLLLDEPTNHLDLDA---VIWLEKWLKGYTGT-LILISHDRDFLDPIVDKII 217
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVqaqIMTLLNELKREFNTaIIMITHDLGVVAGICDKVL 233
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
316-473 |
1.16e-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: 59.17 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 316 EKVSAGYG--ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYFAQHQLE------- 386
Cdd:cd03251 4 KNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRI-LIDGHDVRDYTLASLRrqiglvs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 387 ---FL--------------RADESPLQHLARLA-PQELEQKLRDylggfGFQgDKVSEETRRFSGGEKARLVLALIVWQR 448
Cdd:cd03251 83 qdvFLfndtvaeniaygrpGATREEVEEAARAAnAHEFIMELPE-----GYD-TVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180
....*....|....*....|....*
gi 490290321 449 PNLLLLDEPTNHLDLDMRQALTEAL 473
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAAL 181
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-182 |
1.19e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.46 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADG--GSMTFPGNWQLawvNQEtpalPQ 78
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGapRGARVTGDVTL---NGE----PL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 79 PAIDyvidgDREYRQLEAALQQANER----------------NDGHAIATVHGKLDAIDAWTIRSRAASLlhglgfsneq 142
Cdd:PRK13547 74 AAID-----APRLARLRAVLPQAAQPafafsareivllgrypHARRAGALTHRDGEIAWQALALAGATAL---------- 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490290321 143 LERPVSDFSGGWRMRLNLAQAL---------ICRSDLLLLDEPTNHLDL 182
Cdd:PRK13547 139 VGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-221 |
1.26e-09 |
|
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: 58.70 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlAWVNQETPALpqpai 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDG----LKLTDDKKNI----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 82 dyvidgdREYRQlEAAL--QQAN-------ERNDGHAIATVHGKlDAIDAwtiRSRAASLLHGLGFSNEQLERPvSDFSG 152
Cdd:cd03262 72 -------NELRQ-KVGMvfQQFNlfphltvLENITLAPIKVKGM-SKAEA---EERALELLEKVGLADKADAYP-AQLSG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 153 GWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLEKwlKGYtgTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03262 139 GQQQRVAIARALAMNPKVMLFDEPTSALDpelvgevLDVMKDLAE--EGM--TMVVVTHEMGFAREVADRVIFMDD 210
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
309-505 |
1.43e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.42 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 309 PNPLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGyfAQHQLEFL 388
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQPLE--SWSSKAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 389 RadesplqHLARLaPQELEQ----KLRDY-----------LGGFGFQGDKVSEE--------------TRRFSGGEKARL 439
Cdd:PRK10575 85 R-------KVAYL-PQQLPAaegmTVRELvaigrypwhgaLGRFGAADREKVEEaislvglkplahrlVDSLSGGERQRA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 440 VLALIVWQRPNLLLLDEPTNHLDLDMR---QALTEALIDFEGALVV-VSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQvdvLALVHRLSQERGLTVIaVLHDINMAARYCDYLVALRGGEM 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-205 |
1.59e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.87 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 6 SLQIRRGV-------RVLLDNATATINPGQKVGLVGKNGCGKST----LLSLLKNEisadgGSMTFPGNWQLAWVNQETp 74
Cdd:PRK15134 284 AFPIRKGIlkrtvdhNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWFDGQPLHNLNRRQL- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 75 aLPQpaidyvidgdreYRQLEAALQQANER-----NDGHAIA---TVHGKldAIDAWTIRSRAASLLHGLGFSNEQLERP 146
Cdd:PRK15134 358 -LPV------------RHRIQVVFQDPNSSlnprlNVLQIIEeglRVHQP--TLSAAQREQQVIAVMEEVGLDPETRHRY 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490290321 147 VSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD--LDAVI--WLEKWLKGYTGTLILISHD 205
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktVQAQIlaLLKSLQQKHQLAYLFISHD 485
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
333-485 |
1.68e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.44 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 333 LNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI--------------------------------------GLAKG 374
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdhtttppsrrpvsmlfqennlfshltvaqniglGLNPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 375 IKLGYFAQHQLEFLRADESPLQHLARLaPQELeqklrdylggfgfqgdkvseetrrfSGGEKARLVLA-LIVWQRPnLLL 453
Cdd:PRK10771 100 LKLNAAQREKLHAIARQMGIEDLLARL-PGQL-------------------------SGGQRQRVALArCLVREQP-ILL 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 490290321 454 LDEPTNHLDLDMRQA----LTEALIDFEGALVVVSH 485
Cdd:PRK10771 153 LDEPFSALDPALRQEmltlVSQVCQERQLTLLMVSH 188
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
312-504 |
1.73e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.61 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLQP---VSGEIGL------AKGIK----LG 378
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPhgtWDGEIYWsgsplkASNIRdterAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 379 YFAQHQLEFLRADESPLQHL----------ARLAPQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQR 448
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIflgneitlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 449 PNLLLLDEPTNHLDLDMRQALTEALIDFEG---ALVVVSHDRHLIRSTTDDLYLVHDGK 504
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
10-219 |
2.07e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.19 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPQpaidyvidgdR 89
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEG--------EDISTLKP----------E 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 EYR-QLEAALQQANERNDghaiaTVHGKLdaIDAWTIRSRA---ASLLHGL---GFSNEQLERPVSDFSGGWRMRLNLAQ 162
Cdd:PRK10247 78 IYRqQVSYCAQTPTLFGD-----TVYDNL--IFPWQIRNQQpdpAIFLDDLerfALPDTILTKNIAELSGGEKQRISLIR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 163 ALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTG----TLILISHDRDFLDPiVDKIIHI 219
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVReqniAVLWVTHDKDEINH-ADKVITL 210
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
324-462 |
2.10e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 58.56 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 324 ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGIKLGYFAQHQleflRAdesplQHLARL-- 401
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID-GKDVTKLPEYK----RA-----KYIGRVfq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 402 ------AP-------------------------QELEQKLRDYLGGFGfQG--DKVSEETRRFSGGEkaRLVLALI--VW 446
Cdd:COG1101 88 dpmmgtAPsmtieenlalayrrgkrrglrrgltKKRRELFRELLATLG-LGleNRLDTKVGLLSGGQ--RQALSLLmaTL 164
|
170
....*....|....*.
gi 490290321 447 QRPNLLLLDEPTNHLD 462
Cdd:COG1101 165 TKPKLLLLDEHTAALD 180
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-205 |
2.14e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.29 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 16 LLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG---------------NWQLAWVNQETPALPqpa 80
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrNQKLGFIYQFHHLLP--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 idyvidgdrEYRQLEAAlqqanerndghAIATVHGKLDAIDAwtiRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNL 160
Cdd:PRK11629 101 ---------DFTALENV-----------AMPLLIGKKKPAEI---NSRALEMLAAVGLEHRANHRP-SELSGGERQRVAI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490290321 161 AQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKGYTGTLIL-ISHD 205
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTAFLvVTHD 205
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
298-506 |
2.22e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 60.51 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 298 FHFSFRQPeSLPNP----------LLKMEKVSAGYGER---IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQP 364
Cdd:TIGR00958 455 FEYLDRKP-NIPLTgtlaplnlegLIEFQDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQP 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 365 VSGEIgLAKGI------------KLGYFAQHQLEFLRADESPLQHLARLAPQE------LEQKLRDYLGGFGFQGDKVSE 426
Cdd:TIGR00958 534 TGGQV-LLDGVplvqydhhylhrQVALVGQEPVLFSGSVRENIAYGLTDTPDEeimaaaKAANAHDFIMEFPNGYDTEVG 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 427 ETRRF-SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:TIGR00958 613 EKGSQlSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVV 692
|
.
gi 490290321 506 E 506
Cdd:TIGR00958 693 E 693
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
308-555 |
2.28e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.91 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 308 LPNPLLKME----KVSAGY------GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGiKL 377
Cdd:PLN03130 603 LPNPPLEPGlpaiSIKNGYfswdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRG-TV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 378 GYFAQ-------------------HQLEFLRA-DESPLQHLARLAPqeleqklrdylggfGFQGDKVSEETRRFSGGEKA 437
Cdd:PLN03130 682 AYVPQvswifnatvrdnilfgspfDPERYERAiDVTALQHDLDLLP--------------GGDLTEIGERGVNISGGQKQ 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 438 RLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFE---GALVVVSHDRHLIrSTTDDLYLVHDGKVE---PFD-- 509
Cdd:PLN03130 748 RVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDElrgKTRVLVTNQLHFL-SQVDRIILVHEGMIKeegTYEel 826
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 510 --------------GDLEDYQQWLSDSQKQESQSGEAPKESGNSAQARKDQKRREAELRS 555
Cdd:PLN03130 827 snngplfqklmenaGKMEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKS 886
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
308-458 |
2.60e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.97 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 308 LPNPLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL-AKGIKLGYFAQHQLE 386
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFdGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 387 FLRADESPLQHLARLAPQE-------------LEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLL 453
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEEnlamggffaerdqFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
....*
gi 490290321 454 LDEPT 458
Cdd:PRK11614 161 LDEPS 165
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
315-505 |
2.75e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.60 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 315 MEKVSAGYG-----ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLA----------KGIK--- 376
Cdd:PRK13649 5 LQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtlitstsknKDIKqir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 377 -----LGYFAQHQLeflrADESPLQHLArLAPQ-------ELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALI 444
Cdd:PRK13649 85 kkvglVFQFPESQL----FEETVLKDVA-FGPQnfgvsqeEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 445 VWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA---LVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgmtIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
311-503 |
3.00e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLaKGI-----------KLGY 379
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI-NNInynkldhklaaQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 380 FAQHQlEFLRADE-SPLQHL--ARLAPQ-----------ELEQKLRDYLGGFGFQGDkVSEETRRFSGGEKARLVLALIV 445
Cdd:PRK09700 83 GIIYQ-ELSVIDElTVLENLyiGRHLTKkvcgvniidwrEMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 446 WQRPNLLLLDEPTNhldldmrqALTEALIDF----------EG-ALVVVSHDRHLIRSTTDDLYLVHDG 503
Cdd:PRK09700 161 MLDAKVIIMDEPTS--------SLTNKEVDYlflimnqlrkEGtAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-205 |
3.16e-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: 57.63 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPqpai 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG--------KDITNLP---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 82 dyvidgdreyrqleaalqqANERNdghaIATV--------HG----------KLDAIDAWTIRSRAASLLHGLGFSnEQL 143
Cdd:cd03300 69 -------------------PHKRP----VNTVfqnyalfpHLtvfeniafglRLKKLPKAEIKERVAEALDLVQLE-GYA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 144 ERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLE---KWLKGYTG-TLILISHD 205
Cdd:cd03300 125 NRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQlelKRLQKELGiTFVFVTHD 190
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-182 |
3.45e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 57.79 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTfpgnwqlawvnqetpalpqpa 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVL--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 idyvIDG-------DREY-RQLeAALQQANerndgHAIA--TV------------HGKLDAIDaWTIRSRAASLLHGLGF 138
Cdd:COG4604 60 ----VDGldvattpSRELaKRL-AILRQEN-----HINSrlTVrelvafgrfpysKGRLTAED-REIIDEAIAYLDLEDL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490290321 139 SNEQLErpvsDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL 182
Cdd:COG4604 129 ADRYLD----ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
24-205 |
3.50e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.48 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 24 INPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwQLAWVNQETPA-LPQPAIDYVIDG--------DREYRQL 94
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQ-PLHQMDEEARAkLRAKHVGFVFQSfmliptlnALENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 95 EAALQQANERNDghaiatvhgkldaidawtiRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLD 174
Cdd:PRK10584 112 PALLRGESSRQS-------------------RNGAKALLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 490290321 175 EPTNHLD-------LDAVIWLEkwlKGYTGTLILISHD 205
Cdd:PRK10584 172 EPTGNLDrqtgdkiADLLFSLN---REHGTTLILVTHD 206
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
319-505 |
3.74e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.48 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 319 SAGYGERI--ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGIKLGYFAQHQLEFLRA------ 390
Cdd:PRK10584 15 SVGQGEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLV-GQPLHQMDEEARAKLRAkhvgfv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 -------------DESPLQHLAR-LAPQELEQKLRDYLGGFGFqGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDE 456
Cdd:PRK10584 94 fqsfmliptlnalENVELPALLRgESSRQSRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490290321 457 PTNHLDLDMRQALTEALI----DFEGALVVVSHDRHLIRSTTDDLYLVhDGKV 505
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFslnrEHGTTLILVTHDLQLAARCDRRLRLV-NGQL 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-205 |
3.80e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.64 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 21 TATINPGQKVGLVGKNGCGKSTLLSLL------KNEISADGGSM-TFPGNWQL---AWVNQE-TPALPQPAIDYVidgdr 89
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMagllpgSGSIQFAGQPLeAWSAAELArhrAYLSQQqTPPFAMPVFQYL----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 eyrqleaALQQAnernDGHAIATVHGKLDAIdawtirsraASLLhGLGfsnEQLERPVSDFSGGWRMRLNLAQALI---- 165
Cdd:PRK03695 91 -------TLHQP----DKTRTEAVASALNEV---------AEAL-GLD---DKLGRSVNQLSGGEWQRVRLAAVVLqvwp 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490290321 166 ---CRSDLLLLDEPTNHLDLDAVIWLEKWLK---GYTGTLILISHD 205
Cdd:PRK03695 147 dinPAGQLLLLDEPMNSLDVAQQAALDRLLSelcQQGIAVVMSSHD 192
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-226 |
4.77e-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: 57.24 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqetpalpQPAIDYVIDGDReyRQLEA 96
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG---------------HDVRDYTLASLR--RQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 97 ALQQANERNDGHAIATVHGKLDAIDAWTIrsRAASLLHGLGF---SNEQLERPVSD----FSGGWRMRLNLAQALICRSD 169
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVE--EAARAANAHEFimeLPEGYDTVIGErgvkLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 170 LLLLDEPTNHLDL-------DAviwLEKWLKGYTGtlILISHDrdfLDPI--VDKIIHIEQQTMFE 226
Cdd:cd03251 159 ILILDEATSALDTeserlvqAA---LERLMKNRTT--FVIAHR---LSTIenADRIVVLEDGKIVE 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
324-505 |
4.83e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.11 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 324 ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGI---------------KLGY---FAQHQL 385
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkplrkKVGIvfqFPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 386 eFlraDESPLQHLArLAPQ-------ELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
Cdd:PRK13634 99 -F---EETVEKDIC-FGPMnfgvseeDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490290321 459 NHLDLDMRQALTEALIDF--EGAL--VVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLhkEKGLttVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
328-514 |
5.16e-09 |
|
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: 58.57 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDsIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL--------AKGI-------KLGY-FAQHQL------ 385
Cdd:COG4148 16 LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdsARGIflpphrrRIGYvFQEARLfphlsv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 386 --------EFLRADESP-----------LQHLARLAPQELeqklrdylggfgfqgdkvseetrrfSGGEKARLVL--ALI 444
Cdd:COG4148 95 rgnllygrKRAPRAERRisfdevvellgIGHLLDRRPATL-------------------------SGGERQRVAIgrALL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 445 VwqRPNLLLLDEPTNHLDLDMRQALT---EALID-FEGALVVVSHDRHLIRSTTDDLYLVHDGKVEPFdGDLED 514
Cdd:COG4148 150 S--SPRLLLMDEPLAALDLARKAEILpylERLRDeLDIPILYVSHSLDEVARLADHVVLLEQGRVVAS-GPLAE 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
270-489 |
5.17e-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: 59.64 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 270 ATKAKQAQSRIKML-ERMEliAPAHVD--NPFHFSFRQPESLPNPLLK-MEKVSAGYGeRIILDSIKLNLVPGSRIGLLG 345
Cdd:TIGR01257 887 STREERALEKTEPLtEEME--DPEHPEgiNDSFFERELPGLVPGVCVKnLVKIFEPSG-RPAVDRLNITFYENQITAFLG 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 346 RNGAGKSTLIKLLAGELQPVSGEIGLA-KGIK---------LGYFAQHQLEF--LRADESPL--QHLARLAPQELEQKLR 411
Cdd:TIGR01257 964 HNGAGKTTTLSILTGLLPPTSGTVLVGgKDIEtnldavrqsLGMCPQHNILFhhLTVAEHILfyAQLKGRSWEEAQLEME 1043
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 412 DYLGGFGFQgDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHL 489
Cdd:TIGR01257 1044 AMLEDTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHM 1120
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-277 |
5.34e-09 |
|
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: 59.57 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 11 RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqetpalpqpAIDYVIdgdre 90
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-----------------SVAYVP----- 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 91 yrqleaalQQANERNDGHAIATVHGKLDAIDAWTIRSRAASLLHGL-----GFSNEQLERPVsDFSGGWRMRLNLAQALI 165
Cdd:TIGR00957 706 --------QQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLeilpsGDRTEIGEKGV-NLSGGQKQRVSLARAVY 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 166 CRSDLLLLDEPTNHLD-------LDAVIWLEKWLKGytGTLILISHDRDFLdPIVDKIIHIEQQTMFEyTGNYSSFeVQR 238
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDahvgkhiFEHVIGPEGVLKN--KTRILVTHGISYL-PQVDVIIVMSGGKISE-MGSYQEL-LQR 851
|
250 260 270
....*....|....*....|....*....|....*....
gi 490290321 239 ATRLAQQQAMYESQQQRVAHLQSYIDRFRAKATKAKQAQ 277
Cdd:TIGR00957 852 DGAFAEFLRTYAPDEQQGHLEDSWTALVSGEGKEAKLIE 890
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
310-505 |
5.34e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.19 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 310 NPLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI-------------------- 369
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvthrsiqqrdicmv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 370 --------GLAKGIKLGYfaqhqleflradesPLQHLARlAPQELEQKLRDY-----LGGFgfqGDKVSEEtrrFSGGEK 436
Cdd:PRK11432 84 fqsyalfpHMSLGENVGY--------------GLKMLGV-PKEERKQRVKEAlelvdLAGF---EDRYVDQ---ISGGQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490290321 437 ARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVV----VSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK11432 143 QRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNItslyVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
313-509 |
5.35e-09 |
|
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: 57.31 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGE-RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGI------------KLGY 379
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEI-FIDGEdireqdpvelrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 380 FAQ------H-----------QLEFL-------RADEspLQHLARLAPQELEQKLRDYLggfgfqgdkvseetrrfSGGE 435
Cdd:cd03295 80 VIQqiglfpHmtveenialvpKLLKWpkekireRADE--LLALVGLDPAEFADRYPHEL-----------------SGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 436 KARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLIRSTTDDLYLVHDGKVEPFD 509
Cdd:cd03295 141 QQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgktiVFVTHDIDEAFRLADRIAIMKNGEIVQVG 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
324-505 |
5.70e-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: 57.16 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 324 ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL-------------------------------A 372
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdgvdirdlnlrwlrsqiglvsqepvlfdgtiA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 373 KGIKLGYFAQHQLEFLRAdesplqhlARLAP-----QELEQKLRDYLGGFGFQgdkvseetrrFSGGEKARLVLALIVWQ 447
Cdd:cd03249 95 ENIRYGKPDATDEEVEEA--------AKKANihdfiMSLPDGYDTLVGERGSQ----------LSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 448 RPNLLLLDEPTNHLDLDMRQALTEALIDF-EG-ALVVVSHDRHLIRStTDDLYLVHDGKV 505
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAmKGrTTIVIAHRLSTIRN-ADLIAVLQNGQV 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
328-505 |
5.81e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.44 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGIKLGYFAQHQ------LEFLRADESPLQHLA-- 399
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVM-GREVNAENEKWvrskvgLVFQDPDDQVFSSTVwd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 400 ---------RLAPQELEQKLRDYLGGFGFQgDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470
Cdd:PRK13647 100 dvafgpvnmGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 490290321 471 EALIDF--EGALVVVS-HDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK13647 179 EILDRLhnQGKTVIVAtHDVDLAAEWADQVIVLKEGRV 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
315-509 |
5.89e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 57.71 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 315 MEKVSAGYGERI-----ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGEL-----QPVSGEIGLAKGIK-------- 376
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisetgQTIVGDYAIPANLKkikevkrl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 377 ------LGYFAQHQL--EFLRADES--PLqHLARlAPQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVW 446
Cdd:PRK13645 89 rkeiglVFQFPEYQLfqETIEKDIAfgPV-NLGE-NKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 447 QRPNLLLLDEPTNHLDLDMRQALTEALI----DFEGALVVVSHDRHLIRSTTDDLYLVHDGKV----EPFD 509
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFErlnkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVisigSPFE 237
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-221 |
6.81e-09 |
|
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: 56.82 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLL-------KNEISADGGSMTFPGNWQLawvnqetpalpqpaid 82
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInglerptSGSVLVDGTDLTLLSGKEL---------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 83 yvidgdREYRQ-LEAALQQAN---ERndghaiaTVHG------KLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSG 152
Cdd:cd03258 78 ------RKARRrIGMIFQHFNllsSR-------TVFEnvalplEIAGVPKAEIEERVLELLELVGLEDKADAYP-AQLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490290321 153 GWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKGYTG-TLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALDpetTQSILALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-220 |
8.31e-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: 56.08 E-value: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 4 FSSLQIRrGVRVLLDNATATINPGQKVgLVGKNGCGKSTLLSLLKNEISADGgSMTFPGNWQLAWVNQETPALPQPAIDY 83
Cdd:cd03240 1 IDKLSIR-NIRSFHERSEIEFFSPLTL-IVGQNGAGKTTIIEALKYALTGEL-PPNSKGGAHDPKLIREGEVRAQVKLAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 84 VIDGDREYrqleaalqqanerndghaiaTVHGKLDAIdawtirsRAASLLHGlGFSNEQLERPVSDFSGGWRM------R 157
Cdd:cd03240 78 ENANGKKY--------------------TITRSLAIL-------ENVIFCHQ-GESNWPLLDMRGRCSGGEKVlasliiR 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIW-----LEKWLKGYTGTLILISHDRDFLDPIvDKIIHIE 220
Cdd:cd03240 130 LALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDAA-DHIYRVE 196
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-221 |
9.39e-09 |
|
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: 55.96 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 23 TINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPqPAidyvidgdreYRQLEAALQQAN 102
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--------VDVTAAP-PA----------DRPVSMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 103 -------ERNDGhaIATVHG-KLDAIDawtiRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLD 174
Cdd:cd03298 81 lfahltvEQNVG--LGLSPGlKLTAED----RQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490290321 175 EPTNHLD-------LDAVIWLEKWLKgytGTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03298 154 EPFAALDpalraemLDLVLDLHAETK---MTVLMVTHQPEDAKRLAQRVVFLDN 204
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
303-487 |
1.02e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.05 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 303 RQPESLPNP-----LLKMEKVSAGY-GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI------- 369
Cdd:PRK13657 320 RDPPGAIDLgrvkgAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIlidgtdi 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 370 ------GLAKGIklGYFAQHQLEFLRADESPLQ-----------HLARLAPQELEQKLRDyLGGFGFQgdkVSEETRRFS 432
Cdd:PRK13657 400 rtvtraSLRRNI--AVVFQDAGLFNRSIEDNIRvgrpdatdeemRAAAERAQAHDFIERK-PDGYDTV---VGERGRQLS 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 433 GGEKARLVLALIVWQRPNLLLLDEPTNHLDldmrqALTEALIdfEGALVVVSHDR 487
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALD-----VETEAKV--KAALDELMKGR 521
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-217 |
1.20e-08 |
|
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: 56.26 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 23 TINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSmtfpgnwqlawvnqetPALPQPAIDYvidgdreyrqleaALQQAN 102
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGD----------------IEIELDTVSY-------------KPQYIK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 103 ERNDGHAIATVHGKLDaiDAWTIRSRAASLLHGLGFsnEQL-ERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:cd03237 72 ADYEGTVRDLLSSITK--DFYTHPYFKTEIAKPLQI--EQIlDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490290321 182 LDAVIWLEKWLKGYT----GTLILISHDRDFLDPIVDKII 217
Cdd:cd03237 148 VEQRLMASKVIRRFAenneKTAFVVEHDIIMIDYLADRLI 187
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
327-503 |
1.20e-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: 58.38 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKL---------GYFAQHQLEFLRADEspLQH 397
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFspqtswimpGTIKDNIIFGLSYDE--YRY 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 398 LARLAPQELEQKLRDYLggfgfQGDKV--SEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA--- 472
Cdd:TIGR01271 519 TSVIKACQLEEDIALFP-----EKDKTvlGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESclc 593
|
170 180 190
....*....|....*....|....*....|..
gi 490290321 473 -LIDFEGALVVVSHDRHLIRSttDDLYLVHDG 503
Cdd:TIGR01271 594 kLMSNKTRILVTSKLEHLKKA--DKILLLHEG 623
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-207 |
1.26e-08 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 57.08 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 6 SLQI-----RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwQLAWVNQETPA----- 75
Cdd:COG1118 2 SIEVrniskRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--RDLFTNLPPRErrvgf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 76 LPQpaiDY-------VID----GDREYRQLEAALQqanerndghaiATVHGKLDAIDawtirsraaslLHGLGfsneqlE 144
Cdd:COG1118 80 VFQ---HYalfphmtVAEniafGLRVRPPSKAEIR-----------ARVEELLELVQ-----------LEGLA------D 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 145 RPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDlDAVIW-LEKWL----KGYTGTLILISHDRD 207
Cdd:COG1118 129 RYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALD-AKVRKeLRRWLrrlhDELGGTTVFVTHDQE 195
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-204 |
1.28e-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: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqetpalpQPAIDYvidgDR 89
Cdd:cd03248 23 TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG---------------KPISQY----EH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 EY--RQLEAALQQ----ANERNDGHAIATVHGKLDAIDAWTIRSRAASLLHGL--GFSNEQLERPvSDFSGGWRMRLNLA 161
Cdd:cd03248 84 KYlhSKVSLVGQEpvlfARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELasGYDTEVGEKG-SQLSGGQKQRVAIA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490290321 162 QALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGY--TGTLILISH 204
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH 207
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-205 |
1.33e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.02 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 23 TINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTfpgnwqlawVNQETPalpqpaidyvidgdreYRQleaalQQAN 102
Cdd:COG4586 44 TIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR---------VLGYVP----------------FKR-----RKEF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 103 ERNdghaIATVHGK-------LDAIDAWTI------------RSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQA 163
Cdd:COG4586 94 ARR----IGVVFGQrsqlwwdLPAIDSFRLlkaiyripdaeyKKRLDELVELLDLG-ELLDTPVRQLSLGQRMRCELAAA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490290321 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWLKGY-----TgTLILISHD 205
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrergT-TILLTSHD 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
17-207 |
1.41e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.15 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwQLAWVnqetPALPQPaIDYVIDGDREYRQLEA 96
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV-DLSHV----PPYQRP-INMMFQSYALFPHMTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 97 alqqanERNDGHAIatvhgKLDAIDAWTIRSRAASLLhGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
Cdd:PRK11607 109 ------EQNIAFGL-----KQDKLPKAEIASRVNEML-GLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 490290321 177 TNHLD--------LDAVIWLEKwlkgYTGTLILISHDRD 207
Cdd:PRK11607 177 MGALDkklrdrmqLEVVDILER----VGVTCVMVTHDQE 211
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-219 |
1.46e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.22 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 26 PGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWqlawvnqetpalpqpaiDYVIDgdrEYRQLEaaLQQANERN 105
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDW-----------------DEILD---EFRGSE--LQNYFTKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 106 DGHAIATVHGK--LDAIDAwTIRSRAASLL---HGLGFSNEQ---------LERPVSDFSGGWRMRLNLAQALICRSDLL 171
Cdd:cd03236 83 LEGDVKVIVKPqyVDLIPK-AVKGKVGELLkkkDERGKLDELvdqlelrhvLDRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490290321 172 LLDEPTNHLD----LDAVIWLEKWLKgYTGTLILISHDRDFLDPIVDkIIHI 219
Cdd:cd03236 162 FFDEPSSYLDikqrLNAARLIRELAE-DDNYVLVVEHDLAVLDYLSD-YIHC 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
310-471 |
1.50e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 56.30 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 310 NPLLKMEKVSAGY--GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI-------------GLAKG 374
Cdd:PRK13648 5 NSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 375 IKL----------GYFAQHQLEF-LRADESPLQHLARLAPQELEQKlrDYLggfgfqgDKVSEETRRFSGGEKARLVLAL 443
Cdd:PRK13648 85 IGIvfqnpdnqfvGSIVKYDVAFgLENHAVPYDEMHRRVSEALKQV--DML-------ERADYEPNALSGGQKQRVAIAG 155
|
170 180
....*....|....*....|....*...
gi 490290321 444 IVWQRPNLLLLDEPTNHLDLDMRQALTE 471
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLD 183
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
324-506 |
1.52e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.28 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 324 ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLG----YFAQHQL---------EFLRA 390
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI-IIDGDLLTeenvWDIRHKIgmvfqnpdnQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 ---DESP--LQHLArLAPQELEQKLRDYLGGFGFQGDKvSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
Cdd:PRK13650 98 tveDDVAfgLENKG-IPHEEMKERVNEALELVGMQDFK-EREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490290321 466 RQALTEAL--IDFEGALVVVSHDRHLIRSTTDDLYLV-HDGKVE 506
Cdd:PRK13650 176 RLELIKTIkgIRDDYQMTVISITHDLDEVALSDRVLVmKNGQVE 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-181 |
1.59e-08 |
|
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: 55.57 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGV--RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG--------NW---QLAW 68
Cdd:cd03252 1 ITFEHVRFRYKPdgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpAWlrrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 69 VNQETPALPQPAIDYVIDGDR--EYRQLEAALQQAnernDGHAIatvhgkldaidawtIRSRAasllhgLGFSNEQLERP 146
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPgmSMERVIEAAKLA----GAHDF--------------ISELP------EGYDTIVGEQG 136
|
170 180 190
....*....|....*....|....*....|....*
gi 490290321 147 VSdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:cd03252 137 AG-LSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-181 |
1.60e-08 |
|
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: 54.86 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 11 RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLL--KNEISADGGSMtfpgnwqlaWVN--QETPALPQPAIDYVid 86
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEV---------LINgrPLDKRSFRKIIGYV-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 87 gdreyrqleaalqqanERNDghaiaTVHGKLdaidawTIRS--RAASLLHGLgfsneqlerpvsdfSGGWRMRLNLAQAL 164
Cdd:cd03213 88 ----------------PQDD-----ILHPTL------TVREtlMFAAKLRGL--------------SGGERKRVSIALEL 126
|
170
....*....|....*..
gi 490290321 165 ICRSDLLLLDEPTNHLD 181
Cdd:cd03213 127 VSNPSLLFLDEPTSGLD 143
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
326-473 |
1.67e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.55 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELqPVSGEIgLAKGIKLgyfaqHQLEFlradESPLQHLARLA--P 403
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSL-KINGIEL-----RELDP----ESWRKHLSWVGqnP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 404 QELEQKLRD---------------------YLGGFGFQGDK-----VSEETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
Cdd:PRK11174 433 QLPHGTLRDnvllgnpdasdeqlqqalenaWVSEFLPLLPQgldtpIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170
....*....|....*.
gi 490290321 458 TNHLDLDMRQALTEAL 473
Cdd:PRK11174 513 TASLDAHSEQLVMQAL 528
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
313-486 |
1.70e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 56.62 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI--------GLA---KGIklGYFA 381
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIliggrdvtDLPpkdRNI--AMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 382 Q------HQ-----LEFlradesPLQhLARLAPQELEQK---------LRDYLGgfgfqgdkvseetRR---FSGGEKAR 438
Cdd:COG3839 82 QsyalypHMtvyenIAF------PLK-LRKVPKAEIDRRvreaaellgLEDLLD-------------RKpkqLSGGQRQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 439 lVlAL---IVwQRPNLLLLDEPTNHLD----LDMRQALTEALIDFEGALVVVSHD 486
Cdd:COG3839 142 -V-ALgraLV-REPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
328-620 |
1.75e-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: 58.03 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLaKGiKLGYFAQH---QLEFLRAD------------E 392
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-KG-SVAYVPQQawiQNDSLRENilfgkalnekyyQ 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 393 SPLQHLARLAPQELeqklrdyLGGfgfqGDK--VSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470
Cdd:TIGR00957 732 QVLEACALLPDLEI-------LPS----GDRteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 471 EALIDFEGAL-----VVVSHDRHLIrSTTDDLYLVHDGKVEPF---------DGDLEDY-QQWLSDSQKQESQSGEAPKE 535
Cdd:TIGR00957 801 EHVIGPEGVLknktrILVTHGISYL-PQVDVIIVMSGGKISEMgsyqellqrDGAFAEFlRTYAPDEQQGHLEDSWTALV 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 536 SGNSaqarKDQKRREAELrSQTQPLRKEiarLEKEMDKLNAQLASAEEKLGDSELYDASRKAELTECLQQQASAKSGLEE 615
Cdd:TIGR00957 880 SGEG----KEAKLIENGM-LVTDVVGKQ---LQRQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQTGQVE 951
|
....*
gi 490290321 616 CEMAW 620
Cdd:TIGR00957 952 LSVYW 956
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-462 |
1.79e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTF---------PGNWQLAW---VNQETPALPQP 79
Cdd:PRK10762 16 GVKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgkevtfngPKSSQEAGigiIHQELNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 80 AIDYVIDGDREYRqleaalqqanerndghaiatvhGKLDAIDAWTIRSRAASLLHGLGFSNEQlERPVSDFSGGWRMRLN 159
Cdd:PRK10762 95 TIAENIFLGREFV----------------------NRFGRIDWKKMYAEADKLLARLNLRFSS-DKLVGELSIGEQQMVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 160 LAQALICRSDLLLLDEPTNHL------DLDAVIwleKWLKGYTGTLILISHdrdfldpivdKIIHIeqqtmfeytgnyss 233
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALtdteteSLFRVI---RELKSQGRGIVYISH----------RLKEI-------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 234 FEV-QRATRLAQQQAMYESQqqrVAHLQSyidrfrakatkakqaQSRIKML--ERMELIAPaHVDNPfHFSFRqpeslpn 310
Cdd:PRK10762 205 FEIcDDVTVFRDGQFIAERE---VADLTE---------------DSLIEMMvgRKLEDQYP-RLDKA-PGEVR------- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 plLKMEKVSaGYGeriiLDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI--------------GLAKGI- 375
Cdd:PRK10762 258 --LKVDNLS-GPG----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVtldghevvtrspqdGLANGIv 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 376 ------------------------KLGYFAQHQLEFLRADEsplqhlarlapqelEQKLRDYLGGFGFQGDKVSEETRRF 431
Cdd:PRK10762 331 yisedrkrdglvlgmsvkenmsltALRYFSRAGGSLKHADE--------------QQAVSDFIRLFNIKTPSMEQAIGLL 396
|
490 500 510
....*....|....*....|....*....|.
gi 490290321 432 SGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
299-505 |
1.81e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.96 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 299 HFSFRQPESlpnpllkmekvsagygERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQP---------VSGEI 369
Cdd:PRK13640 10 HVSFTYPDS----------------KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskitVDGIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 370 GLAKGI-----KLG-YFAQHQLEFLRA---DESPLQHLARLAP-QELEQKLRDYLGGFGFQgDKVSEETRRFSGGEKARL 439
Cdd:PRK13640 74 LTAKTVwdireKVGiVFQNPDNQFVGAtvgDDVAFGLENRAVPrPEMIKIVRDVLADVGML-DYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 440 VLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVVVS--HDRHLIrSTTDDLYLVHDGKV 505
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkKNNLTVISitHDIDEA-NMADQVLVLDDGKL 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-181 |
1.99e-08 |
|
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: 54.96 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQI------RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADG---GSMTFPGnwqlawvnq 71
Cdd:cd03233 1 ASTLSWRNIsfttgkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNG--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 72 etpalpqpaIDYviDGDREYRQLEAALqqaNERNDGH-AIATVHGKLDAidawtirsrAASLlhglgfsneQLERPVSDF 150
Cdd:cd03233 72 ---------IPY--KEFAEKYPGEIIY---VSEEDVHfPTLTVRETLDF---------ALRC---------KGNEFVRGI 119
|
170 180 190
....*....|....*....|....*....|.
gi 490290321 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:cd03233 120 SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-230 |
2.11e-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: 55.31 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLL-------KNEISADGGSM-TFPGNW---QLAWVNQETPALPQPAIDYVI 85
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLmrfydpqKGQILIDGIDIrDISRKSlrsMIGVVLQDTFLFSGTIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 86 DGDREYRQ--LEAALQQAnerndghaiatvhGKLDAIDawtirsraaSLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQA 163
Cdd:cd03254 99 LGRPNATDeeVIEAAKEA-------------GAHDFIM---------KLPNGY---DTVLGENGGNLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490290321 164 LICRSDLLLLDEPTNHLD--LDAVIW--LEKWLKGYtgTLILISHDrdfLDPIV--DKIIHIEQQTMFEyTGN 230
Cdd:cd03254 154 MLRDPKILILDEATSNIDteTEKLIQeaLEKLMKGR--TSIIIAHR---LSTIKnaDKILVLDDGKIIE-EGT 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
312-505 |
2.23e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 55.28 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL--------------AKGIkl 377
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 378 GYFAQHQLEF--------------LRADESPLQHLARlAPQELEQ----KLRDYLGgfgfqgdkvseetRRFSGGEKARL 439
Cdd:PRK10895 81 GYLPQEASIFrrlsvydnlmavlqIRDDLSAEQREDR-ANELMEEfhieHLRDSMG-------------QSLSGGERRRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490290321 440 VLALIVWQRPNLLLLDEPTNHLD----LDMRQaLTEALIDFEGALVVVSHDrhlIRSTTD---DLYLVHDGKV 505
Cdd:PRK10895 147 EIARALAANPKFILLDEPFAGVDpisvIDIKR-IIEHLRDSGLGVLITDHN---VRETLAvceRAYIVSQGHL 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
312-475 |
2.48e-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: 54.78 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGER---IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL-AKGI----------KL 377
Cdd:cd03248 11 IVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdGKPIsqyehkylhsKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 378 GYFAQHQLEFLRADESP----LQHLARLAPQELEQKLR--DYLGGF--GFQGDkVSEETRRFSGGEKARLVLALIVWQRP 449
Cdd:cd03248 91 SLVGQEPVLFARSLQDNiaygLQSCSFECVKEAAQKAHahSFISELasGYDTE-VGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180
....*....|....*....|....*.
gi 490290321 450 NLLLLDEPTNHLDLDMRQALTEALID 475
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYD 195
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
338-501 |
2.69e-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: 54.12 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 338 GSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLaKGIKLGYfaqhqleflradesplqhlarlAPQELEqklrdylggf 417
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVY----------------------KPQYID---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 418 gfqgdkvseetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF----EGALVVVSHDRHLIRST 493
Cdd:cd03222 72 -------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYL 138
|
....*...
gi 490290321 494 TDDLYLVH 501
Cdd:cd03222 139 SDRIHVFE 146
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
327-503 |
2.87e-08 |
|
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: 55.63 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKL---------GYFAQHQLEFLRADEspLQH 397
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFssqfswimpGTIKENIIFGVSYDE--YRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 398 LARLAPQELEQKLRDYLggfgfQGDK--VSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA--- 472
Cdd:cd03291 130 KSVVKACQLEEDITKFP-----EKDNtvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEScvc 204
|
170 180 190
....*....|....*....|....*....|..
gi 490290321 473 -LIDFEGALVVVSHDRHLIRSttDDLYLVHDG 503
Cdd:cd03291 205 kLMANKTRILVTSKMEHLKKA--DKILILHEG 234
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
6-205 |
3.30e-08 |
|
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: 54.75 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMT------FPGNW-QLA--------WVN 70
Cdd:COG4181 17 TVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRlagqdlFALDEdARArlrarhvgFVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 71 QETPALPQ-PAIDYVidgdreyrQLEAALQqanerndGHAiatvhgkldaiDAwtiRSRAASLLH--GLGfsnEQLE-RP 146
Cdd:COG4181 97 QSFQLLPTlTALENV--------MLPLELA-------GRR-----------DA---RARARALLErvGLG---HRLDhYP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490290321 147 vSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKGYTG-TLILISHD 205
Cdd:COG4181 145 -AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAatgEQIIDLLFELNRERGtTLVLVTHD 206
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-205 |
3.38e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.93 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqlAWVNQETPALPQPaidyvidgdr 89
Cdd:PRK11701 15 LYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR---DGQLRDLYALSEA---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 EYRQL---EAALQQANERnDG-----HAIATVHGKLDAIDA---WTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRL 158
Cdd:PRK11701 82 ERRRLlrtEWGFVHQHPR-DGlrmqvSAGGNIGERLMAVGArhyGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490290321 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTGTL----ILISHD 205
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglavVIVTHD 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-221 |
3.55e-08 |
|
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: 55.89 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 26 PGQKV-GLVGKNGCGKSTLLSLLKNEISADGGSMTFPGN-WQLAWVNQETPAlPQPAIDYVIDGDREYRQLEAAlqqane 103
Cdd:TIGR02142 21 PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtLFDSRKGIFLPP-EKRRIGYVFQEARLFPHLSVR------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 104 RNdghaiaTVHGKLDAiDAWTIRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL- 182
Cdd:TIGR02142 94 GN------LRYGMKRA-RPSERRISFERVIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDp 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490290321 183 --DAVI-WLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:TIGR02142 166 rkYEILpYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLED 207
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-181 |
3.56e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.09 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGN------WQLAWVNQETP 74
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpvegpgAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 75 ALP-QPAIDYVIDGdreyrqLEAALQQANERndghaiatvhgkldaidawtiRSRAASLLHGLGFSNEQlERPVSDFSGG 153
Cdd:PRK11248 81 LLPwRNVQDNVAFG------LQLAGVEKMQR---------------------LEIAHQMLKKVGLEGAE-KRYIWQLSGG 132
|
170 180
....*....|....*....|....*...
gi 490290321 154 WRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
8-181 |
3.68e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.79 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 8 QIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKN--EISADGGSMTFPGnwqlawvnQETPALPQPAIDYVi 85
Cdd:cd03232 14 PVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILING--------RPLDKNFQRSTGYV- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 86 dgdreyrqleaalqqanERNDGHaiatvhgkldaIDAWTIRS--RAASLLHGLgfSNEQlerpvsdfsggwRMRLNLAQA 163
Cdd:cd03232 85 -----------------EQQDVH-----------SPNLTVREalRFSALLRGL--SVEQ------------RKRLTIGVE 122
|
170
....*....|....*...
gi 490290321 164 LICRSDLLLLDEPTNHLD 181
Cdd:cd03232 123 LAAKPSILFLDEPTSGLD 140
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
313-487 |
3.78e-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: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 313 LKMEKVSAGYGE--RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL------AGELQpVSG----EIGLAKGIK-LGY 379
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALlrllstEGEIQ-IDGvswnSVTLQTWRKaFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 380 FAQHQLEFLRADESPLQHLARLAPQEL-----EQKLRDYLGGFGFQGDKVSEETRR-FSGGEKARLVLALIVWQRPNLLL 453
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLDPYEQWSDEEIwkvaeEVGLKSVIEQFPDKLDFVLVDGGYvLSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190
....*....|....*....|....*....|....*
gi 490290321 454 LDEPTNHLDLDMRQALTEALID-FEGALVVVSHDR 487
Cdd:TIGR01271 1377 LDEPSAHLDPVTLQIIRKTLKQsFSNCTVILSEHR 1411
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-263 |
3.88e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.73 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQLAWVNQET---PALP 77
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLyldTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 78 QPAidyvidgdREYRQLEAALQQANerndghaiatvhgKLDAIDawtiRSRAASLlhglgfsneqLERPVSDFSGGWRMR 157
Cdd:PRK09544 84 LTV--------NRFLRLRPGTKKED-------------ILPALK----RVQAGHL----------IDAPMQKLSGGETQR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTGTL----ILISHDRDFLDPIVDKII----HIEQQTMFEYTG 229
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcavLMVSHDLHLVMAKTDEVLclnhHICCSGTPEVVS 208
|
250 260 270
....*....|....*....|....*....|....
gi 490290321 230 NYSSFEVQRATRLAQQQAMYESQQQRVAHLQSYI 263
Cdd:PRK09544 209 LHPEFISMFGPRGAEQLGIYRHHHNHRHDLQGRI 242
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-207 |
4.17e-08 |
|
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: 54.39 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKN-------EISADGGSMTFPGNWQLAwVNQETPALPQPAIDYVIdgdr 89
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlaqptsgGVILEGKQITEPGPDRMV-VFQNYSLLPWLTVRENI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 eYRQLEAALQQANeRNDGHAIATVHgkldaIDawtirsraaslLHGLGfsnEQLERPVSDFSGGWRMRLNLAQALICRSD 169
Cdd:TIGR01184 76 -ALAVDRVLPDLS-KSERRAIVEEH-----IA-----------LVGLT---EAADKRPGQLSGGMKQRVAIARALSIRPK 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490290321 170 LLLLDEPTNHldLDAV-----------IWLEKWLkgytgTLILISHDRD 207
Cdd:TIGR01184 135 VLLLDEPFGA--LDALtrgnlqeelmqIWEEHRV-----TVLMVTHDVD 176
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
324-484 |
4.48e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.43 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 324 ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQP--VSGEIgLAKGIKLGYFAQHQLEFLRADESPLQHLA-- 399
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTI-LANNRKPTKQILKRTGFVTQDDILYPHLTvr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 400 ---------RLaPQEL--EQKLRDYLGGFGFQGDKVSEET-------RRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
Cdd:PLN03211 159 etlvfcsllRL-PKSLtkQEKILVAESVISELGLTKCENTiignsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180
....*....|....*....|....*
gi 490290321 462 DLD--MRQALTEALIDFEGALVVVS 484
Cdd:PLN03211 238 DATaaYRLVLTLGSLAQKGKTIVTS 262
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-227 |
4.93e-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: 56.46 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLL------KNEISADG---GSMTFPgNWQLAWvnqetPALPQPAidYV 84
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALlrllstEGEIQIDGvswNSVTLQ-TWRKAF-----GVIPQKV--FI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 85 IDGdreyrqleaalqqanerndghaiaTVHGKLDAIDAWT------------IRSRAASLLHGLGFsneQLERPVSDFSG 152
Cdd:TIGR01271 1304 FSG------------------------TFRKNLDPYEQWSdeeiwkvaeevgLKSVIEQFPDKLDF---VLVDGGYVLSN 1356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 153 GWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLK-GYTGTLILISHDRdfLDPIVD--KIIHIEQQTMFEY 227
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKqSFSNCTVILSEHR--VEALLEcqQFLVIEGSSVKQY 1432
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
297-511 |
5.29e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.75 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 297 PFHFSFRQPESLPN-PLLKMEKVSAGYGER-IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKG 374
Cdd:PRK10522 306 PYKAEFPRPQAFPDwQTLELRNVTFAYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI-LLDG 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 375 IKLGyfAQHQLEFLR------ADESPLQHLarLAPQ---ELEQKLRDYLGGFGFQgDKVSEE-----TRRFSGGEKARLV 440
Cdd:PRK10522 385 KPVT--AEQPEDYRKlfsavfTDFHLFDQL--LGPEgkpANPALVEKWLERLKMA-HKLELEdgrisNLKLSKGQKKRLA 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 441 LALIVWQRPNLLLLDEPTNHLDLDMR----QALTEALIDFEGALVVVSHDRHLIRStTDDLYLVHDGKVEPFDGD 511
Cdd:PRK10522 460 LLLALAEERDILLLDEWAADQDPHFRrefyQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSELTGE 533
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-216 |
5.45e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.56 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWqlawVNQETPALP-QPAIDYVidgdreYRQLE 95
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN----YNKLDHKLAaQLGIGII------YQELS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 96 AALQQANERN---DGHAIATVHGkLDAIDAWTIRSRAASLLHGLGFSNEqLERPVSDFSGGWRMRLNLAQALICRSDLLL 172
Cdd:PRK09700 91 VIDELTVLENlyiGRHLTKKVCG-VNIIDWREMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490290321 173 LDEPTNHL---DLDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKI 216
Cdd:PRK09700 169 MDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRY 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
139-486 |
5.59e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 139 SNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWL-KGYTGTLILISHDRDFLDPIVD 214
Cdd:PRK10261 158 AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLqKEMSMGVIFITHDMGVVAEIAD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 215 KIIHIEQQTMFEyTGnySSFEVQRATRLAQQQAMYESQQQRVAHLQSYIDRfRAKATKAKQAQSRIKMLERMELIAPAHV 294
Cdd:PRK10261 238 RVLVMYQGEAVE-TG--SVEQIFHAPQHPYTRALLAAVPQLGAMKGLDYPR-RFPLISLEHPAKQEPPIEQDTVVDGEPI 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 295 DNPFHFSFRQPeslpnpllkmekVSAGYGERII-----LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI 369
Cdd:PRK10261 314 LQVRNLVTRFP------------LRSGLLNRVTrevhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 370 GLaKGIKLGYFAQHQLEFLRAD----------------------ESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVSEE 427
Cdd:PRK10261 382 IF-NGQRIDTLSPGKLQALRRDiqfifqdpyasldprqtvgdsiMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRY 460
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490290321 428 TRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHD 486
Cdd:PRK10261 461 PHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfgiAYLFISHD 523
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
315-505 |
8.09e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.49 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 315 MEKVSAGY-GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI-------------GLAKGIKL--- 377
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldgrplsslshsVLRQGVAMvqq 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 378 -------GYFAQHQLEFLRADESPLQHLARLAPQELEQKLRDYLGG-FGFQGDkvseetrRFSGGEKARLVLALIVWQRP 449
Cdd:PRK10790 423 dpvvladTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTpLGEQGN-------NLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490290321 450 NLLLLDEPTNHLDLDMRQALTEAL--IDFEGALVVVSHdrhliRSTT----DDLYLVHDGKV 505
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALaaVREHTTLVVIAH-----RLSTiveaDTILVLHRGQA 552
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-225 |
9.39e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 53.22 E-value: 9.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLldNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGsmtfpgnwQLAWVNQETPALPqPA 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSG--------RILWNGQDLTALP-PA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 idyvidgdreYRQLEAALQQAN-------ERNDGHAIATvHGKLDAIDawtiRSRAASLLHGLGFSnEQLERPVSDFSGG 153
Cdd:COG3840 70 ----------ERPVSMLFQENNlfphltvAQNIGLGLRP-GLKLTAEQ----RAQVEQALERVGLA-GLLDRLPGQLSGG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 154 WRMRLNLAQALICRSDLLLLDEPTNHLD-------LDaviWLEKWLKGYTGTLILISHDrdfldpiVDKIIHIEQQTMF 225
Cdd:COG3840 134 QRQRVALARCLVRKRPILLLDEPFSALDpalrqemLD---LVDELCRERGLTVLMVTHD-------PEDAARIADRVLL 202
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
331-524 |
1.27e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.11 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 331 IKLNLvPGSRI-GLLGRNGAGKSTLIKLLAGELQPVSGEIGL--------AKGI-------KLGYFAQHqleflradesp 394
Cdd:PRK11144 17 VNLTL-PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfdaEKGIclppekrRIGYVFQD----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 395 lqhlARLAPQ-ELEQKLRdylggFGF------QGDKVSE----ET--RRF----SGGEKARLVLALIVWQRPNLLLLDEP 457
Cdd:PRK11144 85 ----ARLFPHyKVRGNLR-----YGMaksmvaQFDKIVAllgiEPllDRYpgslSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 458 TNHLDLDMRQALT---EALI-DFEGALVVVSHDRHLIRSTTDDLYLVHDGKVEPFdGDLED------YQQWLSDSQK 524
Cdd:PRK11144 156 LASLDLPRKRELLpylERLArEINIPILYVSHSLDEILRLADRVVVLEQGKVKAF-GPLEEvwassaMRPWLPKEEQ 231
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
327-563 |
1.38e-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: 53.32 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAgELQPVSGEIglakgiklgyfaqhQLEFLRADESPLQHLAR---LAP 403
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDI--------------QIDGVSWNSVPLQKWRKafgVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 404 QEL---EQKLRDYLGGFGFQGD----KVSEET------RRFSG---------------GEKARLVLALIVWQRPNLLLLD 455
Cdd:cd03289 84 QKVfifSGTFRKNLDPYGKWSDeeiwKVAEEVglksviEQFPGqldfvlvdggcvlshGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 456 EPTNHLDLDMRQALTEALID-FEGALVVVSHDRHLIRSTTDDLYLVHDGKVEPFDgdleDYQQWLsdSQKQESQSGEAPK 534
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLKQaFADCTVILSEHRIEAMLECQRFLVIEENKVRQYD----SIQKLL--NEKSHFKQAISPS 237
|
250 260
....*....|....*....|....*....
gi 490290321 535 ESGNSAQARKDQKRREaELRSQTQPLRKE 563
Cdd:cd03289 238 DRLKLFPRRNSSKSKR-KPRPQIQALQEE 265
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
7-204 |
1.41e-07 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 52.11 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTfpgnWQLAWVNQETPALPQpAIDYVID 86
Cdd:cd03231 6 LTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVL----LNGGPLDFQRDSIAR-GLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 87 GDrEYRQLEAALQQANERNDGHAIATVHGKLDAIDawtirsraaslLHGLGfsneqlERPVSDFSGGWRMRLNLAQALIC 166
Cdd:cd03231 81 AP-GIKTTLSVLENLRFWHADHSDEQVEEALARVG-----------LNGFE------DRPVAQLSAGQQRRVALARLLLS 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490290321 167 RSDLLLLDEPTNHLDLDAVIWLEKWLKGYT---GTLILISH 204
Cdd:cd03231 143 GRPLWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-220 |
1.45e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 52.48 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLL----------KNEISADGGSMT----------- 59
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlspafsaSGEVLLNGRRLTalpaeqrrigi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 60 -------FP-----GNwqLAWvnqetpALPqPAIdyvidgDREYRQ--LEAALQQANerndghaiatvhgkldaidawti 125
Cdd:COG4136 81 lfqddllFPhlsvgEN--LAF------ALP-PTI------GRAQRRarVEQALEEAG----------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 126 rsraaslLHGLGfsneqlERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTGTL----IL 201
Cdd:COG4136 123 -------LAGFA------DRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRgipaLL 189
|
250 260
....*....|....*....|
gi 490290321 202 ISHDRDflD-PIVDKIIHIE 220
Cdd:COG4136 190 VTHDEE--DaPAAGRVLDLG 207
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-227 |
1.58e-07 |
|
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: 52.41 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqetpalpqpaIDYVIDGDREYRQLEA 96
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG------------------IDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 97 ALQQANERNDGhaiaTVHGKLDAIDAWTIRSRAASLLHGLGFSNeqlerpvsdFSGGWRMRLNLAQALICRSDLLLLDEP 176
Cdd:cd03369 86 IIPQDPTLFSG----TIRSNLDPFDEYSDEEIYGALRVSEGGLN---------LSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 177 TNHLDL--DAVIWlEKWLKGYTG-TLILISHD-RDFLDpiVDKIIHIEQQTMFEY 227
Cdd:cd03369 153 TASIDYatDALIQ-KTIREEFTNsTILTIAHRlRTIID--YDKILVMDAGEVKEY 204
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-181 |
1.63e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 8 QIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISA---DGGSM---------TFPGnwQLAWVNQETPA 75
Cdd:TIGR00956 770 KIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRlvngrpldsSFQR--SIGYVQQQDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 76 LPQPAIdyvidgdREYRQLEAALQQANERNDGHAIATVHgklDAIDAWTIRSRAASL--LHGLGFSNEQlerpvsdfsgg 153
Cdd:TIGR00956 848 LPTSTV-------RESLRFSAYLRQPKSVSKSEKMEYVE---EVIKLLEMESYADAVvgVPGEGLNVEQ----------- 906
|
170 180
....*....|....*....|....*....
gi 490290321 154 wRMRLNLAQALICRSDLLL-LDEPTNHLD 181
Cdd:TIGR00956 907 -RKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
311-495 |
1.70e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.12 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLaGELQPVSGEIGLAKgiKLGYFAQH------Q 384
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEG--RVEFFNQNiyerrvN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 385 LEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQ----------------------GDKVSEETRRFSGGEKARLVLA 442
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRpkleiddivesalkdadlwdeiKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 443 LIVWQRPNLLLLDEPTNHLD----LDMRQALTEALIDFEGALVVVSHDRHLIRSTTD 495
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
311-504 |
1.79e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.68 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI--------GLA------KGIK 376
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIllrgqhieGLPghqiarMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 377 LGY----------------FAQH-QLE------------FLRADESPLQHlarlAPQELEQ-KLRDYlggfgfqgdkVSE 426
Cdd:PRK11300 84 RTFqhvrlfremtvienllVAQHqQLKtglfsgllktpaFRRAESEALDR----AATWLERvGLLEH----------ANR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 427 ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALtEALID-----FEGALVVVSHDRHLIRSTTDDLYLVH 501
Cdd:PRK11300 150 QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKEL-DELIAelrneHNVTVLLIEHDMKLVMGISDRIYVVN 228
|
...
gi 490290321 502 DGK 504
Cdd:PRK11300 229 QGT 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-218 |
2.11e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 26 PGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPQPAIDYVidgdreYRQLEAALQQANERN 105
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG--------QRIDTLSPGKLQAL------RRDIQFIFQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 106 D-----GHAIAT---VHGKLDAIDAwtiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPT 177
Cdd:PRK10261 415 DprqtvGDSIMEplrVHGLLPGKAA---AARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490290321 178 NHLDLD---AVIWLEKWLKGYTG-TLILISHDRdfldPIVDKIIH 218
Cdd:PRK10261 492 SALDVSirgQIINLLLDLQRDFGiAYLFISHDM----AVVERISH 532
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
560-625 |
2.21e-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: 48.23 E-value: 2.21e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 560 LRKEIARLEKEMDKLNAQLASAEEKLGDSELYdaSRKAELTECLQQQASAKSGLEECEMAWLEAQE 625
Cdd:pfam16326 6 EQRELEELEAEIEKLEEEIAELEAQLADPELY--SDYEKLQELSAELEELEAELEELYERWEELEE 69
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-177 |
2.29e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLlkneisadggsmtfpgnwqLAWVNqetpALPQPAIDyVIDGDr 89
Cdd:NF033858 10 RYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSL-------------------IAGAR----KIQQGRVE-VLGGD- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 eyrqleaaLQQANERND-GHAIA--------------TV------HGKLDAIDAWTIRSRAASLLHGLG---FsneqLER 145
Cdd:NF033858 65 --------MADARHRRAvCPRIAympqglgknlyptlSVfenldfFGRLFGQDAAERRRRIDELLRATGlapF----ADR 132
|
170 180 190
....*....|....*....|....*....|..
gi 490290321 146 PVSDFSGGWRMRLNLAQALICRSDLLLLDEPT 177
Cdd:NF033858 133 PAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-177 |
2.45e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.19 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG----NWQLAWVNQEtpal 76
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditDWQTAKIMRE---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 77 pqpAIDYVIDGDREYRQLE-----------AALQQANERndghaIATVHGKLDAIDAWTIRsRAASLlhglgfsneqler 145
Cdd:PRK11614 81 ---AVAIVPEGRRVFSRMTveenlamggffAERDQFQER-----IKWVYELFPRLHERRIQ-RAGTM------------- 138
|
170 180 190
....*....|....*....|....*....|..
gi 490290321 146 pvsdfSGGWRMRLNLAQALICRSDLLLLDEPT 177
Cdd:PRK11614 139 -----SGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-219 |
2.60e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 51.99 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 23 TINPGQKVGLVGKNGCGKSTLLSLL----KNEIsaDGGSMTFPGNWQLAWvnqeTP----------ALPQPAidyVIDGD 88
Cdd:COG0396 22 TIKPGEVHAIMGPNGSGKSTLAKVLmghpKYEV--TSGSILLDGEDILEL----SPderaragiflAFQYPV---EIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 89 REYRQLEAALqqaNERndghaiatvhgKLDAIDAWTIRSRAASLLHGLGFSNEQLERPV-SDFSGGWRMRLNLAQALICR 167
Cdd:COG0396 93 SVSNFLRTAL---NAR-----------RGEELSAREFLKLLKEKMKELGLDEDFLDRYVnEGFSGGEKKRNEILQMLLLE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 168 SDLLLLDEPTNHLDLDAV------IwleKWLKGYTGTLILISHDRDFLDPIVDKIIHI 219
Cdd:COG0396 159 PKLAILDETDSGLDIDALrivaegV---NKLRSPDRGILIITHYQRILDYIKPDFVHV 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
327-505 |
2.83e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.06 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI-----------------GLAKGIK--LGYFAQ----- 382
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtarslsqqkGLIRQLRqhVGFVFQnfnlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 383 -HQLEFLRADESPLQhLARLAPQELEQKLRDYLGGFGFQGdKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
Cdd:PRK11264 98 pHRTVLENIIEGPVI-VKGEPKEEATARARELLAKVGLAG-KETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490290321 462 DLDM-RQALT--EALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK11264 176 DPELvGEVLNtiRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
10-216 |
2.87e-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: 51.49 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqlawvnqetpalpqpaidYVIDGDR 89
Cdd:cd03301 9 RFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR-------------------DVTDLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 EYRQLEAALQQ-------ANERNDGHAIATVHGKLDAIDAWTirSRAASLLHglgfSNEQLERPVSDFSGGWRMRLNLAQ 162
Cdd:cd03301 70 KDRDIAMVFQNyalyphmTVYDNIAFGLKLRKVPKDEIDERV--REVAELLQ----IEHLLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 163 ALICRSDLLLLDEPTNHLD----LDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKI 216
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRI 201
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-181 |
2.88e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.89 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 21 TATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMtfpgnwqlaWVNQETPALPQPAidyvidgdreYRQLEAALQQ 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL---------TLNGQDHTTTPPS----------RRPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 101 AN-------ERNDGHAIATvhG-KLDAIDAWTIRSRAASLlhGLGfsnEQLERPVSDFSGGWRMRLNLAQALICRSDLLL 172
Cdd:PRK10771 80 NNlfshltvAQNIGLGLNP--GlKLNAAQREKLHAIARQM--GIE---DLLARLPGQLSGGQRQRVALARCLVREQPILL 152
|
....*....
gi 490290321 173 LDEPTNHLD 181
Cdd:PRK10771 153 LDEPFSALD 161
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
277-487 |
2.93e-07 |
|
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: 53.67 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 277 QSRIKMlERM-ELIA-PAHVDNPFHfsfRQPESLPNPLLKMEKVSAGY-GERIILDSIKLNLVPGSRIGLLGRNGAGKST 353
Cdd:COG5265 324 QALADM-ERMfDLLDqPPEVADAPD---APPLVVGGGEVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKST 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 354 LIKLLAGELQPVSGEIgLAKGIKLGYFAQHQlefLR---------------------------ADESPLQHLARLApqel 406
Cdd:COG5265 400 LARLLFRFYDVTSGRI-LIDGQDIRDVTQAS---LRaaigivpqdtvlfndtiayniaygrpdASEEEVEAAARAA---- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 407 eqklrdYLGGF------GFQgDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDldmrqALTEALIdfEGAL 480
Cdd:COG5265 472 ------QIHDFieslpdGYD-TRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALD-----SRTERAI--QAAL 537
|
....*..
gi 490290321 481 VVVSHDR 487
Cdd:COG5265 538 REVARGR 544
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
328-511 |
2.95e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.78 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGL---------------------------------AKG 374
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkekekvleklviqktrfkkikkIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 375 IK--LGY---FAQHQLeFLRADESPLQHLAR---LAPQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVW 446
Cdd:PRK13651 103 IRrrVGVvfqFAEYQL-FEQTIEKDIIFGPVsmgVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 447 QRPNLLLLDEPTNHLD----LDMRQALTEalIDFEGALVV-VSHDRHLIRSTTDDLYLVHDGKVePFDGD 511
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDpqgvKEILEIFDN--LNKQGKTIIlVTHDLDNVLEWTKRTIFFKDGKI-IKDGD 248
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-217 |
3.75e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 52.32 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSmTFPGNWQLawvnqetPALPQpAIDYVIDGDRE----YR 92
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDYAI-------PANLK-KIKEVKRLRKEiglvFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 93 QLEAALQQANERNDgHAIATVHGKLDAIDAWtirSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLL 172
Cdd:PRK13645 98 FPEYQLFQETIEKD-IAFGPVNLGENKQEAY---KKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490290321 173 LDEPTNHLD----LDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKII 217
Cdd:PRK13645 174 LDEPTGGLDpkgeEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVI 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-176 |
3.83e-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: 51.39 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALP-----QPAI 81
Cdd:cd03218 6 LSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG--------QDITKLPmhkraRLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 82 DYVIDGDREYRQLEAAlqqANERndghAIATVHGKLDAIdawtIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLA 161
Cdd:cd03218 78 GYLPQEASIFRKLTVE---ENIL----AVLEIRGLSKKE----REEKLEELLEEFHIT-HLRKSKASSLSGGERRRVEIA 145
|
170
....*....|....*
gi 490290321 162 QALICRSDLLLLDEP 176
Cdd:cd03218 146 RALATNPKFLLLDEP 160
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
328-505 |
3.87e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 52.27 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLaKGIKLGYFAQHQLEFLRAD---------------- 391
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYY-QGQDLLKADPEAQKLLRQKiqivfqnpygslnprk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 392 ------ESPLQHLARLAPQELEQKLRDYLGGFGFQgdkvSEETRR----FSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
Cdd:PRK11308 110 kvgqilEEPLLINTSLSAAERREKALAMMAKVGLR----PEHYDRyphmFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490290321 462 DLDMRQALTEALID----FEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK11308 186 DVSVQAQVLNLMMDlqqeLGLSYVFISHDLSVVEHIADEVMVMYLGRC 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
328-369 |
4.12e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 4.12e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI 369
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI 61
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
331-456 |
4.22e-07 |
|
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: 52.88 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 331 IKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGyfaQHQLEFLR-------ADESPLQHLARLAP 403
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI-LLDGQPVT---ADNREAYRqlfsavfSDFHLFDRLLGLDG 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 404 QELEQKLRDYLGGFGFQgDKVSEETRRF-----SGGEKARlvLALIV-W--QRPnLLLLDE 456
Cdd:COG4615 427 EADPARARELLERLELD-HKVSVEDGRFsttdlSQGQRKR--LALLVaLleDRP-ILVFDE 483
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
311-505 |
4.39e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.02 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGeIGLAKGIKLG----YFAQHQLE 386
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGgrsiFNYRDVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 387 F--------LRADESPLQHL---------ARLAPQE----LEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIV 445
Cdd:PRK14271 99 FrrrvgmlfQRPNPFPMSIMdnvlagvraHKLVPRKefrgVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490290321 446 WQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL--VVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLtvIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
324-505 |
4.46e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.09 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 324 ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLA----------KGI-----KLGY---FAQHQL 385
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDditithktkdKYIrpvrkRIGMvfqFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 386 eFlradESPLQHLARLAPQ-------ELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
Cdd:PRK13646 99 -F----EDTVEREIIFGPKnfkmnldEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490290321 459 NHLDLDMRQALTEALIDFE----GALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-182 |
4.91e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.71 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG----NWQLAWVNQETPALPQpaidyvidgdr 89
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpleSWSSKAFARKVAYLPQ----------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 eyrQLEAAlqqanernDGHAIATV--------HGKLDAIDAwTIRSRA--ASLLHGLG-FSNeqleRPVSDFSGGWRMRL 158
Cdd:PRK10575 93 ---QLPAA--------EGMTVRELvaigrypwHGALGRFGA-ADREKVeeAISLVGLKpLAH----RLVDSLSGGERQRA 156
|
170 180
....*....|....*....|....
gi 490290321 159 NLAQALICRSDLLLLDEPTNHLDL 182
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-217 |
5.05e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 51.59 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG------NWQLAWVNQETPALPQ-Paidyvid 86
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkKVKLSDIRKKVGLVFQyP------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 87 gdrEYRQLEAALQQANE---RNDGHAIATVHgkldaidawtIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQA 163
Cdd:PRK13637 93 ---EYQLFEETIEKDIAfgpINLGLSEEEIE----------NRVKRAMNIVGLDY-EDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 164 LICRSDLLLLDEPTNHLD---LDAVIWLEKWL-KGYTGTLILISHDRDFLDPIVDKII 217
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDpkgRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRII 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-205 |
5.14e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.59 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLK-------NEISADGGSMTFPGNWqlawvnqetpalpqpaidYVID 86
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGKDI------------------FQID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 87 GDREYRQLEAALQQANE-------RNDGHAIATvHGKLDAIDawtIRSRAASLLHGLGFSNE---QLERPVSDFSGGWRM 156
Cdd:PRK14246 85 AIKLRKEVGMVFQQPNPfphlsiyDNIAYPLKS-HGIKEKRE---IKKIVEECLRKVGLWKEvydRLNSPASQLSGGQQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490290321 157 RLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTG--TLILISHD 205
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-486 |
5.21e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.72 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvNQETPALPQPAIDyvidgdreyrqlea 96
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG-------KPVRIRSPRDAIA-------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 97 alqqanerndgHAIATVH---------------------GKLDAIDAWTIRSRAASLLHGLGFSNEqLERPVSDFSGGWR 155
Cdd:COG3845 80 -----------LGIGMVHqhfmlvpnltvaenivlglepTKGGRLDRKAARARIRELSERYGLDVD-PDAKVEDLSVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 156 MRLNLAQALICRSDLLLLDEPTNHL------DLDAVIwleKWLKGYTGTLILISHDrdfLDpivdkiihieqqtmfeytg 229
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLtpqeadELFEIL---RRLAAEGKSIIFITHK---LR------------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 230 nyssfEVQRATrlaqqqamyesqqQRVAHLQS--YIDRFRAKATkakqaqSRIKMLERM---ELIAPAHvdnpfhfsfRQ 304
Cdd:COG3845 203 -----EVMAIA-------------DRVTVLRRgkVVGTVDTAET------SEEELAELMvgrEVLLRVE---------KA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 305 PESLPNPLLKMEKVSA-GYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI-------------- 369
Cdd:COG3845 250 PAEPGEVVLEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIrldgeditglspre 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 370 ----GLA--------KGIKLGYFAQHQLEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKA 437
Cdd:COG3845 330 rrrlGVAyipedrlgRGLVPDMSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPARSLSGGNQQ 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 490290321 438 RLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHD 486
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELrdAGaAVLLISED 461
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-181 |
5.30e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 52.03 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSL---LKN----EISADGGSMTFPG--NWQLAWVNQETPALPQPA 80
Cdd:PRK11432 15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLvagLEKptegQIFIDGEDVTHRSiqQRDICMVFQSYALFPHMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 IdyvidGDreyrqleaalqqanerNDGHAIatvhgKLDAIDAWTIRSR---AASLLHGLGFSneqlERPVSDFSGGWRMR 157
Cdd:PRK11432 95 L-----GE----------------NVGYGL-----KMLGVPKEERKQRvkeALELVDLAGFE----DRYVDQISGGQQQR 144
|
170 180
....*....|....*....|....
gi 490290321 158 LNLAQALICRSDLLLLDEPTNHLD 181
Cdd:PRK11432 145 VALARALILKPKVLLFDEPLSNLD 168
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
334-486 |
6.44e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 51.65 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 334 NLVPGSRIGLLGRNGAGKS----TLIKLLAGelqpvSGEI-GLAK--GIKLGYFAQHQLEFLRADE------SPLQHL-- 398
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSqtafALMGLLAA-----NGRIgGSATfnGREILNLPEKELNKLRAEQismifqDPMTSLnp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 399 -ARLAPQELE-QKLRDYLGGF-GFQGD-------KVSEETRR-------FSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
Cdd:PRK09473 113 yMRVGEQLMEvLMLHKGMSKAeAFEESvrmldavKMPEARKRmkmypheFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 192
|
170 180 190
....*....|....*....|....*....|
gi 490290321 462 DLDMrQA-----LTEALIDFEGALVVVSHD 486
Cdd:PRK09473 193 DVTV-QAqimtlLNELKREFNTAIIMITHD 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
316-467 |
6.80e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.43 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 316 EKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGelqpvsgeiglAKGIKLGyfaqhQLEFLRADESPL 395
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG-----------ARKIQQG-----RVEVLGGDMADA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 396 QHLARLA------PQELEQKL------RDYLGGFG--FqGDKVSEETRR------------F--------SGGEKARLVL 441
Cdd:NF033858 69 RHRRAVCpriaymPQGLGKNLyptlsvFENLDFFGrlF-GQDAAERRRRidellratglapFadrpagklSGGMKQKLGL 147
|
170 180
....*....|....*....|....*....
gi 490290321 442 --ALIvwQRPNLLLLDEPTNHLD-LDMRQ 467
Cdd:NF033858 148 ccALI--HDPDLLILDEPTTGVDpLSRRQ 174
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
12-216 |
7.14e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 7.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLSLLkneisadggSMTFP-GNWQLawvnqetpalpqpaiDYVIDGDRe 90
Cdd:PRK13549 17 GVKAL-DNVSLKVRAGEIVSLCGENGAGKSTLMKVL---------SGVYPhGTYEG---------------EIIFEGEE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 91 yrqleaaLQQANERNDGHA-IATVHGKL---------------------DAIDAWTIRSRAASLLHGLGFsNEQLERPVS 148
Cdd:PRK13549 71 -------LQASNIRDTERAgIAIIHQELalvkelsvleniflgneitpgGIMDYDAMYLRAQKLLAQLKL-DINPATPVG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 149 DFSGGWRMRLNLAQALICRSDLLLLDEPTNHL-DLDAVIWLE--KWLKGYTGTLILISHDRDFLDPIVDKI 216
Cdd:PRK13549 143 NLGLGQQQLVEIAKALNKQARLLILDEPTASLtESETAVLLDiiRDLKAHGIACIYISHKLNEVKAISDTI 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-181 |
8.48e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 50.85 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqlawvnqetpalpqpaiDyvIDGDREYR- 92
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK------------------D--VTKLPEYKr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 93 -------------------QLEAALqqanerndghAIATVHGK-------LDAIDAWTIRSRAASLlhGLGFSNeQLERP 146
Cdd:COG1101 79 akyigrvfqdpmmgtapsmTIEENL----------ALAYRRGKrrglrrgLTKKRRELFRELLATL--GLGLEN-RLDTK 145
|
170 180 190
....*....|....*....|....*....|....*
gi 490290321 147 VSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:COG1101 146 VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
17-221 |
9.45e-07 |
|
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: 49.97 E-value: 9.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQLAWVNQETPALPQPAIDYvidgdREYRQLEA 96
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERGLY-----PKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 97 ALQQANERNDGHAIAtvhgkldaidawtiRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
Cdd:cd03269 91 LVYLAQLKGLKKEEA--------------RRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490290321 177 TNHLDLDAVIWLEKW---LKGYTGTLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:cd03269 156 FSGLDPVNVELLKDVireLARAGKTVILSTHQMELVEELCDRVLLLNK 203
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-221 |
9.77e-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: 48.91 E-value: 9.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 26 PGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMtfpgnwqlawvnqetpalpqpaidYVIDGDREYRQLEAALQQANERN 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV------------------------IYIDGEDILEEVLDQLLLIIVGG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 106 DGHAIATVHgkldaidawtirsraasllhglgfsneqlerpvsdfsggwRMRLNLAQALICRSDLLLLDEPTNHLD---- 181
Cdd:smart00382 57 KKASGSGEL----------------------------------------RLRLALALARKLKPDVLILDEITSLLDaeqe 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490290321 182 -----LDAVIWLEKWLKGYTGTLILISHDRDFLDP-----IVDKIIHIEQ 221
Cdd:smart00382 97 allllLEELRLLLLLKSEKNLTVILTTNDEKDLGPallrrRFDRRIVLLL 146
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-182 |
1.00e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.12 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwQLAWVNQETPALPQPAIDYVID---GDREYRQ 93
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQ-DLLKADPEAQKLLRQKIQIVFQnpyGSLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 94 -----LEAALqqanerndghAIATvhgKLDAIDAwtiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRS 168
Cdd:PRK11308 110 kvgqiLEEPL----------LINT---SLSAAER---REKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDP 173
|
170
....*....|....
gi 490290321 169 DLLLLDEPTNHLDL 182
Cdd:PRK11308 174 DVVVADEPVSALDV 187
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-220 |
1.01e-06 |
|
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: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIRRGV-RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLkNEI-SADGGSMTFPGNWQLAWVNQETpalpqp 79
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLwPWGSGRIGMPEGEDLLFLPQRP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 80 aidYVIDGdreyrqleaalqqanerndghaiatvhgkldaidawTIRsraasllhglgfsnEQLERPVSD-FSGGWRMRL 158
Cdd:cd03223 74 ---YLPLG------------------------------------TLR--------------EQLIYPWDDvLSGGEQQRL 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490290321 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTGTLILISHdRDFLDPIVDKIIHIE 220
Cdd:cd03223 101 AFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
312-484 |
1.19e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 50.40 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG------------EL--QPVSGEIGLAKGIK- 376
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagshiELlgRTVQREGRLARDIRk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 377 ----LGY-FAQHQL------------------EFLRadeSPLQHLARLAPQELEQKLRDyLGGFGFQGDKVSEetrrFSG 433
Cdd:PRK09984 84 sranTGYiFQQFNLvnrlsvlenvligalgstPFWR---TCFSWFTREQKQRALQALTR-VGMVHFAHQRVST----LSG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490290321 434 GEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF---EGALVVVS 484
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqnDGITVVVT 209
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-186 |
1.22e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 2 IVFSSLQIR--RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqetpalpQP 79
Cdd:PTZ00243 1309 LVFEGVQMRyrEGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG---------------RE 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 80 AIDYvidGDREYRQLEAALQQANERNDGHAIATVHGKLDAIDA--WT------IRSRAASllhglgfSNEQLERPV---- 147
Cdd:PTZ00243 1374 IGAY---GLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAevWAalelvgLRERVAS-------ESEGIDSRVlegg 1443
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490290321 148 SDFSGGWRMRLNLAQALICR-SDLLLLDEPTNHLD--LDAVI 186
Cdd:PTZ00243 1444 SNYSVGQRQLMCMARALLKKgSGFILMDEATANIDpaLDRQI 1485
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
324-462 |
1.24e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.47 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 324 ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGI-------------KLGYFAQ---HQLEF 387
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-YVDGLdtsdeenlwdirnKAGMVFQnpdNQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 388 LRADES----PlQHLArLAPQELEQKLRDYLGGFGFQgdkvseETRRF-----SGGEKARLVLALIVWQRPNLLLLDEPT 458
Cdd:PRK13633 101 TIVEEDvafgP-ENLG-IPPEEIRERVDESLKKVGMY------EYRRHaphllSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
....
gi 490290321 459 NHLD 462
Cdd:PRK13633 173 AMLD 176
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-176 |
1.32e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.15 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGN-------WQLAWVNQETPALPQP 79
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamsrSRLYTVRKRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 80 A--------IDYVIDGDREYRQLEAALQQanerndghaiATVHGKLDAIDawtIRSrAASLLhglgfsneqlerPvSDFS 151
Cdd:PRK11831 93 GalftdmnvFDNVAYPLREHTQLPAPLLH----------STVMMKLEAVG---LRG-AAKLM------------P-SELS 145
|
170 180
....*....|....*....|....*
gi 490290321 152 GGWRMRLNLAQALICRSDLLLLDEP 176
Cdd:PRK11831 146 GGMARRAALARAIALEPDLIMFDEP 170
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-204 |
1.37e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.42 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGsmtfpgnwQLAWVNQEtpalpqpa 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAG--------EVLWQGEP-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 idyvIDGDRE-YRQLEAALqqanerndGHA---------------IATVHGKLDAIDAWTIRSRAasllhGL-GFsnEQL 143
Cdd:PRK13538 65 ----IRRQRDeYHQDLLYL--------GHQpgikteltalenlrfYQRLHGPGDDEALWEALAQV-----GLaGF--EDV 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 144 erPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYT---GTLILISH 204
Cdd:PRK13538 126 --PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAeqgGMVILTTH 187
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
322-369 |
1.38e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.18 E-value: 1.38e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 490290321 322 YGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI 369
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEI 58
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
323-462 |
1.42e-06 |
|
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: 49.16 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 323 GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--ELQPVSGEI---GLAKGIKL----GYFAQHQLeflrades 393
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEIlinGRPLDKNFqrstGYVEQQDV-------- 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 394 plqHLArlapqelEQKLRDYLggfgfqgdKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:cd03232 90 ---HSP-------NLTVREAL--------RFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
16-221 |
1.56e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.47 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 16 LLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG---------NWQLAWVNQETpALpqpaidyvid 86
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlharDRKVGFVFQHY-AL---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 87 gdreYRQLEAAlqqanernDGHAIA-TVHGKLDAIDAWTIRSRAASLLHGLgfsneQL----ERPVSDFSGGWRMRLNLA 161
Cdd:PRK10851 86 ----FRHMTVF--------DNIAFGlTVLPRRERPNAAAIKAKVTQLLEMV-----QLahlaDRYPAQLSGGQKQRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 162 QALICRSDLLLLDEPTNHLDLDAVIWLEKWLKG----YTGTLILISHDRDFLDPIVDKII-----HIEQ 221
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQlheeLKFTSVFVTHDQEEAMEVADRVVvmsqgNIEQ 217
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
310-505 |
1.61e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 50.80 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 310 NPLLKMEKVSAGYGERIILDSIKLNL---------VPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYF 380
Cdd:PRK10070 17 HPQRAFKYIEQGLSKEQILEKTGLSLgvkdaslaiEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQV-LIDGVDIAKI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 381 AQHQLEFLRADESPL--------------------QHLARLAPQELEQKLRDYLGGFGFQgDKVSEETRRFSGGEKARLV 440
Cdd:PRK10070 96 SDAELREVRRKKIAMvfqsfalmphmtvldntafgMELAGINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 441 LALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK10070 175 LARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAkhqrTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
345-500 |
1.74e-06 |
|
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: 49.14 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 345 GRNGAGKSTLIKL----LAGELQPVSgeiglakgiklgYFAQHQLEFLRADESPLQ-HLA-RLAPQ---ELEQKLRDYLG 415
Cdd:cd03240 29 GQNGAGKTTIIEAlkyaLTGELPPNS------------KGGAHDPKLIREGEVRAQvKLAfENANGkkyTITRSLAILEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 416 G-FGFQGD--KVSEETR-RFSGGEKA------RLVLALIVWQRPNLLLLDEPTNHLDldmRQALTEALID-FEGA----- 479
Cdd:cd03240 97 ViFCHQGEsnWPLLDMRgRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD---EENIEESLAEiIEERksqkn 173
|
170 180
....*....|....*....|...
gi 490290321 480 --LVVVSHDRHLIRStTDDLYLV 500
Cdd:cd03240 174 fqLIVITHDEELVDA-ADHIYRV 195
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
16-227 |
2.00e-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: 49.85 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 16 LLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQLAWVNQETPA---LPQPAIDYV------ID 86
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAfgvIPQKVFIFSgtfrknLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 87 GDREYRQlEAALQQANERNDGHAIATVHGKLDaidaWTIRSRAASLLHGlgfsNEQLerpvsdfsggwrmrLNLAQALIC 166
Cdd:cd03289 99 PYGKWSD-EEIWKVAEEVGLKSVIEQFPGQLD----FVLVDGGCVLSHG----HKQL--------------MCLARSVLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290321 167 RSDLLLLDEPTNHLDLDAVIWLEKWLK-GYTGTLILISHDRdfLDPIVD--KIIHIEQQTMFEY 227
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKqAFADCTVILSEHR--IEAMLEcqRFLVIEENKVRQY 217
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-485 |
2.13e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.53 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 322 YGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--ELQP---VSGEIGL-AKGIklgyFAQHQLEFLRADESPL 395
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPearVSGEVYLdGQDI----FKMDVIELRRRVQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 396 Q------------------HLARLAP--QELEQKLRDYLGGFGFQ---GDKVSEETRRFSGGEKARLVLALIVWQRPNLL 452
Cdd:PRK14247 89 QipnpipnlsifenvalglKLNRLVKskKELQERVRWALEKAQLWdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190
....*....|....*....|....*....|....*
gi 490290321 453 LLDEPTNHLDLDMRQALTEALIDF--EGALVVVSH 485
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELkkDMTIVLVTH 203
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
310-536 |
2.19e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.88 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 310 NPLLKMEKVSAGY--GERII--LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAkGIKLGYFAQHQL 385
Cdd:PRK10535 2 TALLELKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVA-GQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 386 EFLRADE--------SPLQHL------------ARLAPQELEQKLRDYLGGFGFqGDKVSEETRRFSGGEKARLVLALIV 445
Cdd:PRK10535 81 AQLRREHfgfifqryHLLSHLtaaqnvevpavyAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 446 WQRPNLLLLDEPTNHLDL---DMRQALTEALIDFEGALVVVSHDRHlIRSTTDDLYLVHDGKVepfdgdledyqqwLSDS 522
Cdd:PRK10535 160 MNGGQVILADEPTGALDShsgEEVMAILHQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEI-------------VRNP 225
|
250
....*....|....
gi 490290321 523 QKQESQSGEAPKES 536
Cdd:PRK10535 226 PAQEKVNVAGGTEP 239
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
323-473 |
2.46e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.43 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 323 GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQP---VSGEIGL------AKGIKL--GYFAQHQLEF---- 387
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLngmpidAKEMRAisAYVQQDDLFIptlt 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 388 ----------LRADESPLQHLARLAPQELEQKL-----RDYLGGfgfqgdkVSEETRRFSGGEKARLVLALIVWQRPNLL 452
Cdd:TIGR00955 116 vrehlmfqahLRMPRRVTKKEKRERVDEVLQALglrkcANTRIG-------VPGRVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180
....*....|....*....|.
gi 490290321 453 LLDEPTNHLDLDMRQALTEAL 473
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVL 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
143-205 |
2.77e-06 |
|
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: 48.87 E-value: 2.77e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 143 LERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL----DAVIWLEKWLKGYTGTLILISHD 205
Cdd:cd03299 123 LNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVrtkeKLREELKKIRKEFGVTVLHVTHD 189
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-177 |
2.78e-06 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 48.58 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPQPA-----IDYVIDGDREY 91
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG--------RDITGLPPHEraragIGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 92 RQLeaalqqanerndghaiaTVHGKLD-AIDAWTIRSRAASL---------LHglgfsnEQLERPVSDFSGGWRMRLNLA 161
Cdd:cd03224 88 PEL-----------------TVEENLLlGAYARRRAKRKARLervyelfprLK------ERRKQLAGTLSGGEQQMLAIA 144
|
170
....*....|....*.
gi 490290321 162 QALICRSDLLLLDEPT 177
Cdd:cd03224 145 RALMSRPKLLLLDEPS 160
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-181 |
2.81e-06 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 49.69 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFpgnwqlawvnqetpalpqpa 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 idyvidGDREYRQLEAAlqqanERNdghaIA------------TVHG------KLDAIDAWTIRSR---AASLLhGLGfs 139
Cdd:COG3839 63 ------GGRDVTDLPPK-----DRN----IAmvfqsyalyphmTVYEniafplKLRKVPKAEIDRRvreAAELL-GLE-- 124
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490290321 140 nEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:COG3839 125 -DLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
322-462 |
2.88e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 48.86 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 322 YGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLA------------KGI-----KLGY-FAQH 383
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAgnhfdfsktpsdKAIrelrrNVGMvFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 384 QL-------EFL-------------RADESPLQHLARLapqeleqKLRDYLGGFGFQgdkvseetrrFSGGEKARLVLAL 443
Cdd:PRK11124 92 NLwphltvqQNLieapcrvlglskdQALARAEKLLERL-------RLKPYADRFPLH----------LSGGQQQRVAIAR 154
|
170
....*....|....*....
gi 490290321 444 IVWQRPNLLLLDEPTNHLD 462
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALD 173
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-181 |
2.99e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.72 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQLAWVNQETPALpqpaidyvidgdreY 91
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL--------------R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 92 RQLEAALQQAN---ERN--DGHAIATVHGKLDAIDawtIRSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALIC 166
Cdd:PRK10908 79 RQIGMIFQDHHllmDRTvyDNVAIPLIIAGASGDD---IRRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVN 154
|
170
....*....|....*
gi 490290321 167 RSDLLLLDEPTNHLD 181
Cdd:PRK10908 155 KPAVLLADEPTGNLD 169
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
328-584 |
3.02e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.27 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI---GLAKGIKLGYFAQHQLEFLRADEspLQHLARLAPQ 404
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVdikGSAALIAISSGLNGQLTGIENIE--LKGLMMGLTK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 405 ELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFE---GALV 481
Cdd:PRK13545 118 EKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKeqgKTIF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 482 VVSHDRHLIRSTTDDLYLVHDGKVEPFdGDLED----YQQWLsdsqkqesqsgeapKESGNSAQARKDQKRREAELRSQT 557
Cdd:PRK13545 198 FISHSLSQVKSFCTKALWLHYGQVKEY-GDIKEvvdhYDEFL--------------KKYNQMSVEERKDFREEQISQFQH 262
|
250 260
....*....|....*....|....*..
gi 490290321 558 QPLRKEIARLEKEMDKLNAQLASAEEK 584
Cdd:PRK13545 263 GLLQEDQTGRERKRKKGKKTSRKFKKK 289
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
126-244 |
3.95e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.81 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 126 RSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKGYTGTLILI 202
Cdd:PRK10619 129 RERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVV 208
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 490290321 203 SHDRDFLDPIVDKIIHIEQQTMFEYTGNYSSFEVQRATRLAQ 244
Cdd:PRK10619 209 THEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQ 250
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
328-505 |
4.11e-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: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQP---VSGEIgLAKGIKLGYFAQHQLEFLRADE----------S- 393
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEI-LFDGEDLLKLSEKELRKIRGREiqmifqdpmtSl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 394 ------------PLQHLARLAPQELEQKLRDYLggfgfqgDKV--SEETRR-------FSGGEKARLVLA--LIVwqRPN 450
Cdd:COG0444 100 npvmtvgdqiaePLRIHGGLSKAEARERAIELL-------ERVglPDPERRldrypheLSGGMRQRVMIAraLAL--EPK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 451 LLLLDEPTNHLD-------LDMRQALTEaliDFEGALVVVSHDRHLIRSTTDD---LYLvhdGKV 505
Cdd:COG0444 171 LLIADEPTTALDvtiqaqiLNLLKDLQR---ELGLAILFITHDLGVVAEIADRvavMYA---GRI 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-207 |
4.40e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.93 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMtfpgNWQL-AWVNQETPALPQPAIDYVIDGDREYRQL- 94
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI----EWIFkDEKNKKKTKEKEKVLEKLVIQKTRFKKIk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 95 ----------------EAALQQANERND---GhAIATVHGKLDAidawtiRSRAASLLHGLGFSNEQLERPVSDFSGGWR 155
Cdd:PRK13651 99 kikeirrrvgvvfqfaEYQLFEQTIEKDiifG-PVSMGVSKEEA------KKRAAKYIELVGLDESYLQRSPFELSGGQK 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 156 MRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYT---GTLILISHDRD 207
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNkqgKTIILVTHDLD 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-205 |
4.52e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.49 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 16 LLDNATATINPGQKVGLVGKNGCGKSTLLSLLkNEISADGGSMTFPGnwQLAWVNQETpalpqpaIDYVIDGDREYRQLE 95
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEG--RVEFFNQNI-------YERRVNLNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 96 AALQQAN------ERNDGHAIATV--HGKLDAIDAWTIRSRAASLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQALICR 167
Cdd:PRK14258 92 MVHPKPNlfpmsvYDNVAYGVKIVgwRPKLEIDDIVESALKDADLWDEI---KHKIHKSALDLSGGQQQRLCIARALAVK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490290321 168 SDLLLLDEPTNHLDLDAVIWLEKWLKGYT----GTLILISHD 205
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHN 210
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-181 |
4.67e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.71 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG---------NW--QLAWVNQeTP----------- 74
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDipltklqldSWrsRLAVVSQ-TPflfsdtvanni 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 75 ALPQPaidyvidgDREYRQLEAALQQANerndghaiatVHgklDAIdawtirsraasLLHGLGFSNEQLERPVSdFSGGW 154
Cdd:PRK10789 410 ALGRP--------DATQQEIEHVARLAS----------VH---DDI-----------LRLPQGYDTEVGERGVM-LSGGQ 456
|
170 180
....*....|....*....|....*..
gi 490290321 155 RMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:PRK10789 457 KQRISIARALLLNAEILILDDALSAVD 483
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
17-235 |
5.88e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 48.09 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqlawvnqeTPALPQPAIDYVIdgdREYRQ-LE 95
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGH---------QFDFSQKPSEKAI---RLLRQkVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 96 AALQQAN-------ERNDGHAIATVHG--KLDAIDawtirsRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALIC 166
Cdd:COG4161 86 MVFQQYNlwphltvMENLIEAPCKVLGlsKEQARE------KAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490290321 167 RSDLLLLDEPTNHLD---LDAVIWLEKWLKGyTG-TLILISHDRDFLDPIVDKIIHIEQQTMFEYtGNYSSFE 235
Cdd:COG4161 159 EPQVLLFDEPTAALDpeiTAQVVEIIRELSQ-TGiTQVIVTHEVEFARKVASQVVYMEKGRIIEQ-GDASHFT 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
311-360 |
5.95e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 5.95e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG 360
Cdd:PRK13549 4 YLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
323-462 |
6.10e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 323 GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQP--VSGEIGLAKGIKL--------GYFAQH--QLEFLRA 390
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgvITGGDRLVNGRPLdssfqrsiGYVQQQdlHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 DESpLQHLARL-APQELEQK--------------LRDYLGGF-GFQGDKVSEETRRfsggekaRLVLALIVWQRPNLLL- 453
Cdd:TIGR00956 854 RES-LRFSAYLrQPKSVSKSekmeyveeviklleMESYADAVvGVPGEGLNVEQRK-------RLTIGVELVAKPKLLLf 925
|
....*....
gi 490290321 454 LDEPTNHLD 462
Cdd:TIGR00956 926 LDEPTSGLD 934
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
5-223 |
6.94e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.06 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 5 SSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPQPAI--- 81
Cdd:PRK11300 9 SGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG--------QHIEGLPGHQIarm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 82 ------DYVidgdREYRQ-------LEAALQQANERNDGHAIATV---HGKLDAIDawtirsRAASLLHGLG---FSNeq 142
Cdd:PRK11300 81 gvvrtfQHV----RLFREmtvienlLVAQHQQLKTGLFSGLLKTPafrRAESEALD------RAATWLERVGlleHAN-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 143 leRPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHL------DLDAVIwlEKWLKGYTGTLILISHDRDFLDPIVDKI 216
Cdd:PRK11300 149 --RQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLnpketkELDELI--AELRNEHNVTVLLIEHDMKLVMGISDRI 224
|
....*..
gi 490290321 217 IHIEQQT 223
Cdd:PRK11300 225 YVVNQGT 231
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-230 |
6.98e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.10 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 16 LLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISAD--GGSMTFPGnwqlAWVNQETP----------ALPQP-AID 82
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKG----ESILDLEPeerahlgiflAFQYPiEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 83 YVIDGDReyrqLEAAL---QQANERNDghaiatvhgkLDAIDAWTIRSRAASLLhglGFSNEQLERPVSD-FSGGWRMRL 158
Cdd:CHL00131 98 GVSNADF----LRLAYnskRKFQGLPE----------LDPLEFLEIINEKLKLV---GMDPSFLSRNVNEgFSGGEKKRN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEK---WLKGYTGTLILISHDRDFLDPIVDKIIHIEQQTMFEYTGN 230
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEginKLMTSENSIILITHYQRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
328-500 |
7.13e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.17 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQ------PVSGEIGLAKGI-----KLGY-FAQHQLEFLRA---DE 392
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEefegkvKIDGELLTAENVwnlrrKIGMvFQNPDNQFVGAtveDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 393 SPLQHLARLAP-QELEQKLRDYLGGFGFQgDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTE 471
Cdd:PRK13642 103 VAFGMENQGIPrEEMIKRVDEALLAVNML-DFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190
....*....|....*....|....*....|.
gi 490290321 472 ALIDFEGA--LVVVSHDRHLIRSTTDDLYLV 500
Cdd:PRK13642 182 VIHEIKEKyqLTVLSITHDLDEAASSDRILV 212
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-252 |
7.19e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.77 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKS----TLLSLLKNEISADGGSMTFPGnwqlawvnqeTPALPQpaidyvidgdr 89
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDG----------KPVAPC----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 EYRQLEAALQQANER---NDGHAIATvHGK--LDAIDAWTIRSRAASLLHGLGFSNEQ--LERPVSDFSGGWRMRLNLAQ 162
Cdd:PRK10418 75 ALRGRKIATIMQNPRsafNPLHTMHT-HARetCLALGKPADDATLTAALEAVGLENAArvLKLYPFEMSGGMLQRMMIAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 163 ALICRSDLLLLDEPTNhlDLDAVI------WLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIEQQTMFEYTGNYSSFEV 236
Cdd:PRK10418 154 ALLCEAPFIIADEPTT--DLDVVAqarildLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
250 260
....*....|....*....|
gi 490290321 237 QR--ATR--LAQQQAMYESQ 252
Cdd:PRK10418 232 PKhaVTRslVSAHLALYGME 251
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
324-462 |
7.24e-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: 47.65 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 324 ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQP---VSGEI---GLAKGIKL-----GYFAQHQ--LEFLRA 390
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQIlfnGQPRKPDQfqkcvAYVRQDDilLPGLTV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 391 DESpLQHLARLAPQEL----EQKLRDYLGGFGFQGDKVSEETRR--FSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
Cdd:cd03234 99 RET-LTYTAILRLPRKssdaIRKKRVEDVLLRDLALTRIGGNLVkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-505 |
9.48e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.51 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWQ------------LAWVNQETPALPQP 79
Cdd:PRK15439 23 GVEVL-KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltpakahqlgIYLVPQEPLLFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 80 AIDYVI-----DGDREYRQLEAALQQANerndghaiatVHGKLDAidawtirsrAASLLHglgfsneqlerpVSDfsggw 154
Cdd:PRK15439 102 SVKENIlfglpKRQASMQKMKQLLAALG----------CQLDLDS---------SAGSLE------------VAD----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 155 RMRLNLAQALICRSDLLLLDEPTNHL---DLDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKIIHIEQQT--MFEYTG 229
Cdd:PRK15439 146 RQIVEILRGLMRDSRILILDEPTASLtpaETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTiaLSGKTA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 230 NYSSFEVQRA-TRLAQQQAMYESQQqrvahlqsyidrfrakatkakqaqsrikmlerMELIAPAHvdnpfhfsfRQPESL 308
Cdd:PRK15439 226 DLSTDDIIQAiTPAAREKSLSASQK--------------------------------LWLELPGN---------RRQQAA 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 309 PNPLLKMEKVSagyGERIIldSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLA----KGIKLGYFAQHQ 384
Cdd:PRK15439 265 GAPVLTVEDLT---GEGFR--NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNgkeiNALSTAQRLARG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 385 LEFLRAD--------ESPL----------QHLARLAPQELEQKLRDYLGGFGFQGDKVSEETRRFSGGEKARLVLALIVW 446
Cdd:PRK15439 340 LVYLPEDrqssglylDAPLawnvcalthnRRGFWIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLE 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490290321 447 QRPNLLLLDEPTNHLDLDMRQ---ALTEALIDFEGALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK15439 420 ASPQLLIVDEPTRGVDVSARNdiyQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-226 |
1.17e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 47.05 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPgnwqlawvnqetpalpqpa 80
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 81 iDYVIDGDREYRQLEAALQQANERN--------------------DGHAIATVHGKLDAIdawtirSRAASLLHGLGFSN 140
Cdd:PRK11264 64 -DITIDTARSLSQQKGLIRQLRQHVgfvfqnfnlfphrtvleniiEGPVIVKGEPKEEAT------ARARELLAKVGLAG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 141 EQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKII 217
Cdd:PRK11264 137 KETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAI 215
|
....*....
gi 490290321 218 HIEQQTMFE 226
Cdd:PRK11264 216 FMDQGRIVE 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
311-462 |
1.25e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 47.08 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL--AGELQPvsgEIGLAKGIKlgyFAQHQLEFL 388
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNP---EVTITGSIV---YNGHNIYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 389 RADESPLQ----------------------HLARLA----PQELEQKLRDYLGGFGFQG---DKVSEETRRFSGGEKARL 439
Cdd:PRK14239 78 RTDTVDLRkeigmvfqqpnpfpmsiyenvvYGLRLKgikdKQVLDEAVEKSLKGASIWDevkDRLHDSALGLSGGQQQRV 157
|
170 180
....*....|....*....|...
gi 490290321 440 VLALIVWQRPNLLLLDEPTNHLD 462
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALD 180
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
23-242 |
1.57e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 46.93 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 23 TINPGQKVGLVGKNGCGKSTLLSLLKNEISAD---GGSMTFPGNwqlawvnqetpaLPQPAIDYVIDGDREYRQLEAALQ 99
Cdd:PRK09984 26 NIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGR------------TVQREGRLARDIRKSRANTGYIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 100 QANERNDGHAIATVH-GKLDAIDAWTI---------RSRAASLLHGLGFSNEQLERpVSDFSGGWRMRLNLAQALICRSD 169
Cdd:PRK09984 94 QFNLVNRLSVLENVLiGALGSTPFWRTcfswftreqKQRALQALTRVGMVHFAHQR-VSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 170 LLLLDEPTNHLDLDAVIWLEKWLKGYTG----TLILISHDRDFLDPIVDKIIHIEQQTMFeYTGNYSSFEVQRATRL 242
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVALRQGHVF-YDGSSQQFDNERFDHL 248
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-217 |
1.60e-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: 46.50 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEIsaDGGSMTFpGnwQLAWVNQE-TPALPQPAIDYVIDGD---- 88
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTTS-G--QILFNGQPrKPDQFQKCVAYVRQDDillp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 89 ----REYRQLEAALQQANERNDGhaiatVHGKLDAIdawtIRSRAASLLHgLGFSNeqlerpVSDFSGGWRMRLNLAQAL 164
Cdd:cd03234 95 gltvRETLTYTAILRLPRKSSDA-----IRKKRVED----VLLRDLALTR-IGGNL------VKGISGGERRRVSIAVQL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 165 ICRSDLLLLDEPTNHLD----LDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKII 217
Cdd:cd03234 159 LWDPKVLILDEPTSGLDsftaLNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRIL 215
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
311-505 |
1.77e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 45.89 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGYGeriiLDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKgiklgyfaqhqleflra 390
Cdd:cd03215 3 PVLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 391 desplQHLARLAPQELEQKlrdylgGFGFqgdkVSEE------------------TRRFSGGEKARLVLALIVWQRPNLL 452
Cdd:cd03215 62 -----KPVTRRSPRDAIRA------GIAY----VPEDrkreglvldlsvaenialSSLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 453 LLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELadAGkAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-228 |
2.09e-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: 48.02 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTL-LSLL------KNEISADGGSMTFPG----NWQLAWVNQEtP 74
Cdd:TIGR00957 1291 CLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFrinesaEGEIIIDGLNIAKIGlhdlRFKITIIPQD-P 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 75 ALPQPAIDYVIDGDREYRQLEA--ALQqanerndghaIATVHGkldaidawTIRSRAASLLHGLGFSNEQLerpvsdfSG 152
Cdd:TIGR00957 1370 VLFSGSLRMNLDPFSQYSDEEVwwALE----------LAHLKT--------FVSALPDKLDHECAEGGENL-------SV 1424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 153 GWRMRLNLAQALICRSDLLLLDEPTNHLDLDaviwlekwlkgyTGTLILISHDRDFLDPIVDKIIHiEQQTMFEYT 228
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTKILVLDEATAAVDLE------------TDNLIQSTIRTQFEDCTVLTIAH-RLNTIMDYT 1487
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
312-523 |
2.22e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.32 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--ELQPVSGEIGLaKGIKLGYFAQHQleflR 389
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEF-KGKDLLELSPED----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 390 ADESPLqhLARLAPQELE------------QKLRDY-----LGGFGFQgDKVSEE-----------TRR----FSGGEKA 437
Cdd:PRK09580 76 AGEGIF--MAFQYPVEIPgvsnqfflqtalNAVRSYrgqepLDRFDFQ-DLMEEKiallkmpedllTRSvnvgFSGGEKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 438 RLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTE---ALIDFEGALVVVSH-DRHLIRSTTDDLYLVHDGKVEPfDGDLE 513
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVADgvnSLRDGKRSFIIVTHyQRILDYIKPDYVHVLYQGRIVK-SGDFT 231
|
250
....*....|....*..
gi 490290321 514 DYQQ-------WLSDSQ 523
Cdd:PRK09580 232 LVKQleeqgygWLTEQQ 248
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-225 |
2.51e-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: 47.70 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGN---WQLAWVNQETPALPQPAIDYVIDGDRE 90
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdieTNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 91 YRQLEAALQqanerndGHAIATVHGKLDAidawtirsraasLLHGLGFSNEQLERpVSDFSGGWRMRLNLAQALICRSDL 170
Cdd:TIGR01257 1023 HILFYAQLK-------GRSWEEAQLEMEA------------MLEDTGLHHKRNEE-AQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 171 LLLDEPTNHLDLDA--VIWlEKWLKGYTG-TLILISHDRDFLDPIVDKIIHIEQQTMF 225
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSrrSIW-DLLLKYRSGrTIIMSTHHMDEADLLGDRIAIISQGRLY 1139
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
12-244 |
2.95e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 45.78 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwQLAWVNQETPAlpqpAIdyvidgdREY 91
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN-HFDFSKTPSDK----AI-------REL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 92 RQ-LEAALQQAN-------ERNDGHAIATVHGkLDAIDAwtiRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQA 163
Cdd:PRK11124 81 RRnVGMVFQQYNlwphltvQQNLIEAPCRVLG-LSKDQA---LARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 164 LICRSDLLLLDEPTNHLDLD---AVIWLEKWLKGyTG-TLILISHDRDFLDPIVDKIIHIEQQTMFEyTGNYSSFEVQRA 239
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEitaQIVSIIRELAE-TGiTQVIVTHEVEVARKTASRVVYMENGHIVE-QGDASCFTQPQT 233
|
....*
gi 490290321 240 TRLAQ 244
Cdd:PRK11124 234 EAFKN 238
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-181 |
3.08e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 46.88 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTfpgnwqlawvnqetpalpqpaidyvIDGdREYRQLE- 95
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIL-------------------------IDG-TDIRTVTr 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 96 AALQqanerndgHAIATVH----------------GKLDAIDAwTIRsRAASLLHGLGFSNEQL--------ERPvSDFS 151
Cdd:PRK13657 405 ASLR--------RNIAVVFqdaglfnrsiednirvGRPDATDE-EMR-AAAERAQAHDFIERKPdgydtvvgERG-RQLS 473
|
170 180 190
....*....|....*....|....*....|
gi 490290321 152 GGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
126-293 |
3.38e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.27 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 126 RSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTnhldldaviwlekwlkgyTGtlilishd 205
Cdd:NF000106 122 RARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT------------------TG-------- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 206 rdfLDPIVDKIIHIEQQTMFEytgnyssfevQRATRLAQQQAMYESQQqrVAHLQSYIDRFRAKAtKAKQAQSRIKMLER 285
Cdd:NF000106 175 ---LDPRTRNEVWDEVRSMVR----------DGATVLLTTQYMEEAEQ--LAHELTVIDRGRVIA-DGKVDELKTKVGGR 238
|
....*...
gi 490290321 286 MELIAPAH 293
Cdd:NF000106 239 TLQIRPAH 246
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
328-485 |
3.56e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 45.40 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLARLAPQELE 407
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 408 -----------QKLRDYLGGFGFQGD----------KVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD-- 464
Cdd:cd03290 97 enitfgspfnkQRYKAVTDACSLQPDidllpfgdqtEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHls 176
|
170 180
....*....|....*....|....
gi 490290321 465 ---MRQALTEALIDFEGALVVVSH 485
Cdd:cd03290 177 dhlMQEGILKFLQDDKRTLVLVTH 200
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
311-369 |
4.22e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.54 E-value: 4.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 311 PLLKMEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI 369
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSI 61
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-216 |
4.24e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 45.84 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNwqlawvnqetpalpqpAIDYVIDGDREYRQLEA 96
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE----------------PIKYDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 97 ALQQANErndghaiatvhgklDAIDAWTIRSRAASLLHGLGFSNEQLERPVSD-----------------FSGGWRMRLN 159
Cdd:PRK13639 82 IVFQNPD--------------DQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEalkavgmegfenkpphhLSGGQKKRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 160 LAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYT--GTLILIS-HDRDFLDPIVDKI 216
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNkeGITIIIStHDVDLVPVYADKV 207
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
323-486 |
4.69e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.27 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 323 GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKllagelqpvsgEIGLAKGIKLGYFAQHqLEFLRADESPLQHLARLA 402
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILD-----------AIGLALGGAQSATRRR-SGVKAGCIVAAVSAELIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 403 pqeleqkLRDYLggfgfqgdkvseetrrfSGGEKARLVLALIV----WQRPNLLLLDEPTNHLDLDMRQALTEALIDF-- 476
Cdd:cd03227 74 -------TRLQL-----------------SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlv 129
|
170
....*....|.
gi 490290321 477 EGALV-VVSHD 486
Cdd:cd03227 130 KGAQViVITHL 140
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-207 |
4.96e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 45.49 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGsmtfpgnwqlawvnqetpalpqpaiDYVIDGDReyrqlea 96
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESG-------------------------QIIIDGDL------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 97 aLQQANERNDGHAIATVHGKLD-------------------AIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMR 157
Cdd:PRK13650 71 -LTEENVWDIRHKIGMVFQNPDnqfvgatveddvafglenkGIPHEEMKERVNEALELVGMQDFKEREP-ARLSGGQKQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490290321 158 LNLAQALICRSDLLLLDEPTNHLD----LDAVIWLEKWLKGYTGTLILISHDRD 207
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLD 202
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
276-517 |
5.71e-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: 46.48 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 276 AQSRIKMLERMELIAPAHVDNPfhfsfRQPESLPnPLLKME--KVSAGYGERI--ILDSIKLNLVPGSRIGLLGRNGAGK 351
Cdd:TIGR00957 1252 AVERLKEYSETEKEAPWQIQET-----APPSGWP-PRGRVEfrNYCLRYREDLdlVLRHINVTIHGGEKVGIVGRTGAGK 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 352 STLIKLLAGELQPVSGEIgLAKGIKLGYFAQHQLEF---------------LRADESPlqhLARLAPQELEQKLR-DYLG 415
Cdd:TIGR00957 1326 SSLTLGLFRINESAEGEI-IIDGLNIAKIGLHDLRFkitiipqdpvlfsgsLRMNLDP---FSQYSDEEVWWALElAHLK 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 416 GF-GFQGDKV----SEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQaLTEALI--DFEGALVV-VSHDR 487
Cdd:TIGR00957 1402 TFvSALPDKLdhecAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN-LIQSTIrtQFEDCTVLtIAHRL 1480
|
250 260 270
....*....|....*....|....*....|
gi 490290321 488 HLIRSTTDDLYLvHDGKVEPFDGDLEDYQQ 517
Cdd:TIGR00957 1481 NTIMDYTRVIVL-DKGEVAEFGAPSNLLQQ 1509
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
308-505 |
5.79e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.61 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 308 LPNPL-----LKMEKVSAGYGER-----IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLaKGIKL 377
Cdd:PRK13631 12 VPNPLsddiiLRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV-GDIYI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 378 GyfaqHQLEFLRADESPLQ-------HLARLA------PQ------------------------ELEQKLRDYLGGFGFQ 420
Cdd:PRK13631 91 G----DKKNNHELITNPYSkkiknfkELRRRVsmvfqfPEyqlfkdtiekdimfgpvalgvkksEAKKLAKFYLNKMGLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 421 GDKVSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG---ALVVVSHDRHLIRSTTDDL 497
Cdd:PRK13631 167 DSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEV 246
|
....*...
gi 490290321 498 YLVHDGKV 505
Cdd:PRK13631 247 IVMDKGKI 254
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-230 |
5.94e-05 |
|
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: 45.94 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 23 TINPGQKVGLVGKNGCGKSTLLSLL-------KNEISADGgsmtfpgnwqlawvnqetpalpQPaidyVIDGDRE-YRQL 94
Cdd:COG4615 354 TIRRGELVFIVGGNGSGKSTLAKLLtglyrpeSGEILLDG----------------------QP----VTADNREaYRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 95 EAALqqaneRNDGHAIATVHGKLDAIDAwtirSRAASLLHGLgfsneQLERPVS---------DFSGGWRMRLNLAQALI 165
Cdd:COG4615 408 FSAV-----FSDFHLFDRLLGLDGEADP----ARARELLERL-----ELDHKVSvedgrfsttDLSQGQRKRLALLVALL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 166 CRSDLLLLDEptnhldldaviW---------------LEKWLKGYTGTLILISHDRDFLDpIVDKIIHIEQQTMFEYTGN 230
Cdd:COG4615 474 EDRPILVFDE-----------WaadqdpefrrvfyteLLPELKARGKTVIAISHDDRYFD-LADRVLKMDYGKLVELTGP 541
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
315-369 |
7.08e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 7.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 315 MEKVSAGYGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI 369
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 55
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-287 |
7.98e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEIS-ADGGSMTFPGNwqLAWVNQETPALPQPAIDYVIDG-----DRE 90
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShAETSSVVIRGS--VAYVPQVSWIFNATVRENILFGsdfesERY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 91 YRQLEA-ALQQANERNDGHAIATVHgkldaidawtirsraasllhglgfsneqlERPVsDFSGGWRMRLNLAQALICRSD 169
Cdd:PLN03232 711 WRAIDVtALQHDLDLLPGRDLTEIG-----------------------------ERGV-NISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 170 LLLLDEPTNHLD-------LDAVIWLEkwLKGytGTLILISHDRDFLdPIVDKIIHI------EQQTMFEYTGNYSSFE- 235
Cdd:PLN03232 761 IYIFDDPLSALDahvahqvFDSCMKDE--LKG--KTRVLVTNQLHFL-PLMDRIILVsegmikEEGTFAELSKSGSLFKk 835
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490290321 236 -VQRATRLAQQQAMYESQQQrVAHLQSY--IDRFRAKATKAKQAQSRIKMLERME 287
Cdd:PLN03232 836 lMENAGKMDATQEVNTNDEN-ILKLGPTvtIDVSERNLGSTKQGKRGRSVLVKQE 889
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
16-182 |
8.23e-05 |
|
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: 44.51 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 16 LLDNATATINPGQKVGLVGKNGCGKSTL-------LSLLKNEISADGGSMT-FPGNW---QLAWVNQEtPALPQPAIDYV 84
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIVIDGIDISkLPLHTlrsRLSIILQD-PILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 85 IDGDREYR--QLEAALQQANERNdghAIATVHGKLDAIdawtirsraasllhglgfsneqLERPVSDFSGGWRMRLNLAQ 162
Cdd:cd03288 115 LDPECKCTddRLWEALEIAQLKN---MVKSLPGGLDAV----------------------VTEGGENFSVGQRQLFCLAR 169
|
170 180
....*....|....*....|
gi 490290321 163 ALICRSDLLLLDEPTNHLDL 182
Cdd:cd03288 170 AFVRKSSILIMDEATASIDM 189
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
309-505 |
9.60e-05 |
|
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: 45.45 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 309 PNPLLKMEKVS----AGYGERIILDSIKLNLVPGSRIGLLGRNGAGKS----TLIKLLAGELQPVSGEIGLaKGIKLGYF 380
Cdd:COG4172 3 SMPLLSVEDLSvafgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILF-DGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 381 AQHQLEFLRADE------------SPLQ------------HLaRLAPQELEQKLRDYLggfgfqgDKV--SEETRR---- 430
Cdd:COG4172 82 SERELRRIRGNRiamifqepmtslNPLHtigkqiaevlrlHR-GLSGAAARARALELL-------ERVgiPDPERRlday 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 431 ---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLD-------LDMRQALTEALidfeG-ALVVVSHDRHLIRSTTDDLYL 499
Cdd:COG4172 154 phqLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqaqiLDLLKDLQREL----GmALLLITHDLGVVRRFADRVAV 229
|
....*.
gi 490290321 500 VHDGKV 505
Cdd:COG4172 230 MRQGEI 235
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-217 |
1.00e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 44.73 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKStlLSLLkneisADGGSMTFPGNW---QLAWVNQETPALPqpaidyvidgDREYRQ 93
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKS--VSSL-----AIMGLIDYPGRVmaeKLEFNGQDLQRIS----------EKERRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 94 L---EAALQQANERNDGHAIATVHGK-LDAIDAW------TIRSRAASLLHGLGFSN--EQLERPVSDFSGGWRMRLNLA 161
Cdd:PRK11022 86 LvgaEVAMIFQDPMTSLNPCYTVGFQiMEAIKVHqggnkkTRRQRAIDLLNQVGIPDpaSRLDVYPHQLSGGMSQRVMIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490290321 162 QALICRSDLLLLDEPTNHLD-------LDAVIWLEkwlKGYTGTLILISHDRDFLDPIVDKII 217
Cdd:PRK11022 166 MAIACRPKLLIADEPTTALDvtiqaqiIELLLELQ---QKENMALVLITHDLALVAEAAHKII 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-485 |
1.01e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.45 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 322 YGERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIK-----LLAGELQPVSGEIGL------------------------- 371
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLfgrniyspdvdpievrrevgmvfqy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 372 -------------AKGIKLGYFAQHQLEFLRADESPLQHLARLapQELEQKLRDYLGgfgfqgdkvseetrRFSGGEKAR 438
Cdd:PRK14267 94 pnpfphltiydnvAIGVKLNGLVKSKKELDERVEWALKKAALW--DEVKDRLNDYPS--------------NLSGGQRQR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490290321 439 LVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVVVSH 485
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTH 206
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
125-226 |
1.03e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 44.77 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 125 IRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGY----TGTLI 200
Cdd:PRK13646 121 VKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqtdeNKTII 200
|
90 100
....*....|....*....|....*.
gi 490290321 201 LISHDRDFLDPIVDKIIHIEQQTMFE 226
Cdd:PRK13646 201 LVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
430-505 |
1.04e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 44.73 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 430 RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHDRHLIRSTTDDLYLVHDGKV 505
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkenmALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| F-BAR_PACSIN1 |
cd07680 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ... |
511-633 |
1.06e-04 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153364 [Multi-domain] Cd Length: 258 Bit Score: 44.27 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 511 DLEDYQQWLSDSQKQESQSGeapkesgnsaqaRKDQKRREAELRSQTQPLRKEIARLEKEmdKLNAQLASAEEKLGDSEl 590
Cdd:cd07680 91 DLEKVKNWQKDAYHKQIMGG------------FKETKEAEDGFRKAQKPWAKKMKELEAA--KKAYHLACKEEKLAMTR- 155
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 490290321 591 yDASRKAELTECLQQQASAKSGLEECEMAWLEAQEQLERMLQE 633
Cdd:cd07680 156 -EANSKAEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLDD 197
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
126-217 |
1.09e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.84 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 126 RSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKGYTGTLILI 202
Cdd:PRK13631 153 KKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGeheMMQLILDAKANNKTVFVI 232
|
90
....*....|....*
gi 490290321 203 SHDRDFLDPIVDKII 217
Cdd:PRK13631 233 THTMEHVLEVADEVI 247
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
311-505 |
1.17e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 311 PLLKMEKVSAGY----GERIILDSIKLNLVPGSRIGLLGRNGAGKS----TLIKLLAGElqPV---SGEIglakgiklgY 379
Cdd:PRK15134 4 PLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSP--PVvypSGDI---------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 380 FAQHQLefLRADESPLQHL-------------ARLAP-QELEQKLRDYLG---------------------GFGFQGDKV 424
Cdd:PRK15134 73 FHGESL--LHASEQTLRGVrgnkiamifqepmVSLNPlHTLEKQLYEVLSlhrgmrreaargeilncldrvGIRQAAKRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 425 SEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR----QALTEALIDFEGALVVVSHDRHLIRSTTDDLYLV 500
Cdd:PRK15134 151 TDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQaqilQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM 230
|
....*
gi 490290321 501 HDGKV 505
Cdd:PRK15134 231 QNGRC 235
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
10-216 |
1.30e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 44.64 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqetpalpqpaIDYVIDGDR 89
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG------------------VDIAKISDA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 90 EYRQLEA----------ALQQANERNDGHAIATvhgKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLN 159
Cdd:PRK10070 99 ELREVRRkkiamvfqsfALMPHMTVLDNTAFGM---ELAGINAEERREKALDALRQVGLENYAHSYP-DELSGGMRQRVG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 160 LAQALICRSDLLLLDEPTNHLD----LDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKI 216
Cdd:PRK10070 175 LARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRI 235
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
512-633 |
1.30e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 512 LEDYQQWLSDSQKQESQSGeapKESGNSAQARKDQKRREAELRSQTQPLRKEIARLEKEMDKLNAQLASAEEKLGDSELY 591
Cdd:COG1196 276 LEELELELEEAQAEEYELL---AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 490290321 592 DASRKAELTECLQQQASAKSGLEECEMAWLEAQEQLERMLQE 633
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
11-216 |
1.34e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.02 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 11 RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnqetpalpQPAIDYVIdgdRE 90
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG---------------EPITKENI---RE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 91 YRQLEAALQQanERNDGHAIATVHGKLD------AIDAWTIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQAL 164
Cdd:PRK13652 76 VRKFVGLVFQ--NPDDQIFSPTVEQDIAfgpinlGLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490290321 165 ICRSDLLLLDEPTNHLD----LDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKI 216
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYI 208
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
12-54 |
1.51e-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: 44.09 E-value: 1.51e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 490290321 12 GVRVLldNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISAD 54
Cdd:cd01136 54 GVRAI--DGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDAD 94
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
17-222 |
2.73e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 43.78 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwqlawvnQETPALPQpaidyvidgdrEYRQLEA 96
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG--------QDITHVPA-----------ENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 97 ALQQanerndgHAI---ATVHG------KLDAIDAWTIRSRAASLLHGLgfsneQLE----RPVSDFSGGWRMRLNLAQA 163
Cdd:PRK09452 91 VFQS-------YALfphMTVFEnvafglRMQKTPAAEITPRVMEALRMV-----QLEefaqRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490290321 164 LICRSDLLLLDEPTNHLD--LDAVIWLE-KWLKGYTG-TLILISHDRDFLDPIVDKII-----HIEQQ 222
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDykLRKQMQNElKALQRKLGiTFVFVTHDQEEALTMSDRIVvmrdgRIEQD 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
129-221 |
3.05e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 43.18 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 129 AASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGY--TG-TLILISHD 205
Cdd:PRK13643 124 AAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhqSGqTVVLVTHL 203
|
90
....*....|....*.
gi 490290321 206 RDFLDPIVDKIIHIEQ 221
Cdd:PRK13643 204 MDDVADYADYVYLLEK 219
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
312-492 |
3.28e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.17 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 312 LLKMEKVSAGYGERIILDsIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI--------GLAK---------- 373
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyykncninNIAKpyctyighnl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 374 GIKLGYFAQHQLEFLradeSPLQHLARLAPQELEQ-KLRDYLggfgfqgdkvSEETRRFSGGEKARLVLALIVWQRPNLL 452
Cdd:PRK13541 80 GLKLEMTVFENLKFW----SEIYNSAETLYAAIHYfKLHDLL----------DEKCYSLSSGMQKIVAIARLIACQSDLW 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490290321 453 LLDEPTNHLDLDMRQALTEALI---DFEGALVVVSHDRHLIRS 492
Cdd:PRK13541 146 LLDEVETNLSKENRDLLNNLIVmkaNSGGIVLLSSHLESSIKS 188
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
312-369 |
3.75e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 43.25 E-value: 3.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 490290321 312 LLKMEKVSAGYGERII-LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEI 369
Cdd:PRK11153 4 LKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV 62
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-182 |
3.90e-04 |
|
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: 43.75 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 16 LLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGnwQLAWVNQETPALPQPAIDYVIDGDR--EYRq 93
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RISFSPQTSWIMPGTIKDNIIFGLSydEYR- 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 94 leaalqqanerndghaiatvhgkldaidaWTIRSRAASLLHGLGFSNEQLERPVSD----FSGGWRMRLNLAQALICRSD 169
Cdd:TIGR01271 518 -----------------------------YTSVIKACQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDAD 568
|
170
....*....|...
gi 490290321 170 LLLLDEPTNHLDL 182
Cdd:TIGR01271 569 LYLLDSPFTHLDV 581
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
24-217 |
3.98e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 43.09 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 24 INPGQKVGLVGKNGCGKSTLLSLLK--NEISAdgGSMtFPGNWQlawVNQETPAlpQPAIDYVIDGDREYRQLEAAlqqa 101
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLLRMIAglEDITS--GDL-FIGEKR---MNDVPPA--ERGVGMVFQSYALYPHLSVA---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 102 nernDGHAIATvhgKLDAIDAWTIRSR---AASLLHgLGfsnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTN 178
Cdd:PRK11000 94 ----ENMSFGL---KLAGAKKEEINQRvnqVAEVLQ-LA---HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490290321 179 HLD----LDAVIWLEKWLKGYTGTLILISHDRDFLDPIVDKII 217
Cdd:PRK11000 163 NLDaalrVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIV 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-207 |
4.78e-04 |
|
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: 42.25 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGN---------------WQLAWVNQETP 74
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaamsrkelrelrrKKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 75 ALPQPAI-DYVIDGdreyrqLEAALQQANERndghaiatvhgkldaidawtiRSRAASLLHGLGFSNeQLERPVSDFSGG 153
Cdd:cd03294 113 LLPHRTVlENVAFG------LEVQGVPRAER---------------------EERAAEALELVGLEG-WEHKYPDELSGG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 154 WRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLEKWLKgytGTLILISHDRD 207
Cdd:cd03294 165 MQQRVGLARALAVDPDILLMDEAFSALDplirremQDELLRLQAELQ---KTIVFITHDLD 222
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
151-228 |
6.20e-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: 40.81 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 151 SGGWR----MRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKGYTGTLILISHDRDFLDPIvDKIIHIEQQT 223
Cdd:cd03227 79 SGGEKelsaLALILALASLKPRPLYILDEIDRGLDPRdgqALAEAILEHLVKGAQVIVITHLPELAELA-DKLIHIKKVI 157
|
....*
gi 490290321 224 MFEYT 228
Cdd:cd03227 158 TGVYK 162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-63 |
7.26e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.59 E-value: 7.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 490290321 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGN 63
Cdd:PRK11288 16 GVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ 66
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-226 |
8.39e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.80 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISA-DGGSMTFPGNwqLAWVNQETPALPQPAIDYVI-----DG 87
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGT--VAYVPQVSWIFNATVRDNILfgspfDP 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 88 DREYRqleaalqqanerndghaiatvhgkldAIDAwTIRSRAASLLHGlGFSNEQLERPVsDFSGGWRMRLNLAQALICR 167
Cdd:PLN03130 708 ERYER--------------------------AIDV-TALQHDLDLLPG-GDLTEIGERGV-NISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490290321 168 SDLLLLDEPTNHLDLD-AVIWLEKWLKGYTG--TLILISHDRDFLdPIVDKIIHIEQQTMFE 226
Cdd:PLN03130 759 SDVYIFDDPLSALDAHvGRQVFDKCIKDELRgkTRVLVTNQLHFL-SQVDRIILVHEGMIKE 819
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
323-514 |
9.54e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 41.60 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 323 GERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKLGYFAQHQLEFLRAD----------- 391
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSV-LVDGVDLTALSERELRAARRKigmifqhfnll 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 392 ---------ESPLQhLARLAPQELEQKLRDYLggfgfqgDKV--SEETRRF----SGGEKARlV-----LALivwqRPNL 451
Cdd:COG1135 95 ssrtvaenvALPLE-IAGVPKAEIRKRVAELL-------ELVglSDKADAYpsqlSGGQKQR-VgiaraLAN----NPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 452 LLLDEPTNHLD-----------LDMRQ--ALTealidfegaLVVVSHDRHLIRSTTDDLYLVHDGK-VEpfDGDLED 514
Cdd:COG1135 162 LLCDEATSALDpettrsildllKDINRelGLT---------IVLITHEMDVVRRICDRVAVLENGRiVE--QGPVLD 227
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-238 |
9.65e-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: 41.38 E-value: 9.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 16 LLDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNW----QLAWVnqeTPALPQPAIDYVIDGDrEY 91
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIsfssQFSWI---MPGTIKENIIFGVSYD-EY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 92 R--------QLEAALQQANERNDghaiaTVHGKldaidawtirsraasllHGLgfsneqlerpvsDFSGGWRMRLNLAQA 163
Cdd:cd03291 128 RyksvvkacQLEEDITKFPEKDN-----TVLGE-----------------GGI------------TLSGGQRARISLARA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 164 LICRSDLLLLDEPTNHLDldavIWLEKWLKGY-------TGTLILISHDRDFLDpIVDKIIHIEQQTMFEYtGNYSSFEV 236
Cdd:cd03291 174 VYKDADLYLLDSPFGYLD----VFTEKEIFEScvcklmaNKTRILVTSKMEHLK-KADKILILHEGSSYFY-GTFSELQS 247
|
..
gi 490290321 237 QR 238
Cdd:cd03291 248 LR 249
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
148-204 |
1.00e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 41.37 E-value: 1.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490290321 148 SDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWL----KGYtgTLILISH 204
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLfelkKEY--TIVLVTH 206
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
328-492 |
1.35e-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: 40.00 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKllagELQPVSGEIGLAKGIKLgyFAQHQLEFLradeSPLQHLARLapqele 407
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN----EGLYASGKARLISFLPK--FSRNKLIFI----DQLQFLIDV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 408 qklrdylgGFGFQgdKVSEETRRFSGGEKARLVLA--LIVWQRPNLLLLDEPTNHLDLDMRQALTEA---LIDFEGALVV 482
Cdd:cd03238 75 --------GLGYL--TLGQKLSTLSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVikgLIDLGNTVIL 144
|
170
....*....|
gi 490290321 483 VSHDRHLIRS 492
Cdd:cd03238 145 IEHNLDVLSS 154
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
402-492 |
1.54e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 402 APQELEQKLRDYLGGFGFQGDKVS---------------EETRRFSGGEKARLVLAL--IVWQRPN----LLLLDEPTNH 460
Cdd:PRK01156 758 ASQAMTSLTRKYLFEFNLDFDDIDvdqdfnitvsrggmvEGIDSLSGGEKTAVAFALrvAVAQFLNndksLLIMDEPTAF 837
|
90 100 110
....*....|....*....|....*....|....*...
gi 490290321 461 LDLDMRQALTE----ALIDFEG--ALVVVSHDRHLIRS 492
Cdd:PRK01156 838 LDEDRRTNLKDiieySLKDSSDipQVIMISHHRELLSV 875
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
424-539 |
2.27e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 424 VSEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHDRHLIRSTTDDLYL 499
Cdd:PTZ00265 573 VGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnenrITIIIAHRLSTIRYANTIFVL 652
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 490290321 500 VH--DGKVEPFDGDLEDYQQWLSDSQKQESQSGEAPKESGNS 539
Cdd:PTZ00265 653 SNreRGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNN 694
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
512-633 |
2.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 512 LEDYQQWLSDSQKQESQSGEAPKESGNSAQARKdqkrrEAELRSQTQPLRKEIARLEKEMDKLNAQLASAEEKLGdsely 591
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEELLEALD-----EEELEEELEELEEELEELEEELEELREELAELEAELE----- 463
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 490290321 592 DASRKAELTECLQQQASAKSGLEECEMAWLE---AQEQLERMLQE 633
Cdd:COG4717 464 QLEEDGELAELLQELEELKAELRELAEEWAAlklALELLEEAREE 508
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
506-614 |
2.54e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.86 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 506 EPFDGDLEDYQQWLSDSQKQESQSGEAPKesgnsaqARKDQKRreaeLRSQTQPLRKEIARLEkemdklnAQLASAEEKL 585
Cdd:pfam03528 140 ESAEREIADLRRRLSEGQEEENLEDEMKK-------AQEDAEK----LRSVVMPMEKEIAALK-------AKLTEAEDKI 201
|
90 100
....*....|....*....|....*....
gi 490290321 586 GDSElydASRKAELTECLQQQASAKSGLE 614
Cdd:pfam03528 202 KELE---ASKMKELNHYLEAEKSCRTDLE 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-176 |
2.80e-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: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 26 PGQKV-GLVGKNGCGKSTLLSLLKNEISADGGSMTFPGNWqlaWVNQETP-ALP--QPAIDYVidgdreyrqleaaLQQA 101
Cdd:COG4148 23 PGRGVtALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV---LQDSARGiFLPphRRRIGYV-------------FQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 102 N-------ERN--DGHAIATVHGKLDAIDawtirsRAASLLhGLGfsnEQLERPVSDFSGGWRMRLNLAQALICRSDLLL 172
Cdd:COG4148 87 RlfphlsvRGNllYGRKRAPRAERRISFD------EVVELL-GIG---HLLDRRPATLSGGERQRVAIGRALLSSPRLLL 156
|
....
gi 490290321 173 LDEP 176
Cdd:COG4148 157 MDEP 160
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-62 |
3.11e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 3.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 490290321 12 GVRVLlDNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSMTFPG 62
Cdd:PRK10982 10 GVKAL-DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG 59
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
141-204 |
3.38e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 39.51 E-value: 3.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290321 141 EQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKW---LKGYTgTLILISH 204
Cdd:PRK14247 138 DRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLfleLKKDM-TIVLVTH 203
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
504-633 |
3.41e-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: 40.82 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 504 KVEPFDGDLEDYQQWLSDSQKQesqSGEAPKESGNSAQARKDQKRREAELRSQTQPLRKEIARLEKEMDKLNAQLASAEE 583
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRK---IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 490290321 584 KLGDSELYDASRKAELTECLQQQASAKSGLEECEMAWLEAQ-EQLERMLQE 633
Cdd:TIGR02169 773 DLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARlREIEQKLNR 823
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
340-387 |
3.64e-03 |
|
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: 37.60 E-value: 3.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 490290321 340 RIGLLGRNGAGKSTLIKLLAGELQPVSGEIGLAKGIKLGYFAQHQLEF 387
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQI 48
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
135-214 |
4.03e-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: 38.84 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 135 GLGFSneQLERPVSDFSGGWRMRLNLAQALICRSD--LLLLDEPTNHLDLDAVIWLEKWLKGYTG---TLILISHDRDFL 209
Cdd:cd03238 75 GLGYL--TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDlgnTVILIEHNLDVL 152
|
....*...
gi 490290321 210 ---DPIVD 214
Cdd:cd03238 153 ssaDWIID 160
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-177 |
4.51e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.11 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 18 DNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISADGGSmtfpgnwqlAWVnqetpaLPQPaidyvID-GDREYRQLEA 96
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE---------AWL------FGQP-----VDaGDIATRRRVG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 97 ALQQA----NErndghaiATV------HGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALIC 166
Cdd:NF033858 343 YMSQAfslyGE-------LTVrqnlelHARLFHLPAAEIAARVAEMLERFDLADVADALP-DSLPLGIRQRLSLAVAVIH 414
|
170
....*....|.
gi 490290321 167 RSDLLLLDEPT 177
Cdd:NF033858 415 KPELLILDEPT 425
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
562-586 |
4.52e-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: 40.03 E-value: 4.52e-03
10 20
....*....|....*....|....*
gi 490290321 562 KEIARLEKEMDKLNAQLASAEEKLG 586
Cdd:COG0525 815 AERARLEKELAKLEKEIARVEKKLS 839
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
501-628 |
5.84e-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: 40.04 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 501 HDGKVEPFDGDLEDYQQWLSDSQKQ-----------ESQSGEAPKESgNSAQAR-KDQKRREAELRSQTQPLRKEIARLE 568
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAElqeleekleelRLEVSELEEEI-EELQKElYALANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 569 KEMDKLNAQLASAEEKLGDSELYDASRKAELTECLQQQASAKSGLEECEMAWLEAQEQLE 628
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-221 |
5.95e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 39.04 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 17 LDNATATINPGQKVGLVGKNGCGKSTLL----SLLK---NEISADGGSMTF-PGNWQLAWVNQETPALPQ----PAIDYV 84
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMqhfnALLKpssGTITIAGYHITPeTGNKNLKKLRKKVSLVFQfpeaQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 85 IDGDREY--RQLEAALQQAnerndghaiatvhgkldaidawtiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQ 162
Cdd:PRK13641 103 VLKDVEFgpKNFGFSEDEA------------------------KEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490290321 163 ALICRSDLLLLDEPTNHLDLDAVIWLEKWLKGYTG---TLILISHDRDFLDPIVDKIIHIEQ 221
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEH 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
429-477 |
6.15e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 6.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 490290321 429 RRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFE 477
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1405
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
539-632 |
7.14e-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: 38.98 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 539 SAQARKDQKRREAELRSQTQPLRKEIARLEKEMDKLNAQLASAEEKLGDSELYDASRKAELTECLQQQASAKSGLEECEM 618
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|....
gi 490290321 619 AWLEAQEQLERMLQ 632
Cdd:COG4942 98 ELEAQKEELAELLR 111
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
516-633 |
8.61e-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: 39.55 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 516 QQWLSDSQKQESQSGEAPKESGNSAQARKdQKRREAELRSQTQPLRKEIARLEKEMDKLNAQLASAEEKLGDSELYDASR 595
Cdd:COG3096 498 RELLRRYRSQQALAQRLQQLRAQLAELEQ-RLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEA 576
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 490290321 596 KAELTECLQQ--QASAK-SGLEECEMAWLEAQEQLERmLQE 633
Cdd:COG3096 577 VEQRSELRQQleQLRARiKELAARAPAWLAAQDALER-LRE 616
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
324-462 |
8.73e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 38.93 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 324 ERIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELQPVSGEIgLAKGIKL---------GYFA-QHQLEFL----- 388
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI-RFHDIPLtklqldswrSRLAvVSQTPFLfsdtv 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 389 -------RADESPLQ--HLARLA---------PQeleqklrdylggfGFQgDKVSEETRRFSGGEKARLVLALIVWQRPN 450
Cdd:PRK10789 406 annialgRPDATQQEieHVARLAsvhddilrlPQ-------------GYD-TEVGERGVMLSGGQKQRISIARALLLNAE 471
|
170
....*....|..
gi 490290321 451 LLLLDEPTNHLD 462
Cdd:PRK10789 472 ILILDDALSAVD 483
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
12-54 |
9.16e-03 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 38.86 E-value: 9.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 490290321 12 GVRVLldNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISAD 54
Cdd:COG1157 144 GVRAI--DGLLTVGRGQRIGIFAGSGVGKSTLLGMIARNTEAD 184
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
540-633 |
9.69e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290321 540 AQARKDQKRREAELRSQTQPLRKEIARLEKEMDKLNAQLASAEEKLGDSELYDASRKAELTECLQQQASAKSGLEECEMA 619
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
90
....*....|....
gi 490290321 620 WLEAQEQLERMLQE 633
Cdd:COG1196 402 LEELEEAEEALLER 415
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
12-54 |
9.77e-03 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 38.81 E-value: 9.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 490290321 12 GVRVLldNATATINPGQKVGLVGKNGCGKSTLLSLLKNEISAD 54
Cdd:PRK08927 145 GVRAL--NTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD 185
|
|
| |
