|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-549 |
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: 596.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 6 LNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgypqttsygYDEGLIhVLPRGATSAY 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELE--------------PDSGEV-SIPKGLRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 86 LEQVPDYPHGLKVMDNLNLAFEEIDAIEKQMREQEEQMkkvegSTLEKALNKYSSLVHLYEVKGGYERDEKLSKVCTGLK 165
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVLDGDAELRALEAELEELEAKL-----AEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 166 FDESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGIVLIVSHDRYFLDHVATKIV 245
Cdd:COG0488 141 FPEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 246 EIEDMESTSYKGNYSSFVEQKEENLRIQLEQYREQQKKINTMEKQVKDLRDWAIRAdnnkffRRAASIQKRLSKMERLDK 325
Cdd:COG0488 221 ELDRGKLTLYPGNYSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKA------KQAQSRIKALEKLEREEP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 326 PVLERKnMRLTMSESERSGKETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIE 405
Cdd:COG0488 295 PRRDKT-VEIRFPPPERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 406 LGSNVKVAYLPQKISFNNEELMLIEVFREDIS-IVEGKAREYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNL 484
Cdd:COG0488 374 LGETVKIGYFDQHQEELDPDKTVLDELRDGAPgGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 485 LILDEPTNHLDIDSIETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVEDFSLNSYLGNYDYYR 549
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYL 518
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-554 |
8.67e-124 |
|
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: 377.74 E-value: 8.67e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 10 KKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmNYypgypqttsygydEGLIHVLPrGATSAYLEQV 89
Cdd:TIGR03719 12 KVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK-DF-------------NGEARPQP-GIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 90 PDYPHGLKVMDNLNLAFEEI-------DAIEKQMREQEEQMKKV--EGSTLEKALnkysslvhlyEVKGGYERDEKLSKV 160
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGVAEIkdaldrfNEISAKYAEPDADFDKLaaEQAELQEII----------DAADAWDLDSQLEIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 161 CTGLKFDESflQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGIVLIVSHDRYFLDHV 240
Cdd:TIGR03719 147 MDALRCPPW--DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 241 ATKIVEIEDMESTSYKGNYSSFVEQKEENLRIQLEQYREQQKkinTMEKQVkdlrDWaIRAdnNKFFRRAASiQKRLSKM 320
Cdd:TIGR03719 225 AGWILELDRGRGIPWEGNYSSWLEQKQKRLEQEEKEESARQK---TLKREL----EW-VRQ--SPKGRQAKS-KARLARY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 321 ERLDKPVLERKNMRLTM--SESERSGKETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEH 398
Cdd:TIGR03719 294 EELLSQEFQKRNETAEIyiPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 399 PDKGKIELGSNVKVAYLPQ-------------KISFNNEELMlievfredISIVEGKAREYLSKFMFYQSSVFKKVKYLS 465
Cdd:TIGR03719 374 PDSGTIEIGETVKLAYVDQsrdaldpnktvweEISGGLDIIK--------LGKREIPSRAYVGRFNFKGSDQQKKVGQLS 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 466 GGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVEDFS-LNSYLGN 544
Cdd:TIGR03719 446 GGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDShVEWFEGN 525
|
570
....*....|
gi 754786342 545 YDYYRHEKEK 554
Cdd:TIGR03719 526 FSEYEEDKKR 535
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-556 |
4.58e-119 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 365.60 E-value: 4.58e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmNYypgypqttsygydEGLIHVLPrGATSAYLEQVPDYPHGLK 97
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK-EF-------------EGEARPAP-GIKVGYLPQEPQLDPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 98 VMDNLNLAFEEI-------DAIEKQMREQEEQMKKV--EGSTLEKALnkysslvhlyEVKGGYERDEKLSKVCTGLKF-- 166
Cdd:PRK11819 87 VRENVEEGVAEVkaaldrfNEIYAAYAEPDADFDALaaEQGELQEII----------DAADAWDLDSQLEIAMDALRCpp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 167 -DEsflqrDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGIVLIVSHDRYFLDHVATKIV 245
Cdd:PRK11819 157 wDA-----KVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWIL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 246 EIEDMESTSYKGNYSSFVEQKEEnlRIQLEQyREQQKKINTMEKQvkdlRDWaIRAdNNKfFRRAASiQKRLSKMERLDK 325
Cdd:PRK11819 232 ELDRGRGIPWEGNYSSWLEQKAK--RLAQEE-KQEAARQKALKRE----LEW-VRQ-SPK-ARQAKS-KARLARYEELLS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 326 PVLERKN--MRLTMSESERSGKETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGK 403
Cdd:PRK11819 301 EEYQKRNetNEIFIPPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 404 IELGSNVKVAYLPQ-KISFNNEElmliEVFrEDIS-----IVEGK----AREYLSKFMFYQSSVFKKVKYLSGGERIRLK 473
Cdd:PRK11819 381 IKIGETVKLAYVDQsRDALDPNK----TVW-EEISggldiIKVGNreipSRAYVGRFNFKGGDQQKKVGVLSGGERNRLH 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 474 LAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVEDFS-LNSYLGNYDYYrhEK 552
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDSqVEWFEGNFQEY--EE 533
|
....
gi 754786342 553 EKFR 556
Cdd:PRK11819 534 DKKR 537
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-639 |
1.18e-106 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 336.15 E-value: 1.18e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 7 NGIKKYMDATLvLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMnyypgypqttsygyDEGLIhVLPRGATSAYL 86
Cdd:PRK11147 8 GAWLSFSDAPL-LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLL--------------DDGRI-IYEQDLIVARL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 87 EQVPDYPHGLKVMDNLNlafEEIDAIEKQMREQEEQMKKVEGSTLEKALNKYSSLVHLYEVKGGYERDEKLSKVCTGLKF 166
Cdd:PRK11147 72 QQDPPRNVEGTVYDFVA---EGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 167 D-ESFLQRdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGIVLIVSHDRYFLDHVATKIV 245
Cdd:PRK11147 149 DpDAALSS----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 246 EIEDMESTSYKGNYSSFVEQKEENLRIQLEQYREQQKKINTME---KQ-VKdlrdwAIRADNNKFFRraASIQKRLSKME 321
Cdd:PRK11147 225 DLDRGKLVSYPGNYDQYLLEKEEALRVEELQNAEFDRKLAQEEvwiRQgIK-----ARRTRNEGRVR--ALKALRRERSE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 322 RLDkpVLERKNMRLtmSESERSGKETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDK 401
Cdd:PRK11147 298 RRE--VMGTAKMQV--EEASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 402 GKIELGSNVKVAYL--------PQKISFNN-----EELMlievfredisiVEGKARE---YLSKFMFYQSSVFKKVKYLS 465
Cdd:PRK11147 374 GRIHCGTKLEVAYFdqhraeldPEKTVMDNlaegkQEVM-----------VNGRPRHvlgYLQDFLFHPKRAMTPVKALS 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 466 GGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQGTIFFISHDRYFI-NKMSNRIIAVEDFSLNSYLGN 544
Cdd:PRK11147 443 GGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKIGRYVGG 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 545 YDYYRHEKEKFR-QEQESNALVTEAKKQIKPVKAASEKKQSINQARLLE----KIESLEKELEALDEamEVANIDY---- 615
Cdd:PRK11147 523 YHDARQQQAQYLaLKQPAVKKKEEAAAPKAETVKRSSKKLSYKLQRELEqlpqLLEDLEAEIEALQA--QVADADFfsqp 600
|
650 660
....*....|....*....|....*
gi 754786342 616 -NELNNLHNRKVELSEELEVATDLW 639
Cdd:PRK11147 601 hEQTQKVLADLADAEQELEVAFERW 625
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
20-548 |
4.43e-84 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 273.69 E-value: 4.43e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 20 EDVSLEAYDGDKIGIVGVNGSGKSTILKVIAG-IEQMNyypgypqttsygydeGLIHVLPrGATSAYLEQ----VPDYph 94
Cdd:PRK15064 18 ENISVKFGGGNRYGLIGANGCGKSTFMKILGGdLEPSA---------------GNVSLDP-NERLGKLRQdqfaFEEF-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 95 glKVMDNLNLAFEEIDAIeKQMRE---------QEEQMKKVEgstLEKALNKYsslvhlyevkGGYERDEKLSKVCTGLK 165
Cdd:PRK15064 80 --TVLDTVIMGHTELWEV-KQERDriyalpemsEEDGMKVAD---LEVKFAEM----------DGYTAEARAGELLLGVG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 166 FDESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGIVLIVSHDRYFLDHVATKIV 245
Cdd:PRK15064 144 IPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 246 EIEDMESTSYKGNYSSFVEQKEenlriqleQYREQQKKINTMEK-QVKDLRDWAIRADNNKFFRRAASiqkrlSKMERLD 324
Cdd:PRK15064 224 DLDYGELRVYPGNYDEYMTAAT--------QARERLLADNAKKKaQIAELQSFVSRFSANASKAKQAT-----SRAKQID 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 325 KPVLE------RKNMRLTMSESERSGKETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEH 398
Cdd:PRK15064 291 KIKLEevkpssRQNPFIRFEQDKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 399 PDKGKIELGSNVKVAYLPQKISfnneelmliEVFREDISIVEGKA------------REYLSKFMFYQSSVFKKVKYLSG 466
Cdd:PRK15064 371 PDSGTVKWSENANIGYYAQDHA---------YDFENDLTLFDWMSqwrqegddeqavRGTLGRLLFSQDDIKKSVKVLSG 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 467 GERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVEDFSLNSYLGNYD 546
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYE 521
|
..
gi 754786342 547 YY 548
Cdd:PRK15064 522 EY 523
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
29-644 |
1.57e-80 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 267.42 E-value: 1.57e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 29 GDKIGIVGVNGSGKSTILKVIAG-IEQMNYYPGYPQTTSYGYDEGLIHVLPRGAtsayLEQVPDyphglkvmdnlnlAFE 107
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNeISADGGSYTFPGNWQLAWVNQETPALPQPA----LEYVID-------------GDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 108 EIDAIEKQMREQEEQMKKVEGSTLEKALNKysslVHLYEVKGgyerdeKLSKVCTGLKFDESFLQRDFDYLSGGEKTTVI 187
Cdd:PRK10636 90 EYRQLEAQLHDANERNDGHAIATIHGKLDA----IDAWTIRS------RAASLLHGLGFSNEQLERPVSDFSGGWRMRLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 188 LGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGIVLIVSHDRYFLDHVATKIVEIEDMESTSYKGNYSSFVEQKE 267
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 268 ENLRIQLEQYREQQKKINTMEKQVKDLRDWAIRAdnnkffRRAASIQKRLSKMERLdKPVLERKNMRLTMSESERSGKET 347
Cdd:PRK10636 240 TRLAQQQAMYESQQERVAHLQSYIDRFRAKATKA------KQAQSRIKMLERMELI-APAHVDNPFHFSFRAPESLPNPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQ-KISF-NNEE 425
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQhQLEFlRADE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 426 LMLIEVFREDISIVEGKAREYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEA 505
Cdd:PRK10636 393 SPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 506 LEDFQGTIFFISHDRYFINKMSNRIIAVEDFSLNSYLGNY-DYYRHEKEKFRQEQESNAlvteAKKQIKPVKAASEKKQS 584
Cdd:PRK10636 473 LIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLeDYQQWLSDVQKQENQTDE----APKENNANSAQARKDQK 548
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 585 INQARLLEKIESLEKELEALDEAMEVANIDYNELNNL--------HNRKVELSE----------ELEVATDLWLTAME 644
Cdd:PRK10636 549 RREAELRTQTQPLRKEIARLEKEMEKLNAQLAQAEEKlgdselydQSRKAELTAclqqqasaksGLEECEMAWLEAQE 626
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
350-600 |
4.52e-70 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 236.11 E-value: 4.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 350 ATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQ------------ 417
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQeppldddltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 418 ---------------------KISFNNEELMLIEVFREDISIVEG-----KAREYLSKFMFYQSSVFKKVKYLSGGERIR 471
Cdd:COG0488 81 tvldgdaelraleaeleeleaKLAEPDEDLERLAELQEEFEALGGweaeaRAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 472 LKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVEDFSLNSYLGNYDYYRHE 551
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754786342 552 K-EKFRQEQESNAlvtEAKKQIK---------PVKAASEKKqsiNQARL--LEKIESLEKE 600
Cdd:COG0488 241 RaERLEQEAAAYA---KQQKKIAkeeefirrfRAKARKAKQ---AQSRIkaLEKLEREEPP 295
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
348-535 |
3.10e-60 |
|
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: 197.67 E-value: 3.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQkisfnneelm 427
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 428 lievfredisivegkareylskfmfyqssvfkkvkyLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALE 507
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180
....*....|....*....|....*...
gi 754786342 508 DFQGTIFFISHDRYFINKMSNRIIAVED 535
Cdd:cd03221 115 EYPGTVILVSHDRYFLDQVATKIIELED 142
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
29-549 |
4.90e-57 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 205.09 E-value: 4.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 29 GDKIGIVGVNGSGKSTILKVIAgieqMNYYPGYPQTTSygydegLIHVLPR--GATSAYLEQVPDYPhglkvMDNLNLAF 106
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMA----MHAIDGIPKNCQ------ILHVEQEvvGDDTTALQCVLNTD-----IERTQLLE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 107 EEIDAIEKQMREQEEQMKKVEGSTLEKALNKYS---SLVHLY---EVKGGYERDEKLSKVCTGLKFDESFLQRDFDYLSG 180
Cdd:PLN03073 268 EEAQLVAQQRELEFETETGKGKGANKDGVDKDAvsqRLEEIYkrlELIDAYTAEARAASILAGLSFTPEMQVKATKTFSG 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 181 GEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGIVLIVSHDRYFLDHVATKIVEIEDMESTSYKGNYS 260
Cdd:PLN03073 348 GWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYD 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 261 SFVEQKEENLRIQLEQYREQQKKINTMEKQVKDLRDWAiradnnkffRRAASIQKRLSKMERLD--KPVLERKNMRLTM- 337
Cdd:PLN03073 428 TFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNA---------KRASLVQSRIKALDRLGhvDAVVNDPDYKFEFp 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 338 SESERSGKETIKATDLTKSY-GERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLP 416
Cdd:PLN03073 499 TPDDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFS 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 417 Q------KISFNNeelmLIEVFREDISIVEGKAREYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEP 490
Cdd:PLN03073 579 QhhvdglDLSSNP----LLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEP 654
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 754786342 491 TNHLDIDSIETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVEDFSLNSYLGNYDYYR 549
Cdd:PLN03073 655 SNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYK 713
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-265 |
5.74e-47 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 173.33 E-value: 5.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPqttsygyDEGLIHvlpRGAT- 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE-------P-------DSGTVK---LGETv 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 83 -SAYLEQvpdypHGLKVMDNLNLaFEEIDAIEKQMREQ-------------EEQMKKVEGstlekalnkysslvhlyevk 148
Cdd:COG0488 379 kIGYFDQ-----HQEELDPDKTV-LDELRDGAPGGTEQevrgylgrflfsgDDAFKPVGV-------------------- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 149 ggyerdeklskvctglkfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGIVL 228
Cdd:COG0488 433 -----------------------------LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVL 483
|
250 260 270
....*....|....*....|....*....|....*..
gi 754786342 229 IVSHDRYFLDHVATKIVEIEDMESTSYKGNYSSFVEQ 265
Cdd:COG0488 484 LVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-249 |
7.84e-46 |
|
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: 159.15 E-value: 7.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMnyypgypqttsygyDEGLIHVlPRGATS 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEP--------------DEGIVTW-GSTVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 AYLEQvpdyphglkvmdnlnlafeeidaiekqmreqeeqmkkvegstlekalnkysslvhlyevkggyerdeklskvctg 163
Cdd:cd03221 66 GYFEQ--------------------------------------------------------------------------- 70
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 164 lkfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGIVLIVSHDRYFLDHVATK 243
Cdd:cd03221 71 --------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATK 136
|
....*.
gi 754786342 244 IVEIED 249
Cdd:cd03221 137 IIELED 142
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-531 |
2.71e-36 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 143.80 E-value: 2.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 28 DGDKIGIVGVNGSGKSTILKVIAGIEQMNYypGYPQTTsYGYDEglihVLPRGATSA---YLEQVpdYPHGLKVMdnlnL 104
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNL--GDYEEE-PSWDE----VLKRFRGTElqnYFKKL--YNGEIKVV----H 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 105 AFEEIDAIEKQmreqeeqmkkVEGST---LEKAlnkysslvhlyevkggyerDE--KLSKVCTGLKFDEsFLQRDFDYLS 179
Cdd:PRK13409 165 KPQYVDLIPKV----------FKGKVrelLKKV-------------------DErgKLDEVVERLGLEN-ILDRDISELS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 180 GGEKTTVILGKLLIHNPNILLLDEPTNHLDM-------DSIEWLENylknyKGIVLIVSHDRYFLDHVATKIVEIEDMES 252
Cdd:PRK13409 215 GGELQRVAIAAALLRDADFYFFDEPTSYLDIrqrlnvaRLIRELAE-----GKYVLVVEHDLAVLDYLADNVHIAYGEPG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 253 -----TSYKG------NY-SSFVeqKEENLRIqleqyreqqkkintmekqvkdlRDWAIradnnKFFRRAasiqkrlskm 320
Cdd:PRK13409 290 aygvvSKPKGvrvginEYlKGYL--PEENMRI----------------------RPEPI-----EFEERP---------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 321 erldkpvlerknmrltmSESERSGKETIKATDLTKSYGERLLFRDAGVmVHYGERVGLIGPNGSGKTTFLKMLLGEEHPD 400
Cdd:PRK13409 331 -----------------PRDESERETLVEYPDLTKKLGDFSLEVEGGE-IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 401 KGKIElgSNVKVAYLPQKISfnneelmlievfrediSIVEGKAREYLSKFM------FYQSSVFK----------KVKYL 464
Cdd:PRK13409 393 EGEVD--PELKISYKPQYIK----------------PDYDGTVEDLLRSITddlgssYYKSEIIKplqlerlldkNVKDL 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754786342 465 SGGERIRLKLAILLYDEVNLLILDEPTNHLDIdsietlEEAL----------EDFQGTIFFISHDRYFINKMSNRII 531
Cdd:PRK13409 455 SGGELQRVAIAACLSRDADLYLLDEPSAHLDV------EQRLavakairriaEEREATALVVDHDIYMIDYISDRLM 525
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-531 |
1.72e-33 |
|
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: 135.68 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 32 IGIVGVNGSGKSTILKVIAGIEQMNY--YPGYPqttsyGYDEglihVLPRGATSA---YLEQVPDyphglkvmdnlnlaf 106
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLgdYDEEP-----SWDE----VLKRFRGTElqdYFKKLAN--------------- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 107 EEIDAIEKQmrEQEEQMKKVEGSTLEKALNKYSslvhlyevkggyERDeKLSKVCTGLKFDESfLQRDFDYLSGGEKTTV 186
Cdd:COG1245 158 GEIKVAHKP--QYVDLIPKVFKGTVRELLEKVD------------ERG-KLDELAEKLGLENI-LDRDISELSGGELQRV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 187 ILGKLLIHNPNILLLDEPTNHLD----MDSIEWLENYLKNYKgIVLIVSHDRYFLDHVATKIVEIEDMES-----TSYKG 257
Cdd:COG1245 222 AIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIRELAEEGK-YVLVVEHDLAILDYLADYVHILYGEPGvygvvSKPKS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 258 -----NYssFVEQ--KEENLRIqleqyreqqkkintmekqvkdlRDWAIRadnnkFFRRAasiqkrlskmerldkpvler 330
Cdd:COG1245 301 vrvgiNQ--YLDGylPEENVRI----------------------RDEPIE-----FEVHA-------------------- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 331 knmrltmSESERSGKETIKATDLTKSYGERLLFRDAGvMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIElgSNV 410
Cdd:COG1245 332 -------PRREKEEETLVEYPDLTKSYGGFSLEVEGG-EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 411 KVAYLPQKISfnneelmlievfrediSIVEGKAREYLSKFM--FYQSSVF---------------KKVKYLSGGERIRLK 473
Cdd:COG1245 402 KISYKPQYIS----------------PDYDGTVEEFLRSANtdDFGSSYYkteiikplgleklldKNVKDLSGGELQRVA 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754786342 474 LAILLYDEVNLLILDEPTNHLDIDsiETLEEA------LEDFQGTIFFISHDRYFINKMSNRII 531
Cdd:COG1245 466 IAACLSRDADLYLLDEPSAHLDVE--QRLAVAkairrfAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
348-535 |
2.57e-33 |
|
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: 125.59 E-value: 2.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIE-LGSNV---------KVAYLPQ 417
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvLGKDIkkepeevkrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 418 KISFnNEELmlievfredisivegKAREYLskfmfyqssvfkkvkYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDID 497
Cdd:cd03230 81 EPSL-YENL---------------TVRENL---------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 754786342 498 SIETLEEALEDF---QGTIFFISHDRYFINKMSNRIIAVED 535
Cdd:cd03230 130 SRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNN 170
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
348-536 |
1.28e-31 |
|
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: 121.82 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVK---------VAYLPQ 417
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWnGEPIRdaredyrrrLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 418 KISFnNEELMLIE----------VFREDISIVEGKAREYLSKFMfyqssvFKKVKYLSGGERIRLKLAILLYDEVNLLIL 487
Cdd:COG4133 83 ADGL-KPELTVREnlrfwaalygLRADREAIDEALEAVGLAGLA------DLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 754786342 488 DEPTNHLDIDSIETLEEALEDF---QGTIFFISHDRYFINkmSNRIIAVEDF 536
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELA--AARVLDLGDF 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-249 |
1.93e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 118.77 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgypqttsygYDEGLIHV--LPRGA 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDP--------------PTSGEIYLdgKPLSA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 82 TS--------AYLEQVPDYPHGlKVMDNLNLAFeeidaiekQMREQEEQMKKvegstLEKALNKysslvhlyevkggyer 153
Cdd:COG4619 67 MPppewrrqvAYVPQEPALWGG-TVRDNLPFPF--------QLRERKFDRER-----ALELLER---------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 154 deklskvctgLKFDESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS----IEWLENYLKNYKGIVLI 229
Cdd:COG4619 117 ----------LGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLW 186
|
250 260
....*....|....*....|
gi 754786342 230 VSHDRYFLDHVATKIVEIED 249
Cdd:COG4619 187 VSHDPEQIERVADRVLTLEA 206
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
348-535 |
2.00e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 118.77 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV----------KVAYLP 416
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdGKPLsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 417 QK-------ISFNneelmLIEVFR-EDISIVEGKAREYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILD 488
Cdd:COG4619 81 QEpalwggtVRDN-----LPFPFQlRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 754786342 489 EPTNHLDIDSIETLEEALEDF----QGTIFFISHDRYFINKMSNRIIAVED 535
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
358-595 |
2.06e-30 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 126.82 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 358 GERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQKI----------------SF 421
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETpalpqpaleyvidgdrEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 422 NNEELMLIEVFRED----ISIVEGK------------AREYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLL 485
Cdd:PRK10636 92 RQLEAQLHDANERNdghaIATIHGKldaidawtirsrAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 486 ILDEPTNHLDIDSIETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVEDFSLNSYLGNYDYY-RHEKEKFRQEQ----E 560
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFeVQRATRLAQQQamyeS 251
|
250 260 270
....*....|....*....|....*....|....*.
gi 754786342 561 SNALVTEAKKQIKPVKA-ASEKKQSINQARLLEKIE 595
Cdd:PRK10636 252 QQERVAHLQSYIDRFRAkATKAKQAQSRIKMLERME 287
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
349-535 |
1.02e-29 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 115.03 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 349 KATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGsNVKVAYLPQKIsfnneelml 428
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID-GKDIAKLPLEE--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 429 ievFREDISIVEGkareylskfmfyqssvfkkvkyLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALED 508
Cdd:cd00267 71 ---LRRRIGYVPQ----------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRE 125
|
170 180 190
....*....|....*....|....*....|
gi 754786342 509 FQG---TIFFISHDRYFINKMSNRIIAVED 535
Cdd:cd00267 126 LAEegrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
348-519 |
1.31e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 117.09 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIE-LGSNV---------KVAYLPQ 417
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDVardpaevrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 418 KISFNN-----EELMLI-EVFREDISIVEGKAREYLSKFMFyQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPT 491
Cdd:COG1131 81 EPALYPdltvrENLRFFaRLYGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190
....*....|....*....|....*....|.
gi 754786342 492 NHLDIDSIETLEEALEDF--QG-TIFFISHD 519
Cdd:COG1131 160 SGLDPEARRELWELLRELaaEGkTVLLSTHY 190
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-531 |
5.41e-29 |
|
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: 121.16 E-value: 5.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyypgYPQTtsyGYDEGLIHV---- 76
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL--------LPHG---GRISGEVLLdgrd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 77 ---LP---RGATSAYLEQVPDYP-HGLKVMDNLNLAFEEIDAIEKQMREQEEQMkkvegstLEKalnkysslVHLyevkg 149
Cdd:COG1123 73 lleLSealRGRRIGMVFQDPMTQlNPVTVGDQIAEALENLGLSRAEARARVLEL-------LEA--------VGL----- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 150 gyerdeklskvctglkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDM----DSIEWLENYLKNYKG 225
Cdd:COG1123 133 ------------------ERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVttqaEILDLLRELQRERGT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 226 IVLIVSHDryfLDHVATKIVEIEDMestsYKGnyssfveqkeenlRIQLEQYREQqkkintmekqvkdlrdwairadnnk 305
Cdd:COG1123 195 TVLLITHD---LGVVAEIADRVVVM----DDG-------------RIVEDGPPEE------------------------- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 306 FFRRAAsiqkRLSKMERLDKPvlerknmRLTMSESERSGKETIKATDLTKSY-----GERLLFRDAGVMVHYGERVGLIG 380
Cdd:COG1123 230 ILAAPQ----ALAAVPRLGAA-------RGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 381 PNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV------KVAYLPQKIS--FNNEELMLIEVFR-EDIsIVEG--------- 441
Cdd:COG1123 299 ESGSGKSTLARLLLGLLRPTSGSILFdGKDLtklsrrSLRELRRRVQmvFQDPYSSLNPRMTvGDI-IAEPlrlhgllsr 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 442 -----KAREYLskfmfyqssvfKKV--------KY---LSGGERIRLKLA-ILLydeVN--LLILDEPTNHLDIdSI--- 499
Cdd:COG1123 378 aerreRVAELL-----------ERVglppdladRYpheLSGGQRQRVAIArALA---LEpkLLILDEPTSALDV-SVqaq 442
|
570 580 590
....*....|....*....|....*....|....
gi 754786342 500 --ETLEEALEDFQGTIFFISHDRYFINKMSNRII 531
Cdd:COG1123 443 ilNLLRDLQRELGLTYLFISHDLAVVRYIADRVA 476
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-266 |
6.17e-29 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 121.15 E-value: 6.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAG-IEQM--------NYYPGY-PQTTSYgydegl 73
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGeLEPDsgtvkwseNANIGYyAQDHAY------ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 74 ihvlprgatsayleqvpDYPHGLKVMDNLNlafeeidaiekQMREQE--EQMKKvegSTLEKALnkysslvhlyevkggY 151
Cdd:PRK15064 394 -----------------DFENDLTLFDWMS-----------QWRQEGddEQAVR---GTLGRLL---------------F 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 152 ERDE--KLSKVCtglkfdesflqrdfdylSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGIVLI 229
Cdd:PRK15064 428 SQDDikKSVKVL-----------------SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIF 490
|
250 260 270
....*....|....*....|....*....|....*..
gi 754786342 230 VSHDRYFLDHVATKIVEIEDMESTSYKGNYSSFVEQK 266
Cdd:PRK15064 491 VSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
348-531 |
1.27e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.42 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV-----KVAYLPQKISF 421
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPrrarrRIGYVPQRAEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 422 NN------EELML------IEVFR----EDISIV---------EGKAREYLSKfmfyqssvfkkvkyLSGGERIRLKLAI 476
Cdd:COG1121 87 DWdfpitvRDVVLmgrygrRGLFRrpsrADREAVdealervglEDLADRPIGE--------------LSGGQQQRVLLAR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 477 LLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQG---TIFFISHDRYFINKMSNRII 531
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVL 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
348-535 |
5.65e-28 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 112.83 E-value: 5.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV----------KVAYLP 416
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLaslsrrelarRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 417 QKIS----FNNEELML------IEVFR----EDISIVEG----------KAREYLSkfmfyqssvfkkvkyLSGGERIRL 472
Cdd:COG1120 82 QEPPapfgLTVRELVAlgryphLGLFGrpsaEDREAVEEalertglehlADRPVDE---------------LSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754786342 473 KLAILLYDEVNLLILDEPTNHLDIDS-IETLE--EALEDFQG-TIFFISHD-----RYfinkmSNRIIAVED 535
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHqLEVLEllRRLARERGrTVVMVLHDlnlaaRY-----ADRLVLLKD 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
349-519 |
6.10e-28 |
|
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: 111.86 E-value: 6.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 349 KATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL------GSNVKVAYLPQKISFN 422
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkpleKERKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 423 NEelMLIEVFRedisIVEGKAREYLSKFMFYQSSVFKKVKY-----------------LSGGERIRLKLAILLYDEVNLL 485
Cdd:cd03235 81 RD--FPISVRD----VVLMGLYGHKGLFRRLSKADKAKVDEalervglseladrqigeLSGGQQQRVLLARALVQDPDLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 754786342 486 ILDEPTNHLDIDSIETLEEALEDFQG---TIFFISHD 519
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHD 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
349-535 |
1.05e-27 |
|
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: 109.83 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 349 KATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV----------KVAYLPQ 417
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLdGKDLaslspkelarKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 418 KIsfnneELMLIEVFREdisivegkaREYLSkfmfyqssvfkkvkyLSGGERIRLKLAILLYDEVNLLILDEPTNHLDID 497
Cdd:cd03214 81 AL-----ELLGLAHLAD---------RPFNE---------------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 754786342 498 -SIETLE--EAL-EDFQGTIFFISHDryfIN---KMSNRIIAVED 535
Cdd:cd03214 132 hQIELLEllRRLaRERGKTVVMVLHD---LNlaaRYADRVILLKD 173
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-270 |
2.45e-26 |
|
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: 113.49 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPgypqttsygyDEGLIHVlprGATS 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQ----P----------DSGTIEI---GETV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 --AYLEQVPDyphglkVMDNLNLAFEEIDAIEKQMReqeeqmkkvegstlekaLNKYSSLVHLYevkggyerdeklskvC 161
Cdd:TIGR03719 386 klAYVDQSRD------ALDPNKTVWEEISGGLDIIK-----------------LGKREIPSRAY---------------V 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 162 TGLKFDESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGIVLIVSHDRYFLDHVA 241
Cdd:TIGR03719 428 GRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIA 507
|
250 260 270
....*....|....*....|....*....|
gi 754786342 242 TKIVEIE-DMESTSYKGNYSSFVEQKEENL 270
Cdd:TIGR03719 508 THILAFEgDSHVEWFEGNFSEYEEDKKRRL 537
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
348-535 |
2.88e-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: 107.64 E-value: 2.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDagvmVHY----GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV---------KVA 413
Cdd:COG4555 2 IEVENLSKKYGKVPALKD----VSFtakdGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdGEDVrkeprearrQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 414 YLPQKISF-------NNEElMLIEVFREDISIVEGKAREYLSKFmfyQSSVF--KKVKYLSGGERIRLKLAILLYDEVNL 484
Cdd:COG4555 78 VLPDERGLydrltvrENIR-YFAELYGLFDEELKKRIEELIELL---GLEEFldRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 754786342 485 LILDEPTNHLDIDSIETLEEALEDF--QG-TIFFISHDRYFINKMSNRIIAVED 535
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALkkEGkTVLFSSHIMQEVEALCDRVVILHK 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
348-535 |
4.65e-26 |
|
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: 105.35 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVkvaylpqkisfnNEEL 426
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdGEDL------------TDLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 427 MLIEVFREDISIVegkareylskfmfYQS-------SVFKKVKY-LSGGERIRLKLAILLYDEVNLLILDEPTNHLD--- 495
Cdd:cd03229 69 DELPPLRRRIGMV-------------FQDfalfphlTVLENIALgLSGGQQQRVALARALAMDPDVLLLDEPTSALDpit 135
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 754786342 496 IDSIETLEEALEDFQG-TIFFISHDRYFINKMSNRIIAVED 535
Cdd:cd03229 136 RREVRALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRD 176
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
348-595 |
7.21e-26 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 111.91 E-value: 7.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQKiSFNNEELM 427
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQD-QFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 428 LIEV--------------------------------------FRE-DISIVEGKAREYLSKFMFYQSSVFKKVKYLSGGE 468
Cdd:PRK15064 81 VLDTvimghtelwevkqerdriyalpemseedgmkvadlevkFAEmDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 469 RIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVEDFSLNSYLGNYDYY 548
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 754786342 549 RHEKEKFRQEQES-NAlvtEAKKQIKPVKA--------ASEKKQSINQARLLEKIE 595
Cdd:PRK15064 241 MTAATQARERLLAdNA---KKKAQIAELQSfvsrfsanASKAKQATSRAKQIDKIK 293
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
353-590 |
1.05e-25 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 111.75 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 353 LTKSYG-ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQ-------KISFNNE 424
Cdd:PRK11819 12 VSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQepqldpeKTVRENV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 425 ELMLIEVFR-----EDISIVEGKAREYLSKFMFYQSSVF----------------------------KKVKYLSGGERIR 471
Cdd:PRK11819 92 EEGVAEVKAaldrfNEIYAAYAEPDADFDALAAEQGELQeiidaadawdldsqleiamdalrcppwdAKVTKLSGGERRR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 472 LKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVEDFSLNSYLGNYDYYRHE 551
Cdd:PRK11819 172 VALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQ 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 754786342 552 KEKfRQEQESNalvTEAKKQ--IKP----VKAASEKKQSINQARL 590
Cdd:PRK11819 252 KAK-RLAQEEK---QEAARQkaLKRelewVRQSPKARQAKSKARL 292
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-271 |
1.08e-25 |
|
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: 106.10 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEqmnyypgYPQTTSYGYDEGLIHVLPRGATS 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLL-------KPDSGSILIDGEDVRKEPREARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 --AYLEQVPDYPHGLKVMDNLNLaFEEIdaiekqmreqeeqmKKVEGSTLEKALNKYSSLVHLYEVkggyeRDEKLSKvc 161
Cdd:COG4555 75 qiGVLPDERGLYDRLTVRENIRY-FAEL--------------YGLFDEELKKRIEELIELLGLEEF-----LDRRVGE-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 162 tglkfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKG---IVLIVSHDRYFLD 238
Cdd:COG4555 133 ----------------LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVE 196
|
250 260 270
....*....|....*....|....*....|....
gi 754786342 239 HVATKIVEIEDMEsTSYKGNYSSFVEQK-EENLR 271
Cdd:COG4555 197 ALCDRVVILHKGK-VVAQGSLDELREEIgEENLE 229
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-249 |
5.86e-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: 102.93 E-value: 5.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 14 DATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSYGYDEGLIHVLP---RGATSAYLEQVP 90
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLG-------PTSGEVLVDGKDLTKLSlkeLRRKVGLVFQNP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 91 DypHGLkVMDNLnlaFEEI-DAIEKQMREQEEQMKKVegstlekalnkysslvhlyevkggyerDEKLSKVctGLkfdES 169
Cdd:cd03225 85 D--DQF-FGPTV---EEEVaFGLENLGLPEEEIEERV---------------------------EEALELV--GL---EG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 170 FLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK--GI-VLIVSHDRYFLDHVATKIVE 246
Cdd:cd03225 127 LRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaeGKtIIIVTHDLDLLLELADRVIV 206
|
...
gi 754786342 247 IED 249
Cdd:cd03225 207 LED 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
370-492 |
6.82e-25 |
|
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: 100.80 E-value: 6.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 370 VHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG-----------SNVKVAYLPQKISFNN-----EELML-IEVF 432
Cdd:pfam00005 8 LNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQDPQLFPrltvrENLRLgLLLK 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754786342 433 REDISIVEGKAREYLSKF---MFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTN 492
Cdd:pfam00005 88 GLSKREKDARAEEALEKLglgDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
352-535 |
4.14e-24 |
|
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: 100.62 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 352 DLTKSY--GERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVKVAYLPQK-----ISFNN 423
Cdd:cd03225 4 NLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLTKLSLKELrrkvgLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 424 EELMLI-EVFREDISI-----------VEGKAREYLSKFmfyQSSVFKK--VKYLSGGERIRLKLAILLYDEVNLLILDE 489
Cdd:cd03225 84 PDDQFFgPTVEEEVAFglenlglpeeeIEERVEEALELV---GLEGLRDrsPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 754786342 490 PTNHLDIDSIETLEEALEDFQG---TIFFISHDRYFINKMSNRIIAVED 535
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
348-535 |
4.32e-24 |
|
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: 101.26 E-value: 4.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSY-GERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG----SNVKVAYLPQKIS-- 420
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkdiTKKNLRELRRKVGlv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 421 FNNEELMLIE--VFrEDIS-----------IVEGKAREYLSKF-M--FYQSSVFKkvkyLSGGERIRLKLAILLYDEVNL 484
Cdd:COG1122 81 FQNPDDQLFAptVE-EDVAfgpenlglpreEIRERVEEALELVgLehLADRPPHE----LSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 754786342 485 LILDEPTNHLDIDSIETLEEALEDFQG---TIFFISHDRYFINKMSNRIIAVED 535
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
353-534 |
6.79e-24 |
|
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: 100.95 E-value: 6.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 353 LTKSYGERLLFRDAGVmVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELgSNVKVAYLPQKISfnneelmlievf 432
Cdd:cd03237 6 MKKTLGEFTLEVEGGS-ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIK------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 433 rediSIVEGKAREYLSKFM--FYQSSVFK---------------KVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLD 495
Cdd:cd03237 72 ----ADYEGTVRDLLSSITkdFYTHPYFKteiakplqieqildrEVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 754786342 496 IDSIETLEEALEDF----QGTIFFISHDRYFINKMSNRIIAVE 534
Cdd:cd03237 148 VEQRLMASKVIRRFaennEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
348-535 |
1.93e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 98.97 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSY-GERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV------KVAYLPQKI 419
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVnGQDLsrlkrrEIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 420 S--------------FNNEELMLiEVFREDISIVEGKAREYLSKFmfyqsSVFKKVKY----LSGGERIRLKL--AIlly 479
Cdd:COG2884 82 GvvfqdfrllpdrtvYENVALPL-RVTGKSRKEIRRRVREVLDLV-----GLSDKAKAlpheLSGGEQQRVAIarAL--- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754786342 480 deVN---LLILDEPTNHLDIDSIETLEEALEDF--QG-TIFFISHDRYFINKMSNRIIAVED 535
Cdd:COG2884 153 --VNrpeLLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELVDRMPKRVLELED 212
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
348-535 |
2.08e-23 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 97.45 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERL--LFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGsNVKVAYLPQkisfnnee 425
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID-GVDLRDLDL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 426 lmliEVFREDISIVEGKAreylskFMFYQSsvfkkVKY--LSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLE 503
Cdd:cd03228 72 ----ESLRKNIAYVPQDP------FLFSGT-----IREniLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALIL 136
|
170 180 190
....*....|....*....|....*....|....
gi 754786342 504 EALEDFQG--TIFFISHdRYFINKMSNRIIAVED 535
Cdd:cd03228 137 EALRALAKgkTVIVIAH-RLSTIRDADRIIVLDD 169
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
245-335 |
1.56e-22 |
|
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: 91.87 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 245 VEIEDMESTSYKGNYSSFVEQKEENLRIQLEQYREQQKKINTMEKQVKDLRDWAIRAdnnkffRRAASIQKRLSKMERLD 324
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKA------KQAQSRIKALEKMERIE 74
|
90
....*....|.
gi 754786342 325 KPVLERKNMRL 335
Cdd:pfam12848 75 KPERDKPKLRF 85
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-270 |
1.86e-22 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 101.73 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 7 NGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPgypqttsygyDEGLIHVlprGATS--A 84
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQ----P----------DSGTIKI---GETVklA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 85 YLEQVPDyphglkVMDNLNLAFEEI----DAIekqmreqeeQMKKVEGSTleKAlnkYsslVHLYEVKGGyerD-EKLSK 159
Cdd:PRK11819 391 YVDQSRD------ALDPNKTVWEEIsgglDII---------KVGNREIPS--RA---Y---VGRFNFKGG---DqQKKVG 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 160 VctglkfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGIVLIVSHDRYFLDH 239
Cdd:PRK11819 445 V-----------------LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDR 507
|
250 260 270
....*....|....*....|....*....|..
gi 754786342 240 VATKIVEIE-DMESTSYKGNYSSFVEQKEENL 270
Cdd:PRK11819 508 IATHILAFEgDSQVEWFEGNFQEYEEDKKRRL 539
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
348-531 |
3.51e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 94.98 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGsnvkvaylpQKISFNNEELM 427
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFD---------GKSYQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 428 -----LIEV--------FREDISI------VEGKAREYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILD 488
Cdd:cd03268 72 rrigaLIEApgfypnltARENLRLlarllgIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 754786342 489 EPTNHLDIDSIETLEE---ALEDFQGTIFFISHDRYFINKMSNRII 531
Cdd:cd03268 152 EPTNGLDPDGIKELRElilSLRDQGITVLISSHLLSEIQKVADRIG 197
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
348-535 |
7.05e-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: 93.05 E-value: 7.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYG--ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVK----------VAY 414
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISqwdpnelgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 415 LPQkisfnneelmlievfreDISIVEGKAREYLskfmfyqssvfkkvkyLSGGERIRLKLAILLYDEVNLLILDEPTNHL 494
Cdd:cd03246 81 LPQ-----------------DDELFSGSIAENI----------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 754786342 495 DIDSIETLEEALEDFQ---GTIFFISHDRYFInKMSNRIIAVED 535
Cdd:cd03246 128 DVEGERALNQAIAALKaagATRIVIAHRPETL-ASADRILVLED 170
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
348-562 |
7.07e-22 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 100.32 E-value: 7.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLK------------------------------------ 391
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipkncqilhveqevvgddttalqcvln 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 392 ------MLLGEE---HPDKGKIELGSNVKVAYLPQKISFNNEEL--MLIEVFRE----DISIVEGKAREYLSKFMFYQSS 456
Cdd:PLN03073 258 tdiertQLLEEEaqlVAQQRELEFETETGKGKGANKDGVDKDAVsqRLEEIYKRleliDAYTAEARAASILAGLSFTPEM 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 457 VFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVEDF 536
Cdd:PLN03073 338 QVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQ 417
|
250 260
....*....|....*....|....*.
gi 754786342 537 SLNSYLGNYDYYrhekEKFRQEQESN 562
Cdd:PLN03073 418 KLVTYKGDYDTF----ERTREEQLKN 439
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-529 |
8.91e-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: 99.11 E-value: 8.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgypqttsYGYDEG-LIHVLPRGAT 82
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQ------------YEPTSGrIIYHVALCEK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 83 SAYLEQVPDYPHGLKVMDNlNLAFEEIDAIEKQMREQEEQMKKV------------EGSTLEKALNKYSSLvhlyevkgG 150
Cdd:TIGR03269 69 CGYVERPSKVGEPCPVCGG-TLEPEEVDFWNLSDKLRRRIRKRIaimlqrtfalygDDTVLDNVLEALEEI--------G 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 151 YERDEKLSKVC-----TGLKFDESFLQRDfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYL----K 221
Cdd:TIGR03269 140 YEGKEAVGRAVdliemVQLSHRITHIARD---LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeavK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 222 NYKGIVLIVSHDRYFLDHVATKIVEIEDMEStsykgnyssfveqkeenlriqleqyreqqKKINTMEKQVkdlrdwaira 301
Cdd:TIGR03269 217 ASGISMVLTSHWPEVIEDLSDKAIWLENGEI-----------------------------KEEGTPDEVV---------- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 302 dnNKFFRRAASIQKrlSKMERLDKPVLERKNMRLTMSESERSgkeTIKATDltksygerllfrDAGVMVHYGERVGLIGP 381
Cdd:TIGR03269 258 --AVFMEGVSEVEK--ECEVEVGEPIIKVRNVSKRYISVDRG---VVKAVD------------NVSLEVKEGEIFGIVGT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 382 NGSGKTTFLKMLLGEEHPDKGKI------------ELGSNVKvAYLPQKISFNNEELML------IEVFREDISI----- 438
Cdd:TIGR03269 319 SGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtKPGPDGR-GRAKRYIGILHQEYDLyphrtvLDNLTEAIGLelpde 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 439 ---------------VEGKAREYLSKFmfyqssvfkkVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLD----IDSI 499
Cdd:TIGR03269 398 larmkavitlkmvgfDEEKAEEILDKY----------PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVT 467
|
570 580 590
....*....|....*....|....*....|
gi 754786342 500 ETLEEALEDFQGTIFFISHDRYFINKMSNR 529
Cdd:TIGR03269 468 HSILKAREEMEQTFIIVSHDMDFVLDVCDR 497
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
320-535 |
2.50e-21 |
|
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: 98.75 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 320 MERL----DKPVlERKNMRLTMSESERSGKetIKATDLTKSYG--ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKML 393
Cdd:COG2274 445 LERLddilDLPP-EREEGRSKLSLPRLKGD--IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 394 LGEEHPDKGKIEL-GSNVK----------VAYLPQKISF------NNeelmlIEVFREDIS---IVE-----GkAREYLS 448
Cdd:COG2274 522 LGLYEPTSGRILIdGIDLRqidpaslrrqIGVVLQDVFLfsgtirEN-----ITLGDPDATdeeIIEaarlaG-LHDFIE 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 449 KF-MFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQG--TIFFISHDRYFInK 525
Cdd:COG2274 596 ALpMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTI-R 674
|
250
....*....|
gi 754786342 526 MSNRIIAVED 535
Cdd:COG2274 675 LADRIIVLDK 684
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-241 |
8.37e-21 |
|
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: 92.41 E-value: 8.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyypgypQTTSYG---YDEGLIHVLPRG 80
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGL----------LKPSSGevlLDGRDLASLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 81 ATS---AYLEQVPDYPHGLKVMDNLNL-------AFEeidaiekqmREQEEQMKKVEgstleKALnkysslvhlyevkgg 150
Cdd:COG1120 72 ELArriAYVPQEPPAPFGLTVRELVALgryphlgLFG---------RPSAEDREAVE-----EAL--------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 151 yERdeklskvcTGLkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDM----DSIEWLENYLKNYKGI 226
Cdd:COG1120 123 -ER--------TGL---EHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRT 190
|
250 260
....*....|....*....|
gi 754786342 227 VLIVSHD-----RYFlDHVA 241
Cdd:COG1120 191 VVMVLHDlnlaaRYA-DRLV 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-249 |
8.55e-21 |
|
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: 89.76 E-value: 8.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgypqttsygYDEGLIHVL----PR 79
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK--------------PDSGEIKVLgkdiKK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 80 GATSA-----YLEQVPDYPHGLKVMDNLnlafeeidaiekqmreqeeqmkkvegstlekalnkysslvhlyevkggyerd 154
Cdd:cd03230 67 EPEEVkrrigYLPEEPSLYENLTVRENL---------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 155 eklskvctglkfdesflqrdfdYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK---GIVLIVS 231
Cdd:cd03230 95 ----------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSS 152
|
250
....*....|....*...
gi 754786342 232 HDRYFLDHVATKIVEIED 249
Cdd:cd03230 153 HILEEAERLCDRVAILNN 170
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
352-535 |
1.02e-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: 90.78 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 352 DLTKSYGE-RLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNV--------KVAYLPQKISFN 422
Cdd:cd03226 4 NISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPikakerrkSIGYVMQDVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 423 neeLMLIEVFRE------DISIVEGKAREYLSKFMFYQssvfKKVKY---LSGGERIRLKLAILLYDEVNLLILDEPTNH 493
Cdd:cd03226 84 ---LFTDSVREElllglkELDAGNEQAETVLKDLDLYA----LKERHplsLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 754786342 494 LDIDSIETLEEALEDFQG---TIFFISHDRYFINKMSNRIIAVED 535
Cdd:cd03226 157 LDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
348-531 |
1.03e-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: 91.41 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDA--GV--MVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV------------ 410
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKAldDVsfSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdGKDLlklsrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 411 -KVAYLPQKI--SFNneELMLI-EVFREDISIVEG-------KAREYLSKFMFYQSSVFKKvKY---LSGGERIRLKLAI 476
Cdd:cd03257 82 kEIQMVFQDPmsSLN--PRMTIgEQIAEPLRIHGKlskkearKEAVLLLLVGVGLPEEVLN-RYpheLSGGQRQRVAIAR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 754786342 477 LLYDEVNLLILDEPTNHLDIDS----IETLEEALEDFQGTIFFISHDRYFINKMSNRII 531
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVVAKIADRVA 217
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
347-535 |
1.17e-20 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 95.98 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSY-GERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG----SNV-------KVAY 414
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINgvdlSDLdpaswrrQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 415 LPQK-------ISFNneelmlIEVFREDIS---IVEGKAREYLSKFMF-----YQSSVFKKVKYLSGGERIRLKLAILLY 479
Cdd:COG4988 416 VPQNpylfagtIREN------LRLGRPDASdeeLEAALEAAGLDEFVAalpdgLDTPLGEGGRGLSGGQAQRLALARALL 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 480 DEVNLLILDEPTNHLDIDSIETLEEALED-FQG-TIFFISHDRYFINKMsNRIIAVED 535
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRlAKGrTVILITHRLALLAQA-DRILVLDD 546
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-249 |
1.33e-20 |
|
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: 90.23 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSYGYDEGLIHVLPRGATS 83
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP-------PSAGEVLWNGEPIRDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 --AYLEQVPDYPHGLKVMDNLNLAFeeidaiekqmreqeeQMKKVEGS--TLEKALnkysslvhlyevkggyerdEKLsk 159
Cdd:COG4133 76 rlAYLGHADGLKPELTVRENLRFWA---------------ALYGLRADreAIDEAL-------------------EAV-- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 160 vctGLkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK---GIVLIVSHDRYF 236
Cdd:COG4133 120 ---GL---AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLE 193
|
250
....*....|...
gi 754786342 237 LDhvATKIVEIED 249
Cdd:COG4133 194 LA--AARVLDLGD 204
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
322-495 |
2.06e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.97 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 322 RLDKPVLERKNMRLTMSESERSGKETIKATDL---TKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEH 398
Cdd:PRK13536 13 RLELSPIERKHQGISEAKASIPGSMSTVAIDLagvSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 399 PDKGKIE-LGSNV---------KVAYLPQkisFNNEELMLieVFREDIsIVEG-----KAREY------LSKFMFYQSSV 457
Cdd:PRK13536 93 PDAGKITvLGVPVpararlaraRIGVVPQ---FDNLDLEF--TVRENL-LVFGryfgmSTREIeavipsLLEFARLESKA 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 754786342 458 FKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLD 495
Cdd:PRK13536 167 DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
348-495 |
2.58e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.18 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV---------KVAYLPQ 417
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVpsrarharqRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 418 kisFNN--EELMLIE---VFREDISIVEGKAREY---LSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDE 489
Cdd:PRK13537 88 ---FDNldPDFTVREnllVFGRYFGLSAAAARALvppLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
....*.
gi 754786342 490 PTNHLD 495
Cdd:PRK13537 165 PTTGLD 170
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
348-518 |
2.70e-20 |
|
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: 88.25 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSnvkvaylpQKISFNNeelm 427
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------KEVSFAS---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 428 LIEVFREDISIVegkareylskfmfYQssvfkkvkyLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALE 507
Cdd:cd03216 69 PRDARRAGIAMV-------------YQ---------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIR 126
|
170
....*....|....
gi 754786342 508 DF--QG-TIFFISH 518
Cdd:cd03216 127 RLraQGvAVIFISH 140
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-245 |
3.00e-20 |
|
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: 89.57 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 14 DATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnYYPGYPQTTSYGYDEGLIHVLPRGATSAYLEQVPDYP 93
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL----YKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 94 HGlKVMDNLNLAFEEIDaiekqmreQEEQMKKVEGSTLEKALNKYsslvhlyevKGGYERDeklskvctglkfdesfLQR 173
Cdd:cd03245 91 YG-TLRDNITLGAPLAD--------DERILRAAELAGVTDFVNKH---------PNGLDLQ----------------IGE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754786342 174 DFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKG--IVLIVSHDRYFLDHVATKIV 245
Cdd:cd03245 137 RGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLDLVDRIIV 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
14-241 |
8.90e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 88.99 E-value: 8.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 14 DATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTtsygydeGLIHVLPRGATS-----AYLEQ 88
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP-------PTS-------GTVRLFGKPPRRarrriGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 89 V----PDYPhgLKVMDNLNLafeeidaiekqmreqeeqmkkveGSTLEKALNKYSSlvhlyevKGGYER-DEKLSKVctG 163
Cdd:COG1121 83 RaevdWDFP--ITVRDVVLM-----------------------GRYGRRGLFRRPS-------RADREAvDEALERV--G 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 164 LkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK--GI-VLIVSHD-----RY 235
Cdd:COG1121 129 L---EDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRreGKtILVVTHDlgavrEY 205
|
....*.
gi 754786342 236 FlDHVA 241
Cdd:COG1121 206 F-DRVL 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-249 |
1.28e-19 |
|
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: 88.16 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 11 KYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQttsygydEGLIHVlprgatsayleqvp 90
Cdd:COG1122 9 SYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLK-------PT-------SGEVLV-------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 91 dyphglkvmDNLNLAFEEIdaieKQMREQ--------EEQMkkVEgSTLEK--ALnkysSLVHLyevkgGYERDEKLSKV 160
Cdd:COG1122 61 ---------DGKDITKKNL----RELRRKvglvfqnpDDQL--FA-PTVEEdvAF----GPENL-----GLPREEIRERV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 161 -----CTGLkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNY--KGI-VLIVSH 232
Cdd:COG1122 116 eealeLVGL---EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGKtVIIVTH 192
|
250
....*....|....*..
gi 754786342 233 DRYFLDHVATKIVEIED 249
Cdd:COG1122 193 DLDLVAELADRVIVLDD 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
347-533 |
1.56e-19 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 92.35 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSY-GERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNV-----------KVAY 414
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladadadswrdQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 415 LPQK-------ISFNneelmlIEVFREDIS---IVEGKAREYLSKFM-----FYQSSVFKKVKYLSGGERIRLKLAILLY 479
Cdd:TIGR02857 401 VPQHpflfagtIAEN------IRLARPDASdaeIREALERAGLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 754786342 480 DEVNLLILDEPTNHLDIDSIETLEEALEDF-QG-TIFFISHDRYFINKMsNRIIAV 533
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALaQGrTVLLVTHRLALAALA-DRIVVL 529
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
348-490 |
1.61e-19 |
|
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: 87.98 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSN------------VKVAYL 415
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 416 PQKIS-FNN----EELMLI-EVFREDISIVEGKAREYLSKFMFyqSSVFKKVKY-LSGGERIRLKLAILLYDEVNLLILD 488
Cdd:cd03218 81 PQEASiFRKltveENILAVlEIRGLSKKEREEKLEELLEEFHI--THLRKSKASsLSGGERRRVEIARALATNPKFLLLD 158
|
..
gi 754786342 489 EP 490
Cdd:cd03218 159 EP 160
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
373-531 |
1.74e-19 |
|
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: 88.16 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNV----KVAYLpQKISF----NNE---ELMLIEVFR-----EDI 436
Cdd:cd03267 47 GEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrRKKFL-RRIGVvfgqKTQlwwDLPVIDSFYllaaiYDL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 437 SIVEGKAR-EYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEAL----EDFQG 511
Cdd:cd03267 126 PPARFKKRlDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLkeynRERGT 205
|
170 180
....*....|....*....|
gi 754786342 512 TIFFISHDRYFINKMSNRII 531
Cdd:cd03267 206 TVLLTSHYMKDIEALARRVL 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
348-531 |
2.41e-19 |
|
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: 87.49 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGS------------------- 408
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglppheiarlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 409 --------------NVKVAYLPQKISFnneeLMLIEVFREDISIVEgKAREYLsKFMFYQSSVFKKVKYLSGGERIRLKL 474
Cdd:cd03219 81 fqiprlfpeltvleNVMVAAQARTGSG----LLLARARREEREARE-RAEELL-ERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 475 AILLYDEVNLLILDEPT---NHLDIDSIETLEEALEDFQGTIFFISHDRYFINKMSNRII 531
Cdd:cd03219 155 ARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
347-535 |
3.12e-19 |
|
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: 91.75 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSY--GERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVK----------VA 413
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLgGVDLRdldeddlrrrIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 414 YLPQKISF------NN----------EELM----------LIEVFRE--DISIVEGKAReylskfmfyqssvfkkvkyLS 465
Cdd:COG4987 413 VVPQRPHLfdttlrENlrlarpdatdEELWaalervglgdWLAALPDglDTWLGEGGRR-------------------LS 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 466 GGERIRLKLA-ILLYDeVNLLILDEPTNHLDIDS----IETLEEALEDfqGTIFFISHDRYFINKMsNRIIAVED 535
Cdd:COG4987 474 GGERRRLALArALLRD-APILLLDEPTEGLDAATeqalLADLLEALAG--RTVLLITHRLAGLERM-DRILVLED 544
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-233 |
4.39e-19 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 86.66 E-value: 4.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMnyypgypqttsygyDEGLIHVL---PRG 80
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRP--------------TSGEVRVLgedVAR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 81 ATSAYLEQV------PDYPHGLKVMDNLNLAfeeidaiekqmreqeEQMKKVEGSTLEKALNKYSSLVHLYEVkggyeRD 154
Cdd:COG1131 67 DPAEVRRRIgyvpqePALYPDLTVRENLRFF---------------ARLYGLPRKEARERIDELLELFGLTDA-----AD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 155 EKLSKvctglkfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKG---IVLIVS 231
Cdd:COG1131 127 RKVGT------------------LSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAegkTVLLST 188
|
..
gi 754786342 232 HD 233
Cdd:COG1131 189 HY 190
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-241 |
5.24e-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: 86.05 E-value: 5.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 14 DATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyypgYPQTtsygydEGLIHVLPRGATS-----AYLEQ 88
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGL--------LKPT------SGSIRVFGKPLEKerkriGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 89 V----PDYPhgLKVMDNLNLAFeeIDAIEKQMREQEEQMKKVegstlekalnkysslvhlyevkggyerDEKLSKVctGL 164
Cdd:cd03235 76 RrsidRDFP--ISVRDVVLMGL--YGHKGLFRRLSKADKAKV---------------------------DEALERV--GL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 165 kfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK--GI-VLIVSHD----RYFL 237
Cdd:cd03235 123 ---SELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRreGMtILVVTHDlglvLEYF 199
|
....
gi 754786342 238 DHVA 241
Cdd:cd03235 200 DRVL 203
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-249 |
5.43e-19 |
|
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: 84.22 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 7 NGIKKYMDATlVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgypqttsygYDEGLIHVlprgatsayl 86
Cdd:cd00267 4 NLSFRYGGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK--------------PTSGEILI---------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 87 eqvpdyphglkvmDNLNLAFEEIDAIEKQMreqeeqmkkvegstlekalnkysSLVHlyevkggyerdeklskvctglkf 166
Cdd:cd00267 59 -------------DGKDIAKLPLEELRRRI-----------------------GYVP----------------------- 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 167 desflQrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNY--KGI-VLIVSHDRYFLDHVATK 243
Cdd:cd00267 80 -----Q-----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaeEGRtVIIVTHDPELAELAADR 149
|
....*.
gi 754786342 244 IVEIED 249
Cdd:cd00267 150 VIVLKD 155
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
348-535 |
1.03e-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: 85.15 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLL-FRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV------KVAYLPQKI 419
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 420 SFNNEELMLI---EVFrEDIS----IVEGKAREYLSKFMFYQSSVFKKVKY------LSGGERIRLKLAILLYDEVNLLI 486
Cdd:cd03292 81 GVVFQDFRLLpdrNVY-ENVAfaleVTGVPPREIRKRVPAALELVGLSHKHralpaeLSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 754786342 487 LDEPTNHLDIDSIETLEEALEDFQ---GTIFFISHDRYFINKMSNRIIAVED 535
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALER 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
18-241 |
1.06e-18 |
|
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: 84.02 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyypgypqttsygydeglihvLPRGATSAYLEQVPdyphgLK 97
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGL------------------------LKPSSGEILLDGKD-----LA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 98 VMDNLNLAfeeidaiekqmreqeeqmKKVegSTLEKALNKysslvhlyevkggyerdeklskvcTGLkfdESFLQRDFDY 177
Cdd:cd03214 65 SLSPKELA------------------RKI--AYVPQALEL------------------------LGL---AHLADRPFNE 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 178 LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS----IEWLENYLKNYKGIVLIVSHDryfLDHVA 241
Cdd:cd03214 98 LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHqielLELLRRLARERGKTVVMVLHD---LNLAA 162
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-249 |
1.18e-18 |
|
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: 84.62 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 11 KYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSYGYDEGLIHVLPRGATSAYLEQVP 90
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-------ESSGSILLNGKPIKAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 91 DYPHGLK-VMDNLNLAFEEIDAIEKQmreQEEQMKKVegstlekalnkysslvHLYEVKGGYERDeklskvctglkfdes 169
Cdd:cd03226 81 DYQLFTDsVREELLLGLKELDAGNEQ---AETVLKDL----------------DLYALKERHPLS--------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 170 flqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD---MDSIEWLENYLKNYKGIVLIVSHDRYFLDHVATKIVE 246
Cdd:cd03226 127 --------LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLL 198
|
...
gi 754786342 247 IED 249
Cdd:cd03226 199 LAN 201
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
346-496 |
1.45e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.98 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 346 ETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVK----------VAY 414
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLnGRPLAdwspaelarrRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 415 LPQKIS----FNNEElmLIEVFREDISIVEGKAREYLSKFM-----------FYQSsvfkkvkyLSGGERIRLKLAILL- 478
Cdd:PRK13548 81 LPQHSSlsfpFTVEE--VVAMGRAPHGLSRAEDDALVAAALaqvdlahlagrDYPQ--------LSGGEQQRVQLARVLa 150
|
170 180
....*....|....*....|...
gi 754786342 479 -----YDEVNLLILDEPTNHLDI 496
Cdd:PRK13548 151 qlwepDGPPRWLLLDEPTSALDL 173
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
348-535 |
1.46e-18 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 84.85 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYG----ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV------------ 410
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDIsklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 411 --KVAYLPQkiSFN---------NEEL--MLIEVFREDIsivEGKAREYLSKFMFyQSSVFKKVKYLSGGERIRLKLAIL 477
Cdd:cd03255 81 rrHIGFVFQ--SFNllpdltaleNVELplLLAGVPKKER---RERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754786342 478 LYDEVNLLILDEPTNHLDIDS----IETLEEALEDFQGTIFFISHDRyFINKMSNRIIAVED 535
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRD 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
348-531 |
1.63e-18 |
|
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: 84.64 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIE-LGSNV------KVAYLP---- 416
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfDGKPLdiaarnRIGYLPeerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 417 ----QKISfnnEELMLIEVFReDISIVEGKAR--EYLSKF--MFYQSsvfKKVKYLSGGERIRLKLAILLYDEVNLLILD 488
Cdd:cd03269 81 lypkMKVI---DQLVYLAQLK-GLKKEEARRRidEWLERLelSEYAN---KRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 754786342 489 EPTNHLDIDSIETLEEALEDFQG---TIFFISHDRYFINKMSNRII 531
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVL 199
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
347-490 |
1.86e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 85.08 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVK-----------VAY 414
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLdGEDIThlpmhkrarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 415 LPQKIS-FNN----EELMLI-EVFREDISIVEGKAREYLSKFmfyQSSVFKKVK--YLSGGERIRLKLAILLYDEVNLLI 486
Cdd:COG1137 83 LPQEASiFRKltveDNILAVlELRKLSKKEREERLEELLEEF---GITHLRKSKaySLSGGERRRVEIARALATNPKFIL 159
|
....
gi 754786342 487 LDEP 490
Cdd:COG1137 160 LDEP 163
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
348-535 |
2.06e-18 |
|
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: 84.11 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV--------KVAYLPQK 418
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVtgvpperrNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 419 IS----FNNEE-----LMLIEVFREDISIVEGKAREYLSKFMFYQssvfKKVKYLSGGERIRLKLAILLYDEVNLLILDE 489
Cdd:cd03259 81 YAlfphLTVAEniafgLKLRGVPKAEIRARVRELLELVGLEGLLN----RYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 754786342 490 PTNHLDIDSIETLEEALEDFQG----TIFFISHDRYFINKMSNRIIAVED 535
Cdd:cd03259 157 PLSALDAKLREELREELKELQRelgiTTIYVTHDQEEALALADRIAVMNE 206
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
347-490 |
2.91e-18 |
|
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: 84.63 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVK-----------VAY 414
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIdGQDIThlpmherarlgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 415 LPQKIS-FNN----EELMLIEVFREDIS--IVEGKAREYLSKFMFyQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLIL 487
Cdd:TIGR04406 81 LPQEASiFRKltveENIMAVLEIRKDLDraEREERLEALLEEFQI-SHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
...
gi 754786342 488 DEP 490
Cdd:TIGR04406 160 DEP 162
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
348-535 |
3.40e-18 |
|
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: 84.09 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV-------------KVA 413
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdGEDIsglseaelyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 414 YLPQK-------ISFNNEELMLIEVFREDISIVEGKAREYLSkFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLI 486
Cdd:cd03261 81 MLFQSgalfdslTVFENVAFPLREHTRLSEEEIREIVLEKLE-AVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 754786342 487 LDEPTNHLD-------IDSIETLEEALedfQGTIFFISHDRYFINKMSNRIIAVED 535
Cdd:cd03261 160 YDEPTAGLDpiasgviDDLIRSLKKEL---GLTSIMVTHDLDTAFAIADRIAVLYD 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
349-531 |
3.93e-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: 84.32 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 349 KATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGS-------------------- 408
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrditglpphriarlgiartf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 409 -------------NVKVAYLPQ-KISFNNEELMLIEVFREDISIVEgKAREYLsKFMFYQSSVFKKVKYLSGGERIRLKL 474
Cdd:COG0411 86 qnprlfpeltvleNVLVAAHARlGRGLLAALLRLPRARREEREARE-RAEELL-ERVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754786342 475 AILLYDEVNLLILDEPT---NHLDIDSI-ETLEEALEDFQGTIFFISHDRYFINKMSNRII 531
Cdd:COG0411 164 ARALATEPKLLLLDEPAaglNPEETEELaELIRRLRDERGITILLIEHDMDLVMGLADRIV 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-234 |
5.35e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 85.97 E-value: 5.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 3 ELKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPgypqttsygyDEGLIHV------ 76
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLET----P----------DSGRIVLngrdlf 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 77 --LP---RGAtsAYLEQvpDY---PHgLKVMDnlNLAFeeidAIEKQMREQEEQMKKVEgstlekalnKYSSLVHLyevk 148
Cdd:COG1118 68 tnLPpreRRV--GFVFQ--HYalfPH-MTVAE--NIAF----GLRVRPPSKAEIRARVE---------ELLELVQL---- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 149 ggyerdeklskvctglkfdESFLQRdfdY---LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDM---DSIE-WLENYLK 221
Cdd:COG1118 124 -------------------EGLADR---YpsqLSGGQRQRVALARALAVEPEVLLLDEPFGALDAkvrKELRrWLRRLHD 181
|
250
....*....|...
gi 754786342 222 NYKGIVLIVSHDR 234
Cdd:COG1118 182 ELGGTTVFVTHDQ 194
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
342-535 |
7.90e-18 |
|
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: 82.97 E-value: 7.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 342 RSGKETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELgsNVKVAYLpqkISF 421
Cdd:cd03220 17 SSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV--RGRVSSL---LGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 422 N---NEELmlieVFREDISIV---EGKAREYLSKFM-----------FYQssvfKKVKYLSGGERIRLKLAILLYDEVNL 484
Cdd:cd03220 92 GggfNPEL----TGRENIYLNgrlLGLSRKEIDEKIdeiiefselgdFID----LPVKTYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 485 LILDEPT----NHLDIDSIETLEEALEDfQGTIFFISHDRYFINKMSNRIIAVED 535
Cdd:cd03220 164 LLIDEVLavgdAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEK 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
373-541 |
8.17e-18 |
|
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: 82.34 E-value: 8.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG------SNVKVAYLPQ--KISFNNEELMLIEVF--REDISIVEGK 442
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdSRKKINLPPQqrKIGLVFQQYALFPHLnvRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 443 AR--------EYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDS----IETLEEALEDFQ 510
Cdd:cd03297 103 KRnredrisvDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKKNLN 182
|
170 180 190
....*....|....*....|....*....|.
gi 754786342 511 GTIFFISHDRYFINKMSNRIIAVEDFSLNSY 541
Cdd:cd03297 183 IPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
373-535 |
8.79e-18 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 82.64 E-value: 8.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVK----------VAYLPQKIS-FNN---EELMLIEVFREDIS 437
Cdd:cd03245 30 GEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdGTDIRqldpadlrrnIGYVPQDVTlFYGtlrDNITLGAPLADDER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 438 IVEGKAREYLSKFMF-----YQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQG- 511
Cdd:cd03245 110 ILRAAELAGVTDFVNkhpngLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGd 189
|
170 180
....*....|....*....|....*
gi 754786342 512 -TIFFISHdRYFINKMSNRIIAVED 535
Cdd:cd03245 190 kTLIIITH-RPSLLDLVDRIIVMDS 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
356-519 |
1.37e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.13 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 356 SYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQKISFNN------EELMLI 429
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDslpltvRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 430 EVF----------REDISIVE------GKAReyLSKfmfyqssvfKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNH 493
Cdd:NF040873 81 GRWarrglwrrltRDDRAAVDdalervGLAD--LAG---------RQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180
....*....|....*....|....*....
gi 754786342 494 LDIDSIETLEEALEDFQG---TIFFISHD 519
Cdd:NF040873 150 LDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
348-535 |
1.87e-17 |
|
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: 81.42 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL------GSNVKVAYLPQKI-- 419
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdglkltDDKKNINELRQKVgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 420 ---SFN---------NEELMLIEVFREDISIVEGKAREYLskfmfyqssvfKKV-------KY---LSGGERIRLKLAIL 477
Cdd:cd03262 81 vfqQFNlfphltvleNITLAPIKVKGMSKAEAEERALELL-----------EKVgladkadAYpaqLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754786342 478 LYDEVNLLILDEPTNHLDidsIETLEEALEDFQG------TIFFISHDRYFINKMSNRIIAVED 535
Cdd:cd03262 150 LAMNPKVMLFDEPTSALD---PELVGEVLDVMKDlaeegmTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
348-530 |
2.09e-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: 81.65 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGK-IELGSNV---------KVAYLPQ 417
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVvreprevrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 418 KISFNNE----ELMLIEVFREDISIVEGKAR-EYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTN 492
Cdd:cd03265 81 DLSVDDEltgwENLYIHARLYGVPGAERRERiDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 754786342 493 HLDI---DSI-ETLEEALEDFQGTIFFISHDRYFINKMSNRI 530
Cdd:cd03265 161 GLDPqtrAHVwEYIEKLKEEFGMTILLTTHYMEEAEQLCDRV 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-206 |
2.55e-17 |
|
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: 79.23 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 19 LEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSYGYDEGLIHVLPRGATS---AYLEQVP-DYPH 94
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS-------PTEGTILLDGQDLTDDERKSLRkeiGYVFQDPqLFPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 95 gLKVMDNL--NLAFEEIDAIEKQMReqeeqmkkvegstLEKALNKYsSLVHlyevkggyerdeklskvctglkFDESFLQ 172
Cdd:pfam00005 74 -LTVRENLrlGLLLKGLSKREKDAR-------------AEEALEKL-GLGD----------------------LADRPVG 116
|
170 180 190
....*....|....*....|....*....|....
gi 754786342 173 RDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTN 206
Cdd:pfam00005 117 ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
347-520 |
3.59e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 83.27 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG-----SNV-----KVAYLP 416
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNgrdlfTNLpprerRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 417 Q------------KISFNneelmlIEVFREDISIVEGKAREYLSKFmfyQSSVFKKvKY---LSGGERIRLKLAILLYDE 481
Cdd:COG1118 82 QhyalfphmtvaeNIAFG------LRVRPPSKAEIRARVEELLELV---QLEGLAD-RYpsqLSGGQRQRVALARALAVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 754786342 482 VNLLILDEPTNHLDIDSIETLE----EALEDFQGTIFFISHDR 520
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRrwlrRLHDELGGTTVFVTHDQ 194
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
348-534 |
5.05e-17 |
|
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: 79.15 E-value: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVmVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELgSNVKVAYLPQKISfnneelm 427
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELGV-VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVYKPQYID------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 428 lievfredisivegkareylskfmfyqssvfkkvkyLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALE 507
Cdd:cd03222 72 ------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170 180 190
....*....|....*....|....*....|.
gi 754786342 508 DF----QGTIFFISHDRYFINKMSNRIIAVE 534
Cdd:cd03222 116 RLseegKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-234 |
5.18e-17 |
|
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: 80.26 E-value: 5.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMnyypgypqttsygyDEGLI--------H 75
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERP--------------DSGEIlidgrdvtG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 76 VLPRGATSAYLEQVPD-YPHgLKVMDNLNLAFEEIDAIEKQMREQEEQMKKvegstlekalnkyssLVHLyevkggyerd 154
Cdd:cd03259 67 VPPERRNIGMVFQDYAlFPH-LTVAENIAFGLKLRGVPKAEIRARVRELLE---------------LVGL---------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 155 eklskvctglkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNY----KGIVLIV 230
Cdd:cd03259 121 -------------EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELqrelGITTIYV 187
|
....
gi 754786342 231 SHDR 234
Cdd:cd03259 188 THDQ 191
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-249 |
7.56e-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: 80.62 E-value: 7.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMnyypgypqttsygyDEGLIHV----LPRGATSAYLEQVpdyp 93
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP--------------WSGEVTFdgrpVTRRRRKAFRRRV---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 94 hglkvmdnlnlafeeidaiekQMREQEeqmkkVEGS-----TLEKALNKysSLVHLyevkGGYERDEKLSKVCT--GLkf 166
Cdd:COG1124 82 ---------------------QMVFQD-----PYASlhprhTVDRILAE--PLRIH----GLPDREERIAELLEqvGL-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 167 DESFLQRdfdY---LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMdSI--EWLeNYLKNYK---GI-VLIVSHDRYFL 237
Cdd:COG1124 128 PPSFLDR---YphqLSGGQRQRVAIARALILEPELLLLDEPTSALDV-SVqaEIL-NLLKDLReerGLtYLFVSHDLAVV 202
|
250
....*....|..
gi 754786342 238 DHVATKIVEIED 249
Cdd:COG1124 203 AHLCDRVAVMQN 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
348-531 |
9.75e-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: 79.44 E-value: 9.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYG----ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL------GSNVKVAYLPQ 417
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 418 KIS-------FNNEELMLiEVFREDISIVEGKAREYLSKFmfyQSSVFKKvKY---LSGGERIRLKLAILLYDEVNLLIL 487
Cdd:cd03293 81 QDAllpwltvLDNVALGL-ELQGVPKAEARERAEELLELV---GLSGFEN-AYphqLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 754786342 488 DEPTNHLDIDSIETLEEAL----EDFQGTIFFISHDryfINK---MSNRII 531
Cdd:cd03293 156 DEPFSALDALTREQLQEELldiwRETGKTVLLVTHD---IDEavfLADRVV 203
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-249 |
1.00e-16 |
|
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: 79.18 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEqmnyypgypqttsyGYDEGLIHVL------ 77
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI--------------KPDSGEITFDgksyqk 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 78 ---PRGATSAYLEQVPDYPHgLKVMDNLnlafeEIDAIEKQMREQEeqmkkvegstLEKALNkyssLVHLYEvkggyERD 154
Cdd:cd03268 67 nieALRRIGALIEAPGFYPN-LTARENL-----RLLARLLGIRKKR----------IDEVLD----VVGLKD-----SAK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 155 EKLSKVCTGLKfdesflQRdfdylsggekttVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK--GI-VLIVS 231
Cdd:cd03268 122 KKVKGFSLGMK------QR------------LGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRdqGItVLISS 183
|
250
....*....|....*...
gi 754786342 232 HDRYFLDHVATKIVEIED 249
Cdd:cd03268 184 HLLSEIQKVADRIGIINK 201
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
348-519 |
1.12e-16 |
|
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: 80.24 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV----------KVAYLP 416
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLaGVDLhglsrrararRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 417 QKISfNNEELMLIEV-----------FREDISIVEGKAREYLSKfMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLL 485
Cdd:TIGR03873 82 QDSD-TAVPLTVRDVvalgriphrslWAGDSPHDAAVVDRALAR-TELSHLADRDMSTLSGGERQRVHVARALAQEPKLL 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 754786342 486 ILDEPTNHLDIDS-IETLE--EALEDFQGTIFFISHD 519
Cdd:TIGR03873 160 LLDEPTNHLDVRAqLETLAlvRELAATGVTVVAALHD 196
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
348-519 |
2.42e-16 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 78.32 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYG--ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSN----------VKVAYL 415
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkaarQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 416 PQK-ISFNN----EELMLIEVFR-----EDISIVEGKAREY-LSKFMfyqssvFKKVKYLSGGERIRLKLAILLYDEVNL 484
Cdd:cd03263 81 PQFdALFDEltvrEHLRFYARLKglpksEIKEEVELLLRVLgLTDKA------NKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 754786342 485 LILDEPTNHLDIDSIETLEEALEDFQG--TIFFISHD 519
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-249 |
3.43e-16 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 77.72 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKLNgiKKYMDATLvleDVSLEAyDGDKIGIVGVNGSGKSTILKVIAGIEqmNYYPGYPQTTSYGYDEG--LIHVLP 78
Cdd:cd03297 1 MLCVDIE--KRLPDFTL---KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLE--KPDGGTIVLNGTVLFDSrkKINLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 79 RGATSAYL-EQVPDYPHgLKVMDNLnlAFEEIDAIEKQMREQEEQMkkvegstlekalnkySSLVHLyevkggyerdekl 157
Cdd:cd03297 73 QQRKIGLVfQQYALFPH-LNVRENL--AFGLKRKRNREDRISVDEL---------------LDLLGL------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 158 skvctglkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYL----KNYKGIVLIVSHD 233
Cdd:cd03297 122 ----------DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELkqikKNLNIPVIFVTHD 191
|
250
....*....|....*.
gi 754786342 234 RYFLDHVATKIVEIED 249
Cdd:cd03297 192 LSEAEYLADRIVVMED 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-249 |
3.43e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 78.17 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKlNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPqttsygyDEGLIHV---- 76
Cdd:COG2884 1 MIRFE-NVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEER-------P-------TSGQVLVngqd 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 77 ---LPRgatsaylEQVP-----------DY---PHgLKVMDNLNLAFEEIDAIEKQMREQ-EEQMKKVEgstLEKALNKY 138
Cdd:COG2884 66 lsrLKR-------REIPylrrrigvvfqDFrllPD-RTVYENVALPLRVTGKSRKEIRRRvREVLDLVG---LSDKAKAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 139 SslvhlyevkggyerdeklskvctglkfDEsflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLEN 218
Cdd:COG2884 135 P---------------------------HE---------LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIME 178
|
250 260 270
....*....|....*....|....*....|....
gi 754786342 219 YLK--NYKGI-VLIVSHDRYFLDHVATKIVEIED 249
Cdd:COG2884 179 LLEeiNRRGTtVLIATHDLELVDRMPKRVLELED 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
348-530 |
3.52e-16 |
|
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: 78.15 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLfRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV--------KVAYLPQK 418
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDItnlppekrDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 419 IS-------FNNEELMLIEVFREDISIvEGKAREyLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPT 491
Cdd:cd03299 80 YAlfphmtvYKNIAYGLKKRKVDKKEI-ERKVLE-IAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 754786342 492 NHLDIDS----IETLEEALEDFQGTIFFISHDRYFINKMSNRI 530
Cdd:cd03299 158 SALDVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKV 200
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
348-519 |
4.74e-16 |
|
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: 77.61 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKML-----LGEEHPDKGKIEL-GSNVKvaylpqKISF 421
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLdGKDIY------DLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 422 NNEEL-----MlieVF----------REDIS-------IVEGKAREYLSKFMFYQSSVFKKVK------YLSGGERIRLK 473
Cdd:cd03260 75 DVLELrrrvgM---VFqkpnpfpgsiYDNVAyglrlhgIKLKEELDERVEEALRKAALWDEVKdrlhalGLSGGQQQRLC 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 754786342 474 LAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQG--TIFFISHD 519
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
348-530 |
4.92e-16 |
|
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: 77.30 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVkVAYLPQK--------- 418
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD-VTDLPPKdrdiamvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 419 -------------ISFNneeLMLIEVFREDISI-VEGKAR-----EYLSkfmfyqssvfKKVKYLSGGERIRLKLAILLY 479
Cdd:cd03301 80 nyalyphmtvydnIAFG---LKLRKVPKDEIDErVREVAEllqieHLLD----------RKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 480 DEVNLLILDEPTNHLD----IDSIETLEEALEDFQGTIFFISHDRYFINKMSNRI 530
Cdd:cd03301 147 REPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRI 201
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
3-210 |
5.93e-16 |
|
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: 77.93 E-value: 5.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 3 ELKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSYGYDEGLIHVLPRGAT 82
Cdd:TIGR03873 1 GLRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALR-------PDAGTVDLAGVDLHGLSRRAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 83 S---AYLEQVPDYPHGLKVMDNLNLafeeidaiekqmreqeeqmkkveGSTLEKALNKYSSlvhlyevkggyERDEKLSK 159
Cdd:TIGR03873 74 ArrvALVEQDSDTAVPLTVRDVVAL-----------------------GRIPHRSLWAGDS-----------PHDAAVVD 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 754786342 160 VCTGLKFDESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDM 210
Cdd:TIGR03873 120 RALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDV 170
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
348-518 |
8.16e-16 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 76.64 E-value: 8.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSY----GERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELgSNVKVAYLP----QKI 419
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-DGFDVVKEPaearRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 420 SFNNEELMLIEVF--REDISIVEG---------KAR-EYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLIL 487
Cdd:cd03266 81 GFVSDSTGLYDRLtaRENLEYFAGlyglkgdelTARlEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190
....*....|....*....|....*....|....
gi 754786342 488 DEPTNHLDIDSIETLEEALE---DFQGTIFFISH 518
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRqlrALGKCILFSTH 194
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
347-519 |
8.28e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 78.61 E-value: 8.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV------KVAYLPqki 419
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEPLdpedrrRIGYLP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 420 sfnnEE--L---MLIE---VF--------REDIsivEGKAREYLSKF--MFYQSsvfKKVKYLSGGERIRLKLAILLYDE 481
Cdd:COG4152 78 ----EErgLypkMKVGeqlVYlarlkglsKAEA---KRRADEWLERLglGDRAN---KKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 754786342 482 VNLLILDEPTNHLDIDSIETLEEALEDF--QG-TIFFISHD 519
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELaaKGtTVIFSSHQ 188
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
347-503 |
1.15e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.50 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNV-----------KVAYL 415
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvealsaraasrRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 416 PQK--ISFNNEELMLIEVFR------------EDISIVEgKAREYLSKFMFyqssVFKKVKYLSGGERIRLKLAILLYDE 481
Cdd:PRK09536 83 PQDtsLSFEFDVRQVVEMGRtphrsrfdtwteTDRAAVE-RAMERTGVAQF----ADRPVTSLSGGERQRVLLARALAQA 157
|
170 180
....*....|....*....|...
gi 754786342 482 VNLLILDEPTNHLDID-SIETLE 503
Cdd:PRK09536 158 TPVLLLDEPTASLDINhQVRTLE 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-491 |
1.20e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.06 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgypqttsygYDEGLIHVL------ 77
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQ--------------PDSGEILLDgepvrf 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 78 --PRGATSA-----Y--LEQVPDyphgLKVMDNLNLAFEE-----IDaiEKQMREQ-EEQMKKVegstlekalnkysslv 142
Cdd:COG1129 71 rsPRDAQAAgiaiiHqeLNLVPN----LSVAENIFLGREPrrgglID--WRAMRRRaRELLARL---------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 143 hlyevkggyerdeklskvctGLKFDESFLQRDfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWL-----E 217
Cdd:COG1129 129 --------------------GLDIDPDTPVGD---LSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLfriirR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 218 nyLKNyKGI-VLIVSHdryFLDHVAT-----------KIVEIEDMESTSykgnyssfveqkeenlRIQLeqyreqqkkIN 285
Cdd:COG1129 186 --LKA-QGVaIIYISH---RLDEVFEiadrvtvlrdgRLVGTGPVAELT----------------EDEL---------VR 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 286 TMekqV-KDLRDwairadnnKFFRRAASIqkrlskmerlDKPVLErknmrltmsesersgketikATDLTKsygeRLLFR 364
Cdd:COG1129 235 LM---VgRELED--------LFPKRAAAP----------GEVVLE--------------------VEGLSV----GGVVR 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 365 DAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVK-----------VAYLPqkisfnnEE-----LM 427
Cdd:COG1129 270 DVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLdGKPVRirsprdairagIAYVP-------EDrkgegLV 342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 428 LIEVFREDISIV----------------EGKAREYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPT 491
Cdd:COG1129 343 LDLSIRENITLAsldrlsrgglldrrreRALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
348-535 |
1.21e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 76.62 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYG----ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV------------ 410
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdGQDIsslserelarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 411 --KVAYLPQkiSFN---------NEELMLIeVFREDISIVEGKAREYLSKFmfyqsSVFKKVKY----LSGGERIRlkLA 475
Cdd:COG1136 85 rrHIGFVFQ--FFNllpeltaleNVALPLL-LAGVSRKERRERARELLERV-----GLGDRLDHrpsqLSGGQQQR--VA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 476 I---LlydeVN---LLILDEPTNHLDIDS----IETLEEALEDFQGTIFFISHDRyFINKMSNRIIAVED 535
Cdd:COG1136 155 IaraL----VNrpkLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRD 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
348-530 |
1.48e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 76.51 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQKISFNNeelm 427
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNT---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 428 lieVF----------------------REDISIVEGKAREYLsKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLL 485
Cdd:cd03300 77 ---VFqnyalfphltvfeniafglrlkKLPKAEIKERVAEAL-DLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 754786342 486 ILDEPTNHLDIDSIETLEEALEDFQG----TIFFISHDRYFINKMSNRI 530
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQEEALTMSDRI 201
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
338-531 |
1.65e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.66 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 338 SESERSGKETIKATDLTKsYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELgsNVKVAYLpq 417
Cdd:COG1134 18 HEPSRSLKELLLRRRRTR-REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV--NGRVSAL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 418 kISFN---NEEL----------MLIEVFREDISIVEGKAREY--LSKFmFYQssvfkKVKYLSGGERIRLKLAILLYDEV 482
Cdd:COG1134 93 -LELGagfHPELtgreniylngRLLGLSRKEIDEKFDEIVEFaeLGDF-IDQ-----PVKTYSSGMRARLAFAVATAVDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 754786342 483 NLLILDEPTNHLDID----SIETLEEALEDfQGTIFFISHDRYFINKMSNRII 531
Cdd:COG1134 166 DILLVDEVLAVGDAAfqkkCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAI 217
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
348-535 |
1.80e-15 |
|
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: 74.66 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGE--RLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGsnvkvaylpqkisfnnee 425
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 426 lmlievfREDISIVEGKAREYLS----KFMFYQSSVFKKV-KYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDS-- 498
Cdd:cd03247 63 -------GVPVSDLEKALSSLISvlnqRPYLFDTTLRNNLgRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITer 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 754786342 499 --IETLEEALEDfqGTIFFISHDRYFINKMsNRIIAVED 535
Cdd:cd03247 136 qlLSLIFEVLKD--KTLIWITHHLTGIEHM-DKILFLEN 171
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
348-495 |
1.98e-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: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRD------AGVMvhygervGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVK--------- 411
Cdd:cd03264 1 LQLENLTKRYGKKRALDGvsltlgPGMY-------GLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLkqpqklrrr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 412 VAYLPQKI----SFNNEELMLIEVFREDISIVEGKAR--EYLSKFMFYQsSVFKKVKYLSGGERIRLKLAILLYDEVNLL 485
Cdd:cd03264 74 IGYLPQEFgvypNFTVREFLDYIAWLKGIPSKEVKARvdEVLELVNLGD-RAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170
....*....|
gi 754786342 486 ILDEPTNHLD 495
Cdd:cd03264 153 IVDEPTAGLD 162
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
348-531 |
4.06e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 76.66 E-value: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYgeRLLFRDAGVM-----------------------VHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKI 404
Cdd:COG4586 2 IEVENLSKTY--RVYEKEPGLKgalkglfrreyreveavddisftIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 405 ELGSNV----KVAYLpQKISF---NNEELM----LIEVFR-----EDISIVEGKAR-EYLSKfMFYQSSVFKK-VKYLSG 466
Cdd:COG4586 80 RVLGYVpfkrRKEFA-RRIGVvfgQRSQLWwdlpAIDSFRllkaiYRIPDAEYKKRlDELVE-LLDLGELLDTpVRQLSL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754786342 467 GERIRLKL-AILLYD-EVnlLILDEPTNHLDIDSIETLEEAL----EDFQGTIFFISHDRYFINKMSNRII 531
Cdd:COG4586 158 GQRMRCELaAALLHRpKI--LFLDEPTIGLDVVSKEAIREFLkeynRERGTTILLTSHDMDDIEALCDRVI 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-233 |
4.45e-15 |
|
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: 74.82 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMD----ATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgypqttsygYDEGLIHVL-- 77
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLER--------------PTSGEVLVDge 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 78 ----PRGATsAYLEQvpDY---PHgLKVMDNLNLAFEEIDAIEKQMREQ-EEQMKKVEgstLEKALNKYSSlvhlyevkg 149
Cdd:cd03293 67 pvtgPGPDR-GYVFQ--QDallPW-LTVLDNVALGLELQGVPKAEARERaEELLELVG---LSGFENAYPH--------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 150 gyerdeklskvctglkfdesflQrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD----MDSIEWLENYLKNYKG 225
Cdd:cd03293 131 ----------------------Q-----LSGGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGK 183
|
....*...
gi 754786342 226 IVLIVSHD 233
Cdd:cd03293 184 TVLLVTHD 191
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-249 |
5.79e-15 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 74.45 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKY----MDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSYGYDEGLIHVLPR 79
Cdd:cd03255 1 IELKNLSKTygggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR-------PTSGEVRVDGTDISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 80 GATSAY-LEQV----PDY---PHgLKVMDNLNLAFEEIDAIEKQMREQEEQM-KKVEgstLEKALNKYSSlvhlyevkgg 150
Cdd:cd03255 74 KELAAFrRRHIgfvfQSFnllPD-LTALENVELPLLLAGVPKKERRERAEELlERVG---LGDRLNHYPS---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 151 yerdeklskvctglkfdesflQrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS----IEWLENYLKNYKGI 226
Cdd:cd03255 140 ---------------------E-----LSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTT 193
|
250 260
....*....|....*....|...
gi 754786342 227 VLIVSHDRYFLDHvATKIVEIED 249
Cdd:cd03255 194 IVVVTHDPELAEY-ADRIIELRD 215
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-320 |
7.36e-15 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 77.90 E-value: 7.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 17 LVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSYGydeglihvLPRGATSAYLEQvpdypHGL 96
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELA-------PVSGEIG--------LAKGIKLGYFAQ-----HQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 97 kvmdnlnlafEEIDAIEKQMreqeEQMKKVEGSTLEKALNKYsslvhlyevKGGYE-RDEKLSKVCtglkfdESFlqrdf 175
Cdd:PRK10636 386 ----------EFLRADESPL----QHLARLAPQELEQKLRDY---------LGGFGfQGDKVTEET------RRF----- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 176 dylSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGIVLIVSHDRYFLDHVATKIVEIEDMESTSY 255
Cdd:PRK10636 432 ---SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPF 508
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 256 KGNYSSFVE-----QKEENlriQLEQYREQQKKINTMEKQVKDLRDWAIRADNNKFFRRAASIQKRLSKM 320
Cdd:PRK10636 509 DGDLEDYQQwlsdvQKQEN---QTDEAPKENNANSAQARKDQKRREAELRTQTQPLRKEIARLEKEMEKL 575
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-233 |
1.11e-14 |
|
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: 73.81 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPGYPQTTSYGYDeglIHVLPrgats 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFET----PTSGEILLDGKD---ITNLP----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 AYLEQV----PDY---PHgLKVMDNLnlAFeeidaiekQMReqeeqMKKVEGSTLEKALNKYSSLVHLyevkggyerdek 156
Cdd:cd03300 69 PHKRPVntvfQNYalfPH-LTVFENI--AF--------GLR-----LKKLPKAEIKERVAEALDLVQL------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 157 lskvctglkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK---GIVLI-VSH 232
Cdd:cd03300 121 -----------EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQkelGITFVfVTH 189
|
.
gi 754786342 233 D 233
Cdd:cd03300 190 D 190
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
18-249 |
1.37e-14 |
|
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: 77.11 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGieqmnYYPgyPQTTSY---GYDeglIHVLPRGATSAYLEQVPDYPH 94
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR-----FLD--PQSGSItlgGVD---LRDLDEDDLRRRIAVVPQRPH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 95 gL---KVMDNLNLAFEEIDaiekqmreqEEQMKKVegstLEKAlnkysSLVHLYE-VKGGYER--DEklskvcTGLKfde 168
Cdd:COG4987 420 -LfdtTLRENLRLARPDAT---------DEELWAA----LERV-----GLGDWLAaLPDGLDTwlGE------GGRR--- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 169 sflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSI-EWLENYLKNYKG-IVLIVSHDRYFLDHvATKIVE 246
Cdd:COG4987 472 ---------LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEqALLADLLEALAGrTVLLITHRLAGLER-MDRILV 541
|
...
gi 754786342 247 IED 249
Cdd:COG4987 542 LED 544
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
356-519 |
1.38e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.99 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 356 SYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQKISFNNEELMLIEVF--- 432
Cdd:PRK09544 13 SFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLTVNRFlrl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 433 -----REDI--SIVEGKAREYLSKFMfyqssvfkkvKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDI-------DS 498
Cdd:PRK09544 93 rpgtkKEDIlpALKRVQAGHLIDAPM----------QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVngqvalyDL 162
|
170 180
....*....|....*....|.
gi 754786342 499 IETLEEALEdfqGTIFFISHD 519
Cdd:PRK09544 163 IDQLRRELD---CAVLMVSHD 180
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-253 |
1.62e-14 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 73.00 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGdKIGIVGVNGSGKSTILKVIAGIEQMnyypgypqttsygyDEGLIHVLPRGATS 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPP--------------SSGTIRIDGQDVLK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 ---------AYLEQVPDYPHGLKVMDNLN-LAFeeidaiekqmreqeeqMKKVEGSTLEKALNKYSSLVHLYEVKggyer 153
Cdd:cd03264 66 qpqklrrriGYLPQEFGVYPNFTVREFLDyIAW----------------LKGIPSKEVKARVDEVLELVNLGDRA----- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 154 DEKLSKvctglkfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNykgivliVSHD 233
Cdd:cd03264 125 KKKIGS------------------LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSE-------LGED 179
|
250 260
....*....|....*....|
gi 754786342 234 RYFLdhVATKIVeiEDMEST 253
Cdd:cd03264 180 RIVI--LSTHIV--EDVESL 195
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
359-495 |
1.99e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.68 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 359 ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEE--HPDKGKIELGSNvkvaylpqKISfnnEELMLIEVFREDI 436
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDN--------QFG---REASLIDAIGRKG 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754786342 437 SIVEGK---AREYLSKFMFYqssvFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLD 495
Cdd:COG2401 111 DFKDAVellNAVGLSDAVLW----LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
348-531 |
2.82e-14 |
|
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: 72.70 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIE-LGSNV------KVAYLPQKIS 420
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvDGQDItglsekELYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 421 --------------FNNEELMLIEVFREDISIVEGKAREYLSkfMFYQSSVFKkvKY---LSGGERIRLKLA-------- 475
Cdd:COG1127 86 mlfqggalfdsltvFENVAFPLREHTDLSEAEIRELVLEKLE--LVGLPGAAD--KMpseLSGGMRKRVALAralaldpe 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754786342 476 ILLYdevnllilDEPTNHLD------IDS-IETLEEALedfQGTIFFISHDRYFINKMSNRII 531
Cdd:COG1127 162 ILLY--------DEPTAGLDpitsavIDElIRELRDEL---GLTSVVVTHDLDSAFAIADRVA 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-249 |
3.05e-14 |
|
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: 75.95 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 12 YMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGieqmnYYPGYpqttsygydEGLIHV-------LPRGATS- 83
Cdd:COG4988 346 YPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG-----FLPPY---------SGSILIngvdlsdLDPASWRr 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 --AYLEQVPDYPHGlKVMDNLNLAfeEIDAIEKQMREqeeqmkkvegstlekALNKysslVHLYEvkggyerdeklskvc 161
Cdd:COG4988 412 qiAWVPQNPYLFAG-TIRENLRLG--RPDASDEELEA---------------ALEA----AGLDE--------------- 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 162 tglkFDESfLQRDFDY--------LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKG--IVLIVS 231
Cdd:COG4988 455 ----FVAA-LPDGLDTplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILIT 529
|
250
....*....|....*...
gi 754786342 232 HDRYFLDHvATKIVEIED 249
Cdd:COG4988 530 HRLALLAQ-ADRILVLDD 546
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-233 |
3.76e-14 |
|
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: 75.47 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 12 YMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSYGYDEGLIHVLPRGATSAYLEQVPD 91
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-------PLQGEVTLDGVPVSSLDQDEVRRRVSVCAQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 92 YPH--GLKVMDNLNLAFEEIDaiekqmreQEEQMKKVEGSTLEKalnkysslvHLYEVKGGYErdeklSKVCTGLKFdes 169
Cdd:TIGR02868 417 DAHlfDTTVRENLRLARPDAT--------DEELWAALERVGLAD---------WLRALPDGLD-----TVLGEGGAR--- 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754786342 170 flqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMD-SIEWLENYLKNYKG-IVLIVSHD 233
Cdd:TIGR02868 472 --------LSGGERQRLALARALLADAPILLLDEPTEHLDAEtADELLEDLLAALSGrTVVLITHH 529
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-266 |
4.86e-14 |
|
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: 75.64 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 14 DATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQttsygydEGLIHVlprgatsayleqvpdyp 93
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE-------PT-------SGRILI----------------- 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 94 hglkvmDNLNLAFEEIDAIEKQMR--EQEEQMkkVEGSTLEkalNkysslvhlyeVKGGYER--DEKLSKVC--TGLkfd 167
Cdd:COG2274 535 ------DGIDLRQIDPASLRRQIGvvLQDVFL--FSGTIRE---N----------ITLGDPDatDEEIIEAArlAGL--- 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 168 ESFLQRD---FDY--------LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKG--IVLIVSH-- 232
Cdd:COG2274 591 HDFIEALpmgYDTvvgeggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHrl 670
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 754786342 233 ------DR-YFLDHvaTKIVEIEDMES-TSYKGNYSSFVEQK 266
Cdd:COG2274 671 stirlaDRiIVLDK--GRIVEDGTHEElLARKGLYAELVQQQ 710
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
348-535 |
6.12e-14 |
|
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: 71.83 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGE-RLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG----SNVKVAYLPQ---KI 419
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdiNKLKGKALRQlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 420 SFNNEELMLIE-------------------------VFREDISivegKAREYLSKFMFyQSSVFKKVKYLSGGERIRLKL 474
Cdd:cd03256 81 GMIFQQFNLIErlsvlenvlsgrlgrrstwrslfglFPKEEKQ----RALAALERVGL-LDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 475 AILLYDEVNLLILDEPTNHLDIDS----IETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVED 535
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASsrqvMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
347-507 |
6.19e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.85 E-value: 6.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG------------SNVKVAY 414
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdedisllplharARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 415 LPQKIS-------FNNeeLMLIEVFREDISIVEGKAREYLSKFMFYQSSVFKKV-KYLSGGERIRLKLAILLYDEVNLLI 486
Cdd:PRK10895 83 LPQEASifrrlsvYDN--LMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMgQSLSGGERRRVEIARALAANPKFIL 160
|
170 180
....*....|....*....|.
gi 754786342 487 LDEPTNHLDIDSIETLEEALE 507
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIE 181
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
348-538 |
9.56e-14 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 70.84 E-value: 9.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLL----FRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG-------SNVKVAYLP 416
Cdd:TIGR02211 2 LKCENLGKRYQEGKLdtrvLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNgqslsklSSNERAKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 417 QK------------ISFNNEELMLIEVFREDISIVEGKAREY--LSKFMFyQSSVFKKVKYLSGGERIRLKLAILLYDEV 482
Cdd:TIGR02211 82 NKklgfiyqfhhllPDFTALENVAMPLLIGKKSVKEAKERAYemLEKVGL-EHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 483 NLLILDEPTNHLDIDSIETLEEALEDF---QGTIFFI-SHDRYFINKMSnRIIAVEDFSL 538
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELnreLNTSFLVvTHDLELAKKLD-RVLEMKDGQL 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
18-247 |
1.07e-13 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 71.00 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSYGYDEGLIHVL------PRGATSAYLEQVPd 91
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK-------PTSGSIIFDGKDLLKLsrrlrkIRRKEIQMVFQDP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 92 yphglkvMDNLNLAFeeidAIEKQMREqeeqmkkvegstlekalnkysSLVHLYEVKGGYERDEKLSKVCTGLKFDESFL 171
Cdd:cd03257 92 -------MSSLNPRM----TIGEQIAE---------------------PLRIHGKLSKKEARKEAVLLLLVGVGLPEEVL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 172 QRdfdY---LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS----IEWLENyLKNYKGI-VLIVSHD----RYFLDH 239
Cdd:cd03257 140 NR---YpheLSGGQRQRVAIARALALNPKLLIADEPTSALDVSVqaqiLDLLKK-LQEELGLtLLFITHDlgvvAKIADR 215
|
250
....*....|..
gi 754786342 240 VAT----KIVEI 247
Cdd:cd03257 216 VAVmyagKIVEE 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
350-508 |
1.12e-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: 70.08 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 350 ATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNV----------KVAYLPQKI 419
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPlaeqrdepheNILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 420 SFNNeELMLIEVFR--------EDISIVEGKAREYLSKFmfyqssVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPT 491
Cdd:TIGR01189 83 GLKP-ELSALENLHfwaaihggAQRTIEDALAAVGLTGF------EDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170
....*....|....*..
gi 754786342 492 NHLDIDSIETLEEALED 508
Cdd:TIGR01189 156 TALDKAGVALLAGLLRA 172
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
348-495 |
1.48e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 70.79 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG------SNVKVAYLPQKI-- 419
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDgedltdSKKDINKLRRKVgm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 420 ---SFN---------NEELMLIEVFREDISIVEGKAREYLskfmfyqssvfKKV-------KY---LSGGE--RIrlklA 475
Cdd:COG1126 82 vfqQFNlfphltvleNVTLAPIKVKKMSKAEAEERAMELL-----------ERVgladkadAYpaqLSGGQqqRV----A 146
|
170 180
....*....|....*....|....
gi 754786342 476 I---LLYD-EVnlLILDEPTNHLD 495
Cdd:COG1126 147 IaraLAMEpKV--MLFDEPTSALD 168
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
347-519 |
1.74e-13 |
|
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: 70.45 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG----SNVKV---------- 412
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedaTDVPVqernvgfvfq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 413 --AYLPQKISFNNEELMLIE---VFREDISIVEGKAREYLsKFMfyQSSVFKKvKY---LSGGERIRLKLAILLYDEVNL 484
Cdd:cd03296 82 hyALFRHMTVFDNVAFGLRVkprSERPPEAEIRAKVHELL-KLV--QLDWLAD-RYpaqLSGGQRQRVALARALAVEPKV 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 754786342 485 LILDEPTNHLDIDSIETLEEAL----EDFQGTIFFISHD 519
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLrrlhDELHVTTVFVTHD 196
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
348-518 |
1.89e-13 |
|
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: 70.50 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGK------IELGsNVKVAYLPQKISF 421
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgERRG-GEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 422 NNEELML-------------------IEVFREDISIVEGKAREYLSKF-MFYQSSvfKKVKYLSGGERIRLKLAILLyde 481
Cdd:COG1119 83 VSPALQLrfprdetvldvvlsgffdsIGLYREPTDEQRERARELLELLgLAHLAD--RPFGTLSQGEQRRVLIARAL--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 754786342 482 VN---LLILDEPTNHLDIDSIETLEEALEDF--QG--TIFFISH 518
Cdd:COG1119 158 VKdpeLLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTH 201
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
335-534 |
2.23e-13 |
|
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: 73.24 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 335 LTMSESERSGKET--------IKATDLTKSYG-ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIE 405
Cdd:TIGR01193 453 LVDSEFINKKKRTelnnlngdIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIL 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 406 LG----SNVK-------VAYLPQK-----------ISFNNEELMLIEVFREDISIVEGKAReyLSKF-MFYQSSVFKKVK 462
Cdd:TIGR01193 533 LNgfslKDIDrhtlrqfINYLPQEpyifsgsilenLLLGAKENVSQDEIWAACEIAEIKDD--IENMpLGYQTELSEEGS 610
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754786342 463 YLSGGERIRLKLAILLYDEVNLLILDEPTNHLD-IDSIETLEEALEDFQGTIFFISHdRYFINKMSNRIIAVE 534
Cdd:TIGR01193 611 SISGGQKQRIALARALLTDSKVLILDESTSNLDtITEKKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLD 682
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
343-519 |
2.30e-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: 72.78 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 343 SGKETIKATDLTKSY-GERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG----SNVKVAYLPQ 417
Cdd:TIGR02868 330 LGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDgvpvSSLDQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 418 KISFNNEELML--------IEVFREDISivEGKAREYLSKFMF----------YQSSVFKKVKYLSGGERIRLKLAILLY 479
Cdd:TIGR02868 410 RVSVCAQDAHLfdttvrenLRLARPDAT--DEELWAALERVGLadwlralpdgLDTVLGEGGARLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 754786342 480 DEVNLLILDEPTNHLDidsIETLEEALED-FQG----TIFFISHD 519
Cdd:TIGR02868 488 ADAPILLLDEPTEHLD---AETADELLEDlLAAlsgrTVVLITHH 529
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
373-531 |
2.33e-13 |
|
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: 69.12 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLG--EEHPDKGKIEL-GSNVKVAYLPQKISFnneelmlieVFREDISIVEGKAREYLsk 449
Cdd:cd03213 35 GELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLInGRPLDKRSFRKIIGY---------VPQDDILHPTLTVRETL-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 450 fMFyqsSVfkKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLD----IDSIETLeEALEDFQGTIFFISHD-RYFIN 524
Cdd:cd03213 104 -MF---AA--KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDsssaLQVMSLL-RRLADTGRTIICSIHQpSSEIF 176
|
....*..
gi 754786342 525 KMSNRII 531
Cdd:cd03213 177 ELFDKLL 183
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
373-519 |
2.37e-13 |
|
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: 72.86 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKI-------------ELGSNVkvAYLPQKIsfnneELMlievfreDISIV 439
Cdd:COG4618 358 GEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdreELGRHI--GYLPQDV-----ELF-------DGTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 440 EGKAReylskfmFYQSSVFKKVK-----------------Y----------LSGGERIRLKLAILLYDEVNLLILDEPTN 492
Cdd:COG4618 424 ENIAR-------FGDADPEKVVAaaklagvhemilrlpdgYdtrigeggarLSGGQRQRIGLARALYGDPRLVVLDEPNS 496
|
170 180 190
....*....|....*....|....*....|
gi 754786342 493 HLDIDSIETLEEALEDF---QGTIFFISHD 519
Cdd:COG4618 497 NLDDEGEAALAAAIRALkarGATVVVITHR 526
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
350-507 |
2.70e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.13 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 350 ATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV-------KVAYLPQKiSF 421
Cdd:PRK13539 5 GEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdGGDIddpdvaeACHYLGHR-NA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 422 NNEELMLIE--VF------REDISIVEGKAREYLS-----KFmfyqssvfkkvKYLSGGERIRLKLAILLYDEVNLLILD 488
Cdd:PRK13539 84 MKPALTVAEnlEFwaaflgGEELDIAAALEAVGLAplahlPF-----------GYLSAGQKRRVALARLLVSNRPIWILD 152
|
170
....*....|....*....
gi 754786342 489 EPTNHLDIDSIETLEEALE 507
Cdd:PRK13539 153 EPTAALDAAAVALFAELIR 171
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-87 |
2.91e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.73 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 3 ELKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnYYPgypqttsygyDEGLIHVlpRGAT 82
Cdd:COG1134 26 ELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI----LEP----------TSGRVEV--NGRV 89
|
....*
gi 754786342 83 SAYLE 87
Cdd:COG1134 90 SALLE 94
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
338-530 |
3.06e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.79 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 338 SESERSGKETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG----SNVKVA 413
Cdd:PRK11607 10 AKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvdlSHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 414 YLPQKISFNNEEL---MLIE------VFREDISIVEGKAR--EYLSkFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEV 482
Cdd:PRK11607 90 QRPINMMFQSYALfphMTVEqniafgLKQDKLPKAEIASRvnEMLG-LVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 754786342 483 NLLILDEPTNHLDIDSIETLE----EALEDFQGTIFFISHDRYFINKMSNRI 530
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQlevvDILERVGVTCVMVTHDQEEAMTMAGRI 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-209 |
3.50e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 71.26 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMnyypgypqttsygyDEGLIHV---- 76
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDP--------------TSGEILIggrd 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 77 ---LP---RGAtsAYLEQVPD-YPHgLKVMDnlNLAFeeidaiekQMReqeeqMKKVEGSTLEKALNKYSSLVHLyevkg 149
Cdd:COG3839 67 vtdLPpkdRNI--AMVFQSYAlYPH-MTVYE--NIAF--------PLK-----LRKVPKAEIDRRVREAAELLGL----- 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 150 gyerdeklskvctglkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:COG3839 124 ------------------EDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
360-518 |
4.85e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 67.56 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 360 RLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQKISFnneelmlievfredisiV 439
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYL-----------------P 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754786342 440 EGKAREYLSkfmfYQSSvfkkvKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQGTIFFISH 518
Cdd:cd03223 77 LGTLREQLI----YPWD-----DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH 146
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-209 |
5.01e-13 |
|
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: 68.44 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMN----YYPGYPQTTSYGYDEGLIHVLPR 79
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTsgriYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 80 GATsayleqvpdYPHgLKVMDNLNLAFEeidaiekqMREQEEQmkkvegstlekalnkysslvhlyevkggyERDEKLSK 159
Cdd:cd03301 81 YAL---------YPH-MTVYDNIAFGLK--------LRKVPKD-----------------------------EIDERVRE 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 754786342 160 VCTGLKFDEsFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:cd03301 114 VAELLQIEH-LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
348-518 |
5.73e-13 |
|
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: 68.65 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGER---LLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG----SNVKVAYLPQKIS 420
Cdd:cd03248 12 VKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDgkpiSQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 421 FNNEELMLI-EVFREDIS----------IVEGK----AREYLSKFMF-YQSSVFKKVKYLSGGERIRLKLAILLYDEVNL 484
Cdd:cd03248 92 LVGQEPVLFaRSLQDNIAyglqscsfecVKEAAqkahAHSFISELASgYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 754786342 485 LILDEPTNHLDIDSIETLEEALEDF--QGTIFFISH 518
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH 207
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
350-506 |
6.02e-13 |
|
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: 67.90 E-value: 6.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 350 ATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELgSNVKVAYLPQKISFN------- 422
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL-NGGPLDFQRDSIARGllylgha 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 423 ---------NEELMLIEVFREDISIVEGKAREYLSKFMfyqssvFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNH 493
Cdd:cd03231 82 pgikttlsvLENLRFWHADHSDEQVEEALARVGLNGFE------DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170
....*....|...
gi 754786342 494 LDIDSIETLEEAL 506
Cdd:cd03231 156 LDKAGVARFAEAM 168
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-249 |
6.38e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 68.89 E-value: 6.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 2 LELKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIE-----QM---NYYPGYPQTTSygydEGL 73
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLEtpdsgQLniaGHQFDFSQKPS----EKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 74 IHVLpRGATSAYLEQVPDYPHgLKVMDNLnlafeeidaIEKQMreqeeqmkKVEGSTLEKALnkysslvhlyevkggyer 153
Cdd:COG4161 77 IRLL-RQKVGMVFQQYNLWPH-LTVMENL---------IEAPC--------KVLGLSKEQAR------------------ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 154 dEKLSKVCTGLKFDEsFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK--GIV-LIV 230
Cdd:COG4161 120 -EKAMKLLARLRLTD-KADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSqtGITqVIV 197
|
250
....*....|....*....
gi 754786342 231 SHDRYFLDHVATKIVEIED 249
Cdd:COG4161 198 THEVEFARKVASQVVYMEK 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-245 |
7.32e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.50 E-value: 7.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 2 LELKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMNyyPGYpqTTSYGYDEGLIHVLPRGA 81
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT--SGH--IRFHGTDVSRLHARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 82 TSAYlEQVPDYPHgLKVMDnlNLAFeEIDAIEKQMREQEEQMKKVEGSTLEKAlnkysSLVHLYEvkggyerdeklskvc 161
Cdd:PRK10851 77 GFVF-QHYALFRH-MTVFD--NIAF-GLTVLPRRERPNAAAIKAKVTQLLEMV-----QLAHLAD--------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 162 tglkfdesflqRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD----MDSIEWLENYLKNYKGIVLIVSHDRYFL 237
Cdd:PRK10851 132 -----------RYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDaqvrKELRRWLRQLHEELKFTSVFVTHDQEEA 200
|
....*...
gi 754786342 238 DHVATKIV 245
Cdd:PRK10851 201 MEVADRVV 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-241 |
8.69e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 67.26 E-value: 8.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQttsygydEGLIHVlPRGATSAYLEQ---VPD-YP 93
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR-------PT-------SGTVRR-AGGARVAYVPQrseVPDsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 94 hgLKVMDNLNL-AFEEIDAIEKQMREQEeqmkkvegSTLEKALnkysslvhlyevkggyERdeklskvcTGLkfdESFLQ 172
Cdd:NF040873 72 --LTVRDLVAMgRWARRGLWRRLTRDDR--------AAVDDAL----------------ER--------VGL---ADLAG 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754786342 173 RDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKG---IVLIVSHDryfLDHVA 241
Cdd:NF040873 115 RQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD---LELVR 183
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-240 |
8.82e-13 |
|
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: 68.36 E-value: 8.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKK-YMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMnyypgypqttsygyDEGLIHVLPRGAT 82
Cdd:cd03256 1 IEVENLSKtYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP--------------TSGSVLIDGTDIN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 83 SAYLEQVPDYPH--GLkVMDNLNLafeeidaIEKQmreqeeqmkkvegSTLEKAL-------NKYSSLVHLYEVKGGYER 153
Cdd:cd03256 67 KLKGKALRQLRRqiGM-IFQQFNL-------IERL-------------SVLENVLsgrlgrrSTWRSLFGLFPKEEKQRA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 154 DEKLSKVctGLkfDESFLQRdFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLK---NYKGIVLIV 230
Cdd:cd03256 126 LAALERV--GL--LDKAYQR-ADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKrinREEGITVIV 200
|
250
....*....|....*
gi 754786342 231 S-HD----RYFLDHV 240
Cdd:cd03256 201 SlHQvdlaREYADRI 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-249 |
1.39e-12 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 67.38 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKlnGIKKY----MDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSYGYDEGLIHV 76
Cdd:COG1136 4 LLELR--NLTKSygtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDR-------PTSGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 77 LPRGATSAY-------------LeqVPDyphgLKVMDNLNLAFEeIDAIEKQMREQ--EEQMKKVEgstLEKALNKYSSl 141
Cdd:COG1136 75 LSERELARLrrrhigfvfqffnL--LPE----LTALENVALPLL-LAGVSRKERREraRELLERVG---LGDRLDHRPS- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 142 vhlyevkggyerdeklskvctglkfdesflQrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS----IEWLE 217
Cdd:COG1136 144 ------------------------------Q-----LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLR 188
|
250 260 270
....*....|....*....|....*....|..
gi 754786342 218 NYLKNYKGIVLIVSHDRYFLDHvATKIVEIED 249
Cdd:COG1136 189 ELNRELGTTIVMVTHDPELAAR-ADRVIRLRD 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-249 |
1.41e-12 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 66.44 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMN----YYPGYPQTtsygyDEGLIHVLPR 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDsgsiLIDGEDLT-----DLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 80 GATSAYLEQVPDYPHgLKVMDNLNLAfeeidaiekqmreqeeqmkkvegstlekalnkysslvhlyevkggyerdeklsk 159
Cdd:cd03229 76 RRIGMVFQDFALFPH-LTVLENIALG------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 160 vctglkfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK---GI-VLIVSHDRY 235
Cdd:cd03229 101 ------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQaqlGItVVLVTHDLD 162
|
250
....*....|....
gi 754786342 236 FLDHVATKIVEIED 249
Cdd:cd03229 163 EAARLADRVVVLRD 176
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
373-535 |
1.48e-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: 70.52 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG----SNVKVAYLPQKISFNNEELMLI--------------EVFRE 434
Cdd:TIGR02203 358 GETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghdlADYTLASLRRQVALVSQDVVLFndtianniaygrteQADRA 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 435 DI--SIVEGKAREYLSKF-MFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQG 511
Cdd:TIGR02203 438 EIerALAAAYAQDFVDKLpLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ 517
|
170 180
....*....|....*....|....*.
gi 754786342 512 --TIFFISHDRYFINKmSNRIIAVED 535
Cdd:TIGR02203 518 grTTLVIAHRLSTIEK-ADRIVVMDD 542
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
348-526 |
1.68e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 66.78 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGeeHPDKgKIELGsnvkvaylpqKISFNNEELM 427
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKY-EVTEG----------EILFKGEDIT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 428 lievfreDISIVEgKAREYLskFMFYQSSV----FKKVKYL-------SGGERIRLKLAILLYDEVNLLILDEPTNHLDI 496
Cdd:cd03217 68 -------DLPPEE-RARLGI--FLAFQYPPeipgVKNADFLryvnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190
....*....|....*....|....*....|...
gi 754786342 497 DSIETLEEALEDFQG---TIFFISHDRYFINKM 526
Cdd:cd03217 138 DALRLVAEVINKLREegkSVLIITHYQRLLDYI 170
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
337-496 |
1.89e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.89 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 337 MSESERSGKETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNV------ 410
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswss 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 411 -----KVAYLPQKISfnNEELMLIevfREDISI-------------VEGKAR-EYLSKFMFYQSSVFKKVKYLSGGERIR 471
Cdd:PRK10575 81 kafarKVAYLPQQLP--AAEGMTV---RELVAIgrypwhgalgrfgAADREKvEEAISLVGLKPLAHRLVDSLSGGERQR 155
|
170 180
....*....|....*....|....*
gi 754786342 472 LKLAILLYDEVNLLILDEPTNHLDI 496
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-249 |
2.57e-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: 66.69 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGieqmNYYPgypqttsygyDEGLIHVLPRGATsayleqvpdyphglk 97
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG----NYLP----------DSGSILVRHDGGW--------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 98 vmdnLNLAfeeiDAIEKQM---REQE----EQ----MKKVegSTLEKAlnkYSSLVHLyevkgGYERDEKLSKVctglkf 166
Cdd:COG4778 77 ----VDLA----QASPREIlalRRRTigyvSQflrvIPRV--SALDVV---AEPLLER-----GVDREEARARA------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 167 dESFLQR-------------DFdylSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS----IEWLENYLKNykGIVLI 229
Cdd:COG4778 133 -RELLARlnlperlwdlppaTF---SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKAR--GTAII 206
|
250 260
....*....|....*....|.
gi 754786342 230 -VSHDRYFLDHVATKIVEIED 249
Cdd:COG4778 207 gIFHDEEVREAVADRVVDVTP 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
347-496 |
2.78e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.35 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAY----LPQKISFN 422
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLssrqLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 423 NEELM---------LIEVFR------------EDISIVEgKAREYLSKFMFYQssvfKKVKYLSGGERIRLKLAILLYDE 481
Cdd:PRK11231 82 PQHHLtpegitvreLVAYGRspwlslwgrlsaEDNARVN-QAMEQTRINHLAD----RRLTDLSGGQRQRAFLAMVLAQD 156
|
170
....*....|....*
gi 754786342 482 VNLLILDEPTNHLDI 496
Cdd:PRK11231 157 TPVVLLDEPTTYLDI 171
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-247 |
3.05e-12 |
|
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: 69.16 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKY-----MDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPgypqttsygyDEGLIHV-- 76
Cdd:COG1123 261 LEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR----P----------TSGSILFdg 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 77 -----LPRGATSAYLEQVpdyphglkvmdnlnlafeeidaiekQMREQeeqmkkvegstlekalNKYSSL---------- 141
Cdd:COG1123 327 kdltkLSRRSLRELRRRV-------------------------QMVFQ----------------DPYSSLnprmtvgdii 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 142 ---VHLYEVKGGYERDEK----LSKVctGLkfDESFLQRdfdY---LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMD 211
Cdd:COG1123 366 aepLRLHGLLSRAERRERvaelLERV--GL--PPDLADR---YpheLSGGQRQRVAIARALALEPKLLILDEPTSALDVS 438
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 754786342 212 SIEWLENYLKNYK---GI-VLIVSHD----RYFLDHVAT----KIVEI 247
Cdd:COG1123 439 VQAQILNLLRDLQrelGLtYLFISHDlavvRYIADRVAVmydgRIVED 486
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-240 |
3.38e-12 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 64.76 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyypgypqttsYGYDEGLIHVlprgats 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGL--------------YKPDSGEILV------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 ayleqvpdypHGlkvmdnlnlafeeidaiekqmreqeeqmKKVEGSTLEKALNKYSSLVHlyevkggyerdeklskvctg 163
Cdd:cd03216 60 ----------DG----------------------------KEVSFASPRDARRAGIAMVY-------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 164 lkfdesflQrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK--GI-VLIVSHdryFLDHV 240
Cdd:cd03216 82 --------Q-----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRaqGVaVIFISH---RLDEV 145
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
373-518 |
3.54e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 69.42 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG----SNVKVAYLPQKISFNNEELML--------IEVFREDIS--- 437
Cdd:COG1132 366 GETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDgvdiRDLTLESLRRQIGVVPQDTFLfsgtirenIRYGRPDATdee 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 438 IVE----GKAREYLSKFMF-YQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDF-QG 511
Cdd:COG1132 446 VEEaakaAQAHEFIEALPDgYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLmKG 525
|
....*...
gi 754786342 512 -TIFFISH 518
Cdd:COG1132 526 rTTIVIAH 533
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
12-245 |
4.23e-12 |
|
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: 68.85 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 12 YMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGieQMNYYPGypqTTSYGyDEGLIHVLP--RGATSAYLEQV 89
Cdd:TIGR02857 331 YPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG--FVDPTEG---SIAVN-GVPLADADAdsWRDQIAWVPQH 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 90 PDYPHGlKVMDNLNLAfeEIDAIEKQMREQEEQmkkVEGSTLEKALnkysslvhlyevKGGYERdeKLSKVCTGLkfdes 169
Cdd:TIGR02857 405 PFLFAG-TIAENIRLA--RPDASDAEIREALER---AGLDEFVAAL------------PQGLDT--PIGEGGAGL----- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 170 flqrdfdylSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS----IEWLENYLKNYkgIVLIVSHDRYFLdHVATKIV 245
Cdd:TIGR02857 460 ---------SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETeaevLEALRALAQGR--TVLLVTHRLALA-ALADRIV 527
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-216 |
4.30e-12 |
|
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: 66.65 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGieqmNYYPGYPQTtsygydeglIHVL--PRGA 81
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG----DLPPTYGND---------VRLFgeRRGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 82 T------------SAYLEQvpDYPHGLKVMDNLNLAFEeiDAIEKQMREQEEQMKKVEgSTLEkalnkyssLVHLyevkg 149
Cdd:COG1119 71 EdvwelrkriglvSPALQL--RFPRDETVLDVVLSGFF--DSIGLYREPTDEQRERAR-ELLE--------LLGL----- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754786342 150 gyerdeklskvctglkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWL 216
Cdd:COG1119 133 ------------------AHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELL 181
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
18-249 |
4.92e-12 |
|
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: 64.71 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyypgypqttsYGYDEGLIHVlprgatsayleqvpdyphglk 97
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRL--------------YDPTSGEILI--------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 98 vmDNLNLAfeEIDaiekqmreqeeqmkkvegstlEKALNKYSSLVhlyevkggyerdeklskvctglkFDESFLqrdFDY 177
Cdd:cd03228 62 --DGVDLR--DLD---------------------LESLRKNIAYV-----------------------PQDPFL---FSG 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 178 ------LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS-IEWLENYLKNYKG-IVLIVSHDRYFLDHvATKIVEIED 249
Cdd:cd03228 91 tireniLSGGQRQRIAIARALLRDPPILILDEATSALDPETeALILEALRALAKGkTVIVIAHRLSTIRD-ADRIIVLDD 169
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
348-534 |
6.19e-12 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 66.37 E-value: 6.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFR---------DAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGS---------- 408
Cdd:TIGR02769 3 LEVRDVTHTYRTGGLFGakqrapvltNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 409 ------NVKVAYLPQKISFNNE---ELMLIEVFR--EDISIVEGKAR-EYLSKFMFYQSSVFKKV-KYLSGGERIRLKLA 475
Cdd:TIGR02769 83 rrafrrDVQLVFQDSPSAVNPRmtvRQIIGEPLRhlTSLDESEQKARiAELLDMVGLRSEDADKLpRQLSGGQLQRINIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754786342 476 ILLYDEVNLLILDEPTNHLDI---DSIETLEEALEDFQGTIF-FISHDRYFINKMSNRIIAVE 534
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMvlqAVILELLRKLQQAFGTAYlFITHDLRLVQSFCQRVAVMD 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
348-518 |
6.75e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.13 E-value: 6.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGerllfrdaGVM--------VHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GsnvkvaylpQK 418
Cdd:COG3845 6 LELRGITKRFG--------GVVanddvsltVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdG---------KP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 419 ISFNN-------------EELMLIEVF----------------REDISIVEGKAREYLSKFMFyqsSV--FKKVKYLSGG 467
Cdd:COG3845 69 VRIRSprdaialgigmvhQHFMLVPNLtvaenivlgleptkggRLDRKAARARIRELSERYGL---DVdpDAKVEDLSVG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 754786342 468 ERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDF--QG-TIFFISH 518
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITH 199
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-254 |
8.38e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.91 E-value: 8.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 14 DATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyYPgypqttsYGydEGLIHvLPRGATSAYLEQVPDYP 93
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL-----WP-------YG--SGRIA-RPAGARVLFLPQRPYLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 94 HG-LKvmDNL---NLAfEEIDaiekqmreqEEQMKKVegstLEKAlnkysSLVHLYEvkggyerdeklskvctglKFDEs 169
Cdd:COG4178 439 LGtLR--EALlypATA-EAFS---------DAELREA----LEAV-----GLGHLAE------------------RLDE- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 170 flQRDFDY-LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKN-YKGIVLI-VSHdRYFLDHVATKIVE 246
Cdd:COG4178 479 --EADWDQvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPGTTVIsVGH-RSTLAAFHDRVLE 555
|
....*...
gi 754786342 247 IEDMESTS 254
Cdd:COG4178 556 LTGDGSWQ 563
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-252 |
8.91e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.91 E-value: 8.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKY---MDATLV--LEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGI-----EQMNYYPG--YPQTTSYGYDE 71
Cdd:TIGR03269 280 IKVRNVSKRyisVDRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVleptsGEVNVRVGdeWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 72 glihvlpRGATSAYL----EQVPDYPHGlKVMDNLNlafeeiDAIEKQMREQEEQMKKVegSTLEKAlnkysslvhlyev 147
Cdd:TIGR03269 360 -------RGRAKRYIgilhQEYDLYPHR-TVLDNLT------EAIGLELPDELARMKAV--ITLKMV------------- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 148 kgGYERDEKlskvctglkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD-MDSIEWLENYLKNYKGI 226
Cdd:TIGR03269 411 --GFDEEKA-----------EEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILKAREEM 477
|
250 260 270
....*....|....*....|....*....|....*..
gi 754786342 227 ---VLIVSHDRYFLDHVAT--------KIVEIEDMES 252
Cdd:TIGR03269 478 eqtFIIVSHDMDFVLDVCDraalmrdgKIVKIGDPEE 514
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
348-535 |
9.25e-12 |
|
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: 64.82 E-value: 9.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDagVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSnVKVAYLP----------- 416
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFD--LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-VDVTAAPpadrpvsmlfq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 417 -----------QKISFN-NEELMLIEVFREDISIVegKAREYLSKFMfyqssvFKKVKYLSGGERIRLKLAILLYDEVNL 484
Cdd:cd03298 78 ennlfahltveQNVGLGlSPGLKLTAEDRQAIEVA--LARVGLAGLE------KRLPGELSGGERQRVALARVLVRDKPV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 485 LILDEPTNHLD----IDSIETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVED 535
Cdd:cd03298 150 LLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDN 204
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
347-531 |
1.13e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 66.65 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV--------KVAYLPQ 417
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhGTDVsrlhardrKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 418 KIS-------FNNEEL---MLIEVFREDISIVEGKAREYLSKFMF------YQSSvfkkvkyLSGGERIRLKLAILLYDE 481
Cdd:PRK10851 82 HYAlfrhmtvFDNIAFgltVLPRRERPNAAAIKAKVTQLLEMVQLahladrYPAQ-------LSGGQKQRVALARALAVE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 754786342 482 VNLLILDEPTNHLDIDSIETLEEAL----EDFQGTIFFISHDRYFINKMSNRII 531
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRVV 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-232 |
1.17e-11 |
|
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: 64.61 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnYYPgypqttsygyDEGLIHVLPRGATS 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGI----ILP----------DSGEVLFDGKPLDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 A------YL-EQVPDYPHgLKVMDNLN-LAfeeidaiekqmreqeeQMKKVEGSTLEKALNKYSSLVHLYEVKggYERDE 155
Cdd:cd03269 67 AarnrigYLpEERGLYPK-MKVIDQLVyLA----------------QLKGLKKEEARRRIDEWLERLELSEYA--NKRVE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 156 KLSKvctglkfdesflqrdfdylsgGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKG---IVLIVSH 232
Cdd:cd03269 128 ELSK---------------------GNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTH 186
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
14-233 |
1.52e-11 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 65.11 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 14 DATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPqttsygyDEGLIH-----VLPRGATSAYLEQ 88
Cdd:COG1116 22 GGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEK-------P-------TSGEVLvdgkpVTGPGPDRGVVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 89 VPD-YPHgLKVMDNLNLAFEEIDAIEKQMREQ-EEQMKKVEgstLEKALNKYSSlvhlyevkggyerdeklskvctglkf 166
Cdd:COG1116 88 EPAlLPW-LTVLDNVALGLELRGVPKAERRERaRELLELVG---LAGFEDAYPH-------------------------- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754786342 167 desflQrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD------MDsiEWLENYLKNYKGIVLIVSHD 233
Cdd:COG1116 138 -----Q-----LSGGMRQRVAIARALANDPEVLLMDEPFGALDaltrerLQ--DELLRLWQETGKTVLFVTHD 198
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
359-534 |
1.62e-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: 64.81 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 359 ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSN----VKVAYLPQKISFN-NEELMLIEVFR 433
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlalADPAWLRRQVGVVlQENVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 434 EDIS----------IVEGK----AREYLSKF-MFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDS 498
Cdd:cd03252 94 DNIAladpgmsmerVIEAAklagAHDFISELpEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 754786342 499 IETLEEALEDFQG--TIFFISHdRYFINKMSNRIIAVE 534
Cdd:cd03252 174 EHAIMRNMHDICAgrTVIIIAH-RLSTVKNADRIIVME 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-249 |
1.88e-11 |
|
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: 64.09 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgypqttsygYDEGLIHV--LPRGA 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEE--------------PDSGTIIIdgLKLTD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 82 TSAYLEQVPD-----------YPHgLKVMDNLNLAFEEIdaieKQMREQEEQmkkvegstlEKALnkysslvhlyevkgg 150
Cdd:cd03262 67 DKKNINELRQkvgmvfqqfnlFPH-LTVLENITLAPIKV----KGMSKAEAE---------ERAL--------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 151 yerdEKLSKVctGL--KFDESFLQrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKN--YKGI 226
Cdd:cd03262 118 ----ELLEKV--GLadKADAYPAQ-----LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlaEEGM 186
|
250 260
....*....|....*....|....
gi 754786342 227 -VLIVSHDRYFLDHVATKIVEIED 249
Cdd:cd03262 187 tMVVVTHEMGFAREVADRVIFMDD 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-234 |
1.89e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 65.89 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPgypqttsygyDEGLIHV---- 76
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFET----P----------DSGRILLdgrd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 77 ---LP---RGAtsAYLEQvpDY---PHgLKVMDnlNLAFeeidAIEKQMREQEEQMKKVegstlEKALNkyssLVHLyev 147
Cdd:COG3842 69 vtgLPpekRNV--GMVFQ--DYalfPH-LTVAE--NVAF----GLRMRGVPKAEIRARV-----AELLE----LVGL--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 148 kggyerdeklskvctglkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNY---K 224
Cdd:COG3842 126 --------------------EGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqreL 185
|
250
....*....|.
gi 754786342 225 GI-VLIVSHDR 234
Cdd:COG3842 186 GItFIYVTHDQ 196
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
351-530 |
2.16e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.07 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 351 TDLTKSYGERLL----FRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVKVAYLPQKISFNNEE 425
Cdd:PRK11629 9 DNLCKRYQEGSVqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFnGQPMSKLSSAAKAELRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 426 LMLIEVFRE---DISIVEG-----------------KAREYLSKFMFYQSSVFKKVKyLSGGERIRLKLAILLYDEVNLL 485
Cdd:PRK11629 89 LGFIYQFHHllpDFTALENvamplligkkkpaeinsRALEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 754786342 486 ILDEPTNHLDI---DSIETLEEALEDFQGTIFF-ISHDRYFINKMSNRI 530
Cdd:PRK11629 168 LADEPTGNLDArnaDSIFQLLGELNRLQGTAFLvVTHDLQLAKRMSRQL 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
350-508 |
2.21e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.67 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 350 ATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVKvaylPQKISFNNEELML 428
Cdd:PRK13538 4 ARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIR----RQRDEYHQDLLYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 429 -----IevfREDISivegkAREYLSkfmFYQS-----------SVFKKV----------KYLSGGERIRLKLAILLYDEV 482
Cdd:PRK13538 80 ghqpgI---KTELT-----ALENLR---FYQRlhgpgddealwEALAQVglagfedvpvRQLSAGQQRRVALARLWLTRA 148
|
170 180
....*....|....*....|....*.
gi 754786342 483 NLLILDEPTNHLDIDSIETLEEALED 508
Cdd:PRK13538 149 PLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-233 |
2.86e-11 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 63.89 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMdATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSYGYDEGLIHVLP---RG 80
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK-------PDSGKILLNGKDITNLPpekRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 81 AtsAYLEQvpDY---PHgLKVMDNlnlafeeidaIEKQMREQEEqMKKvegstlekalnkysslvhlyevkggyERDEKL 157
Cdd:cd03299 73 I--SYVPQ--NYalfPH-MTVYKN----------IAYGLKKRKV-DKK--------------------------EIERKV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 158 SKVCTGLKFDEsFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLK----NYKGIVLIVSHD 233
Cdd:cd03299 111 LEIAEMLGIDH-LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKkirkEFGVTVLHVTHD 189
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-54 |
3.00e-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: 63.71 E-value: 3.00e-11
10 20 30
....*....|....*....|....*....|....*..
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQ 54
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP 73
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
348-535 |
3.08e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.36 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSY-GERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG-------SNVKVAYLPQKI 419
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghditrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 420 S--FNNEELMLIEVFREDIS---IVEGKAREYLSKFMfyqSSVFKKVKY----------LSGGERIRLKLAILLYDEVNL 484
Cdd:PRK10908 82 GmiFQDHHLLMDRTVYDNVAiplIIAGASGDDIRRRV---SAALDKVGLldkaknfpiqLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 754786342 485 LILDEPTNHLDIDSIETLEEALEDFQG---TIFFISHDRYFINKMSNRIIAVED 535
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-232 |
3.55e-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: 63.66 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 14 DATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnYYPGYPQTTSYGYDEGLIhvlprgATSAYLEQVpdyp 93
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF----YVPENGRVLVDGHDLALA------DPAWLRRQV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 94 hGLKVMDNLNLAFEEIDAIeKQMREQEEQMKKVEGSTLEKALNKYSSLVHLYEVKGGyERDEKlskvctglkfdesflqr 173
Cdd:cd03252 79 -GVVLQENVLFNRSIRDNI-ALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVG-EQGAG----------------- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754786342 174 dfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSiewLENYLKNYKGI-----VLIVSH 232
Cdd:cd03252 139 ----LSGGQRQRIAIARALIHNPRILIFDEATSALDYES---EHAIMRNMHDIcagrtVIIIAH 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
348-518 |
3.58e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVK-----------VAYL 415
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPVRfrsprdaqaagIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 416 PQkisfnneELMLIevfrEDISIVE----G----------------KAREYLSKFMFyQSSVFKKVKYLSGGERirlKL- 474
Cdd:COG1129 85 HQ-------ELNLV----PNLSVAEniflGreprrgglidwramrrRARELLARLGL-DIDPDTPVGDLSVAQQ---QLv 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 754786342 475 AIL--LYDEVNLLILDEPTNHLDIDSIETLEEALEDF--QG-TIFFISH 518
Cdd:COG1129 150 EIAraLSRDARVLILDEPTASLTEREVERLFRIIRRLkaQGvAIIYISH 198
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
4-249 |
4.05e-11 |
|
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: 65.13 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLvleDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMnyypgypqttsygyDEGLIHV------- 76
Cdd:TIGR02142 1 LSARFSKRLGDFSL---DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRP--------------DEGEIVLngrtlfd 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 77 ------LP--RGATSAYLEQVPDYPHgLKVMDNLNLAFEEIDAIEKQMREQEeqmkkvegstLEKALNkyssLVHLyevk 148
Cdd:TIGR02142 64 srkgifLPpeKRRIGYVFQEARLFPH-LSVRGNLRYGMKRARPSERRISFER----------VIELLG----IGHL---- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 149 ggyerdeklskvctglkfdesfLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS----IEWLENYLKNYK 224
Cdd:TIGR02142 125 ----------------------LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRkyeiLPYLERLHAEFG 182
|
250 260
....*....|....*....|....*
gi 754786342 225 GIVLIVSHDRYFLDHVATKIVEIED 249
Cdd:TIGR02142 183 IPILYVSHSLQEVLRLADRVVVLED 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
348-535 |
4.36e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.94 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLF---------RDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIE-LGSNVKVAYLPQ 417
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 418 KISFNNEELMlieVFREDISIV-------------------------EGKAREYLSKFMFYQSSVFKKVKYLSGGERIRL 472
Cdd:PRK10419 84 RKAFRRDIQM---VFQDSISAVnprktvreiireplrhllsldkaerLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754786342 473 KLAILLYDEVNLLILDEPTNHLDI---DSIETLEEALEDFQGTIF-FISHDRYFINKMSNRIIAVED 535
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLvlqAGVIRLLKKLQQQFGTAClFITHDLRLVERFCQRVMVMDN 227
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
373-532 |
4.67e-11 |
|
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: 61.24 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIelgsnvkvaylpqkISFNNEELMLIEVFREDISIVEGKAREylskfmf 452
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------------IYIDGEDILEEVLDQLLLIIVGGKKAS------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 453 yqssvfkkvkyLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQG---------TIFFISHDRYFI 523
Cdd:smart00382 61 -----------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllkseknlTVILTTNDEKDL 129
|
....*....
gi 754786342 524 NKMSNRIIA 532
Cdd:smart00382 130 GPALLRRRF 138
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
373-496 |
4.98e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.58 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKI----------------ELGS--------NVKVAYLPQKISfnneelML 428
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkrfrgtELQDyfkklangEIKVAHKPQYVD------LI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 429 IEVFRedisiveGKAREYLSK------------FMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDI 496
Cdd:COG1245 173 PKVFK-------GTVRELLEKvdergkldelaeKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-277 |
5.14e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.11 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQ--------MNYYPGYPQTTsygyDEGLIH 75
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMprsgtlniAGNHFDFSKTP----SDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 76 VLpRGATSAYLEQVPDYPHgLKVMDNLnlafeeidaIEKQMReqeeqmkkVEGSTLEKALnkysslvhlyevkggyerdE 155
Cdd:PRK11124 79 EL-RRNVGMVFQQYNLWPH-LTVQQNL---------IEAPCR--------VLGLSKDQAL-------------------A 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 156 KLSKVCTGLKFDEsFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD-------MDSIEWLENylknyKGIV- 227
Cdd:PRK11124 121 RAEKLLERLRLKP-YADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqiVSIIRELAE-----TGITq 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 754786342 228 LIVSHDRYFLDHVATKIVEIED---MEstsyKGNYSSFVEQKEEnlriQLEQY 277
Cdd:PRK11124 195 VIVTHEVEVARKTASRVVYMENghiVE----QGDASCFTQPQTE----AFKNY 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-209 |
5.69e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 64.86 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPGYPQTTSYGYDegLIHVLP-RGAT 82
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQ----PTAGQIMLDGVD--LSHVPPyQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 83 SAYLEQVPDYPHgLKVMDNLNLAFeeidaiekqmreQEEQMKKVEgstLEKALNKYSSLVHLYEvkggyerdeklskvct 162
Cdd:PRK11607 94 NMMFQSYALFPH-MTVEQNIAFGL------------KQDKLPKAE---IASRVNEMLGLVHMQE---------------- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 754786342 163 glkfdesFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:PRK11607 142 -------FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
348-520 |
6.29e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 64.35 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG----SNVK-----VAYLPQK 418
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvTGLPpekrnVGMVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 419 ------------ISFNneeLMLIEVFREDIsivEGKAREYLSkfMF----YQSsvfKKVKYLSGGERIRLKLAILLYDEV 482
Cdd:COG3842 86 yalfphltvaenVAFG---LRMRGVPKAEI---RARVAELLE--LVglegLAD---RYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 754786342 483 NLLILDEPTNHLDIDSIETLEEAL----EDFQGTIFFISHDR 520
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELrrlqRELGITFIYVTHDQ 196
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
347-531 |
6.96e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.85 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGS------------NVKVAY 414
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslsqqKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 415 LPQKISFNNEELML----------IE----VFREDISIVEGKAREYLSKFMFYQssvfKKVKY---LSGGERIRLKLAIL 477
Cdd:PRK11264 83 LRQHVGFVFQNFNLfphrtvleniIEgpviVKGEPKEEATARARELLAKVGLAG----KETSYprrLSGGQQQRVAIARA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 754786342 478 LYDEVNLLILDEPTNHLDIDSI-ETLE--EALEDFQGTIFFISHDRYFINKMSNRII 531
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVgEVLNtiRQLAQEKRTMVIVTHEMSFARDVADRAI 215
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
378-534 |
7.35e-11 |
|
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: 61.85 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 378 LIGPNGSGKTTF---LKMLLGEEHPDKGKielgsnvKVAYLPqKISFNNEELMLIEVFREDISIVEGKAREYLSKF---- 450
Cdd:cd03240 27 IVGQNGAGKTTIieaLKYALTGELPPNSK-------GGAHDP-KLIREGEVRAQVKLAFENANGKKYTITRSLAILenvi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 451 MFYQSSVFK----KVKYLSGGER------IRLKLAILLYDEVNLLILDEPTNHLDIDSIET-LEEALEDFQGTIFF---- 515
Cdd:cd03240 99 FCHQGESNWplldMRGRCSGGEKvlasliIRLALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKNFqliv 178
|
170
....*....|....*....
gi 754786342 516 ISHDRYFINKMSNrIIAVE 534
Cdd:cd03240 179 ITHDEELVDAADH-IYRVE 196
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
348-535 |
7.45e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 62.79 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKM---LLGeehPDKGKIEL-GSNV----------KVA 413
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMisrLLP---PDSGEVLVdGLDVattpsrelakRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 414 YLPQKISFNN----EELmlieV-F-----------REDISIVEgKAREYLS------KFMfyqssvfkkvKYLSGGERIR 471
Cdd:COG4604 79 ILRQENHINSrltvREL----VaFgrfpyskgrltAEDREIID-EAIAYLDledladRYL----------DELSGGQRQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754786342 472 LKLAILLYDEVNLLILDEPTNHLDI----DSIETLEEALEDFQGTIFFISHDryfIN---KMSNRIIAVED 535
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD---INfasCYADHIVAMKD 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-249 |
9.02e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.77 E-value: 9.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgypqtTSYGydegliHVLprgATS 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLET----------PSAG------ELL---AGT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 AYLEQVPDYPHGL----------KVMDNLNLAfeeidaiekqmreqeeqmkkVEGSTLEKALnkysslvhlyevkggyer 153
Cdd:PRK11247 74 APLAEAREDTRLMfqdarllpwkKVIDNVGLG--------------------LKGQWRDAAL------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 154 dEKLSKVctGLKfdesflQRDFDY---LSGGEKTTVILGKLLIHNPNILLLDEPTNHLD-MDSIEW---LENYLKNYKGI 226
Cdd:PRK11247 116 -QALAAV--GLA------DRANEWpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDaLTRIEMqdlIESLWQQHGFT 186
|
250 260
....*....|....*....|...
gi 754786342 227 VLIVSHDRYFLDHVATKIVEIED 249
Cdd:PRK11247 187 VLLVTHDVSEAVAMADRVLLIEE 209
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
348-535 |
9.56e-11 |
|
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: 62.24 E-value: 9.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGE-RLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL----GSNVKVAYLPQKISFN 422
Cdd:cd03254 3 IEFENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdgidIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 423 NEELML--------IEVFREDIS----IVEGKAREYLSKFMF----YQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLI 486
Cdd:cd03254 83 LQDTFLfsgtimenIRLGRPNATdeevIEAAKEAGAHDFIMKlpngYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 754786342 487 LDEPTNHLDIDSIETLEEALED-FQG-TIFFISHdRYFINKMSNRIIAVED 535
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKlMKGrTSIIIAH-RLSTIKNADKILVLDD 212
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
352-535 |
1.27e-10 |
|
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: 61.86 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 352 DLTKSYG--ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG----SNVKVAYLPQKISFNNEE 425
Cdd:cd03251 5 NVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghdvRDYTLASLRRQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 426 LMLI-EVFREDISI---------VEGKARE-YLSKFMF-----YQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDE 489
Cdd:cd03251 85 VFLFnDTVAENIAYgrpgatreeVEEAARAaNAHEFIMelpegYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 754786342 490 PTNHLDIDSIETLEEALEDFQG--TIFFISHdRYFINKMSNRIIAVED 535
Cdd:cd03251 165 ATSALDTESERLVQAALERLMKnrTTFVIAH-RLSTIENADRIVVLED 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
348-518 |
1.73e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 63.97 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGER---LLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELgSNVKVA-----YLPQKI 419
Cdd:TIGR00958 479 IEFQDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-DGVPLVqydhhYLHRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 420 SFNNEELMLIE-VFREDI--------------SIVEGKAREYLSKF-MFYQSSVFKKVKYLSGGERIRLKLAILLYDEVN 483
Cdd:TIGR00958 558 ALVGQEPVLFSgSVRENIaygltdtpdeeimaAAKAANAHDFIMEFpNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
|
170 180 190
....*....|....*....|....*....|....*
gi 754786342 484 LLILDEPTNHLDIDSIETLEEALEDFQGTIFFISH 518
Cdd:TIGR00958 638 VLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-232 |
2.19e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.66 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 17 LVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSYGYDEGLIHVLPRGATSAYLEqvpdypH-- 94
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP-------PAAGTIKLDGGDIDDPDVAEACHYLG------Hrn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 95 GLKvmDNL----NLAFEeidaieKQMREQEEqmkkvegSTLEKALNKYSsLVHLYEVKGGYerdeklskvctglkfdesf 170
Cdd:PRK13539 83 AMK--PALtvaeNLEFW------AAFLGGEE-------LDIAAALEAVG-LAPLAHLPFGY------------------- 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 171 lqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLK---NYKGIVLIVSH 232
Cdd:PRK13539 128 -------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRahlAQGGIVIAATH 185
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
352-518 |
2.20e-10 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 61.09 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 352 DLTKSYG-ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG----SNVKVAYLPQKIS------ 420
Cdd:cd03253 5 NVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdiREVTLDSLRRAIGvvpqdt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 421 --FNNEELMLIEVFREDIS---IVEG--KAR--EYLSKFMF-YQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEP 490
Cdd:cd03253 85 vlFNDTIGYNIRYGRPDATdeeVIEAakAAQihDKIMRFPDgYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190
....*....|....*....|....*....|
gi 754786342 491 TNHLDIDSIETLEEALED-FQG-TIFFISH 518
Cdd:cd03253 165 TSALDTHTEREIQAALRDvSKGrTTIVIAH 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
348-535 |
2.21e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.93 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQKISFNNEELM 427
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 428 LIEVFREDISIVEGKAR-EYLSKFMFYQ-------------------SSVFKKVKYLSGGERIRLKLAILLYDEVNLLIL 487
Cdd:PRK10253 88 QNATTPGDITVQELVARgRYPHQPLFTRwrkedeeavtkamqatgitHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 754786342 488 DEPTNHLD----IDSIETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVED 535
Cdd:PRK10253 168 DEPTTWLDishqIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALRE 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
373-496 |
2.29e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 61.39 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEeHPDKGKIEL-GSNVKV----------AYLPQkisfNNEELMLIEVFredisiveg 441
Cdd:COG4138 22 GELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLnGRPLSDwsaaelarhrAYLSQ----QQSPPFAMPVF--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 442 karEYLSkfmFYQSSVF-----------------------KKVKYLSGGE--RIRLKLAIL-LYDEVN----LLILDEPT 491
Cdd:COG4138 88 ---QYLA---LHQPAGAsseaveqllaqlaealgledklsRPLTQLSGGEwqRVRLAAVLLqVWPTINpegqLLLLDEPM 161
|
....*
gi 754786342 492 NHLDI 496
Cdd:COG4138 162 NSLDV 166
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-240 |
2.33e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 61.24 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyyPGYPQTtsygydEGLIHVlpRGATsaYLEQVPD------ 91
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH------PKYEVT------SGSILL--DGED--ILELSPDerarag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 92 ------YP---HGLKVMDNLNLAFEEIDAIEKQMREQEEQMKkvegstlekalnkysslvhlyevkggyerdEKLSKvct 162
Cdd:COG0396 79 iflafqYPveiPGVSVSNFLRTALNARRGEELSAREFLKLLK------------------------------EKMKE--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 163 gLKFDESFLQRDFDY-LSGGE-KTTVILgKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKG---IVLIVSHDRYFL 237
Cdd:COG0396 126 -LGLDEDFLDRYVNEgFSGGEkKRNEIL-QMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpdrGILIITHYQRIL 203
|
...
gi 754786342 238 DHV 240
Cdd:COG0396 204 DYI 206
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-250 |
2.55e-10 |
|
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: 59.47 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 14 DATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyypgYPqttsygYDEGLIHvLPRGATSAYLEQVPDYP 93
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL--------WP------WGSGRIG-MPEGEDLLFLPQRPYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 94 HGlkvmdnlNLafeeidaiekqmREQeeqmkkvegstlekalnkyssLVHLYEvkggyerdeklskvctglkfdesflqr 173
Cdd:cd03223 77 LG-------TL------------REQ---------------------LIYPWD--------------------------- 89
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754786342 174 dfDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGIVLIVSHdRYFLDHVATKIVEIEDM 250
Cdd:cd03223 90 --DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGE 163
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
351-531 |
3.18e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.14 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 351 TDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGS-----------NVKVAYLPQKI 419
Cdd:PRK10619 9 IDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgQLKVADKNQLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 420 SFNNEELMLIEVFR----------------EDISIVEGKARE----YLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLY 479
Cdd:PRK10619 89 LLRTRLTMVFQHFNlwshmtvlenvmeapiQVLGLSKQEAREravkYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 480 DEVNLLILDEPTNHLD---IDSIETLEEALEDFQGTIFFISHDRYFINKMSNRII 531
Cdd:PRK10619 169 MEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-233 |
3.21e-10 |
|
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: 60.66 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMnyYPGYPQTTSYGYDEGLIHVLPRGATS 83
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDL--IPGAPDEGEVLLDGKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 -----AYLEQVPdYPHGLKVMDNLNLAfeeidaiekqmreqeeqmKKVEGSTLEKALNkysslvhlyevkggyERDEK-L 157
Cdd:cd03260 79 lrrrvGMVFQKP-NPFPGSIYDNVAYG------------------LRLHGIKLKEELD---------------ERVEEaL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 158 SKVctGLkFDESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKG--IVLIVSHD 233
Cdd:cd03260 125 RKA--AL-WDEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-232 |
3.28e-10 |
|
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: 60.63 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSYGYDEGLIHVLP----R 79
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVK-------PDSGKILLDGQDITKLPmhkrA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 80 GATSAYLEQVPDYPHGLKVMDNLNLAFEEIDAIEKqmreqeEQMKKVEgstlekALNKYSSLVHLYEVKGgyerdeklsk 159
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKK------EREEKLE------ELLEEFHITHLRKSKA---------- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754786342 160 vctglkfdesflqrdfDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK--GI-VLIVSH 232
Cdd:cd03218 132 ----------------SSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKdrGIgVLITDH 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-542 |
4.18e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.38 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMN----YYPGYPQTtsygydegliHVLPR 79
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDsgtlEIGGNPCA----------RLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 80 GATSAYLEQVPDYPH---GLKVMDNLNLAFEEIDAIEKQMREQEEQMK-----KVEGSTLEKAlnkysslvhlyevkggy 151
Cdd:PRK15439 82 KAHQLGIYLVPQEPLlfpNLSVKENILFGLPKRQASMQKMKQLLAALGcqldlDSSAGSLEVA----------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 152 erDEKLSKVCTGlkfdesflqrdfdylsggekttvilgklLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK----GIV 227
Cdd:PRK15439 145 --DRQIVEILRG----------------------------LMRDSRILILDEPTASLTPAETERLFSRIRELLaqgvGIV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 228 LIvSHdryfldhvatKIVEIedmestsykgnyssfveqkeenlriqleqyREQQKKINTMekqvkdlRDWAIR-ADNNKF 306
Cdd:PRK15439 195 FI-SH----------KLPEI------------------------------RQLADRISVM-------RDGTIAlSGKTAD 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 307 FRRAASIQ--KRLSKMERLD---KPVLERKNMRLTmsesERSGKETIKATDLTksyGERllFRDAGVMVHYGERVGLIGP 381
Cdd:PRK15439 227 LSTDDIIQaiTPAAREKSLSasqKLWLELPGNRRQ----QAAGAPVLTVEDLT---GEG--FRNISLEVRAGEILGLAGV 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 382 NGSGKTTFLKMLLGEEHPDKGKIELG----SNVKVA--------YLPQK-----------ISFN------NEELMLIEVF 432
Cdd:PRK15439 298 VGAGRTELAETLYGLRPARGGRIMLNgkeiNALSTAqrlarglvYLPEDrqssglyldapLAWNvcalthNRRGFWIKPA 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 433 REDiSIVEGKAREYLSKFmfyqSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDF--Q 510
Cdd:PRK15439 378 REN-AVLERYRRALNIKF----NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIaaQ 452
|
570 580 590
....*....|....*....|....*....|...
gi 754786342 511 GT-IFFISHDRYFINKMSNRIIAVEDFSLNSYL 542
Cdd:PRK15439 453 NVaVLFISSDLEEIEQMADRVLVMHQGEISGAL 485
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
348-519 |
4.62e-10 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 60.39 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGE-RLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKML--LGEehPDKGKIEL-GSNV----------KVA 413
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrLIE--PTSGEIFIdGEDIreqdpvelrrKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 414 YLPQKISfnneeLMLIEVFREDISIV-----------EGKAREYLsKFMFYQSSVFKKvKY---LSGGERIRLKLAILLY 479
Cdd:cd03295 79 YVIQQIG-----LFPHMTVEENIALVpkllkwpkekiRERADELL-ALVGLDPAEFAD-RYpheLSGGQQQRVGVARALA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 754786342 480 DEVNLLILDEPTNHLDIDSIETLEEALEDFQ----GTIFFISHD 519
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQqelgKTIVFVTHD 195
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
352-535 |
4.84e-10 |
|
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: 61.67 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 352 DLTKSYGERLLfrDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNV-----KVAYLP---QKISFNN 423
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrKGIFLPpekRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 424 EELMLI------EVFREDISIVEGKAR----EYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNH 493
Cdd:TIGR02142 82 QEARLFphlsvrGNLRYGMKRARPSERrisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 754786342 494 LDIDS----IETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVED 535
Cdd:TIGR02142 162 LDDPRkyeiLPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLED 207
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-249 |
5.15e-10 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 59.81 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAydGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPGYPQTTSYGYDEGLIHVLPRGATS 83
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFAQ--GEITAIVGPSGSGKSTLLNLIAGFET----PQSGRVLINGVDVTAAPPADRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 AYLEQvPDYPHgLKVMDNLNLAfeeidaIEKQMREQEEQMKKVEgstleKALNKysslvhlyevkggyerdeklskvcTG 163
Cdd:cd03298 75 LFQEN-NLFAH-LTVEQNVGLG------LSPGLKLTAEDRQAIE-----VALAR------------------------VG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 164 LkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD---MDSIEWLENYLKNYKGI-VLIVSHDRYFLDH 239
Cdd:cd03298 118 L---AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalRAEMLDLVLDLHAETKMtVLMVTHQPEDAKR 194
|
250
....*....|
gi 754786342 240 VATKIVEIED 249
Cdd:cd03298 195 LAQRVVFLDN 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-245 |
6.30e-10 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 59.99 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKlnGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPgypqttsygyDEGLIHVLPR- 79
Cdd:COG1127 5 MIEVR--NLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR----P----------DSGEILVDGQd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 80 --GATSAYLEQVPD-----YPHG-----LKVMDnlNLAF---EEIDAIEKQMREQ-EEQMKKVEgstLEKALNKYSSlvh 143
Cdd:COG1127 69 itGLSEKELYELRRrigmlFQGGalfdsLTVFE--NVAFplrEHTDLSEAEIRELvLEKLELVG---LPGAADKMPS--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 144 lyEvkggyerdeklskvctglkfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD---MDSIEWLENYL 220
Cdd:COG1127 141 --E-------------------------------LSGGMRKRVALARALALDPEILLYDEPTAGLDpitSAVIDELIREL 187
|
250 260
....*....|....*....|....*.
gi 754786342 221 -KNYKGIVLIVSHDRYFLDHVATKIV 245
Cdd:COG1127 188 rDELGLTSVVVTHDLDSAFAIADRVA 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
373-518 |
6.95e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.90 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSN---VKVAYLPQKISFNNEELML--------IEVFREDIS--- 437
Cdd:PRK13657 361 GQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDirtVTRASLRRNIAVVFQDAGLfnrsiednIRVGRPDATdee 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 438 IVEGKAREYLSKFMFYQSSVFKKV-----KYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDF-QG 511
Cdd:PRK13657 441 MRAAAERAQAHDFIERKPDGYDTVvgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELmKG 520
|
....*...
gi 754786342 512 -TIFFISH 518
Cdd:PRK13657 521 rTTFIIAH 528
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-241 |
7.71e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.41 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 11 KYMDAT-LVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnYYPgypqttsygyDEGLIHVLPRGATSAYLEQV 89
Cdd:PRK13635 14 RYPDAAtYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL----LLP----------EAGTITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 90 ----------PDYPH-GLKVMDNLnlAFeeidAIEKQMREQEEQMKKVEgstleKALNkyssLVHLyevkggyerdekls 158
Cdd:PRK13635 80 rrqvgmvfqnPDNQFvGATVQDDV--AF----GLENIGVPREEMVERVD-----QALR----QVGM-------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 159 kvctglkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD-MDSIEWLENY--LKNYKGI-VLIVSHDr 234
Cdd:PRK13635 131 ---------EDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDpRGRREVLETVrqLKEQKGItVLSITHD- 200
|
....*..
gi 754786342 235 yfLDHVA 241
Cdd:PRK13635 201 --LDEAA 205
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-234 |
7.73e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.12 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMnyypgypqttsygyDEGLIHVLPRGATS 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETP--------------DSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 AYLEQVPD---------YPHgLKVMDnlNLAFeeidaiekQMReqeeqMKKVEGSTLEKALNKYSSLVHLyevkggyerd 154
Cdd:PRK09452 81 VPAENRHVntvfqsyalFPH-MTVFE--NVAF--------GLR-----MQKTPAAEITPRVMEALRMVQL---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 155 eklskvctglkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK---GIVLI-V 230
Cdd:PRK09452 135 -------------EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQrklGITFVfV 201
|
....
gi 754786342 231 SHDR 234
Cdd:PRK09452 202 THDQ 205
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-245 |
8.56e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.98 E-value: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKLNGI---KKYMDATlVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMNyypgypqttsygydEGLIHVl 77
Cdd:PRK10619 1 MSENKLNVIdlhKRYGEHE-VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPS--------------EGSIVV- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 78 prgaTSAYLEQVPDYPHGLKVMDnlnlafeeidaiEKQMreqeeQMKKVEGSTLEKALNKYSSLVHLYEVK--------- 148
Cdd:PRK10619 65 ----NGQTINLVRDKDGQLKVAD------------KNQL-----RLLRTRLTMVFQHFNLWSHMTVLENVMeapiqvlgl 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 149 GGYERDEKLSKVCTGLKFDESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSI-EWLE--NYLKNYKG 225
Cdd:PRK10619 124 SKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRimQQLAEEGK 203
|
250 260
....*....|....*....|
gi 754786342 226 IVLIVSHDRYFLDHVATKIV 245
Cdd:PRK10619 204 TMVVVTHEMGFARHVSSHVI 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
10-249 |
8.65e-10 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 58.96 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 10 KKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTtsygydeGLIHV-------LPRGAT 82
Cdd:cd03292 8 KTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEEL-------PTS-------GTIRVngqdvsdLRGRAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 83 sAYLEQ-----------VPDyphgLKVMDNLNLAFEEIDAIEKQMREQeeqmkkvegstlekalnkysslvhlyeVKGGY 151
Cdd:cd03292 74 -PYLRRkigvvfqdfrlLPD----RNVYENVAFALEVTGVPPREIRKR---------------------------VPAAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 152 ERdeklskvcTGLKFDEsflqRDF-DYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLK--NYKGI-V 227
Cdd:cd03292 122 EL--------VGLSHKH----RALpAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKkiNKAGTtV 189
|
250 260
....*....|....*....|..
gi 754786342 228 LIVSHDRYFLDHVATKIVEIED 249
Cdd:cd03292 190 VVATHAKELVDTTRHRVIALER 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-233 |
9.19e-10 |
|
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: 59.44 E-value: 9.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 6 LNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPgypqttsygyDEGLIHVLprGATSAY 85
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR----P----------DSGEVLID--GEDISG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 86 LEQVPDYPHGLKV---------MDNL----NLAFeeidaiekQMREQEeqmKKVEGSTLEKALnkysslvhlyevkggye 152
Cdd:cd03261 67 LSEAELYRLRRRMgmlfqsgalFDSLtvfeNVAF--------PLREHT---RLSEEEIREIVL----------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 153 rdEKLSKVctGLKFDESFLQRDfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD---MDSIEWLENYLKNYKGI-VL 228
Cdd:cd03261 119 --EKLEAV--GLRGAEDLYPAE---LSGGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGLtSI 191
|
....*
gi 754786342 229 IVSHD 233
Cdd:cd03261 192 MVTHD 196
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-233 |
9.84e-10 |
|
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: 59.27 E-value: 9.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPqttsygyDEGLIHVL---PRGATSAYLEQVpdyph 94
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQ-------P-------TSGEVRVAglvPWKRRKKFLRRI----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 95 GLkVMDNLNLAFEEIDAIEKqmreqeeqmkkvegstlekalnkYSSLVHLYEVKGGYERdEKLSKVCTGLKFdESFLQRD 174
Cdd:cd03267 97 GV-VFGQKTQLWWDLPVIDS-----------------------FYLLAAIYDLPPARFK-KRLDELSELLDL-EELLDTP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754786342 175 FDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNY----KGIVLIVSHD 233
Cdd:cd03267 151 VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHY 213
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
373-519 |
1.09e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.18 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEhPDKGKIELGSN-----------VKVAYLPQKISfnneELMLIEVFR-------- 433
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQpleawsaaelaRHRAYLSQQQT----PPFAMPVFQyltlhqpd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 434 -EDISIVEgKAREYLSKFMFYQSSVFKKVKYLSGGE--RIRLKLAIL-LYDEVN----LLILDEPTNHLDIDSIETLEEA 505
Cdd:PRK03695 97 kTRTEAVA-SALNEVAEALGLDDKLGRSVNQLSGGEwqRVRLAAVVLqVWPDINpagqLLLLDEPMNSLDVAQQAALDRL 175
|
170
....*....|....*..
gi 754786342 506 LEDF--QG-TIFFISHD 519
Cdd:PRK03695 176 LSELcqQGiAVVMSSHD 192
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
352-535 |
1.34e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 59.31 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 352 DLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGS--------NVKVAY-----LPQK 418
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTaplaeareDTRLMFqdarlLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 419 ISFNNEELMLIEVFRED----ISIV--EGKAREYLSKfmfyqssvfkkvkyLSGGERIRLKLAILLYDEVNLLILDEPTN 492
Cdd:PRK11247 97 KVIDNVGLGLKGQWRDAalqaLAAVglADRANEWPAA--------------LSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 754786342 493 HLD-IDSIET--LEEALEDFQG-TIFFISHDRYFINKMSNRIIAVED 535
Cdd:PRK11247 163 ALDaLTRIEMqdLIESLWQQHGfTVLLVTHDVSEAVAMADRVLLIEE 209
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-209 |
1.38e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.43 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIE------------QMNYYPgyPQTTSYG 68
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEditsgdlfigekRMNDVP--PAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 69 YdeglihVLPRGATsayleqvpdYPHgLKVMDNLNLAFEEIDAIEKQMREQEEQMKKVegstLEkalnkyssLVHLyevk 148
Cdd:PRK11000 79 M------VFQSYAL---------YPH-LSVAENMSFGLKLAGAKKEEINQRVNQVAEV----LQ--------LAHL---- 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754786342 149 ggyerdeklskvctglkfdesfLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:PRK11000 127 ----------------------LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-245 |
1.55e-09 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 58.89 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 2 LELKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPGYPQTTSYGYDEGLIHVLPRGA 81
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLER----PDSGTILFGGEDATDVPVQERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 82 TSAYlEQVPDYPHgLKVMDNLNLAFEEIDAIEkqmREQEEQMKKVEGSTLEkalnkyssLVHLyevkggyerdeklskvc 161
Cdd:cd03296 77 GFVF-QHYALFRH-MTVFDNVAFGLRVKPRSE---RPPEAEIRAKVHELLK--------LVQL----------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 162 tglkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGIV----LIVSHDRYFL 237
Cdd:cd03296 127 ------DWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHDQEEA 200
|
....*...
gi 754786342 238 DHVATKIV 245
Cdd:cd03296 201 LEVADRVV 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
336-535 |
1.57e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 60.35 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 336 TMSESERSGKETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV---- 410
Cdd:PRK09452 3 KLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLdGQDIthvp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 411 -----------KVAYLPQKISFNNEE--LMLIEVFREDIsivEGKAREYLsKFMFYQSSVFKKVKYLSGGERIRLKLAIL 477
Cdd:PRK09452 83 aenrhvntvfqSYALFPHMTVFENVAfgLRMQKTPAAEI---TPRVMEAL-RMVQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754786342 478 LYDEVNLLILDEPTNHLDIDSIETLEEALEDFQG----TIFFISHDRYFINKMSNRIIAVED 535
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklgiTFVFVTHDQEEALTMSDRIVVMRD 220
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
337-506 |
2.00e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.94 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 337 MSESERSGKETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVKVAYL 415
Cdd:PRK13543 1 MIEPLHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATRGDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 416 PQKISFnneeLMLIEVFREDISIVEG----------KAREYLSKFMF------YQSSVfkkVKYLSGGERIRLKLAILLY 479
Cdd:PRK13543 81 SRFMAY----LGHLPGLKADLSTLENlhflcglhgrRAKQMPGSALAivglagYEDTL---VRQLSAGQKKRLALARLWL 153
|
170 180
....*....|....*....|....*..
gi 754786342 480 DEVNLLILDEPTNHLDIDSIETLEEAL 506
Cdd:PRK13543 154 SPAPLWLLDEPYANLDLEGITLVNRMI 180
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
310-518 |
2.08e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.59 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 310 AASIQkRLS----KMERLDKPVLERknmrltmSESERSGKETIKATDLT-KSYGERLLFRDAGVMVHYGERVGLIGPNGS 384
Cdd:COG4178 329 RATVD-RLAgfeeALEAADALPEAA-------SRIETSEDGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 385 GKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQK------------------ISFNNEELM--LIEV----FREDISIVE 440
Cdd:COG4178 401 GKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRpylplgtlreallypataEAFSDAELReaLEAVglghLAERLDEEA 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 441 GKAREylskfmfyqssvfkkvkyLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALED--FQGTIFFISH 518
Cdd:COG4178 481 DWDQV------------------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH 542
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
364-519 |
2.11e-09 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 58.25 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 364 RDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVKVAYLPQKISFNNEELMLIEVFREDISIVEGK 442
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 443 AREYLSK------------FMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEAL---- 506
Cdd:TIGR01184 82 VLPDLSKserraiveehiaLVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiw 161
|
170
....*....|...
gi 754786342 507 EDFQGTIFFISHD 519
Cdd:TIGR01184 162 EEHRVTVLMVTHD 174
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
17-232 |
2.35e-09 |
|
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: 57.76 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 17 LVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMnyypgypqttsygyDEGLIHVlprgatsayleqvpdyphgl 96
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEP--------------DAGFATV-------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 97 kvmdnlnlafEEIDAIeKQMREQEEQMKKVEGST-LEKALNKYSSLVH---LYEVKGgYERDEKLSKVCTGLKFDEsFLQ 172
Cdd:cd03266 65 ----------DGFDVV-KEPAEARRRLGFVSDSTgLYDRLTARENLEYfagLYGLKG-DELTARLEELADRLGMEE-LLD 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754786342 173 RDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGI---VLIVSH 232
Cdd:cd03266 132 RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgkcILFSTH 194
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
348-535 |
2.35e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 58.23 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLfrDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGsNVKVAYLP---QKIS--FN 422
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN-GQDLTALPpaeRPVSmlFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 423 NEELmlievF--------------------REDISIVEGKAR----EYLSKFMFYQssvfkkvkyLSGGERIRLKLAILL 478
Cdd:COG3840 79 ENNL-----FphltvaqniglglrpglkltAEQRAQVEQALErvglAGLLDRLPGQ---------LSGGQRQRVALARCL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754786342 479 YDEVNLLILDEPTNHLDI----DSIETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVED 535
Cdd:COG3840 145 VRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVAD 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
348-491 |
2.59e-09 |
|
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: 57.83 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVK-----------VAYL 415
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdGRDITglppheraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 416 PQ--KIsFNN----EELMLIEVFREDISIVEGKAREYlskfmfyqsSVF--------KKVKYLSGGERIRLKLAILLYDE 481
Cdd:cd03224 81 PEgrRI-FPEltveENLLLGAYARRRAKRKARLERVY---------ELFprlkerrkQLAGTLSGGEQQMLAIARALMSR 150
|
170
....*....|
gi 754786342 482 VNLLILDEPT 491
Cdd:cd03224 151 PKLLLLDEPS 160
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
348-518 |
3.03e-09 |
|
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: 57.42 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERL--LFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELgSNVKVAYLPqkisfnnee 425
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDISTIP--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 426 lmlIEVFREDISIV-------EGKAREYLSKF-MFYQSSVFKKVKY------LSGGERIRLKLAILLYDEVNLLILDEPT 491
Cdd:cd03369 77 ---LEDLRSSLTIIpqdptlfSGTIRSNLDPFdEYSDEEIYGALRVsegglnLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180
....*....|....*....|....*....
gi 754786342 492 NHLDIDSIETLEEAL-EDFQG-TIFFISH 518
Cdd:cd03369 154 ASIDYATDALIQKTIrEEFTNsTILTIAH 182
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
14-233 |
3.05e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.22 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 14 DATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgypqttsygYDEGLIhvlprgatsaYLEQVPDYP 93
Cdd:PRK13648 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEK--------------VKSGEI----------FYNNQAITD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 94 HGLKvmdnlnlafeeidaiekqmreqeeQMKKVEGSTLEKALNKYSSLVHLYEVKGGYER-----DEKLSKVCTGLKFDE 168
Cdd:PRK13648 76 DNFE------------------------KLRKHIGIVFQNPDNQFVGSIVKYDVAFGLENhavpyDEMHRRVSEALKQVD 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754786342 169 SFLQRDFD--YLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMD---SIEWLENYLKNYKGIVLI-VSHD 233
Cdd:PRK13648 132 MLERADYEpnALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDarqNLLDLVRKVKSEHNITIIsITHD 202
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
348-535 |
3.43e-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: 57.59 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGER----LLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV------------ 410
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDLtllsgkelrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 411 -KVAYLPQ-------KISFNNEELMLiEVFREDISIVEGKAREYLS------KFMFYQSSvfkkvkyLSGGERIRLKLAI 476
Cdd:cd03258 82 rRIGMIFQhfnllssRTVFENVALPL-EIAGVPKAEIEERVLELLElvgledKADAYPAQ-------LSGGQKQRVGIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754786342 477 LLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQG----TIFFISHDRYFINKMSNRIIAVED 535
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRelglTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
16-211 |
4.00e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 59.08 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 16 TLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSYGYDEGLIHVLPRGATSAYLEQVPDyphg 95
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLT-------PTAGTVLVAGDDVEALSARAASRRVASVPQ---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 96 lkvmdNLNLAFE-EIDAIEKQMREQEEQMKKVEGSTLEKALnkysslvhlyevkggyerDEKLSKVCTglkfdESFLQRD 174
Cdd:PRK09536 85 -----DTSLSFEfDVRQVVEMGRTPHRSRFDTWTETDRAAV------------------ERAMERTGV-----AQFADRP 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 754786342 175 FDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMD 211
Cdd:PRK09536 137 VTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-232 |
4.62e-09 |
|
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: 57.28 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPGYPQTTSYGYDEGL--IHVLPRGA 81
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVR----PDAGKILIDGQDITHlpMHERARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 82 TSaYLEQVPDYPHGLKVMDNLNLAFEEIDAIEKQMREQEeqmkkvegstLEKALNKYSsLVHLYEVKGGYerdeklskvc 161
Cdd:TIGR04406 78 IG-YLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREER----------LEALLEEFQ-ISHLRDNKAMS---------- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 162 tglkfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD---MDSIEWLENYLKNyKGI-VLIVSH 232
Cdd:TIGR04406 136 ----------------LSGGERRRVEIARALATNPKFILLDEPFAGVDpiaVGDIKKIIKHLKE-RGIgVLITDH 193
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
373-490 |
4.73e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 56.71 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSnvKVAYLPQK-----------I----SFNNEEL-MLIEV--FRE 434
Cdd:cd03250 31 GELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEpwiqngtirenIlfgkPFDEERYeKVIKAcaLEP 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 754786342 435 DISIVEGKAreylskfmfyQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEP 490
Cdd:cd03250 109 DLEILPDGD----------LTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDP 154
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-251 |
5.16e-09 |
|
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: 56.38 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyyPGYPQTtsygydEGLIhvlprgatsayleqvpdyphglk 97
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH------PKYEVT------EGEI----------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 98 vmdnlnlAFEEIDAIEKQMreqEEQMKKveGSTLekalnkysslvhlyevkgGYERDEKLSkvctGLKFDEsFLqRDFDY 177
Cdd:cd03217 60 -------LFKGEDITDLPP---EERARL--GIFL------------------AFQYPPEIP----GVKNAD-FL-RYVNE 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 178 -LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLE---NYLKNYKGIVLIVSHDRYFLDHVAT---------KI 244
Cdd:cd03217 104 gFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAeviNKLREEGKSVLIITHYQRLLDYIKPdrvhvlydgRI 183
|
....*..
gi 754786342 245 VEIEDME 251
Cdd:cd03217 184 VKSGDKE 190
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
347-531 |
5.62e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 57.75 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSYGERLLFR-----DAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL------GSNVKVAYL 415
Cdd:PRK13637 2 SIKIENLTHIYMEGTPFEkkaldNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 416 PQKIS--FNNEELMLIE--VFR-------------EDISIVEGKAREY--LSKFMFYQSSVFKkvkyLSGGERIRLKLAI 476
Cdd:PRK13637 82 RKKVGlvFQYPEYQLFEetIEKdiafgpinlglseEEIENRVKRAMNIvgLDYEDYKDKSPFE----LSGGQKRRVAIAG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 754786342 477 LLYDEVNLLILDEPTNHLDI----DSIETLEEALEDFQGTIFFISHDRYFINKMSNRII 531
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSHSMEDVAKLADRII 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-240 |
5.75e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.79 E-value: 5.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 2 LELKLNGIKKYMDATL-----VLEDVSLEAYDGDKIGIVGVNGSGKSTIlkviagIEQMNyypgypqttsygydeGLIhv 76
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTF------IEHLN---------------ALL-- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 77 LPRGATSAYL--EQVPDYPHGLK--VMDNLNLA---FEEIDAIeKQMREQ--------EEQMKKvegSTLEK--ALNKYS 139
Cdd:PRK13651 58 LPDTGTIEWIfkDEKNKKKTKEKekVLEKLVIQktrFKKIKKI-KEIRRRvgvvfqfaEYQLFE---QTIEKdiIFGPVS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 140 SLVHLYEVKggyERDEKLSKVcTGLkfDESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD----MDSIEW 215
Cdd:PRK13651 134 MGVSKEEAK---KRAAKYIEL-VGL--DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEI 207
|
250 260
....*....|....*....|....*
gi 754786342 216 LENYLKNYKGIVlIVSHDryfLDHV 240
Cdd:PRK13651 208 FDNLNKQGKTII-LVTHD---LDNV 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-209 |
6.41e-09 |
|
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: 56.74 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 10 KKYMDAT-LVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMN----YYPGYPQTTSygydeglihvlpRGATSA 84
Cdd:cd03263 8 KTYKKGTkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTsgtaYINGYSIRTD------------RKAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 85 YLEQVPDY---PHGLKVMDNLNLaFEEIDAI-EKQMREQEEQMKKVEGstLEKALNKYSSlvhlyevkggyerdeklskv 160
Cdd:cd03263 76 SLGYCPQFdalFDELTVREHLRF-YARLKGLpKSEIKEEVELLLRVLG--LTDKANKRAR-------------------- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 754786342 161 ctglkfdesflqrdfdYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:cd03263 133 ----------------TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-233 |
6.53e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.83 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMNyypgypqTTSYGYDEGLIHVLPRG 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD-------AGNIIIDDEDISLLPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 81 ATS----AYLEQVPDYPHGLKVMDNLNLAFEEIDAIEKQMREQ--EEQMKKVEGSTLEKALNKysslvhlyevkggyerd 154
Cdd:PRK10895 74 ARArrgiGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDraNELMEEFHIEHLRDSMGQ----------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 155 eklskvctglkfdesflqrdfdYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS---IEWLENYLKNYKGIVLIVS 231
Cdd:PRK10895 137 ----------------------SLSGGERRRVEIARALAANPKFILLDEPFAGVDPISvidIKRIIEHLRDSGLGVLITD 194
|
..
gi 754786342 232 HD 233
Cdd:PRK10895 195 HN 196
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
359-495 |
7.76e-09 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 56.51 E-value: 7.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 359 ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHpdKGKIELGsnvkvaylpqKISFNNEElMLIEVFREDISI 438
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSG----------QILFNGQP-RKPDQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 439 VEG--------KAREYLskfmfYQSSVFK------------------------------KVKYLSGGERIRLKLAILLYD 480
Cdd:cd03234 86 VRQddillpglTVRETL-----TYTAILRlprkssdairkkrvedvllrdlaltriggnLVKGISGGERRRVSIAVQLLW 160
|
170
....*....|....*
gi 754786342 481 EVNLLILDEPTNHLD 495
Cdd:cd03234 161 DPKVLILDEPTSGLD 175
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-232 |
8.70e-09 |
|
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: 55.30 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPGYPQTTSYGYDEGLIHVLPRGATSAYLEQvpdyphglk 97
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR----PTSGRVRLDGADISQWDPNELGDHVGYLPQ--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 98 vmdnlnlafeeidaiekqmreqeeqmkkvegstlekalnkysslvhlyevkggyerDEKLskvctglkFDESFLQrdfDY 177
Cdd:cd03246 84 --------------------------------------------------------DDEL--------FSGSIAE---NI 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 178 LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK---GIVLIVSH 232
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAH 154
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-257 |
9.05e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 56.26 E-value: 9.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSYGYDEGLIHVLP----R 79
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS-------PTSGTLLFEGEDISTLKpeiyR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 80 GATSaYLEQVPDYpHGLKVMDNLNLAFeeidaiekQMREQEEQMKKvegstLEKALNKYsslvhlyevkggyerdeklsk 159
Cdd:PRK10247 81 QQVS-YCAQTPTL-FGDTVYDNLIFPW--------QIRNQQPDPAI-----FLDDLERF--------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 160 vctGLkfDESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSI----EWLENYLKNYKGIVLIVSHDRY 235
Cdd:PRK10247 125 ---AL--PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKhnvnEIIHRYVREQNIAVLWVTHDKD 199
|
250 260
....*....|....*....|....*.
gi 754786342 236 FLDHvATKIVEIE----DMESTSYKG 257
Cdd:PRK10247 200 EINH-ADKVITLQphagEMQEARYEL 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
346-519 |
9.46e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 56.79 E-value: 9.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 346 ETIKATDLTKSYG----ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNV----------- 410
Cdd:COG4525 2 SMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrgvv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 411 --KVAYLPQKISFNNEELML-------IEvfREDIsivegkAREYLSKF---MFYQSSVFKkvkyLSGGERIRLKLAILL 478
Cdd:COG4525 82 fqKDALLPWLNVLDNVAFGLrlrgvpkAE--RRAR------AEELLALVglaDFARRRIWQ----LSGGMRQRVGIARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 754786342 479 YDEVNLLILDEPTNHLDIDSIETLEEALEDF----QGTIFFISHD 519
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVwqrtGKGVFLITHS 194
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-205 |
1.02e-08 |
|
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: 55.90 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyypgypqTTSYGydeGLIHVLPRGATS 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGL-----------LPPRS---GSIRFDGRDITG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 -----------AYLEQVPDYPHGLKVMDNLNLAfeeidAIEKQMREQEEQMKKVegstlekalnkysslvhlyevkggYE 152
Cdd:cd03224 67 lppheraragiGYVPEGRRIFPELTVEENLLLG-----AYARRRAKRKARLERV------------------------YE 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 754786342 153 RDEKLskvctglkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPT 205
Cdd:cd03224 118 LFPRL----------KERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
349-405 |
1.14e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.47 E-value: 1.14e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 754786342 349 KATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIE 405
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
373-535 |
1.24e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 57.89 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGsNVKV------AYLpQKIS--FNN----EELMLIEVFREDisive 440
Cdd:COG4615 358 GELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLD-GQPVtadnreAYR-QLFSavFSDfhlfDRLLGLDGEADP----- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 441 GKAREYLSKFmfyQSSvfKKVKY---------LSGGERIRLKLAILLYDEVNLLILDE------PTnhldidsietleea 505
Cdd:COG4615 431 ARARELLERL---ELD--HKVSVedgrfsttdLSQGQRKRLALLVALLEDRPILVFDEwaadqdPE-------------- 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 754786342 506 ledF--------------QG-TIFFISHD-RYFInkMSNRIIAVED 535
Cdd:COG4615 492 ---FrrvfytellpelkaRGkTVIAISHDdRYFD--LADRVLKMDY 532
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
348-535 |
1.39e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 56.63 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERL-----LFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELgsnvkvAYLPQKisfN 422
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW------IFKDEK---N 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 423 NEELMLIEVFREDISIVEGKAREY-----LSK-----FMFYQSSVFKKV------------------------KY----- 463
Cdd:PRK13651 74 KKKTKEKEKVLEKLVIQKTRFKKIkkikeIRRrvgvvFQFAEYQLFEQTiekdiifgpvsmgvskeeakkraaKYielvg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 464 ------------LSGGERIRLKLAILLYDEVNLLILDEPTNHLD-IDSIETLE--EALEDFQGTIFFISHDRYFINKMSN 528
Cdd:PRK13651 154 ldesylqrspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEifDNLNKQGKTIILVTHDLDNVLEWTK 233
|
....*..
gi 754786342 529 RIIAVED 535
Cdd:PRK13651 234 RTIFFKD 240
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
348-519 |
1.41e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 56.25 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVKVAYLPQKISFNNEEL 426
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdGKPVEGPGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 427 M-----LIEV-FREDISIVEGKAREYLSKFMFYQSSVF----KKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDI 496
Cdd:PRK11248 82 LpwrnvQDNVaFGLQLAGVEKMQRLEIAHQMLKKVGLEgaekRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180
....*....|....*....|....*..
gi 754786342 497 DSIETLEE-ALEDFQGT---IFFISHD 519
Cdd:PRK11248 162 FTREQMQTlLLKLWQETgkqVLLITHD 188
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-233 |
1.44e-08 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 55.91 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnYYPgypqttsygyDEGLIHV------- 76
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF----LRP----------TSGSVLFdgeditg 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 77 LP------RGATSAYleQVPDYPHGLKVMDNLNLAFE----EIDAIEKQMREQEEQMKKVEgSTLEkalnkyssLVHLYE 146
Cdd:cd03219 67 LPpheiarLGIGRTF--QIPRLFPELTVLENVMVAAQartgSGLLLARARREEREARERAE-ELLE--------RVGLAD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 147 VkggyeRDEKLSKvctglkfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLK--NYK 224
Cdd:cd03219 136 L-----ADRPAGE------------------LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRelRER 192
|
250
....*....|
gi 754786342 225 GI-VLIVSHD 233
Cdd:cd03219 193 GItVLLVEHD 202
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
362-496 |
1.47e-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: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 362 LFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSnvKVAYLPQ-------KISFNNEELMLIEVFRE 434
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RISFSPQtswimpgTIKDNIIFGLSYDEYRY 518
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754786342 435 DISIVEGKAREYLSKFMFYQSSVFKKVKY-LSGGERIRLKLAILLYDEVNLLILDEPTNHLDI 496
Cdd:TIGR01271 519 TSVIKACQLEEDIALFPEKDKTVLGEGGItLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
347-416 |
1.55e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 57.01 E-value: 1.55e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVkVAYLP 416
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD-VTDLP 71
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
359-495 |
1.61e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.57 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 359 ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQK----------ISFNNEELML 428
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkplrkkvgIVFQFPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 429 IE-VFREDISI-----------VEGKAREYLsKFMFYQSSVFKKVKY-LSGGERIRLKLAILLYDEVNLLILDEPTNHLD 495
Cdd:PRK13634 99 FEeTVEKDICFgpmnfgvseedAKQKAREMI-ELVGLPEELLARSPFeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-240 |
1.63e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 56.27 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKlnGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnYYPgypqttsygyDEGLIHVLPRG 80
Cdd:COG4152 1 MLELK--GLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGI----LAP----------DSGEVLWDGEP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 81 ATSAYLEQV---PD----YPhGLKVMDNLN-LAfeeidaiekqmreqeeQMKKVEGSTLEKALNKYSSLVHLYEVkggye 152
Cdd:COG4152 65 LDPEDRRRIgylPEerglYP-KMKVGEQLVyLA----------------RLKGLSKAEAKRRADEWLERLGLGDR----- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 153 RDEKLSKvctglkfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK--G-IVLI 229
Cdd:COG4152 123 ANKKVEE------------------LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAakGtTVIF 184
|
250
....*....|.
gi 754786342 230 VSHDryfLDHV 240
Cdd:COG4152 185 SSHQ---MELV 192
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
359-518 |
1.74e-08 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 55.62 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 359 ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVK---VAYLPQKISFNNEELMLIE-VFR 433
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRdlnLRWLRSQIGLVSQEPVLFDgTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 434 EDIS----------IVEGKAREYLSKFMF-----YQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDS 498
Cdd:cd03249 95 ENIRygkpdatdeeVEEAAKKANIHDFIMslpdgYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180
....*....|....*....|..
gi 754786342 499 IETLEEALEDFQG--TIFFISH 518
Cdd:cd03249 175 EKLVQEALDRAMKgrTTIVIAH 196
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-246 |
2.58e-08 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 54.89 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKlnGIKKYMDAT----LVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgypqttsygYDEGLIHV 76
Cdd:cd03258 1 MIELK--NVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLER--------------PTSGSVLV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 77 lprgatsayleqvpdypHGLKVMDnLNlafeeidaiEKQMREQEEQMKKV-EGSTLEKALNKYSSLVHLYEVkGGYERDE 155
Cdd:cd03258 65 -----------------DGTDLTL-LS---------GKELRKARRRIGMIfQHFNLLSSRTVFENVALPLEI-AGVPKAE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 156 KLSKVCTGLKFDESFLQRDFdY---LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLK--NYK-GI-VL 228
Cdd:cd03258 117 IEERVLELLELVGLEDKADA-YpaqLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRdiNRElGLtIV 195
|
250 260
....*....|....*....|....*.
gi 754786342 229 IVSHD----RYFLDHVAT----KIVE 246
Cdd:cd03258 196 LITHEmevvKRICDRVAVmekgEVVE 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-552 |
2.60e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.72 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyypgYPQTTsygydeGLIHVLPRgats 83
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI--------HEPTK------GTITINNI---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 ayleqvpDYP---HGLKVMDNLNLAFEEIDAIEkqmreqeeqmkkvEGSTLEkalNKYSSLVHLYEVKGGYERDEKLSKV 160
Cdd:PRK09700 68 -------NYNkldHKLAAQLGIGIIYQELSVID-------------ELTVLE---NLYIGRHLTKKVCGVNIIDWREMRV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 161 CTGLKFDESFLQRDFDY----LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWL---ENYLKNY-KGIVLIvsh 232
Cdd:PRK09700 125 RAAMMLLRVGLKVDLDEkvanLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEgTAIVYI--- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 233 dryflDHVATKIVEIEDMESTSYKGNY--SSFVEQKEENLRIQLEQYREQQKKINTMEKQVKDLRdwairadnnkffrra 310
Cdd:PRK09700 202 -----SHKLAEIRRICDRYTVMKDGSSvcSGMVSDVSNDDIVRLMVGRELQNRFNAMKENVSNLA--------------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 311 asiqkrlskmerlDKPVLERKNMrltmseserSGKETIKATDLTKSygerllfrdagvmVHYGERVGLIGPNGSGKTTFL 390
Cdd:PRK09700 262 -------------HETVFEVRNV---------TSRDRKKVRDISFS-------------VCRGEILGFAGLVGSGRTELM 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 391 KMLLGEEHPDKGKIEL-GSNVK-----------VAYlpqkISFNNEELMLIEVF--REDISIV----------------- 439
Cdd:PRK09700 307 NCLFGVDKRAGGEIRLnGKDISprspldavkkgMAY----ITESRRDNGFFPNFsiAQNMAISrslkdggykgamglfhe 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 440 --EGKAREYLSKFMFYQ-SSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDS---IETLEEALEDFQGTI 513
Cdd:PRK09700 383 vdEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAkaeIYKVMRQLADDGKVI 462
|
570 580 590
....*....|....*....|....*....|....*....
gi 754786342 514 FFISHDRYFINKMSNRIIAVEDFSLNSYLGNYDYYRHEK 552
Cdd:PRK09700 463 LMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEE 501
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
373-535 |
2.84e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 56.76 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVKvAY----LPQKISFNNEElmlIEVF----REDISIVEGKA 443
Cdd:PRK11160 366 GEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLnGQPIA-DYseaaLRQAISVVSQR---VHLFsatlRDNLLLAAPNA 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 444 R-EYLSKfmfyqssVFKKV--------------------KYLSGGERIRLKLA-ILLYDeVNLLILDEPTNHLDIDS-IE 500
Cdd:PRK11160 442 SdEALIE-------VLQQVgleklleddkglnawlgeggRQLSGGEQRRLGIArALLHD-APLLLLDEPTEGLDAETeRQ 513
|
170 180 190
....*....|....*....|....*....|....*.
gi 754786342 501 TLEEALEDFQG-TIFFISHDRYFINKMsNRIIAVED 535
Cdd:PRK11160 514 ILELLAEHAQNkTVLMITHRLTGLEQF-DRICVMDN 548
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-209 |
2.88e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.01 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKLNGIKK-YMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEqmnyypgypQTTSygydeGLIHVLPR 79
Cdd:PRK11650 1 MAGLKLQAVRKsYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLE---------RITS-----GEIWIGGR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 80 GATSayLEqvPD-------------YPHgLKVMDNLNLAFeeidaiekqmreqeeqmkKVEGstLEKAlnkysslvhlye 146
Cdd:PRK11650 67 VVNE--LE--PAdrdiamvfqnyalYPH-MSVRENMAYGL------------------KIRG--MPKA------------ 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754786342 147 vkggyERDEKLSKVCTGLKFdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:PRK11650 110 -----EIEERVAEAARILEL-EPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
337-535 |
3.03e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 337 MSESERSGKETIKATDLTKSYgerllfrdAGVMV--------HYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGS 408
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQY--------SGVEVlkgidftlHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 409 NVKVAYLPQK-----ISFNNEELMLI--EVFREDISIveGKAREYLSKfmfyqssvfKKVKYLSGGERIRLKLA------ 475
Cdd:PRK15439 73 NPCARLTPAKahqlgIYLVPQEPLLFpnLSVKENILF--GLPKRQASM---------QKMKQLLAALGCQLDLDssagsl 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754786342 476 ---------IL--LYDEVNLLILDEPTNHLDIDSIETLEEALEDFQGT---IFFISHDRYFINKMSNRIIAVED 535
Cdd:PRK15439 142 evadrqiveILrgLMRDSRILILDEPTASLTPAETERLFSRIRELLAQgvgIVFISHKLPEIRQLADRISVMRD 215
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-245 |
3.59e-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: 54.72 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 11 KYMDATLVLEDVSLEA-----YDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPqttsygyDEGLIHVLprGATSAY 85
Cdd:cd03237 2 TYPTMKKTLGEFTLEVeggsiSESEVIGILGPNGIGKTTFIKMLAGVLK-------P-------DEGDIEIE--LDTVSY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 86 LEQ--VPDYPhglkvmdnlnlafeeidaiekqMREQEEQMKKVEGSTLEKALNkysslvhlyevkggyerdeklSKVCTG 163
Cdd:cd03237 66 KPQyiKADYE----------------------GTVRDLLSSITKDFYTHPYFK---------------------TEIAKP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 164 LKFdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMD----SIEWLENYLKNYKGIVLIVSHDRYFLDH 239
Cdd:cd03237 103 LQI-EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASKVIRRFAENNEKTAFVVEHDIIMIDY 181
|
....*.
gi 754786342 240 VATKIV 245
Cdd:cd03237 182 LADRLI 187
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
373-496 |
4.49e-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: 54.68 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIE------------------------LGSNVKVAYLPQKI-----SFNN 423
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildefrgselqnyftklLEGDVKVIVKPQYVdlipkAVKG 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754786342 424 EELMLIEvfREDisivEGKAREYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDI 496
Cdd:cd03236 106 KVGELLK--KKD----ERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-248 |
4.69e-08 |
|
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: 53.77 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 34 IVGVNGSGKSTIlkviagIEQMNY--YPGYPQTTSYGydEGLIHVLPRGATSAYLEqvpdyphglkvmdnlnLAFEeiDA 111
Cdd:cd03240 27 IVGQNGAGKTTI------IEALKYalTGELPPNSKGG--AHDPKLIREGEVRAQVK----------------LAFE--NA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 112 IEKQMreqeeqmkkvegsTLEKALNKYSSLVhlyevkggYERDEKLSKvctglkfdesFLQRDFDYLSGGEKTTV----- 186
Cdd:cd03240 81 NGKKY-------------TITRSLAILENVI--------FCHQGESNW----------PLLDMRGRCSGGEKVLAsliir 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 187 -ILGKLLIHNPNILLLDEPTNHLDMDSIEW-LENYLKNYKGI----VLIVSHDRYFLDHvATKIVEIE 248
Cdd:cd03240 130 lALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQknfqLIVITHDEELVDA-ADHIYRVE 196
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-209 |
4.80e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 54.71 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKY-----MDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGieqmNYYPgypqttsygyDEGLIHV-- 76
Cdd:COG1101 2 LELKNLSKTfnpgtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAG----SLPP----------DSGSILIdg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 77 -----LPRGATSAYLEQV---------PDyphgLKVMDNLNLAFeeidaiekqmreqeeqmKKVEGSTLEKALNKysslv 142
Cdd:COG1101 68 kdvtkLPEYKRAKYIGRVfqdpmmgtaPS----MTIEENLALAY-----------------RRGKRRGLRRGLTK----- 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 143 hlyevkggYERD---EKLSKVCTGLkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:COG1101 122 --------KRRElfrELLATLGLGL---ENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-240 |
5.60e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGieqmnyYPGYPQTtsygydEGLIhvLPRGATS 83
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG------HPAYKIL------EGDI--LFKGESI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 AYLE-------------QVPDYPHGLKVMDNLNLAFeeidaiekqmREQEEQMKKVEGSTLEkalnkysslvhLYEVKgg 150
Cdd:CHL00131 74 LDLEpeerahlgiflafQYPIEIPGVSNADFLRLAY----------NSKRKFQGLPELDPLE-----------FLEII-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 151 yerDEKLSKVctglKFDESFLQRDF-DYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLE---NYLKNYKGI 226
Cdd:CHL00131 131 ---NEKLKLV----GMDPSFLSRNVnEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAegiNKLMTSENS 203
|
250
....*....|....
gi 754786342 227 VLIVSHDRYFLDHV 240
Cdd:CHL00131 204 IILITHYQRLLDYI 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-209 |
7.31e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 54.84 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyypgypqTTSygyDEGLIHVL--- 77
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGM-----------TSP---DAGKITVLgvp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 78 -PRGATSAY--LEQVPDYphglkvmDNLNLAF---EEIDAIEKQMREQEEQMKKVEGSTLEKAlnkysslvhlyevkggy 151
Cdd:PRK13536 105 vPARARLARarIGVVPQF-------DNLDLEFtvrENLLVFGRYFGMSTREIEAVIPSLLEFA----------------- 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 152 eRDEKlskvctglKFDESFLQrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:PRK13536 161 -RLES--------KADARVSD-----LSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
10-233 |
7.38e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 53.67 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 10 KKYMDATL---VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMN----YYPGYPQTTSYGYDEGLIHVLPRGAT 82
Cdd:PRK11629 13 KRYQEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTsgdvIFNGQPMSKLSSAAKAELRNQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 83 SAYLEQVPDYphglKVMDNLNLAFEEIDAIEKQMREQEEQMKKVEGstLEKALNKYSSlvhlyevkggyerdeklskvct 162
Cdd:PRK11629 93 YQFHHLLPDF----TALENVAMPLLIGKKKPAEINSRALEMLAAVG--LEHRANHRPS---------------------- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 163 glkfdesflqrdfdYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDM---DSIEWLENYLKNYKGIV-LIVSHD 233
Cdd:PRK11629 145 --------------ELSGGERQRVAIARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTAfLVVTHD 205
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
348-533 |
7.95e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.86 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDK---GKIEL----------------GS 408
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELlgrtvqregrlardirKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 409 NVKVAYLPQKISFNNEELMLIEV--------------FREDISIVEGKAREYLSKFMFYQSSvFKKVKYLSGGERIRLKL 474
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVligalgstpfwrtcFSWFTREQKQRALQALTRVGMVHFA-HQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754786342 475 AILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQG----TIFFISHDRYFINKMSNRIIAV 533
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVAL 226
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
370-531 |
7.98e-08 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 53.43 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 370 VHYGERVGLIGPNGSGKTTFLK----MLLGEEHPDKGKIELGSNVKVAYLPQKISF---NNEELMLIE--------VFRE 434
Cdd:cd03279 25 LDNNGLFLICGPTGAGKSTILDaityALYGKTPRYGRQENLRSVFAPGEDTAEVSFtfqLGGKKYRVErsrgldydQFTR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 435 DISIVEGKAREYLSkfmfyqssvfKKVKYLSGGE--RIRLKLAILLYDEV--------NLLILDEPTNHLDIDSIETLEE 504
Cdd:cd03279 105 IVLLPQGEFDRFLA----------RPVSTLSGGEtfLASLSLALALSEVLqnrggarlEALFIDEGFGTLDPEALEAVAT 174
|
170 180 190
....*....|....*....|....*....|
gi 754786342 505 ALEDFQGT---IFFISHDRYFINKMSNRII 531
Cdd:cd03279 175 ALELIRTEnrmVGVISHVEELKERIPQRLE 204
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
362-496 |
9.28e-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: 54.09 E-value: 9.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 362 LFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNV----KVAY-LPQKISFNNEELMLIEVFREDI 436
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIsfssQFSWiMPGTIKENIIFGVSYDEYRYKS 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754786342 437 SIVEGKAREYLSKFMFYQSSVFKKVKY-LSGGERIRLKLAILLYDEVNLLILDEPTNHLDI 496
Cdd:cd03291 132 VVKACQLEEDITKFPEKDNTVLGEGGItLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
353-535 |
9.57e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.83 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 353 LTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGeEHPD---KGKIEL-GSNVKVAYLPQK----ISFNNE 424
Cdd:TIGR02633 7 IVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWsGSPLKASNIRDTeragIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 425 ELMLIevfrEDISIVEG---------------------KAREYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVN 483
Cdd:TIGR02633 86 ELTLV----PELSVAENiflgneitlpggrmaynamylRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 484 LLILDEPTNHLDIDSIETLEEALEDFQG---TIFFISHDRYFINKMSNRIIAVED 535
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRD 216
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
348-547 |
1.06e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.49 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGeeHPD----KGKI----------------ELG 407
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDIlfkgesildlepeeraHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 408 --------------SN---VKVAYLPQKISFNNEELMLIEVF---REDISIVEGKAReYLSKfmfYQSSVFkkvkylSGG 467
Cdd:CHL00131 86 iflafqypieipgvSNadfLRLAYNSKRKFQGLPELDPLEFLeiiNEKLKLVGMDPS-FLSR---NVNEGF------SGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 468 ERIR---LKLAILlydEVNLLILDEPTNHLDIDSIETLEEALEDFQGT---IFFISHdrY----------FINKMSN-RI 530
Cdd:CHL00131 156 EKKRneiLQMALL---DSELAILDETDSGLDIDALKIIAEGINKLMTSensIILITH--YqrlldyikpdYVHVMQNgKI 230
|
250
....*....|....*..
gi 754786342 531 IAVEDFSLNSYLGNYDY 547
Cdd:CHL00131 231 IKTGDAELAKELEKKGY 247
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-233 |
1.10e-07 |
|
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: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAydGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPqttsygyDEGLIHVLPRGATS 83
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFDLTIAA--GERVAILGPSGAGKSTLLNLIAGFLP-------P-------DSGRILWNGQDLTA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 AYLEQVP------D---YPHgLKVMDNLNLAfeeidaIEKQMREQEEQMKKVEgstlekalnkysslvhlyevkggyerd 154
Cdd:COG3840 66 LPPAERPvsmlfqEnnlFPH-LTVAQNIGLG------LRPGLKLTAEQRAQVE--------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 155 EKLSKVctGLkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD------MdsIEWLENYLKNYKGIVL 228
Cdd:COG3840 112 QALERV--GL---AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrqeM--LDLVDELCRERGLTVL 184
|
....*
gi 754786342 229 IVSHD 233
Cdd:COG3840 185 MVTHD 189
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
352-525 |
1.12e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 352 DLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVK--VAYLPQKISFN------ 422
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKkdLCTYQKQLCFVghrsgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 423 NEELMLIEVFREDISIVEGKAR-EYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIET 501
Cdd:PRK13540 86 NPYLTLRENCLYDIHFSPGAVGiTELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|....*..
gi 754786342 502 LEEALEDFQ---GTIFFISHDRYFINK 525
Cdd:PRK13540 166 IITKIQEHRakgGAVLLTSHQDLPLNK 192
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-244 |
1.12e-07 |
|
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: 53.52 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 28 DGDKIGIVGVNGSGKSTILKVIAGIEQMNY--YPGYPQttsygYDEGLIHVlpRG-ATSAYLEQVPDyphglkvmdnlnl 104
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLgkFDDPPD-----WDEILDEF--RGsELQNYFTKLLE------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 105 afEEIDAIEK-QMREQEEqmKKVEGSTLEkALNKysslvhlyevkggyeRDE--KLSKVCTGLKFdESFLQRDFDYLSGG 181
Cdd:cd03236 85 --GDVKVIVKpQYVDLIP--KAVKGKVGE-LLKK---------------KDErgKLDELVDQLEL-RHVLDRNIDQLSGG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754786342 182 EKTTVILGKLLIHNPNILLLDEPTNHLDMD---SIEWLENYLKNYKGIVLIVSHDRYFLDHVATKI 244
Cdd:cd03236 144 ELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-209 |
1.16e-07 |
|
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: 53.04 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 17 LVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMNYypgypqtTSYGydegliHVLPRGATS---------AYLE 87
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGG-------TTSG------QILFNGQPRkpdqfqkcvAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 88 QVPDYPHGLKVMDNLnlAFEEIDAIEKQMREqeEQMKKVEGSTLEKALnkysslvHLYEVKGGYerdeklskvctglkfd 167
Cdd:cd03234 88 QDDILLPGLTVRETL--TYTAILRLPRKSSD--AIRKKRVEDVLLRDL-------ALTRIGGNL---------------- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 754786342 168 esflqrdFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:cd03234 141 -------VKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
343-534 |
1.22e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.46 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 343 SGKETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNvKVAYLP-QKIS- 420
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ-HIEGLPgHQIAr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 421 ------FNNeelmlIEVFREdISIVE----GKAREYLSKFMfyqSSVFKKVKY--------------------------- 463
Cdd:PRK11300 80 mgvvrtFQH-----VRLFRE-MTVIEnllvAQHQQLKTGLF---SGLLKTPAFrraesealdraatwlervgllehanrq 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 464 ---LSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEAL----EDFQGTIFFISHDRYFINKMSNRIIAVE 534
Cdd:PRK11300 151 agnLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaelrNEHNVTVLLIEHDMKLVMGISDRIYVVN 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-209 |
1.29e-07 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 52.17 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGieqmnyypgypqTTSYGYDEGLIhvlprgatsaYLEQVPDYPHGLK 97
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG------------RRTGLGVSGEV----------LINGRPLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 98 vmdnlnlafeeidaieKQMR--EQEEQMkkVEGSTLEKALnKYSSlvhlyEVKGgyerdeklskvctglkfdesflqrdf 175
Cdd:cd03213 82 ----------------KIIGyvPQDDIL--HPTLTVRETL-MFAA-----KLRG-------------------------- 111
|
170 180 190
....*....|....*....|....*....|....
gi 754786342 176 dyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:cd03213 112 --LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
34-215 |
1.37e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 53.46 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 34 IVGVNGSGKSTILKVIA--------GIEQMNYYPGYPQTTSYGYDEGLIHVLP--RGATSAYLEQVPDYPH-GLKVMDNL 102
Cdd:COG3950 30 LVGENGSGKTTLLEAIAlalsgllsRLDDVKFRKLLIRNGEFGDSAKLILYYGtsRLLLDGPLKKLERLKEeYFSRLDGY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 103 NLAFEE---IDAIEKQMREQEEQMKKVEGSTLEKALNKYSS-----LVHLYEVKggYERDEKlskvcTGLKFDESFLQRD 174
Cdd:COG3950 110 DSLLDEdsnLREFLEWLREYLEDLENKLSDELDEKLEAVREalnklLPDFKDIR--IDRDPG-----RLVILDKNGEELP 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 175 FDYLSGGEKTTV-----ILGKLLIHNPN---------ILLLDEPTNHLdmdSIEW 215
Cdd:COG3950 183 LNQLSDGERSLLalvgdLARRLAELNPAlenplegegIVLIDEIDLHL---HPKW 234
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
357-518 |
1.55e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.20 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 357 YGERLLFrDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQK----------ISFNNEEL 426
Cdd:PRK13643 17 FASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrkkvgVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 427 MLIE---------------VFREDISIVEGKAREY--LSKfMFYQSSVFKkvkyLSGGERIRLKLAILLYDEVNLLILDE 489
Cdd:PRK13643 96 QLFEetvlkdvafgpqnfgIPKEKAEKIAAEKLEMvgLAD-EFWEKSPFE----LSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190
....*....|....*....|....*....|..
gi 754786342 490 PTNHLDIDS-IETLE--EALEDFQGTIFFISH 518
Cdd:PRK13643 171 PTAGLDPKArIEMMQlfESIHQSGQTVVLVTH 202
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
335-535 |
1.60e-07 |
|
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: 53.03 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 335 LTMSESERSGKETIKATDLTksygerLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVkva 413
Cdd:cd03294 18 FKLLAKGKSKEEILKKTGQT------VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIdGQDI--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 414 ylpqkISFNNEELmlIEVFREDISIV------------------------------EGKAREYLSKfMFYQSSVFKKVKY 463
Cdd:cd03294 89 -----AAMSRKEL--RELRRKKISMVfqsfallphrtvlenvafglevqgvpraerEERAAEALEL-VGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754786342 464 LSGGERIRLKLAILLYDEVNLLILDEPTNHLD----IDSIETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVED 535
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKD 236
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-399 |
1.69e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 16 TLVLEDVSLEAydGDKIGIVGVNGSGKSTILKVIAGieQMNYYPGypqttsygydeglihvlprgatsaylEQVPDYPHG 95
Cdd:PRK10938 18 TLQLPSLTLNA--GDSWAFVGANGSGKSALARALAG--ELPLLSG--------------------------ERQSQFSHI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 96 LkvmdnlNLAFEEIdaieKQMREQEEQMKKVEG-STLEKALNKYSSLVHLYEVKGGyERDEKLSKvctglKFD-ESFLQR 173
Cdd:PRK10938 68 T------RLSFEQL----QKLVSDEWQRNNTDMlSPGEDDTGRTTAEIIQDEVKDP-ARCEQLAQ-----QFGiTALLDR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 174 DFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLK--NYKGIVLIVSHDRY-----FLDHVATkive 246
Cdd:PRK10938 132 RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLAslHQSGITLVLVLNRFdeipdFVQFAGV---- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 247 IEDMESTSykgnyssfveqkeenlriqleqyreqqkkinTMEKQvkdlrdwAIRADnnkffrraaSIQKRLSKMERLDkp 326
Cdd:PRK10938 208 LADCTLAE-------------------------------TGERE-------EILQQ---------ALVAQLAHSEQLE-- 238
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754786342 327 vlerkNMRLTMSESER------SGKETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGeEHP 399
Cdd:PRK10938 239 -----GVQLPEPDEPSarhalpANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHP 311
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-209 |
1.92e-07 |
|
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: 52.62 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 12 YMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIagieqMNYYPgyPQTTSYGYDEGLIhvlpRGATSAYLEQ--- 88
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL-----FRFYD--VSSGSILIDGQDI----REVTLDSLRRaig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 89 -VP-DyphglKVMDN----LNLAFEEIDAIEKQMREQEEQMKKVEgsTLEKALNKYSSLVHlyevkggyERdeklskvct 162
Cdd:cd03253 79 vVPqD-----TVLFNdtigYNIRYGRPDATDEEVIEAAKAAQIHD--KIMRFPDGYDTIVG--------ER--------- 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 754786342 163 GLKfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:cd03253 135 GLK------------LSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
313-495 |
1.94e-07 |
|
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: 54.57 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 313 IQKRLSKmERLDKPVLERKNMRltmseSERSGKETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKM 392
Cdd:TIGR00957 610 LRIFLSH-EELEPDSIERRTIK-----PGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSA 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 393 LLGEEHPDKGKIEL-GSnvkVAYLPQKISFNNEELmlievfREDI----SIVEGKAREYLSKFMFY----------QSSV 457
Cdd:TIGR00957 684 LLAEMDKVEGHVHMkGS---VAYVPQQAWIQNDSL------RENIlfgkALNEKYYQQVLEACALLpdleilpsgdRTEI 754
|
170 180 190
....*....|....*....|....*....|....*...
gi 754786342 458 FKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLD 495
Cdd:TIGR00957 755 GEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
370-559 |
1.96e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 370 VHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVKVAY---LPQKIS-FNNEEL--MLIEVFREDISIVEGK 442
Cdd:PRK13545 47 VPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAALIAIssgLNGQLTgIENIELkgLMMGLTKEKIKEIIPE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 443 AREY--LSKFMfyqssvFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDF--QG-TIFFIS 517
Cdd:PRK13545 127 IIEFadIGKFI------YQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFkeQGkTIFFIS 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 754786342 518 HDRYFINKMSNRIIAV------EDFSLNSYLGNYDYY--------RHEKEKFRQEQ 559
Cdd:PRK13545 201 HSLSQVKSFCTKALWLhygqvkEYGDIKEVVDHYDEFlkkynqmsVEERKDFREEQ 256
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
348-535 |
2.02e-07 |
|
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: 54.04 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLG--EEHPDKGKI-----------------ELGS 408
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 409 NVKV---AYLPQKISFNNEELMLIEVFREDISIV--------------------------EGKAREYLSKFMFYQSSVFK 459
Cdd:TIGR03269 81 PCPVcggTLEPEEVDFWNLSDKLRRRIRKRIAIMlqrtfalygddtvldnvlealeeigyEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 460 KVKY----LSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSI----ETLEEALEDFQGTIFFISHDRYFINKMSNRII 531
Cdd:TIGR03269 161 RITHiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
....
gi 754786342 532 AVED 535
Cdd:TIGR03269 241 WLEN 244
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-233 |
2.09e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 52.47 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAG-IEqmnyyPGYPQTTSYGYDeglIHVLPRGATSAYLEQVPDYPHgl 96
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLS-----PDSGEVRLNGRP---LADWSPAELARRRAVLPQHSS-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 97 kvmdnlnLAF----EEIDAiekqmreqeeqMKKVEGSTLEKALNkysSLVhlyevkggyerDEKLSKV-CTGLKfdesfl 171
Cdd:PRK13548 87 -------LSFpftvEEVVA-----------MGRAPHGLSRAEDD---ALV-----------AAALAQVdLAHLA------ 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754786342 172 QRDFDYLSGGEKTTVILGKLL--IHNPN----ILLLDEPTNHLD----MDSIEWLENYLKNYKGIVLIVSHD 233
Cdd:PRK13548 129 GRDYPQLSGGEQQRVQLARVLaqLWEPDgpprWLLLDEPTSALDlahqHHVLRLARQLAHERGLAVIVVLHD 200
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-266 |
2.15e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 54.06 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 2 LELKLNGIK-KYMDATL-VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIagieqmnyypgypqTTSYGYDEGLIhVLPR 79
Cdd:PRK11160 337 VSLTLNNVSfTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL--------------TRAWDPQQGEI-LLNG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 80 GATSAYLEQ--------VPDYPH----GLKvmDNLNLAFEeiDAIEKQMREQeeqMKKVEGSTL---EKALNKYsslvhL 144
Cdd:PRK11160 402 QPIADYSEAalrqaisvVSQRVHlfsaTLR--DNLLLAAP--NASDEALIEV---LQQVGLEKLledDKGLNAW-----L 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 145 YEvkGGYErdeklskvctglkfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS-IEWLENYLKNY 223
Cdd:PRK11160 470 GE--GGRQ-------------------------LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETeRQILELLAEHA 522
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 754786342 224 KG-IVLIVSHDRYFLDHVaTKIVEIED---MEStsykGNYSSFVEQK 266
Cdd:PRK11160 523 QNkTVLMITHRLTGLEQF-DRICVMDNgqiIEQ----GTHQELLAQQ 564
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-209 |
2.16e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 52.54 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 19 LEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyYPGypqttsygydEGLIHVLPRGATS----------AYLEQ 88
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-----LPG----------QGEILLNGRPLSDwsaaelarhrAYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 89 VPDYPHGLKVMDNLNLAfeeidaiekqmreqeeQMKKVEGSTLEKALNKYSSLVHLyevkggyerDEKLSkvctglkfde 168
Cdd:COG4138 77 QQSPPFAMPVFQYLALH----------------QPAGASSEAVEQLLAQLAEALGL---------EDKLS---------- 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 754786342 169 sflqRDFDYLSGGEKTTVILGK--LLIH---NPN--ILLLDEPTNHLD 209
Cdd:COG4138 122 ----RPLTQLSGGEWQRVRLAAvlLQVWptiNPEgqLLLLDEPMNSLD 165
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-232 |
2.23e-07 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 52.09 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 15 ATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIagieqMNYYPgyPQTTSYGYDEGLIhvlprgatsayleqvPDYPH 94
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL-----ENFYQ--PQGGQVLLDGKPI---------------SQYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 95 GLkVMDNLNLAFEEIDAIEKQMREQ-EEQMKKVEGSTLEKALNKYSSLVHLYEVKGGY--ERDEKLSKvctglkfdesfl 171
Cdd:cd03248 84 KY-LHSKVSLVGQEPVLFARSLQDNiAYGLQSCSFECVKEAAQKAHAHSFISELASGYdtEVGEKGSQ------------ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754786342 172 qrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLEN--YLKNYKGIVLIVSH 232
Cdd:cd03248 151 ------LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQalYDWPERRTVLVIAH 207
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
18-222 |
2.61e-07 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 52.85 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGieqmnYYPGypqttsygyDEGLIHVLPRGATSAYLEqvpdyphglk 97
Cdd:TIGR03522 17 ALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITG-----YLPP---------DSGSVQVCGEDVLQNPKE---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 98 VMDNLNLAFEE----IDAIEKQMREQEEQMKKVEGSTLEKALNKYSSLVHLyevkgGYERDEKLSKvctglkfdesflqr 173
Cdd:TIGR03522 73 VQRNIGYLPEHnplyLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGL-----RPEQHKKIGQ-------------- 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 754786342 174 dfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKN 222
Cdd:TIGR03522 134 ----LSKGYRQRVGLAQALIHDPKVLILDEPTTGLDPNQLVEIRNVIKN 178
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
376-531 |
3.15e-07 |
|
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: 50.78 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 376 VGLIGPNGSGKTTFLKMLLGEEhpdkGKIELGSNVKVAYlPQKISFNNEELMLIEVfredisivegkAREYLSkfmfyqs 455
Cdd:cd03238 24 VVVTGVSGSGKSTLVNEGLYAS----GKARLISFLPKFS-RNKLIFIDQLQFLIDV-----------GLGYLT------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 456 sVFKKVKYLSGGERIRLKLAILLYDEV--NLLILDEPTNHLDIDSIETLEEALEDF--QG-TIFFISHDRYFInKMSNRI 530
Cdd:cd03238 81 -LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLidLGnTVILIEHNLDVL-SSADWI 158
|
.
gi 754786342 531 I 531
Cdd:cd03238 159 I 159
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
342-565 |
3.18e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 342 RSGKETIKATDLTKSYGERLL-FRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQKIS 420
Cdd:PRK13546 18 RTNKERMKDALIPKHKNKTFFaLDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 421 F------NNEELMLIEVF-REDISIVEGKAREY--LSKFmfyqssVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPT 491
Cdd:PRK13546 98 GqltgieNIEFKMLCMGFkRKEIKAMTPKIIEFseLGEF------IYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 492 NHLD-------IDSIETLEEAledfQGTIFFISHDRYFINKMSNRIIAVEDFSLNSY------LGNYDYY--------RH 550
Cdd:PRK13546 172 SVGDqtfaqkcLDKIYEFKEQ----NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYgelddvLPKYEAFlndfkkksKA 247
|
250
....*....|....*
gi 754786342 551 EKEKFRQEQESNALV 565
Cdd:PRK13546 248 EQKEFRNKLDESRFV 262
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
19-240 |
3.26e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.86 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 19 LEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyypgypqtTSYgydEGLIHVLPRGATS----------AYLEQ 88
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL------------LPG---SGSIQFAGQPLEAwsaaelarhrAYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 89 VPDYPHGLKVMDNLNLafeeidaiekqmreqeEQMKKVEGSTLEKALNKYSSLVHLyevkggyerDEKLSkvctglkfde 168
Cdd:PRK03695 77 QQTPPFAMPVFQYLTL----------------HQPDKTRTEAVASALNEVAEALGL---------DDKLG---------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 169 sflqRDFDYLSGGEKTTVILGK--LLIH---NPN--ILLLDEPTNHLDMDSIEWLENYLKNY--KGI-VLIVSHDryfLD 238
Cdd:PRK03695 122 ----RSVNQLSGGEWQRVRLAAvvLQVWpdiNPAgqLLLLDEPMNSLDVAQQAALDRLLSELcqQGIaVVMSSHD---LN 194
|
..
gi 754786342 239 HV 240
Cdd:PRK03695 195 HT 196
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-531 |
4.40e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKS-TILKViagieqMNYYPG----YPQTTSYGYDEGLIHVLP------RGATSAYL 86
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSI------LRLLPSppvvYPSGDIRFHGESLLHASEqtlrgvRGNKIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 87 EQVPdyphglkvMDNLNlafeEIDAIEKQmreqeeqmkkvegstlekalnkysslvhLYEV-------KGGYERDEKLSk 159
Cdd:PRK15134 98 FQEP--------MVSLN----PLHTLEKQ----------------------------LYEVlslhrgmRREAARGEILN- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 160 vC---TGLKFDESFLqRDFDY-LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMD---SIEWLENYLKNYKGI-VLIVS 231
Cdd:PRK15134 137 -CldrVGIRQAAKRL-TDYPHqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSvqaQILQLLRELQQELNMgLLFIT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 232 HD----RYFLDHVATkiveiedMEStsykgnySSFVEQKEENLRIQLEQYREQQKKINtmekqvkdlrdwairadnnkff 307
Cdd:PRK15134 215 HNlsivRKLADRVAV-------MQN-------GRCVEQNRAATLFSAPTHPYTQKLLN---------------------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 308 rraASIQKRLSKMERLDKPVLERKNMRLTMSesersgketIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKT 387
Cdd:PRK15134 259 ---SEPSGDPVPLPEPASPLLDVEQLQVAFP---------IRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKS 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 388 T----FLKMLlgeehPDKGKIE----------------LGSNVKVAYLPQKISFNNEELML------IEVFREDISIVEG 441
Cdd:PRK15134 327 TtglaLLRLI-----NSQGEIWfdgqplhnlnrrqllpVRHRIQVVFQDPNSSLNPRLNVLqiieegLRVHQPTLSAAQR 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 442 KAR--EYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDID---SIETLEEAL-EDFQGTIFF 515
Cdd:PRK15134 402 EQQviAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTvqaQILALLKSLqQKHQLAYLF 481
|
570
....*....|....*.
gi 754786342 516 ISHDRYFINKMSNRII 531
Cdd:PRK15134 482 ISHDLHVVRALCHQVI 497
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-232 |
4.85e-07 |
|
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: 51.07 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIagieqMNYYPgyPQTTSYGYDEGLIHVLPRGATSAYLEQVPDYPHGLK 97
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLL-----MRFYD--PQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 98 --VMDNLNLAFEEIDaiekqmreQEEQMKkvegstLEKALNKYSSLVHLyevKGGYerdeklskvctglkfdESFLQRDF 175
Cdd:cd03254 91 gtIMENIRLGRPNAT--------DEEVIE------AAKEAGAHDFIMKL---PNGY----------------DTVLGENG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 754786342 176 DYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKN-YKG-IVLIVSH 232
Cdd:cd03254 138 GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKlMKGrTSIIIAH 196
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-51 |
5.03e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.47 E-value: 5.03e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAG 51
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA 54
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-247 |
5.51e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 52.47 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 12 YMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnYYPgypqttsygyDEGLIHV-------LPRgatSA 84
Cdd:COG1132 349 YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF----YDP----------TSGRILIdgvdirdLTL---ES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 85 YLEQVpdyphGL----------KVMDNLNLAFEEIDaiekqmreQEEqmkkvegstLEKALNKysslVHLYEV----KGG 150
Cdd:COG1132 412 LRRQI-----GVvpqdtflfsgTIRENIRYGRPDAT--------DEE---------VEEAAKA----AQAHEFiealPDG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 151 Y-----ERdeklskvctGLKfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS----IEWLENYLK 221
Cdd:COG1132 466 YdtvvgER---------GVN------------LSGGQRQRIAIARALLKDPPILILDEATSALDTETealiQEALERLMK 524
|
250 260 270
....*....|....*....|....*....|....*
gi 754786342 222 NYkgIVLIVSH--------DR-YFLDHvaTKIVEI 247
Cdd:COG1132 525 GR--TTIVIAHrlstirnaDRiLVLDD--GRIVEQ 555
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
345-535 |
6.26e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 51.55 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 345 KETIKATDLTKSY--GERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG----SNVKVAYLPQK 418
Cdd:PRK13635 3 EEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 419 IS--FNNEE---------------LMLIEVFREDI--SIVEGKAREYLSKFMFYQSSvfkkvkYLSGGERIRLKLAILLY 479
Cdd:PRK13635 83 VGmvFQNPDnqfvgatvqddvafgLENIGVPREEMveRVDQALRQVGMEDFLNREPH------RLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754786342 480 DEVNLLILDEPTNHLD----IDSIETLEEALEDFQGTIFFISHDryfINKM--SNRIIAVED 535
Cdd:PRK13635 157 LQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITHD---LDEAaqADRVIVMNK 215
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-249 |
6.44e-07 |
|
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: 52.52 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGI------EQMNYYPGYPQTTSYGYDE-----G 72
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwDGEIYWSGSPLKASNIRDTeragiV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 73 LIHvlprgatsAYLEQVPDyphgLKVMDNLNLAFEeidaiekqmreqeeqmkkvegSTLEKALNKYSSLVHlyevkggye 152
Cdd:TIGR02633 82 IIH--------QELTLVPE----LSVAENIFLGNE---------------------ITLPGGRMAYNAMYL--------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 153 RDEKLSKvctGLKFDESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK--GIVLI- 229
Cdd:TIGR02633 120 RAKNLLR---ELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKahGVACVy 196
|
250 260
....*....|....*....|
gi 754786342 230 VSHDRYFLDHVATKIVEIED 249
Cdd:TIGR02633 197 ISHKLNEVKAVCDTICVIRD 216
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-248 |
6.52e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 50.86 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKlnGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMN---YYPGYPQTTSYGYDEGLIhvl 77
Cdd:PRK09493 1 MIEFK--NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITsgdLIVDGLKVNDPKVDERLI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 78 pRGATSAYLEQVPDYPHglkvMDNL-NLAFEEIdaiekQMReqeeQMKKVEGSTLEKALnkysslvhlyevkggyerdek 156
Cdd:PRK09493 76 -RQEAGMVFQQFYLFPH----LTALeNVMFGPL-----RVR----GASKEEAEKQAREL--------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 157 LSKVctGLKfdesflQRDFDY---LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMdsiEWLENYLKNYKGI------V 227
Cdd:PRK09493 121 LAKV--GLA------ERAHHYpseLSGGQQQRVAIARALAVKPKLMLFDEPTSALDP---ELRHEVLKVMQDLaeegmtM 189
|
250 260
....*....|....*....|.
gi 754786342 228 LIVSHDRYFLDHVATKIVEIE 248
Cdd:PRK09493 190 VIVTHEIGFAEKVASRLIFID 210
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
373-535 |
6.78e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 52.33 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNVK----------VAYLPQKISF------NNEELMLIEVF-RE 434
Cdd:PRK11176 369 GKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdGHDLRdytlaslrnqVALVSQNVHLfndtiaNNIAYARTEQYsRE 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 435 DIsivEGKAReylskfMFYQSSVFKKVKY------------LSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETL 502
Cdd:PRK11176 449 QI---EEAAR------MAYAMDFINKMDNgldtvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAI 519
|
170 180 190
....*....|....*....|....*....|....*
gi 754786342 503 EEALEDFQG--TIFFISHDRYFINKmSNRIIAVED 535
Cdd:PRK11176 520 QAALDELQKnrTSLVIAHRLSTIEK-ADEILVVED 553
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-232 |
7.40e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGieqmNYYPgypqttsygyDEGLIHVlpRGATS 83
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSG----NYQP----------DAGSILI--DGQEM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 AY-----------------LEQVPDyphgLKVMDNLNLAfeeidaiekqmreqeeQMKKVEGSTLEKALNkysslvhlye 146
Cdd:PRK11288 69 RFasttaalaagvaiiyqeLHLVPE----MTVAENLYLG----------------QLPHKGGIVNRRLLN---------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 147 vkggYERDEKLSKVctGLKFDEsflQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLE---NYLKNY 223
Cdd:PRK11288 119 ----YEAREQLEHL--GVDIDP---DTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFrviRELRAE 189
|
....*....
gi 754786342 224 KGIVLIVSH 232
Cdd:PRK11288 190 GRVILYVSH 198
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
352-534 |
8.13e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 50.48 E-value: 8.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 352 DLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKI------ELGSNVKVA------------ 413
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLivdglkVNDPKVDERlirqeagmvfqq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 414 -YL-PQKISFNNEELMLIEVFREDISIVEGKAREYLSKFMF------YQSSvfkkvkyLSGGERIRLKLAILLYDEVNLL 485
Cdd:PRK09493 86 fYLfPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLaerahhYPSE-------LSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 486 ILDEPTNHLDidsIETLEEALEDFQG------TIFFISHDRYFINKMSNRIIAVE 534
Cdd:PRK09493 159 LFDEPTSALD---PELRHEVLKVMQDlaeegmTMVIVTHEIGFAEKVASRLIFID 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
373-534 |
8.40e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.98 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG--------SNVKVAYLPQKIS----------FNNEELMLIEVFRE 434
Cdd:PRK13641 33 GSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhitpetGNKNLKKLRKKVSlvfqfpeaqlFENTVLKDVEFGPK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 435 DISIVEGKARE----YLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQ 510
Cdd:PRK13641 113 NFGFSEDEAKEkalkWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQ 192
|
170 180
....*....|....*....|....*..
gi 754786342 511 G---TIFFISHDRYFINKMSNRIIAVE 534
Cdd:PRK13641 193 KaghTVILVTHNMDDVAEYADDVLVLE 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-232 |
9.45e-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: 49.80 E-value: 9.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 14 DATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQ-------MNYYPGYPQTTSYGydEGLihvlprgatsAYL 86
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPplagrvlLNGGPLDFQRDSIA--RGL----------LYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 87 EQVPDYPHGLKVMDNLNLaFEEIDAIEkqmreqeeqmkkvegsTLEKALNKysslVHLyevkGGYErdeklskvctglkf 166
Cdd:cd03231 79 GHAPGIKTTLSVLENLRF-WHADHSDE----------------QVEEALAR----VGL----NGFE-------------- 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754786342 167 desflQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNY---KGIVLIVSH 232
Cdd:cd03231 120 -----DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-268 |
1.08e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 51.65 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYM----DATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSY---GYDeglihv 76
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDK-------PTSGTYrvaGQD------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 77 lprgatsayleqvpdyphgLKVMDNlnlafeeiDAIEKQMREQeeqmkkvegstLEKALNKYSSLVHLYE--------VK 148
Cdd:PRK10535 72 -------------------VATLDA--------DALAQLRREH-----------FGFIFQRYHLLSHLTAaqnvevpaVY 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 149 GGYERDEKLSKVctglkfdESFLQR-----DFDY----LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENY 219
Cdd:PRK10535 114 AGLERKQRLLRA-------QELLQRlgledRVEYqpsqLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAI 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 220 LKNYKG---IVLIVSHDryflDHVAT---KIVEIEDMESTSYKGNYSSFVEQKEE 268
Cdd:PRK10535 187 LHQLRDrghTVIIVTHD----PQVAAqaeRVIEIRDGEIVRNPPAQEKVNVAGGT 237
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
348-519 |
1.14e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 50.37 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYG--ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNV----KVAYLPQKIS- 420
Cdd:PRK13632 8 IKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITiskeNLKEIRKKIGi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 421 -FNNEELMLIEVFRE-DISI-VEGK--AREYLSKFMfyqSSVFKKV----------KYLSGGERIRLKLAILLYDEVNLL 485
Cdd:PRK13632 88 iFQNPDNQFIGATVEdDIAFgLENKkvPPKKMKDII---DDLAKKVgmedyldkepQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 754786342 486 ILDEPTNHLDIDSIETLEEALEDFQG----TIFFISHD 519
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKtrkkTLISITHD 202
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
357-535 |
1.24e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.88 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 357 YGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQKIsfnneelmlievFREDI 436
Cdd:PRK11614 15 YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI------------MREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 437 SIV-EGK-------AREYLSKFMF------YQSSV--------------FKKVKYLSGGERIRLKLAILLYDEVNLLILD 488
Cdd:PRK11614 83 AIVpEGRrvfsrmtVEENLAMGGFfaerdqFQERIkwvyelfprlherrIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 489 EPTNHLD-------IDSIETLEEaledfQG-TIFFISHDRYFINKMSNRIIAVED 535
Cdd:PRK11614 163 EPSLGLApiiiqqiFDTIEQLRE-----QGmTIFLVEQNANQALKLADRGYVLEN 212
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
353-519 |
1.31e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.78 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 353 LTKSYG--ERLLFRDAGV--MVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV-------KVAYLPQKIS 420
Cdd:PRK10584 12 LKKSVGqgEHELSILTGVelVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvGQPLhqmdeeaRAKLRAKHVG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 421 FNNEELMLIEVF--REDISI-------VEGKAREYlSKFMFYQSSVFKKVKY----LSGGERIRLKLAILLYDEVNLLIL 487
Cdd:PRK10584 92 FVFQSFMLIPTLnaLENVELpallrgeSSRQSRNG-AKALLEQLGLGKRLDHlpaqLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 754786342 488 DEPTNHLDIDSIETLEEAL----EDFQGTIFFISHD 519
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
345-519 |
1.38e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 50.27 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 345 KETIKATDLTKSY--GERLLfRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIE-LGSNVK-------VAY 414
Cdd:PRK15056 4 QAGIVVNDVTVTWrnGHTAL-RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISiLGQPTRqalqknlVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 415 LPQKISFNNEELMLIEVF----------------REDISIVEGK-AREYLSKFMFYQssvfkkVKYLSGGERIRLKLAIL 477
Cdd:PRK15056 83 VPQSEEVDWSFPVLVEDVvmmgryghmgwlrrakKRDRQIVTAAlARVDMVEFRHRQ------IGELSGGQKKRVFLARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 754786342 478 LYDEVNLLILDEPTNHLDIDS---IETLEEALEDFQGTIFFISHD 519
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTearIISLLRELRDEGKTMLVSTHN 201
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
378-519 |
1.51e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 49.24 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 378 LIGPNGSGKTTFL---KMLLGEEHPDKGKI------------------ELGSNVKVAYLPQK--ISFNNEE--------- 425
Cdd:COG0419 28 IVGPNGAGKSTILeaiRYALYGKARSRSKLrsdlinvgseeasvelefEHGGKRYRIERRQGefAEFLEAKpserkealk 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 426 ----LMLIEVFREDISIVEGKAREYLSKF---------MFYQSSVFKKVKYLSGGERIRLKLAILLYdevnlLILDepTN 492
Cdd:COG0419 108 rllgLEIYEELKERLKELEEALESALEELaelqklkqeILAQLSGLDPIETLSGGERLRLALADLLS-----LILD--FG 180
|
170 180
....*....|....*....|....*..
gi 754786342 493 HLDIDSIETLEEALEDfqgtIFFISHD 519
Cdd:COG0419 181 SLDEERLERLLDALEE----LAIITHV 203
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-268 |
1.55e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.05 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 12 YMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQM--NYYPGYPQTTSYGYDEGLIHVLP-RGATSAYLEQ 88
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydSKIKVDGKVLYFGKDIFQIDAIKlRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 89 VPDYPHgLKVMDNLNLAFEEIDAIEKQmreqeeQMKKVegstLEKALNKysslVHLYevKGGYERdeklskvctglkfde 168
Cdd:PRK14246 99 PNPFPH-LSIYDNIAYPLKSHGIKEKR------EIKKI----VEECLRK----VGLW--KEVYDR--------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 169 sfLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDM---DSIEWLENYLKNYKGIVlIVSHDRYFLDHVATKIV 245
Cdd:PRK14246 147 --LNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIvnsQAIEKLITELKNEIAIV-IVSHNPQQVARVADYVA 223
|
250 260
....*....|....*....|...
gi 754786342 246 EIEDMESTSYKGNYSSFVEQKEE 268
Cdd:PRK14246 224 FLYNGELVEWGSSNEIFTSPKNE 246
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-232 |
1.60e-06 |
|
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: 51.29 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyYPGYpqttsygydEGLIHVLPRGAtsayLEQVPDYPHglk 97
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-----WPVY---------GGRLTKPAKGK----LFYVPQRPY--- 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 98 vMDNLNLAfeeiDAIEKQMREQEEQMKKVEGSTLEKALNKYSsLVHLYEVKGGYE--RDEKlskvctglkfdesflqrdf 175
Cdd:TIGR00954 526 -MTLGTLR----DQIIYPDSSEDMKRRGLSDKDLEQILDNVQ-LTHILEREGGWSavQDWM------------------- 580
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 176 DYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYkGIVLI-VSH 232
Cdd:TIGR00954 581 DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF-GITLFsVSH 637
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
352-534 |
1.65e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.80 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 352 DLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGsNVKVAYLPQK------------- 418
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG-EKRMNDVPPAergvgmvfqsyal 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 419 ---------ISFNneeLMLIEVFREDISIVEGKAREYLSKFMFYQssvfKKVKYLSGGERIRLKLAILLYDEVNLLILDE 489
Cdd:PRK11000 87 yphlsvaenMSFG---LKLAGAKKEEINQRVNQVAEVLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 754786342 490 PTNHLD--------IDsIETLEEALedfQGTIFFISHDRYFINKMSNRIIAVE 534
Cdd:PRK11000 160 PLSNLDaalrvqmrIE-ISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLD 208
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
309-518 |
1.66e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 51.00 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 309 RAASIQKRLSKMERLDKPVLERKNMRLTMSESErsgKETIKATDLT-KSY-GERLL----FRdagvmVHYGERVGLIGPN 382
Cdd:PRK11174 314 KAQAVGAAESLVTFLETPLAHPQQGEKELASND---PVTIEAEDLEiLSPdGKTLAgplnFT-----LPAGQRIALVGPS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 383 GSGKTTFLKMLLGeEHPDKGK-----IELgSNVKVAYLPQKISFNNEELMLIE-VFREDISIVEGKARE----------Y 446
Cdd:PRK11174 386 GAGKTSLLNALLG-FLPYQGSlkingIEL-RELDPESWRKHLSWVGQNPQLPHgTLRDNVLLGNPDASDeqlqqalenaW 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 447 LSKFMfyqSSVFKKVKY--------LSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDS----IETLEEALEDfQGTIf 514
Cdd:PRK11174 464 VSEFL---PLLPQGLDTpigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSeqlvMQALNAASRR-QTTL- 538
|
....
gi 754786342 515 FISH 518
Cdd:PRK11174 539 MVTH 542
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
340-495 |
1.72e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 340 SERSGKETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGkiELGSNVKVAYLPQK- 418
Cdd:PTZ00243 653 SERSAKTPKMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG--RVWAERSIAYVPQQa 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 419 ----------ISFNNEE--LMLIEVFRedISIVEGKAREyLSKFMfyQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLI 486
Cdd:PTZ00243 731 wimnatvrgnILFFDEEdaARLADAVR--VSQLEADLAQ-LGGGL--ETEIGEKGVNLSGGQKARVSLARAVYANRDVYL 805
|
....*....
gi 754786342 487 LDEPTNHLD 495
Cdd:PTZ00243 806 LDDPLSALD 814
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
10-245 |
1.82e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.94 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 10 KKYMDATLVLEdvSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPqttsygyDEGlihVLPRGATSAYLEQ- 88
Cdd:COG1245 349 KSYGGFSLEVE--GGEIREGEVLGIVGPNGIGKTTFAKILAGVLK-------P-------DEG---EVDEDLKISYKPQy 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 89 -VPDYPhgLKVMDNLNLAFEEidaiekqmreqeeqmkKVEGSTLEKALNKYSSLVHLYEvkggyerdeklskvctglkfd 167
Cdd:COG1245 410 iSPDYD--GTVEEFLRSANTD----------------DFGSSYYKTEIIKPLGLEKLLD--------------------- 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 168 esflqRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD----MDSIEWLENYLKNYKGIVLIVSHDRYFLDHVATK 243
Cdd:COG1245 451 -----KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDR 525
|
..
gi 754786342 244 IV 245
Cdd:COG1245 526 LM 527
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-233 |
1.85e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 49.99 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 5 KLNGIK-KYMDAT-LVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQttsygydEGLIHVLPRGAT 82
Cdd:PRK13632 9 KVENVSfSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLK-------PQ-------SGEIKIDGITIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 83 SAYLEQV----------PDYPH-GLKVMDNLNLAFEEIdaiekqmREQEEQMKKVegstlekaLNKYSSLVHLyevkggy 151
Cdd:PRK13632 75 KENLKEIrkkigiifqnPDNQFiGATVEDDIAFGLENK-------KVPPKKMKDI--------IDDLAKKVGM------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 152 erdeklskvctglkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD----MDSIEWLENYLKNYKGIV 227
Cdd:PRK13632 133 ----------------EDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTL 196
|
....*.
gi 754786342 228 LIVSHD 233
Cdd:PRK13632 197 ISITHD 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
368-511 |
1.95e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 368 VMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIElGSNVKVAYLP----QKI-----SFNNEELM----------L 428
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ-SQFSHITRLSfeqlQKLvsdewQRNNTDMLspgeddtgrtT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 429 IEVFREDisiVEGKAR-EYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALE 507
Cdd:PRK10938 103 AEIIQDE---VKDPARcEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLA 179
|
....
gi 754786342 508 DFQG 511
Cdd:PRK10938 180 SLHQ 183
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
378-519 |
2.40e-06 |
|
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: 47.74 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 378 LIGPNGSGKTTFLK----MLLGEEHPDKGKIELGSNVKVAYlpQKISFNneelmlievfredisivegkareylskFMFY 453
Cdd:cd03227 26 ITGPNGSGKSTILDaiglALGGAQSATRRRSGVKAGCIVAA--VSAELI---------------------------FTRL 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754786342 454 QssvfkkvkyLSGGER----IRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDF---QGTIFFISHD 519
Cdd:cd03227 77 Q---------LSGGEKelsaLALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvkGAQVIVITHL 140
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-233 |
2.46e-06 |
|
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: 49.56 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 9 IKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAG-IEqmnyypgyPQTTSYGYDEGLIHVLPRGATSA--- 84
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRlIE--------PTSGKVLIDGQDIAAMSRKELRElrr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 85 -YLEQVPD----YPHgLKVMDNLNLAFeEIDAIEKQMREqeeqmkkvegstlEKALnkysslvhlyevkggyerdEKLSK 159
Cdd:cd03294 102 kKISMVFQsfalLPH-RTVLENVAFGL-EVQGVPRAERE-------------ERAA-------------------EALEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 160 VctGLkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD------MDSiEWLENYLKNYKGIVLIvSHD 233
Cdd:cd03294 148 V--GL---EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirreMQD-ELLRLQAELQKTIVFI-THD 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
370-533 |
2.55e-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: 49.67 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 370 VHYGERVGLIGPNGSGKTTFLKMLLG-EEHP--DKGKIEL-GSNV--------------KVAYLPQ----------KISF 421
Cdd:COG0444 28 VRRGETLGLVGESGSGKSTLARAILGlLPPPgiTSGEILFdGEDLlklsekelrkirgrEIQMIFQdpmtslnpvmTVGD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 422 nneelMLIEVFR--EDISIVEGKAR--EYLSKF-MFYQSSVFKKvkY---LSGGERIRLKLAILLYDEVNLLILDEPTNH 493
Cdd:COG0444 108 -----QIAEPLRihGGLSKAEARERaiELLERVgLPDPERRLDR--YpheLSGGMRQRVMIARALALEPKLLIADEPTTA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 754786342 494 LDIdSI-----ETLEEALEDFQGTIFFISHDRYFINKMSNRiIAV 533
Cdd:COG0444 181 LDV-TIqaqilNLLKDLQRELGLAILFITHDLGVVAEIADR-VAV 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-233 |
2.71e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.40 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIagieqmnyypGYPQTTSYGydEGLIHVLPRGA--TSAYLEQVPDYPhg 95
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML----------GRHQPPSEG--EILLDAQPLESwsSKAFARKVAYLP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 96 lkvmdnlnlafeeidaiekqmreqeEQMKKVEGSTLEK--ALNKYSSlvHLYEVKGGYERDEKLSKVCT--GLKfdeSFL 171
Cdd:PRK10575 92 -------------------------QQLPAAEGMTVRElvAIGRYPW--HGALGRFGAADREKVEEAISlvGLK---PLA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754786342 172 QRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDM-DSIEWLE--NYLKNYKGIVLI-VSHD 233
Cdd:PRK10575 142 HRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIaHQVDVLAlvHRLSQERGLTVIaVLHD 207
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
18-54 |
2.87e-06 |
|
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: 48.97 E-value: 2.87e-06
10 20 30
....*....|....*....|....*....|....*..
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQ 54
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDR 63
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-233 |
3.33e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 49.32 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 19 LEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnYYPgypqttsygyDEGLIHVL---PRGATSAYLEQV------ 89
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGI----LVP----------TSGEVRVLgyvPFKRRKEFARRIgvvfgq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 90 -----PDYPhglkVMDNLNLafeeidaiekqMREqeeqMKKVEGSTLEKALNKYSSLVHLyevkggyerdeklskvctgl 164
Cdd:COG4586 104 rsqlwWDLP----AIDSFRL-----------LKA----IYRIPDAEYKKRLDELVELLDL-------------------- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754786342 165 kfdESFLQRDFDYLSGGEKttvILGKL---LIHNPNILLLDEPTNHLDMDSIEWLENYLKNY---KGI-VLIVSHD 233
Cdd:COG4586 145 ---GELLDTPVRQLSLGQR---MRCELaaaLLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnreRGTtILLTSHD 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-249 |
3.52e-06 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 49.71 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKLNgiKKYMDATLvleDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPqttsygyDEGLIHVlpRG 80
Cdd:COG4148 2 MLEVDFR--LRRGGFTL---DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLER-------P-------DSGRIRL--GG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 81 AT---SAYLEQVPDY--------------PHgLKVMDNLNLAfeeidaiekqmreqeeqMKKVEGStlekalnkysslvh 143
Cdd:COG4148 61 EVlqdSARGIFLPPHrrrigyvfqearlfPH-LSVRGNLLYG-----------------RKRAPRA-------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 144 lyevkggyERDEKLSKVCT--GLkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS----IEWLE 217
Cdd:COG4148 109 --------ERRISFDEVVEllGI---GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkaeiLPYLE 177
|
250 260 270
....*....|....*....|....*....|....*.
gi 754786342 218 NyLKNYKGI-VLIVSHDryfLDHV---ATKIVEIED 249
Cdd:COG4148 178 R-LRDELDIpILYVSHS---LDEVarlADHVVLLEQ 209
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
349-406 |
3.81e-06 |
|
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: 48.44 E-value: 3.81e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 349 KATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL 406
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRF 62
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-298 |
3.86e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.24 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 19 LEDVSLEAYDGDKIGIVGVNGSGKSTILKVIagieqmnyypgypqttsygydEGLIhVLPRGATSayleqVPDY--PHGL 96
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLT---------------------NGLI-ISETGQTI-----VGDYaiPANL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 97 KVMDNLNLAFEEIDAIEKQMREQEEQmkkvegSTLEKALNkySSLVHLYEVKggYERDEKLSKVCTGLKFDESFLQRDFD 176
Cdd:PRK13645 80 KKIKEVKRLRKEIGLVFQFPEYQLFQ------ETIEKDIA--FGPVNLGENK--QEAYKKVPELLKLVQLPEDYVKRSPF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 177 YLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD----MDSIEWLENYLKNYKGIVLIVSHDRYFLDHVATKIVEIEDMES 252
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDpkgeEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 754786342 253 TSYKGNYSSFVEQkEENLRIQLE-------QYREQQKKINTMEKQVKDLRDWA 298
Cdd:PRK13645 230 ISIGSPFEIFSNQ-ELLTKIEIDppklyqlMYKLKNKGIDLLNKNIRTIEEFA 281
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
352-520 |
3.91e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 49.33 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 352 DLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKI--------------------------- 404
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvthrsiqqrdicmvfqsyalf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 405 ---ELGSNVKVAYLPQKISfnNEELMliEVFREDISIV--EGKAREYlskfmfyqssvfkkVKYLSGGERIRLKLAILLY 479
Cdd:PRK11432 91 phmSLGENVGYGLKMLGVP--KEERK--QRVKEALELVdlAGFEDRY--------------VDQISGGQQQRVALARALI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 754786342 480 DEVNLLILDEPTNHLDID---SI-ETLEEALEDFQGTIFFISHDR 520
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANlrrSMrEKIRELQQQFNITSLYVTHDQ 197
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-257 |
4.11e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 48.76 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMnyypgYPQTTSYG--YDEGL----- 73
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIEL-----YPEARVSGevYLDGQdifkm 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 74 -IHVLPRGATSAYleQVPDYPHGLKVMDNLNLAFEeIDAIEKQMREQEEQMKKvegsTLEKAlnkysslvHLYEvkggyE 152
Cdd:PRK14247 76 dVIELRRRVQMVF--QIPNPIPNLSIFENVALGLK-LNRLVKSKKELQERVRW----ALEKA--------QLWD-----E 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 153 RDEKLSKVCTGLkfdesflqrdfdylSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS---IEWLENYLKNYKGIVLI 229
Cdd:PRK14247 136 VKDRLDAPAGKL--------------SGGQQQRLCIARALAFQPEVLLADEPTANLDPENtakIESLFLELKKDMTIVLV 201
|
250 260
....*....|....*....|....*...
gi 754786342 230 VshdryfldHVATKIVEIEDMESTSYKG 257
Cdd:PRK14247 202 T--------HFPQQAARISDYVAFLYKG 221
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-52 |
4.11e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.66 E-value: 4.11e-06
10 20 30
....*....|....*....|....*....|....
gi 754786342 19 LEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGI 52
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGS 73
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
18-233 |
4.22e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.57 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPqttsygyDEGLIhVLPRGATSAYLeqvpdyPHGLK 97
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVA-------P-------DEGVI-KRNGKLRIGYV------PQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 98 VMDNLNLAfeeidaIEKQMReqeeqmkkvegstLEKALNKYSSLVHLYEVKGGYERDEKLSKvctglkfdesflqrdfdy 177
Cdd:PRK09544 78 LDTTLPLT------VNRFLR-------------LRPGTKKEDILPALKRVQAGHLIDAPMQK------------------ 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754786342 178 LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDM-------DSIEWLENYLkNYKgiVLIVSHD 233
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVngqvalyDLIDQLRREL-DCA--VLMVSHD 180
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
349-495 |
4.31e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.88 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 349 KATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPD--KGKIeLGSNVKVA-YLPQKISFNN-- 423
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTI-LANNRKPTkQILKRTGFVTqd 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 424 ----------EELMLIEVFR--------EDISIVEGKAREY-LSKFmfyQSSVFKK--VKYLSGGERIRLKLAILLYDEV 482
Cdd:PLN03211 149 dilyphltvrETLVFCSLLRlpksltkqEKILVAESVISELgLTKC---ENTIIGNsfIRGISGGERKRVSIAHEMLINP 225
|
170
....*....|...
gi 754786342 483 NLLILDEPTNHLD 495
Cdd:PLN03211 226 SLLILDEPTSGLD 238
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-245 |
4.39e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 9 IKKYMDATLVLEdvSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPqttsygyDEGLIHVLPRgatSAYLEQ 88
Cdd:PRK13409 347 TKKLGDFSLEVE--GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLK-------P-------DEGEVDPELK---ISYKPQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 89 --VPDYPhgLKVMDNLnlafeeidaiekqmreqEEQMKKVEGSTLEKALNKYSSLVHLYEvkggyerdeklskvctglkf 166
Cdd:PRK13409 408 yiKPDYD--GTVEDLL-----------------RSITDDLGSSYYKSEIIKPLQLERLLD-------------------- 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 167 desflqRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDmdsIEW-------LENYLKNYKGIVLIVSHDRYFLDH 239
Cdd:PRK13409 449 ------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD---VEQrlavakaIRRIAEEREATALVVDHDIYMIDY 519
|
....*.
gi 754786342 240 VATKIV 245
Cdd:PRK13409 520 ISDRLM 525
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-233 |
5.23e-06 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 48.58 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 14 DATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnYYPgypqttsygyDEGLIHVLprgatsayleqvpdyp 93
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL----LLP----------TSGKVTVD---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 94 hGLKVMDNLNL---------------------------AFeeidAIEKQMREQEEQMKKVegstlekalnkysslvhlye 146
Cdd:TIGR04520 63 -GLDTLDEENLweirkkvgmvfqnpdnqfvgatveddvAF----GLENLGVPREEMRKRV-------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 147 vkggyerDEKLSKVctGLkfdESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD-------MDSIewleNY 219
Cdd:TIGR04520 118 -------DEALKLV--GM---EDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDpkgrkevLETI----RK 181
|
250
....*....|....*
gi 754786342 220 LKNYKGIVLI-VSHD 233
Cdd:TIGR04520 182 LNKEEGITVIsITHD 196
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
373-535 |
5.43e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 48.58 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIE-LGSNVK------------------------------VAYLPQKISF 421
Cdd:PRK13647 31 GSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvMGREVNaenekwvrskvglvfqdpddqvfsstvwddVAFGPVNMGL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 422 NNEElmlievfredisiVEGKAREYLsKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIET 501
Cdd:PRK13647 111 DKDE-------------VERRVEEAL-KAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 754786342 502 LEEALEDF--QG-TIFFISHDRYFINKMSNRIIAVED 535
Cdd:PRK13647 177 LMEILDRLhnQGkTVIVATHDVDLAAEWADQVIVLKE 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-241 |
5.50e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 48.47 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQT-TSYGYDEGLIHVLPR--GATSAYLEQVPDYPH 94
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLT-------PQSgTVFLGDKPISMLSSRqlARRLALLPQHHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 95 GLKVMD--------NLNLAfeeidaieKQMREQEEQMkkvegstLEKALNKySSLVHLYEvkggyerdeklskvctglkf 166
Cdd:PRK11231 90 GITVRElvaygrspWLSLW--------GRLSAEDNAR-------VNQAMEQ-TRINHLAD-------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 167 desflqRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMD-SIEW--LENYLKNYKGIVLIVSHD-----RYfLD 238
Cdd:PRK11231 134 ------RRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINhQVELmrLMRELNTQGKTVVTVLHDlnqasRY-CD 206
|
...
gi 754786342 239 HVA 241
Cdd:PRK11231 207 HLV 209
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
5.99e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 48.54 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKlNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPqttsygyDEGliHVLPRG 80
Cdd:PRK13639 1 ILETR-DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILK-------P-------TSG--EVLIKG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 81 ATSAYleqvpDYPHGLKVMDNLNLAFEEIDaiekqmreqeEQM--KKVEGSTLEKALNKysslvhlyevkgGYERDEKLS 158
Cdd:PRK13639 64 EPIKY-----DKKSLLEVRKTVGIVFQNPD----------DQLfaPTVEEDVAFGPLNL------------GLSKEEVEK 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 159 KVCTGLKF--DESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLK--NYKGIVLIVS-HD 233
Cdd:PRK13639 117 RVKEALKAvgMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYdlNKEGITIIIStHD 196
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-233 |
6.67e-06 |
|
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: 47.75 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 7 NGIKKYmDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPGYPQTTSYGYDeglihVLPRGAtsayl 86
Cdd:cd03265 5 NLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK----PTSGRATVAGHD-----VVREPR----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 87 eqvpdyphglKVMDNLNLAFEEIdaiekqmreqeeqmkkvegsTLEKALNKYSSLV---HLYEVKGGyERDEKLSKVCTG 163
Cdd:cd03265 70 ----------EVRRRIGIVFQDL--------------------SVDDELTGWENLYihaRLYGVPGA-ERRERIDELLDF 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754786342 164 LKFDEsFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKG----IVLIVSHD 233
Cdd:cd03265 119 VGLLE-AADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefgmTILLTTHY 191
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
348-518 |
6.67e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 47.65 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYgERLLFRdAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQK----ISFNN 423
Cdd:PRK10771 2 LKLTDITWLY-HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRrpvsMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 424 EELMLIEVFREDISI----------VEGKAREYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNH 493
Cdd:PRK10771 80 NNLFSHLTVAQNIGLglnpglklnaAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180
....*....|....*....|....*....
gi 754786342 494 LD----IDSIETLEEALEDFQGTIFFISH 518
Cdd:PRK10771 160 LDpalrQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
366-518 |
8.05e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 366 AGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIElgsnvkvaYLPQKISFNN-------------EELMLIevf 432
Cdd:PRK10762 23 AALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIL--------YLGKEVTFNGpkssqeagigiihQELNLI--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 433 rEDISIVEG--KAREYLSKF-------MFYQSSVFKK---VKY--------LSGGERIRLKLAILLYDEVNLLILDEPTN 492
Cdd:PRK10762 92 -PQLTIAENifLGREFVNRFgridwkkMYAEADKLLArlnLRFssdklvgeLSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180
....*....|....*....|....*....
gi 754786342 493 HLDIDSIETLEEALEDF--QGT-IFFISH 518
Cdd:PRK10762 171 ALTDTETESLFRVIRELksQGRgIVYISH 199
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-247 |
8.39e-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: 48.13 E-value: 8.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMNyypgypqttsyGYDEGLIHVlpRGatsayleqvpdyphglk 97
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPP-----------GITSGEILF--DG----------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 98 vmdnlnlafEEIDAI-EKQMRE---QEEQM------------KKVeGSTLEKALnkyssLVHlyEVKGGYERDEK----L 157
Cdd:COG0444 70 ---------EDLLKLsEKELRKirgREIQMifqdpmtslnpvMTV-GDQIAEPL-----RIH--GGLSKAEARERaielL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 158 SKVctGLKFDESFLQRdfdY---LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMdSIEW--LeNYLKNYK-----GIV 227
Cdd:COG0444 133 ERV--GLPDPERRLDR---YpheLSGGMRQRVMIARALALEPKLLIADEPTTALDV-TIQAqiL-NLLKDLQrelglAIL 205
|
250 260
....*....|....*....|....*...
gi 754786342 228 LIvSHD----RYFLDHVAT----KIVEI 247
Cdd:COG0444 206 FI-THDlgvvAEIADRVAVmyagRIVEE 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-280 |
8.47e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 47.82 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 1 MLELKlNGIKKYMDATlVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMNyyPGYPQTTSYGYDEGLIHVLPRG 80
Cdd:PRK11264 3 AIEVK-NLVKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPE--AGTIRVGDITIDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 81 ATSAYLEQVpdyphGLkVMDNLNLaFEEIDAIEKQMreqeEQMKKVEGSTLEKALNKYSSLvhlyevkggyerdekLSKV 160
Cdd:PRK11264 79 LIRQLRQHV-----GF-VFQNFNL-FPHRTVLENII----EGPVIVKGEPKEEATARAREL---------------LAKV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 161 ctGLKFDESFLQRDfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSI-EWLENY--LKNYKGIVLIVSHDRYFL 237
Cdd:PRK11264 133 --GLAGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVgEVLNTIrqLAQEKRTMVIVTHEMSFA 207
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 754786342 238 DHVATKIVEIEDMESTSYKGNYSSFVEQKEENLRIQLEQYREQ 280
Cdd:PRK11264 208 RDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLEKFLLQ 250
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-531 |
9.17e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.46 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyypgypqttsYGYDEGLIHVL------ 77
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGI--------------YTRDAGSILYLgkevtf 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 78 --PRGATSA-------YLEQVPDyphgLKVMDNLNL------AFEEIDAieKQMREqeeqmkkvEGSTLEKALN-KYSSl 141
Cdd:PRK10762 71 ngPKSSQEAgigiihqELNLIPQ----LTIAENIFLgrefvnRFGRIDW--KKMYA--------EADKLLARLNlRFSS- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 142 vhlyevkggyerDEKLSKvctglkfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLK 221
Cdd:PRK10762 136 ------------DKLVGE------------------LSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 222 NYK----GIVLIvshdryflDHVATKIVEIEDMESTSYKGNY---SSFVEQKEENLrIQL-------EQYreqqkkintm 287
Cdd:PRK10762 186 ELKsqgrGIVYI--------SHRLKEIFEICDDVTVFRDGQFiaeREVADLTEDSL-IEMmvgrkleDQY---------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 288 ekqvkdlrdwairadnnkffrraasiqkrlskmERLDKPvleRKNMRLTMSESERSGKETIKATdltksygerllfrdag 367
Cdd:PRK10762 247 ---------------------------------PRLDKA---PGEVRLKVDNLSGPGVNDVSFT---------------- 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 368 vmVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQK-----ISFNNEE-----LMLIEVFREDIS 437
Cdd:PRK10762 275 --LRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangIVYISEDrkrdgLVLGMSVKENMS 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 438 IVegkAREYLSKFMFY------QSSV--FKK------------VKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDID 497
Cdd:PRK10762 353 LT---ALRYFSRAGGSlkhadeQQAVsdFIRlfniktpsmeqaIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVG 429
|
570 580 590
....*....|....*....|....*....|....*..
gi 754786342 498 SIETLEEALEDFQG---TIFFISHDRYFINKMSNRII 531
Cdd:PRK10762 430 AKKEIYQLINQFKAeglSIILVSSEMPEVLGMSDRIL 466
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
370-530 |
9.60e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 9.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 370 VHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG--------------SNVKVAY-------------------LP 416
Cdd:PRK11288 27 CRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqemrfasttaalaAGVAIIYqelhlvpemtvaenlylgqLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 417 QKISFNNEELMLIEvfredisivegkAREYLSKfMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDI 496
Cdd:PRK11288 107 HKGGIVNRRLLNYE------------AREQLEH-LGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 754786342 497 DSIETLEEALEDF--QGT-IFFISHDRYFINKMSNRI 530
Cdd:PRK11288 174 REIEQLFRVIRELraEGRvILYVSHRMEEIFALCDAI 210
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
348-534 |
1.06e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 47.49 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSY-GERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKI-------------ELGSNVKVA 413
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepitkenirEVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 414 Y-----------LPQKISFNNEELMLievfreDISIVEGKAREYLSkfMFYQSSVFKKV-KYLSGGERIRLKLAILLYDE 481
Cdd:PRK13652 84 FqnpddqifsptVEQDIAFGPINLGL------DEETVAHRVSSALH--MLGLEELRDRVpHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 754786342 482 VNLLILDEPTNHLDIDSIETLEEALEDFQG----TIFFISHDRYFINKMSNRIIAVE 534
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMD 212
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
373-535 |
1.11e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.38 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNvkvaylpqKISFNNEELMLIE-----VFR------------ED 435
Cdd:PRK13639 28 GEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE--------PIKYDKKSLLEVRktvgiVFQnpddqlfaptveED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 436 ISI-----------VEGKAREYLSKFMF--YQSsvfKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLD---IDSI 499
Cdd:PRK13639 100 VAFgplnlglskeeVEKRVKEALKAVGMegFEN---KPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgASQI 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 754786342 500 ETLEEALEDFQGTIFFISHDRYFINKMSNRIIAVED 535
Cdd:PRK13639 177 MKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSD 212
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
12-248 |
1.12e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 47.67 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 12 YMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPGYPQTTSYGYDEGLIHVLP--RGATSAYLEQV 89
Cdd:PRK13644 11 YPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLR----PQKGKVLVSGIDTGDFSKLQgiRKLVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 90 PDYPHGLKVMDNLNLAFEEIDAIEKQMReqeeqmKKVEGSTLEKALNKYSslvhlyevkggyerdeklskvctglkfdes 169
Cdd:PRK13644 87 ETQFVGRTVEEDLAFGPENLCLPPIEIR------KRVDRALAEIGLEKYR------------------------------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 170 flQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS-IEWLENYLK-NYKGIVLI-VSHDRYFLdHVATKIVE 246
Cdd:PRK13644 131 --HRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKlHEKGKTIVyITHNLEEL-HDADRIIV 207
|
..
gi 754786342 247 IE 248
Cdd:PRK13644 208 MD 209
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
12-249 |
1.17e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 47.42 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 12 YMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyypgypqttsYGYDEGLIHVLPRGATSAYLEQvpd 91
Cdd:PRK13647 14 YKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI--------------YLPQRGRVKVMGREVNAENEKW--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 92 yphglkVMDNLNLAFEEIDaiekqmreqeeqmKKVEGSTLEKAlnkysslVHLYEVKGGYERDEKLSKVCTGLKF--DES 169
Cdd:PRK13647 77 ------VRSKVGLVFQDPD-------------DQVFSSTVWDD-------VAFGPVNMGLDKDEVERRVEEALKAvrMWD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 170 FLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD---MDSIEWLENYLKNYKGIVLIVSHDRYFLDHVATKIVE 246
Cdd:PRK13647 131 FRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIV 210
|
...
gi 754786342 247 IED 249
Cdd:PRK13647 211 LKE 213
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
348-404 |
1.17e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.45 E-value: 1.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKI 404
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-233 |
1.26e-05 |
|
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: 46.91 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 7 NGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVI-------------AGIEQMNYYPgypqttsygydegl 73
Cdd:cd03295 5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrlieptsgeifiDGEDIREQDP-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 74 ihVLPRGATSAYLEQVPDYPHgLKVMDNlnlafeeIDAIEKQMREQEEQMKkvegstlEKAlnkysslvhlyevkggyer 153
Cdd:cd03295 71 --VELRRKIGYVIQQIGLFPH-MTVEEN-------IALVPKLLKWPKEKIR-------ERA------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 154 DEKLSKVctGLKfDESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNY-----KGIVL 228
Cdd:cd03295 115 DELLALV--GLD-PAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLqqelgKTIVF 191
|
....*
gi 754786342 229 iVSHD 233
Cdd:cd03295 192 -VTHD 195
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-209 |
1.30e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 47.49 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyypGYPqttsygyDEGLIHV----LPR 79
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL-------THP-------DAGSISLcgepVPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 80 GATSAYLE--QVPDYphglkvmDNLNLAFeeidaiekQMREQEEQMKKVEGSTLEKALNKYSSLVHLYEVKGgyERDEKL 157
Cdd:PRK13537 74 RARHARQRvgVVPQF-------DNLDPDF--------TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLEN--KADAKV 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 754786342 158 SKvctglkfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:PRK13537 137 GE------------------LSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
370-518 |
1.55e-05 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 46.60 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 370 VHYGERVGLIGPNGSGKTTFLKMLLGeeHPD----KGKIEL-GSN--------------------------VKVAYLpQK 418
Cdd:COG0396 23 IKPGEVHAIMGPNGSGKSTLAKVLMG--HPKyevtSGSILLdGEDilelspderaragiflafqypveipgVSVSNF-LR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 419 ISFNNeelmlieVFREDISIVE--GKAREYLSKF-M---FYQSSVFKKvkyLSGGERIRLKLAILLYDEVNLLILDEPTN 492
Cdd:COG0396 100 TALNA-------RRGEELSAREflKLLKEKMKELgLdedFLDRYVNEG---FSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180
....*....|....*....|....*....
gi 754786342 493 HLDIDSIETLEEALEDFQG---TIFFISH 518
Cdd:COG0396 170 GLDIDALRIVAEGVNKLRSpdrGILIITH 198
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
16-209 |
1.68e-05 |
|
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: 45.77 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 16 TLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGieqmnyypgypqttsygydeglihvlprgatsayleqvpDYphg 95
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG---------------------------------------DL--- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 96 lkvmdnlnlafeeidaiekQMREQEEQMKKVEGSTLEKALNKYSSLV----HLyevkggyerdeklskvctglkFDESFL 171
Cdd:cd03247 53 -------------------KPQQGEITLDGVPVSDLEKALSSLISVLnqrpYL---------------------FDTTLR 92
|
170 180 190
....*....|....*....|....*....|....*...
gi 754786342 172 QRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:cd03247 93 NNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
178-233 |
1.76e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.01 E-value: 1.76e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 178 LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNY--KGIVLIVSHD 233
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHN 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-245 |
1.87e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 46.96 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 15 ATLVLEDVSLEAYDGDKIGIVGVNGSGKSTIlkviagIEQMNyypGYPQTTSYGYDEGLIHVLPRGATSAYLEQ----VP 90
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTL------IQHLN---GLLKPTSGKIIIDGVDITDKKVKLSDIRKkvglVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 91 DYP-HGLkvmdnlnlaFEEidAIEKQMR--------EQEEQMKKVEgstleKALNkyssLVhlyevkggyerdeklskvc 161
Cdd:PRK13637 90 QYPeYQL---------FEE--TIEKDIAfgpinlglSEEEIENRVK-----RAMN----IV------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 162 tGLKFDESFLQRDFDyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDM----DSIEWLENYLKNYKGIVLIVSHDRYFL 237
Cdd:PRK13637 131 -GLDYEDYKDKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSHSMEDV 208
|
....*...
gi 754786342 238 DHVATKIV 245
Cdd:PRK13637 209 AKLADRII 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
4-209 |
1.98e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.10 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYmdatlVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEqmnyypgypqttsygydeglihvlpRGATS 83
Cdd:COG2401 36 VELRVVERY-----VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL-------------------------KGTPV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 AYLEQVPDYPHGlkvmDNLNLafeeIDAIEKqmreqeeqmkkvEGSTLEKAlnkysslvhlyevkggyerdEKLSKVctG 163
Cdd:COG2401 86 AGCVDVPDNQFG----REASL----IDAIGR------------KGDFKDAV--------------------ELLNAV--G 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 754786342 164 LKfDESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:COG2401 124 LS-DAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
178-232 |
2.67e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.79 E-value: 2.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 754786342 178 LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDM----DSIEWLENYLKNYKGIVLIVSH 232
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSH 187
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-233 |
2.70e-05 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 45.55 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSYG---YDEGLIHVLP-- 78
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLS-------PAFSASGevlLNGRRLTALPae 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 79 -RGAtsAYLEQ-VPDYPHgLKVMDNLnlAFEEIDAIEKQMREQE-EQMkkvegstLEKAlnkysSLVHLYEvkggyerde 155
Cdd:COG4136 75 qRRI--GILFQdDLLFPH-LSVGENL--AFALPPTIGRAQRRARvEQA-------LEEA-----GLAGFAD--------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 156 klskvctglkfdesflqRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMD---SI-EWLENYLKNYKGIVLIVS 231
Cdd:COG4136 129 -----------------RDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAlraQFrEFVFEQIRQRGIPALLVT 191
|
..
gi 754786342 232 HD 233
Cdd:COG4136 192 HD 193
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
359-518 |
2.94e-05 |
|
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: 47.05 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 359 ERLLFRdagvmVHYGERVGLIGPNGSGKTTfLKMLLGEEHPDK-GKIELGSNVKVAYLPQKISFNNEEL--MLI------ 429
Cdd:TIGR00954 469 ESLSFE-----VPSGNNLLICGPNGCGKSS-LFRILGELWPVYgGRLTKPAKGKLFYVPQRPYMTLGTLrdQIIypdsse 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 430 EVFREDIS------IVEGKAREYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLE 503
Cdd:TIGR00954 543 DMKRRGLSdkdleqILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMY 622
|
170
....*....|....*
gi 754786342 504 EALEDFQGTIFFISH 518
Cdd:TIGR00954 623 RLCREFGITLFSVSH 637
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
370-531 |
3.29e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.89 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 370 VHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSnvkvaylpQKISFNNeelmlIEVFREDISIV---------- 439
Cdd:PRK10522 346 IKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG--------KPVTAEQ-----PEDYRKLFSAVftdfhlfdql 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 440 ---EGKAREYLSKFMFYQSSVFK-KVKY---------LSGGERIRLKLAILLYDEVNLLILDE------PtnHLDIDSIE 500
Cdd:PRK10522 413 lgpEGKPANPALVEKWLERLKMAhKLELedgrisnlkLSKGQKKRLALLLALAEERDILLLDEwaadqdP--HFRREFYQ 490
|
170 180 190
....*....|....*....|....*....|..
gi 754786342 501 TLEEALEDFQGTIFFISH-DRYFInkMSNRII 531
Cdd:PRK10522 491 VLLPLLQEMGKTIFAISHdDHYFI--HADRLL 520
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-249 |
4.20e-05 |
|
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: 45.15 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 14 DATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAG-IEQMnyypgypqttsygydEGLIHVlprGATSAYLEQVPDY 92
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEKL---------------SGSVSV---PGSIAYVSQEPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 93 PHGlKVMDNLnLAFEEIDAiekqmreqeeqmkkvegstlekalnkysslvhlyevkggyERDEKLSKVCTglkfdesfLQ 172
Cdd:cd03250 78 QNG-TIRENI-LFGKPFDE----------------------------------------ERYEKVIKACA--------LE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 173 RDFDY---------------LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWL-EN----YLKNYKGIVLiVSH 232
Cdd:cd03250 108 PDLEIlpdgdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENcilgLLLNNKTRIL-VTH 186
|
250
....*....|....*..
gi 754786342 233 DRYFLDHvATKIVEIED 249
Cdd:cd03250 187 QLQLLPH-ADQIVVLDN 202
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-232 |
5.99e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 45.15 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMNyyPGYPQTTSYGYDEGLIHVlPRGATS 83
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLN--PEVTITGSIVYNGHNIYS-PRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 ------AYLEQVPDyPHGLKVMDNLNLAfeeidaiekqMREQEEQMKKVEGSTLEKALnKYSSLVHlyEVKggyerdEKL 157
Cdd:PRK14239 83 dlrkeiGMVFQQPN-PFPMSIYENVVYG----------LRLKGIKDKQVLDEAVEKSL-KGASIWD--EVK------DRL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754786342 158 SKVCTGLkfdesflqrdfdylSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKG--IVLIVSH 232
Cdd:PRK14239 143 HDSALGL--------------SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTR 205
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-205 |
6.65e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 15 ATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMnyypgypQTtsygydeGLIHVLprG---ATSAYLEQV-P 90
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKI-------QQ-------GRVEVL--GgdmADARHRRAVcP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 91 D--Y-PHGL-KvmdnlNL-----AFEEID---------AIEKQMREQEeqmkkvegstLEKAlnkysslvhlyevkggye 152
Cdd:NF033858 77 RiaYmPQGLgK-----NLyptlsVFENLDffgrlfgqdAAERRRRIDE----------LLRA------------------ 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 153 rdeklskvcTGLkfdESFLQRDFDYLSGGEKTtvilgKL-----LIHNPNILLLDEPT 205
Cdd:NF033858 124 ---------TGL---APFADRPAGKLSGGMKQ-----KLglccaLIHDPDLLILDEPT 164
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
588-640 |
6.82e-05 |
|
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: 41.30 E-value: 6.82e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 588 ARLLEKIESLEKELEALDEAMEVANI--DYNELNNLHNRKVELSEELEVATDLWL 640
Cdd:pfam16326 11 EELEAEIEKLEEEIAELEAQLADPELysDYEKLQELSAELEELEAELEELYERWE 65
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
178-232 |
7.84e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 7.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 754786342 178 LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKG----IVLIVSH 232
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnenrITIIIAH 638
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
370-409 |
8.25e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 44.72 E-value: 8.25e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 754786342 370 VHYGE-RVgLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSN 409
Cdd:COG4674 33 VDPGElRV-IIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT 72
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-234 |
8.41e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 45.10 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 2 LELKlNGIKKYMDATlVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQttsygydEGLIHVLPRGA 81
Cdd:PRK11432 7 VVLK-NITKRFGSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEK-------PT-------EGQIFIDGEDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 82 TSAYLEQvPD----------YPHgLKVMDNLNLAfeeidaIEKQMREQEEQMKKVEgstleKALnkysSLVHLyevkGGY 151
Cdd:PRK11432 71 THRSIQQ-RDicmvfqsyalFPH-MSLGENVGYG------LKMLGVPKEERKQRVK-----EAL----ELVDL----AGF 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 152 ErdeklskvctglkfdesflQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD------M-DSIEWLENYLknyk 224
Cdd:PRK11432 130 E-------------------DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDanlrrsMrEKIRELQQQF---- 186
|
250
....*....|.
gi 754786342 225 GIV-LIVSHDR 234
Cdd:PRK11432 187 NITsLYVTHDQ 197
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
373-535 |
9.52e-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: 44.24 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVK---------------VAYLPQK---------------ISFN 422
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNEsepsfeatrsrnrysVAYAAQKpwllnatveenitfgSPFN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 423 NEEL-MLIEV--FREDISIVEGKAreylskfmfyQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSI 499
Cdd:cd03290 107 KQRYkAVTDAcsLQPDIDLLPFGD----------QTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 754786342 500 ETLEEA-----LEDFQGTIFFISHD-RYFINkmSNRIIAVED 535
Cdd:cd03290 177 DHLMQEgilkfLQDDKRTLVLVTHKlQYLPH--ADWIIAMKD 216
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
352-407 |
1.12e-04 |
|
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: 44.71 E-value: 1.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 754786342 352 DLTKSYGERLLfrDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG 407
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLG 59
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
347-538 |
1.26e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 44.41 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPD---KGKIelgsNVKVAYLPQK----- 418
Cdd:PRK13640 7 EFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKI----TVDGITLTAKtvwdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 419 -----ISFNNEELMLIEVFRED----------------ISIVegkaREYLSK--FMFYQSSvfkKVKYLSGGERIRLKLA 475
Cdd:PRK13640 83 rekvgIVFQNPDNQFVGATVGDdvafglenravprpemIKIV----RDVLADvgMLDYIDS---EPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754786342 476 ILLYDEVNLLILDEPTNHLDIDS----IETLEEALEDFQGTIFFISHDryfINK--MSNRIIAVEDFSL 538
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGkeqiLKLIRKLKKKNNLTVISITHD---IDEanMADQVLVLDDGKL 221
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
358-495 |
1.28e-04 |
|
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: 43.39 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 358 GERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHpdKGKIElgSNVKVAYLPQKISFNNEelmLIEVFREDIS 437
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT--AGVIT--GEILINGRPLDKNFQRS---TGYVEQQDVH 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 438 IVEGKAREYLskfMFyqSSvfkKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLD 495
Cdd:cd03232 91 SPNLTVREAL---RF--SA---LLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-205 |
1.39e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.02 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnYYPgypqttsygyDEGLIHVL------ 77
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGL----YQP----------DSGEILIDgkpvri 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 78 --PRGATSA---YLEQ----VPDyphgLKVMDNLNLAFEEIDAIEKQMREQEEQmkkvegstLEKALNKYsslvhlyevk 148
Cdd:COG3845 72 rsPRDAIALgigMVHQhfmlVPN----LTVAENIVLGLEPTKGGRLDRKAARAR--------IRELSERY---------- 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 149 ggyerdeklskvctGLKFDesfLQRDFDYLSGGEKTTV-ILgKLLIHNPNILLLDEPT 205
Cdd:COG3845 130 --------------GLDVD---PDAKVEDLSVGEQQRVeIL-KALYRGARILILDEPT 169
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-75 |
1.41e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.92 E-value: 1.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyYPgypqttsYGYDEGLIH 75
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-----YP-------HGTYEGEII 65
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
373-495 |
1.43e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.04 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 373 GERVGLIGPNGSGKTTFLKMLLGEEHPDkgkIELGSNVKVAYLPqkisFNNEELMLIEVF--REDISIVEGKAREYLskf 450
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKG---VKGSGSVLLNGMP----IDAKEMRAISAYvqQDDLFIPTLTVREHL--- 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 451 MF-----YQSSVFKK----------------------------VKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLD 495
Cdd:TIGR00955 121 MFqahlrMPRRVTKKekrervdevlqalglrkcantrigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-240 |
1.45e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.61 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 19 LEDVSLEaYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyypgYPQTTSYGYDEGLIHV-----LPRGATSAYLEQVpdyp 93
Cdd:COG3593 14 IKDLSIE-LSDDLTVLVGENNSGKSSILEALRLL--------LGPSSSRKFDEEDFYLgddpdLPEIEIELTFGSL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 94 hgLKVMDNLNLAFEEIDAIEKQMREQEEQMKKvEGSTLEKALNKYSSLVHLY---EVKGGYERDEKLSKVCTgLKFDESF 170
Cdd:COG3593 81 --LSRLLRLLLKEEDKEELEEALEELNEELKE-ALKALNELLSEYLKELLDGldlELELSLDELEDLLKSLS-LRIEDGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 171 lQRDFDYLSGGEKTTVILG-------KLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGI---VLIVSHDRYFLDHV 240
Cdd:COG3593 157 -ELPLDRLGSGFQRLILLAllsalaeLKRAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKpnqVIITTHSPHLLSEV 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-246 |
1.46e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 43.91 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPGYPQTTSYGYDeglIHVLPRGATSAYLEQVpdyphglk 97
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLES----PSQGNVSWRGEP---LAKLNRAQRKAFRRDI-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 98 vmdnlNLAFEE-IDAIEKQMREQE---EQMKKVegSTLEKAlnkysslvhlyevkggyERDEKLSKVCTGLKFDESFLQR 173
Cdd:PRK10419 92 -----QMVFQDsISAVNPRKTVREiirEPLRHL--LSLDKA-----------------ERLARASEMLRAVDLDDSVLDK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 174 DFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDM----DSIEWLENyLKNYKGIV-LIVSHD----RYFLDHVAT-- 242
Cdd:PRK10419 148 RPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKK-LQQQFGTAcLFITHDlrlvERFCQRVMVmd 226
|
....*.
gi 754786342 243 --KIVE 246
Cdd:PRK10419 227 ngQIVE 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-519 |
1.53e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 43.88 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 339 ESERSGKETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKML--LGEEHPDKGKIElgsnVKVAYLP 416
Cdd:PRK14246 2 EAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrLIEIYDSKIKVD----GKVLYFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 417 QKIsFNNEELMLIE----VFRE-----DISIVEG----------KAREYLSKFM---FYQSSVFKKV--------KYLSG 466
Cdd:PRK14246 78 KDI-FQIDAIKLRKevgmVFQQpnpfpHLSIYDNiayplkshgiKEKREIKKIVeecLRKVGLWKEVydrlnspaSQLSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 467 GERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQG--TIFFISHD 519
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
17-46 |
1.69e-04 |
|
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: 43.25 E-value: 1.69e-04
10 20 30
....*....|....*....|....*....|
gi 754786342 17 LVLEDVSLEAYDGDKIGIVGVNGSGKSTIL 46
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLL 47
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
371-519 |
2.12e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 43.94 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 371 HYGERVGLIGPNGSGK--TTFLKM-LLGeehpDKGKIElGSNV----KVAYLPQK------------------ISFN--- 422
Cdd:PRK09473 40 RAGETLGIVGESGSGKsqTAFALMgLLA----ANGRIG-GSATfngrEILNLPEKelnklraeqismifqdpmTSLNpym 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 423 --NEELMLI----------EVFREDISIVEG-KAREYLSKFMFYQSSvfkkvkyLSGGERIRLKLAILLYDEVNLLILDE 489
Cdd:PRK09473 115 rvGEQLMEVlmlhkgmskaEAFEESVRMLDAvKMPEARKRMKMYPHE-------FSGGMRQRVMIAMALLCRPKLLIADE 187
|
170 180 190
....*....|....*....|....*....|....
gi 754786342 490 PTNHLDID---SIETL-EEALEDFQGTIFFISHD 519
Cdd:PRK09473 188 PTTALDVTvqaQIMTLlNELKREFNTAIIMITHD 221
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
178-238 |
2.43e-04 |
|
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: 42.31 E-value: 2.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754786342 178 LSGGEKTTVILGKLLIHNP--NILLLDEPTNHLDMDSIEWLENYLK---NYKGIVLIVSHDRYFLD 238
Cdd:cd03238 88 LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKgliDLGNTVILIEHNLDVLS 153
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
347-538 |
3.35e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 42.84 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 347 TIKATDLTKSYG-----ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIELG-----SNVKVAYLP 416
Cdd:PRK13646 2 TIRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDdititHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 417 Q-----KISFNNEELMLIE--VFRE----------DISIVEGKAREYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLY 479
Cdd:PRK13646 82 PvrkriGMVFQFPESQLFEdtVEREiifgpknfkmNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754786342 480 DEVNLLILDEPTNHLDIDSIETLEEALEDFQ----GTIFFISHDRYFINKMSNRIIAVEDFSL 538
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
376-585 |
3.63e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 43.15 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 376 VGLIGPNGSGKTTFLKMLLGEEHPDKGKIELGSNVKVAYLPQKISFNNEELMLIEVFREDISIVEGKAREYLSKFMFYQS 455
Cdd:pfam13304 2 NVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLERE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 456 SVFKKVKYLSGGERIRlklaILLYDEVNLLILDEPTNHLDIDSIETLEEALEDF---QGTIFFISHDRYFINKMSnRIIA 532
Cdd:pfam13304 82 DVEEKLSSKPTLLEKR----LLLREDSEEREPKFPPEAEELRLGLDVEERIELSlseLSDLISGLLLLSIISPLS-FLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 754786342 533 VEDFSLNSYLGNYDYYRHEKEKFRQEQESNALVTEAKKQIKPVKAASEKKQSI 585
Cdd:pfam13304 157 LDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKS 209
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-241 |
3.81e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 42.80 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 19 LEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMnyypgypqttsygyDEGLIHVLPRGATSaylEQVPDYPHglkv 98
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEA--------------ESGQIIIDGDLLTE---ENVWDIRH---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 99 mdNLNLAFEEIDaiekqmreqeeqmKKVEGSTLEKAL-----NKysslvhlyevkgGYERDEKLSKVCTGLKF--DESFL 171
Cdd:PRK13650 82 --KIGMVFQNPD-------------NQFVGATVEDDVafgleNK------------GIPHEEMKERVNEALELvgMQDFK 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754786342 172 QRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD----MDSIEWLENYLKNYKGIVLIVSHDryfLDHVA 241
Cdd:PRK13650 135 EREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
352-507 |
4.26e-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: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 352 DLTKSYGE--RLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLL------GEEHPDK---GKIELGSNVKV-AYLPQKI 419
Cdd:TIGR01271 1222 GLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLrllsteGEIQIDGvswNSVTLQTWRKAfGVIPQKV 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 420 sfnneeLMLIEVFREDISIVEGKAREYLSKF-----------MFYQSSVFKKVK---YLSGGERIRLKLAILLYDEVNLL 485
Cdd:TIGR01271 1302 ------FIFSGTFRKNLDPYEQWSDEEIWKVaeevglksvieQFPDKLDFVLVDggyVLSNGHKQLMCLARSILSKAKIL 1375
|
170 180
....*....|....*....|..
gi 754786342 486 ILDEPTNHLDIDSIETLEEALE 507
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLK 1397
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
359-496 |
4.33e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 359 ERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDK--GKIELG------SNVKVAyLPQKISFNNEE----- 425
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNisGTVFKDgkevdvSTVSDA-IDAGLAYVTEDrkgyg 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 426 LMLIEVFREDISIV---------------EGK-AREYLSKFMFYQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDE 489
Cdd:NF040905 351 LNLIDDIKRNITLAnlgkvsrrgvideneEIKvAEEYRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDE 430
|
....*..
gi 754786342 490 PTNHLDI 496
Cdd:NF040905 431 PTRGIDV 437
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-233 |
4.50e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.92 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 2 LELKLNGIKKYMDATLVLEDVSLeaydgdkIGIVGVNGSGKSTILKVIAgieqmnyYPGYPQTTSYGydEGLIHVLPRGA 81
Cdd:COG0419 3 LRLRLENFRSYRDTETIDFDDGL-------NLIVGPNGAGKSTILEAIR-------YALYGKARSRS--KLRSDLINVGS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 82 TSAYLEqvpdyphglkvmdnlnLAFEEIDAIEKQMREQEEQMKKVEGSTLEKA--------LNKYSSLV-HLYEVKGGYE 152
Cdd:COG0419 67 EEASVE----------------LEFEHGGKRYRIERRQGEFAEFLEAKPSERKealkrllgLEIYEELKeRLKELEEALE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 153 rdEKLSKVCTGLKFDESFLQRDFDY-----LSGGEKTTVILGKLLihnpnILLLDepTNHLDMDSIEWLENYLKNykgiV 227
Cdd:COG0419 131 --SALEELAELQKLKQEILAQLSGLdpietLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEE----L 197
|
....*.
gi 754786342 228 LIVSHD 233
Cdd:COG0419 198 AIITHV 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
178-209 |
4.61e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.99 E-value: 4.61e-04
10 20 30
....*....|....*....|....*....|..
gi 754786342 178 LSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
151-209 |
4.83e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 42.53 E-value: 4.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 754786342 151 YERDEKLSKVCTGLKFDESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:PRK13631 150 SEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
337-410 |
5.41e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 42.33 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 337 MSESERSGKETIKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKML--LGEEHPD---KGKIEL-GSNV 410
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGarvEGEILLdGEDI 80
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
178-231 |
6.05e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 6.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 178 LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS---IEWLENYL-KNYKGIVLIVS 231
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAkfeIYQLIAELaKKDKGIIIISS 449
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
176-209 |
6.11e-04 |
|
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: 41.26 E-value: 6.11e-04
10 20 30
....*....|....*....|....*....|....
gi 754786342 176 DYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:cd03215 103 SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
363-519 |
6.85e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 42.14 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 363 FRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKI---------------ELGSNVKV-----------AYLP 416
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkglmKLRESVGMvfqdpdnqlfsASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 417 QKISFN--NEELMLIEVFREDISIVEGKAREYLSKfmfyqssvfKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHL 494
Cdd:PRK13636 102 QDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKD---------KPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180
....*....|....*....|....*....
gi 754786342 495 DIDSI----ETLEEALEDFQGTIFFISHD 519
Cdd:PRK13636 173 DPMGVseimKLLVEMQKELGLTIIIATHD 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-230 |
7.73e-04 |
|
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: 42.50 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 19 LEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyYPGYPQTTSYGYDEGLIHVLPRGATSAYLEQVPD--YPHG- 95
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGA-----YPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEdrKRHGi 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 96 ---LKVMDNLNLAfeeidaiekqmreqeeqmkkvegstlekALNKYSSLVHLYEVKGGYERDEKLSKVctGLKFDESFLQ 172
Cdd:TIGR02633 351 vpiLGVGKNITLS----------------------------VLKSFCFKMRIDAAAELQIIGSAIQRL--KVKTASPFLP 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754786342 173 rdFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS---IEWLENYLKNyKGIVLIV 230
Cdd:TIGR02633 401 --IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQ-EGVAIIV 458
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-54 |
7.75e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 41.99 E-value: 7.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 754786342 1 MLELKlnGIKKY----MDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQ 54
Cdd:COG1135 1 MIELE--NLSKTfptkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLER 56
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-212 |
7.80e-04 |
|
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: 41.37 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIagieQMNYYPgypqttsygyDEGLIHVlprgatsayleqvpdyphglk 97
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL----ERFYDP----------TSGEILL--------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 98 vmDNLNLAFEEIDAIEKQMR--EQEEQMkkVEGSTLEK-ALNKYSSLVhlyevkggyERDEKLSKVCTGLKFDESFLQRd 174
Cdd:cd03249 63 --DGVDIRDLNLRWLRSQIGlvSQEPVL--FDGTIAENiRYGKPDATD---------EEVEEAAKKANIHDFIMSLPDG- 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 754786342 175 FD--------YLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS 212
Cdd:cd03249 129 YDtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-241 |
8.27e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 41.74 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 19 LEDVSLEAYDGDKIGIVGVNGSGKSTI-------LKVIAGIEQMNYYPGYPQTTSYGYDE-----GLIHVLPRGA--TSA 84
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLmqhfnalLKPSSGTITIAGYHITPETGNKNLKKlrkkvSLVFQFPEAQlfENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 85 YLEQVPDYPhglkvmdnLNLAFEEIDAIEKQMreqeEQMKKVegstlekalnkysslvhlyevkggyerdeklskvctGL 164
Cdd:PRK13641 103 VLKDVEFGP--------KNFGFSEDEAKEKAL----KWLKKV------------------------------------GL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 165 kfDESFLQRDFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKG---IVLIVSHDryfLDHVA 241
Cdd:PRK13641 135 --SEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHN---MDDVA 209
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-249 |
1.16e-03 |
|
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: 41.06 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 14 DATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIagieqmnyypgypqTTSYGYDEGLIHVLP---RGATSAYL-EQV 89
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI--------------PRFYDVDSGRILIDGhdvRDYTLASLrRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 90 pdyphGLKVMDNL--------NLAFEEIDAIEKQMREQEEQ-------MKKVEGstlekalnkysslvhlYEVKGGyERd 154
Cdd:cd03251 79 -----GLVSQDVFlfndtvaeNIAYGRPGATREEVEEAARAanahefiMELPEG----------------YDTVIG-ER- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 155 eklskvctGLKfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDS----IEWLENYLKNYKGIVliV 230
Cdd:cd03251 136 --------GVK------------LSGGQRQRIAIARALLKDPPILILDEATSALDTESerlvQAALERLMKNRTTFV--I 193
|
250
....*....|....*....
gi 754786342 231 SHDRYFLDHvATKIVEIED 249
Cdd:cd03251 194 AHRLSTIEN-ADRIVVLED 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-232 |
1.20e-03 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 42.02 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTilkVIAGIEqmNYY-PGYPQTTSYG-----YDEGLIHvlprgATSAYLEQVPD 91
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQ--NLYqPTGGQVLLDGvplvqYDHHYLH-----RQVALVGQEPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 92 YPHGlKVMDNLNLAFEeidaiekqmREQEEQMKKVegSTLEKALNKYSSLVHLYEVkggyERDEKLSKvctglkfdesfl 171
Cdd:TIGR00958 566 LFSG-SVRENIAYGLT---------DTPDEEIMAA--AKAANAHDFIMEFPNGYDT----EVGEKGSQ------------ 617
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754786342 172 qrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGIVLIVSH 232
Cdd:TIGR00958 618 ------LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
453-531 |
1.24e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 453 YQSSVFKKVKYLSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQG----TIFFISHdRYFINKMSN 528
Cdd:PTZ00265 1348 YDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAH-RIASIKRSD 1426
|
...
gi 754786342 529 RII 531
Cdd:PTZ00265 1427 KIV 1429
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
361-518 |
1.41e-03 |
|
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: 41.85 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 361 LLFRDAGVMVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV----------KVAYLPQK-ISFNNEELML 428
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdGLNIakiglhdlrfKITIIPQDpVLFSGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 429 IEVF----REDISIvegkAREyLSKFMFYQSSVFKKVKY--------LSGGERIRLKLAILLYDEVNLLILDEPTNHLDI 496
Cdd:TIGR00957 1380 LDPFsqysDEEVWW----ALE-LAHLKTFVSALPDKLDHecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180
....*....|....*....|....*.
gi 754786342 497 DSIE----TLEEALEDFqgTIFFISH 518
Cdd:TIGR00957 1455 ETDNliqsTIRTQFEDC--TVLTIAH 1478
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
178-209 |
1.47e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 41.57 E-value: 1.47e-03
10 20 30
....*....|....*....|....*....|..
gi 754786342 178 LSGGEKTTVILGKLLIHNPNILLLDEPTNHLD 209
Cdd:TIGR00955 167 LSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
178-249 |
1.83e-03 |
|
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: 40.39 E-value: 1.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754786342 178 LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDM---DSI--EWLENYLKNYKGIVLIVSHDRYFLDHvATKIVEIED 249
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIhlsDHLmqEGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKD 216
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-49 |
1.92e-03 |
|
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: 40.09 E-value: 1.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 754786342 3 ELKLNGIK-KYM-DATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVI 49
Cdd:cd03369 6 EIEVENLSvRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILAL 54
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-233 |
1.95e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 40.56 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 18 VLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgyPQTTSygydeglihVLPRGA--TSAYLEQVPDYphg 95
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILK-------PTSGS---------VLIRGEpiTKENIREVRKF--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 96 lkvmdnLNLAFEEID-AIEKQMREQEEQMKKVE-GSTLEKALNKYSSLVHLyevkggyerdeklskvcTGLkfdESFLQR 173
Cdd:PRK13652 80 ------VGLVFQNPDdQIFSPTVEQDIAFGPINlGLDEETVAHRVSSALHM-----------------LGL---EELRDR 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754786342 174 DFDYLSGGEKTTVILGKLLIHNPNILLLDEPTNHLD----MDSIEWLENYLKNYKGIVLIVSHD 233
Cdd:PRK13652 134 VPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQ 197
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
348-491 |
2.71e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGE-----RLLFRdagvmVHYGERVGLIGPNGSGKTTFLKMLLGEEHPDKGKIEL-GSNV---------KV 412
Cdd:NF033858 267 IEARGLTMRFGDftavdHVSFR-----IRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfGQPVdagdiatrrRV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 413 AYLPQKISFNNE-------EL--MLIEVFREDIsivEGKAREYLSKFMF--YQSSvfkkvkyLSG----GERIRLKLAIL 477
Cdd:NF033858 342 GYMSQAFSLYGEltvrqnlELhaRLFHLPAAEI---AARVAEMLERFDLadVADA-------LPDslplGIRQRLSLAVA 411
|
170
....*....|....
gi 754786342 478 LYDEVNLLILDEPT 491
Cdd:NF033858 412 VIHKPELLILDEPT 425
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
178-224 |
2.94e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.78 E-value: 2.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 754786342 178 LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYK 224
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1405
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
11-234 |
2.96e-03 |
|
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: 39.84 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 11 KYMDA-TLVLEDVSLEAYDGDKIGIVGVNGSGKSTILkviagieqmnyypgypqttsygydeglihvlprgatSAYLEQV 89
Cdd:cd03289 11 KYTEGgNAVLENISFSISPGQRVGLLGRTGSGKSTLL------------------------------------SAFLRLL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 90 pdYPHGLKVMDNLNLAFEEIDAIEKQMREQEEQMKKVEGsTLEKALNKYsslvhlyevkgGYERDEKLSKVC--TGLK-- 165
Cdd:cd03289 55 --NTEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSG-TFRKNLDPY-----------GKWSDEEIWKVAeeVGLKsv 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754786342 166 FDESFLQRDFDY------LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKN-YKGIVLIVSHDR 234
Cdd:cd03289 121 IEQFPGQLDFVLvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQaFADCTVILSEHR 196
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
11-47 |
3.42e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 39.69 E-value: 3.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 754786342 11 KYMDA-----TLVLEDVSLEAYDGDKIGIVGVNGSGKSTILK 47
Cdd:PRK13633 13 KYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAK 54
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-56 |
3.53e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.26 E-value: 3.53e-03
10 20 30
....*....|....*....|....*....|....*...
gi 754786342 19 LEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQMN 56
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPN 77
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
178-248 |
3.76e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 38.71 E-value: 3.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754786342 178 LSGGEKTTVILGKLLIHNPNILLLDEPTNHLD----MDSIEWLENYLKNYKGIVLIVSHDRYFLDHVATKIVEIE 248
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
464-530 |
3.90e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.79 E-value: 3.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754786342 464 LSGGERIRLKLAILLYDEVNLLILDEPTNHLDIDS----IETLEEALEDFQGTIFFISHDRYFINKMSNRI 530
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqiFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
177-232 |
3.93e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 39.02 E-value: 3.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 754786342 177 YLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNY---KGIVLIVSH 232
Cdd:PRK13538 129 QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHaeqGGMVILTTH 187
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
442-507 |
4.34e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 442 KAREYLSKFMF---------------YQSSVFKKVKYLSGGER------IRLKLAILLYDEVNLLILDEPTNHLDIDSIE 500
Cdd:PRK01156 765 LTRKYLFEFNLdfddidvdqdfnitvSRGGMVEGIDSLSGGEKtavafaLRVAVAQFLNNDKSLLIMDEPTAFLDEDRRT 844
|
....*..
gi 754786342 501 TLEEALE 507
Cdd:PRK01156 845 NLKDIIE 851
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
348-518 |
4.76e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 39.44 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRDAGVMVHYGERVGLIGPNGSGKTTFLKML-----LGEEHPDKGKIEL-GSNVKvaylpqkisf 421
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLfGRNIY---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 422 nNEELMLIEVFRE------------DISIVEG-----------KAREYLS---KFMFYQSSVFKKVK--------YLSGG 467
Cdd:PRK14267 75 -SPDVDPIEVRREvgmvfqypnpfpHLTIYDNvaigvklnglvKSKKELDervEWALKKAALWDEVKdrlndypsNLSGG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 754786342 468 ERIRLKLAILLYDEVNLLILDEPTNHLDIDSIETLEEALEDFQG--TIFFISH 518
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-75 |
5.51e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 5.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIeqmnyYPgypqttsYGYDEGLIH 75
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-----YP-------HGSYEGEIL 61
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-268 |
5.87e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.00 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 4 LKLNGIKKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyypgypqttsYGYDEGliHVLPRGATs 83
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRED------------YEVTGG--TVEFKGKD- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 84 aYLEQVPDYPHGLKVMdnlnLAFE---EIDAIEKQMREQeeqmkkvegsTLEKALNKYSSLVHLYEVKGGYERDEKLSKv 160
Cdd:PRK09580 67 -LLELSPEDRAGEGIF----MAFQypvEIPGVSNQFFLQ----------TALNAVRSYRGQEPLDRFDFQDLMEEKIAL- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 161 ctgLKFDESFLQRDFDY-LSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLE---NYLKNYKGIVLIVSHDRYF 236
Cdd:PRK09580 131 ---LKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAdgvNSLRDGKRSFIIVTHYQRI 207
|
250 260 270
....*....|....*....|....*....|..
gi 754786342 237 LDHVATKIVEIEDMESTSYKGNYsSFVEQKEE 268
Cdd:PRK09580 208 LDYIKPDYVHVLYQGRIVKSGDF-TLVKQLEE 238
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
531-602 |
5.91e-03 |
|
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: 36.40 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 531 IAVEDFSLNSYLGNYDYYRHEKEKFRQEQESnalvtEAKKQIKPVK---------AASEKKQSINQARL--LEKIESLEK 599
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEK-----AYEKQQKEIKkleefidrfRAKASKAKQAQSRIkaLEKMERIEK 75
|
...
gi 754786342 600 ELE 602
Cdd:pfam12848 76 PER 78
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-46 |
7.08e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.76 E-value: 7.08e-03
10 20 30
....*....|....*....|....*....|
gi 754786342 17 LVLEDVSLEAYDGDKIGIVGVNGSGKSTIL 46
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLL 1353
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
147-232 |
7.25e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 38.67 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 147 VKGGYERDEKLSKVCTGLKFDESFLQRDFDY---LSGGEKTTVILGKLLIHNPNILLLDEPTNHLD---MDSIEWLENYL 220
Cdd:PRK14267 116 VKSKKELDERVEWALKKAALWDEVKDRLNDYpsnLSGGQRQRLVIARALAMKPKILLMDEPTANIDpvgTAKIEELLFEL 195
|
90
....*....|..
gi 754786342 221 KNYKGIVLiVSH 232
Cdd:PRK14267 196 KKEYTIVL-VTH 206
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-234 |
7.63e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 38.32 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 10 KKYMDATLVLEDVSLEAYDGDKIGIVGVNGSGKSTILKVIAGIEQmnyyPGYPQTTSYGYDeglIHVLPRGATSAYLEQV 89
Cdd:PRK10908 9 KAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIER----PSAGKIWFSGHD---ITRLKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 90 ----PDYpHGL---KVMDNLNLAFEEIDAIEKQMREQ-EEQMKKVegSTLEKALNkysslvhlYEVKggyerdeklskvc 161
Cdd:PRK10908 82 gmifQDH-HLLmdrTVYDNVAIPLIIAGASGDDIRRRvSAALDKV--GLLDKAKN--------FPIQ------------- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754786342 162 tglkfdesflqrdfdyLSGGEKTTVILGKLLIHNPNILLLDEPTNHLDMDSIEWLENYLKNYKGI---VLIVSHDR 234
Cdd:PRK10908 138 ----------------LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVgvtVLMATHDI 197
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
348-417 |
7.88e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.34 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754786342 348 IKATDLTKSYGERLLFRD------AGVMVhygervGLIGPNGSGKTTFLKMLLGEEHPDKGKIE-LGSNV---------- 410
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDvsldipAGCMV------GLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGDMadarhrravc 75
|
....*...
gi 754786342 411 -KVAYLPQ 417
Cdd:NF033858 76 pRIAYMPQ 83
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
464-519 |
8.01e-03 |
|
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: 39.28 E-value: 8.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754786342 464 LSGGERIRLKLAILLYDEVNLLILDEPTNHLDIdsieTLE----EALEDFQ---GT-IFFISHD 519
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaqilDLLKDLQrelGMaLLLITHD 216
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
464-530 |
9.09e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 38.73 E-value: 9.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754786342 464 LSGGERIRLKLAILLYDEVNLLILDEPTNHLDI---DSIETLEEALEDFQGT-IFFISHDRYFINKMSNRI 530
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESttqAQIFRLLARLNQLQGTsILLISHDLESISQWADTI 229
|
|
| |
