|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
84-600 |
3.87e-177 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 511.92 E-value: 3.87e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 84 LSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYP------IPEHIDI-YLLDEPAEPSELSALD 156
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPdsgevsIPKGLRIgYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 157 YVVtEAQHELKRIE---DLVEKTILEDGPESELLEPLYERMDSLDPDTFESRAAIILIGLGFNKKTILKKTKDMSGGWKM 233
Cdd:COG0488 81 TVL-DGDAELRALEaelEELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 234 RVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYGGNYDSYHK 313
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 314 TRSELETNQMKQYNKQQEEIQHIKKFIASAGTYANLVKQAKSRQKILDKMEADglvQPVVPDKVFSFRFPQVERLPPPVL 393
Cdd:COG0488 240 QRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLERE---EPPRRDKTVEIRFPPPERLGKKVL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 394 AFDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYSQHsQDQLDL 473
Cdd:COG0488 317 ELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQH-QEELDP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 474 TKSALEFVRDKYSNISQdfQFWRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDS 553
Cdd:COG0488 393 DKTVLDELRDGAPGGTE--QEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEA 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 285811661 554 LADAINEFNGGVVVVSHDFRLLDKIAQDIFVVENKTATRWDGSILQY 600
Cdd:COG0488 471 LEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDY 517
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-604 |
1.68e-138 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 420.04 E-value: 1.68e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 30 RKLGRKKEAAAEESEVDAAAREIKMMKLQQDKDGLSDRVVTgvlssletsRDIKLSSVSLLFHGKVLIQDSGLELNYGRR 109
Cdd:PLN03073 135 RKEERQREVQYQAHVAEMEAAKAGMPGVYVNHDGNGGGPAI---------KDIHMENFSISVGGRDLIVDASVTLAFGRH 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 110 YGLLGENGCGKSTFLKALATREYP-IPEHIDIYLLDEPAEPSELSALDYVVT-----------EAQ-HELKRIEDLVEKT 176
Cdd:PLN03073 206 YGLVGRNGTGKTTFLRYMAMHAIDgIPKNCQILHVEQEVVGDDTTALQCVLNtdiertqlleeEAQlVAQQRELEFETET 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 177 ILEDGPE---------SELLEPLYERMDSLDPDTFESRAAIILIGLGFNKKTILKKTKDMSGGWKMRVALAKALFVKPTL 247
Cdd:PLN03073 286 GKGKGANkdgvdkdavSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 248 LLLDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYGGNYDSYHKTRSELETNQMKQYN 327
Cdd:PLN03073 366 LLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 328 KQQEEIQHIKKFIASAGTYANLVKQAKSRQKILDKMeadGLVQPVVPDKVFSFRFPQVERLP-PPVLAFDDISFHYESNP 406
Cdd:PLN03073 446 SNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRL---GHVDAVVNDPDYKFEFPTPDDRPgPPIISFSDASFGYPGGP 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 407 SenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYSQHSQDQLDLTKSALEFVRDKYS 486
Cdd:PLN03073 523 L--LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFP 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 487 NISQdfQFWRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGGVV 566
Cdd:PLN03073 601 GVPE--QKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVL 678
|
570 580 590
....*....|....*....|....*....|....*...
gi 285811661 567 VVSHDFRLLDKIAQDIFVVENKTATRWDGSILQYKNKL 604
Cdd:PLN03073 679 MVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKTL 716
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
72-605 |
1.42e-102 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 324.43 E-value: 1.42e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 72 VLSSLETSRDIKlssvsllfhgkVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATR------EYPIPEHIDIYLLDE 145
Cdd:PRK10636 3 VFSSLQIRRGVR-----------VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEisadggSYTFPGNWQLAWVNQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 146 PAEPSELSALDYVVtEAQHELKRIE-DLVEKTILEDGpesELLEPLYERMDSLDPDTFESRAAIILIGLGFNKKTILKKT 224
Cdd:PRK10636 72 ETPALPQPALEYVI-DGDREYRQLEaQLHDANERNDG---HAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 225 KDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAY 304
Cdd:PRK10636 148 SDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 305 GGNYDSYHKTRSELETNQMKQYNKQQEEIQHIKKFIASAGTYANLVKQAKSRQKILDKMEadgLVQPVVPDKVFSFRFPQ 384
Cdd:PRK10636 228 TGNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERME---LIAPAHVDNPFHFSFRA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 385 VERLPPPVLAFDDISFHYESNpseNLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYS 464
Cdd:PRK10636 305 PESLPNPLLKMEKVSAGYGDR---IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 465 QHSQDQLDLTKSALE-FVRDKYSNISQDFqfwRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPT 543
Cdd:PRK10636 382 QHQLEFLRADESPLQhLARLAPQELEQKL---RDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 544 NGLDIPTIDSLADAINEFNGGVVVVSHDFRLLDKIAQDIFVVENKTATRWDGSILQYKNKLA 605
Cdd:PRK10636 459 NHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLS 520
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
107-571 |
2.84e-88 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 283.71 E-value: 2.84e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 107 GRRYGLLGENGCGKSTFLKALATREYPIPEHIDIylldEPAEP-----------SELSALDYVVT------EAQHELKRI 169
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL----DPNERlgklrqdqfafEEFTVLDTVIMghtelwEVKQERDRI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 170 EDLVEKTiLEDGPESELLEPLYERMDSLdpdTFESRAAIILIGLGFNKKTILKKTKDMSGGWKMRVALAKALFVKPTLLL 249
Cdd:PRK15064 103 YALPEMS-EEDGMKVADLEVKFAEMDGY---TAEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 250 LDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYGGNYDSYHKTRSELETNQMKQYNKQ 329
Cdd:PRK15064 179 LDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAATQARERLLADNAKK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 330 QEEIQHIKKFIASAGTYANLVKQAKSRQKILDKMEADGlVQP---VVPdkvfSFRFPQVERLPPPVLAFDDISFHYESNP 406
Cdd:PRK15064 259 KAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLEE-VKPssrQNP----FIRFEQDKKLHRNALEVENLTKGFDNGP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 407 senLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYSQHSQDQLDLTKSALEFVrDKYS 486
Cdd:PRK15064 334 ---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDLTLFDWM-SQWR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 487 NISQDFQFWRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGGVV 566
Cdd:PRK15064 410 QEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLI 489
|
....*
gi 285811661 567 VVSHD 571
Cdd:PRK15064 490 FVSHD 494
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
93-593 |
4.67e-71 |
|
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: 239.07 E-value: 4.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 93 GKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALA------TREYPIPEHIDI-YLLDEPAEPSELSALDYV---VTEA 162
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAgvdkdfNGEARPQPGIKVgYLPQEPQLDPTKTVRENVeegVAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 163 QHELKRIEDLVEKTILEDGPESELLEP---LYERMDSLDPDTFESRAAIILIGL----GFNKKTILkktkdmSGGWKMRV 235
Cdd:TIGR03719 97 KDALDRFNEISAKYAEPDADFDKLAAEqaeLQEIIDAADAWDLDSQLEIAMDALrcppWDADVTKL------SGGERRRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 236 ALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYGGNYDSYHKTR 315
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 316 SELETNQMKQYNKQQEEIQHIKKFIASAGTyanlVKQAKSRQKI--LDKMEADGLVQPVVPDKVFsfrFPQVERLPPPVL 393
Cdd:TIGR03719 251 QKRLEQEEKEESARQKTLKRELEWVRQSPK----GRQAKSKARLarYEELLSQEFQKRNETAEIY---IPPGPRLGDKVI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 394 AFDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYSQhSQDQLDL 473
Cdd:TIGR03719 324 EAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQ-SRDALDP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 474 TKSALEFVRDKYSNIS-QDFQF-WRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTI 551
Cdd:TIGR03719 400 NKTVWEEISGGLDIIKlGKREIpSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETL 479
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 285811661 552 DSLADAINEFNGGVVVVSHDFRLLDKIAQDIFVVENKTATRW 593
Cdd:TIGR03719 480 RALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEW 521
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
82-576 |
3.35e-64 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 222.52 E-value: 3.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALAtREYPIPEHIDIY--------LLDEPAEPSELS 153
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN-GEVLLDDGRIIYeqdlivarLQQDPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 154 ALDYV---VTEAQHELKR---IEDLVEktilEDGPESEL--LEPLYERMDSLDPDTFESRAAIILIGLGFNKKTILKktk 225
Cdd:PRK11147 83 VYDFVaegIEEQAEYLKRyhdISHLVE----TDPSEKNLneLAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALS--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 226 DMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYG 305
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 306 GNYDSYHKTRSE---LETNQMKQYNKQ--QEEI---QHIKkfiASAGTYANLVKQAKS-RQKILDKMEADGLVQPVVPDK 376
Cdd:PRK11147 236 GNYDQYLLEKEEalrVEELQNAEFDRKlaQEEVwirQGIK---ARRTRNEGRVRALKAlRRERSERREVMGTAKMQVEEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 377 VFSFRFpqverlpppVLAFDDISFHYesnPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHT 456
Cdd:PRK11147 313 SRSGKI---------VFEMENVNYQI---DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 457 HVKLGVYSQHSQDqLDLTKSALEFVRDKYSNIS------------QDFQF--WRgqlgrygltgeGQTVQMAtLSEGQRS 522
Cdd:PRK11147 381 KLEVAYFDQHRAE-LDPEKTVMDNLAEGKQEVMvngrprhvlgylQDFLFhpKR-----------AMTPVKA-LSGGERN 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 285811661 523 RVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGGVVVVSHDFRLLD 576
Cdd:PRK11147 448 RLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVD 501
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
93-582 |
1.59e-58 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 205.35 E-value: 1.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 93 GKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPI------PEHIDI-YLLDEPAEPSELSALDYV---VTEA 162
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFegearpAPGIKVgYLPQEPQLDPEKTVRENVeegVAEV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 163 QHELKRIEDLVEKTILEDGPESELLEP---LYERMDSLDPDTFESRAAIILIGL----GFNKKTILkktkdmSGGWKMRV 235
Cdd:PRK11819 99 KAALDRFNEIYAAYAEPDADFDALAAEqgeLQEIIDAADAWDLDSQLEIAMDALrcppWDAKVTKL------SGGERRRV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 236 ALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYGGNYDSYhktr 315
Cdd:PRK11819 173 ALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSW---- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 316 seLETNQ--MKQYNKQQEEIQH-IKK---FIASA--GtyanlvKQAKSRQKI--LDKMEADGLVQPVVPDKVFsfrFPQV 385
Cdd:PRK11819 249 --LEQKAkrLAQEEKQEAARQKaLKReleWVRQSpkA------RQAKSKARLarYEELLSEEYQKRNETNEIF---IPPG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 386 ERLPPPVLAFDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGvYSQ 465
Cdd:PRK11819 318 PRLGDKVIEAENLSKSFGDRL---LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLA-YVD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 466 HSQDQLDLTKSALEFVRDKYSNIS-QDFQF-WRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPT 543
Cdd:PRK11819 394 QSRDALDPNKTVWEEISGGLDIIKvGNREIpSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPT 473
|
490 500 510
....*....|....*....|....*....|....*....
gi 285811661 544 NGLDIPTIDSLADAINEFNGGVVVVSHDFRLLDKIAQDI 582
Cdd:PRK11819 474 NDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI 512
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
393-589 |
1.43e-49 |
|
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: 168.78 E-value: 1.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYSQhsqdqld 472
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 ltksalefvrdkysnisqdfqfwrgqlgrygltgegqtvqmatLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTID 552
Cdd:cd03221 71 -------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIE 107
|
170 180 190
....*....|....*....|....*....|....*..
gi 285811661 553 SLADAINEFNGGVVVVSHDFRLLDKIAQDIFVVENKT 589
Cdd:cd03221 108 ALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
82-300 |
2.73e-41 |
|
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: 146.44 E-value: 2.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIpehidiylldepaepselsaldyvvte 161
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPD--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 162 aqhelkriedlvektiledgpesellEPLYERMDSLDPDTFESraaiiliglgfnkktilkktkdMSGGWKMRVALAKAL 241
Cdd:cd03221 54 --------------------------EGIVTWGSTVKIGYFEQ----------------------LSGGEKMRLALAKLL 85
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 242 FVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQK 300
Cdd:cd03221 86 LENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
33-313 |
1.16e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 137.89 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 33 GRKKeaAAEESEVDAAAREIKMMKLQQDKDGLSDRVVtgvlssletsrdIKLSSVSLLFHGKVLIQDSGLELNYGRRYGL 112
Cdd:COG0488 281 SRIK--ALEKLEREEPPRRDKTVEIRFPPPERLGKKV------------LELEGLSKSYGDKTLLDDLSLRIDRGDRIGL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 113 LGENGCGKSTFLKALATREYP------IPEHIDI-YLldepaepselsaldyvvteAQHElkriEDL-VEKTILEDgpes 184
Cdd:COG0488 347 IGPNGAGKSTLLKLLAGELEPdsgtvkLGETVKIgYF-------------------DQHQ----EELdPDKTVLDE---- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 185 elleplyerMDSLDPDTFESRAAIILIGLGFNKKTILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVW 264
Cdd:COG0488 400 ---------LRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEA 470
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 285811661 265 LEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYGGNYDSYHK 313
Cdd:COG0488 471 LEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
389-571 |
1.83e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.51 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 389 PPPVLAFDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS------RHTHVKLGv 462
Cdd:COG1121 3 MMPAIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 463 Y-SQHSQDQLDLTKSALEFVRdkysnisqdfqfwrgqLGRYGLTGEGQ---------------TVQMA--------TLSE 518
Cdd:COG1121 79 YvPQRAEVDWDFPITVRDVVL----------------MGRYGRRGLFRrpsradreavdealeRVGLEdladrpigELSG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 285811661 519 GQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNG---GVVVVSHD 571
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHD 198
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
411-544 |
4.67e-31 |
|
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: 118.13 E-value: 4.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 411 YEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS-----------RHTHVKLGVYSQHsqDQLDLTKSALE 479
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderKSLRKEIGYVFQD--PQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 480 FVRD-------KYSNISQDFQFWRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTN 544
Cdd:pfam00005 79 NLRLglllkglSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
86-584 |
1.89e-30 |
|
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: 125.40 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 86 SVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALatreypipehidIYLLDEPAEPSELSALDYvvteaqhe 165
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAL------------MGLLPHGGRISGEVLLDG-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 166 lkriEDLVEKTILEDGPESELLepLYERMDSLDPDTFESRAAIILIGLGFNKKTILKKTKDM-----------------S 228
Cdd:COG1123 71 ----RDLLELSEALRGRRIGMV--FQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELleavglerrldryphqlS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 229 GGWKMRVALAKALFVKPTLLLLDDPTAHLD----LEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAY 304
Cdd:COG1123 145 GGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVED 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 305 GgnydsyhktrselETNQMKQYNKQQEEIQHIKKFIASAGTyanlvkQAKSRQKILdkmEADGLvqpvvpdkvfSFRFPQ 384
Cdd:COG1123 225 G-------------PPEEILAAPQALAAVPRLGAARGRAAP------AAAAAEPLL---EVRNL----------SKRYPV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 385 veRLPPPVLAFDDISFHyesnpsenLYEHlnfgvdmdSRIALVGPNGVGKSTLLKIMTGELTPQSGRV-------SRHTH 457
Cdd:COG1123 273 --RGKGGVRAVDDVSLT--------LRRG--------ETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdlTKLSR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 458 VKLGVYS-------QHSQDQLD--LT-KSALEFVRDKYSNISQDfqfWRGQ-----LGRYGLTGEgqtvqMA-----TLS 517
Cdd:COG1123 335 RSLRELRrrvqmvfQDPYSSLNprMTvGDIIAEPLRLHGLLSRA---ERRErvaelLERVGLPPD-----LAdryphELS 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 518 EGQRSRVVFA-LLALEqPNVLLLDEPTNGLDIPT----IDSLADAINEFNGGVVVVSHDFRLLDKIAQDIFV 584
Cdd:COG1123 407 GGQRQRVAIArALALE-PKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDLAVVRYIADRVAV 477
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
97-255 |
3.01e-30 |
|
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: 115.82 E-value: 3.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 97 IQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIdiyLLDEPAEPSElsaldyvvtEAQHELKRIEDLVEKT 176
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTI---LLDGQDLTDD---------ERKSLRKEIGYVFQDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 177 ILedGPESELLEPLYE--RMDSLDPDTFESRAAIILIGLG---FNKKTILKKTKDMSGGWKMRVALAKALFVKPTLLLLD 251
Cdd:pfam00005 69 QL--FPRLTVRENLRLglLLKGLSKREKDARAEEALEKLGlgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
....
gi 285811661 252 DPTA 255
Cdd:pfam00005 147 EPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
395-594 |
4.36e-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: 4.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 395 FDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS------RHTHVKLGVYSQHSQ 468
Cdd:cd03235 2 VEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 469 DQLDLTKSALEFV---RDKYSNisqdFQFWRGQ---------LGRYGLTGEGQTvQMATLSEGQRSRVVFALLALEQPNV 536
Cdd:cd03235 79 IDRDFPISVRDVVlmgLYGHKG----LFRRLSKadkakvdeaLERVGLSELADR-QIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 537 LLLDEPTNGLDIPTIDSLADAINEFNG---GVVVVSHDFRLLDKIAQDIFVVeNKTATRWD 594
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
393-587 |
6.81e-28 |
|
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: 110.17 E-value: 6.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRhthvklgvysqhsqDQLD 472
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVL-KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI--------------DGVD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 LTKSALEFVRDKYSNISQDFQFWRGQLgRYGLtgegqtvqmatLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTID 552
Cdd:cd03228 66 LRDLDLESLRKNIAYVPQDPFLFSGTI-RENI-----------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180 190
....*....|....*....|....*....|....*..
gi 285811661 553 SLADAINEFNGG--VVVVSHDFRLLDKiAQDIFVVEN 587
Cdd:cd03228 134 LILEALRALAKGktVIVIAHRLSTIRD-ADRIIVLDD 169
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
402-571 |
9.54e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 110.40 E-value: 9.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 402 YESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYSQHSQ--DQLDLTksale 479
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEvpDSLPLT----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 480 fVRDKYSnisqdFQFW--RGQLGRY---------------GLTG-EGQtvQMATLSEGQRSRVVFALLALEQPNVLLLDE 541
Cdd:NF040873 74 -VRDLVA-----MGRWarRGLWRRLtrddraavddalervGLADlAGR--QLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|...
gi 285811661 542 PTNGLDIPTIDSLADAINEFNG---GVVVVSHD 571
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
395-587 |
2.80e-27 |
|
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: 107.72 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 395 FDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHvklgvysqhsqdqlDLT 474
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK--------------DIA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 475 KSALEFVRDKYSNISQdfqfwrgqlgrygltgegqtvqmatLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSL 554
Cdd:cd00267 65 KLPLEELRRRIGYVPQ-------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|....*.
gi 285811661 555 ADAINEFNGG---VVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:cd00267 120 LELLRELAEEgrtVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
393-587 |
6.41e-27 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 107.48 E-value: 6.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPSenlYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRhthvkLGVysqhsqdqlD 472
Cdd:cd03230 1 IEVRNLSKRYGKKTA---LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-----LGK---------D 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 LTKSALEfVRDKYSNISQDFQFWrgqlgrYGLTGEgqtvQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTID 552
Cdd:cd03230 64 IKKEPEE-VKRRIGYLPEEPSLY------ENLTVR----ENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190
....*....|....*....|....*....|....*...
gi 285811661 553 SLADAINEFN---GGVVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:cd03230 133 EFWELLRELKkegKTILLSSHILEEAERLCDRVAILNN 170
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
393-587 |
3.17e-26 |
|
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: 107.03 E-value: 3.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYesNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVsrhtHVklgvysqhsqDQLD 472
Cdd:COG1122 1 IELENLSFSY--PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEV----LV----------DGKD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 LTKSALEFVRDK-------------YSNISQDFQFwrGqLGRYGLTGE---------GQTVQMA--------TLSEGQRS 522
Cdd:COG1122 65 ITKKNLRELRRKvglvfqnpddqlfAPTVEEDVAF--G-PENLGLPREeirerveeaLELVGLEhladrpphELSGGQKQ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 523 RVVFA-LLALEqPNVLLLDEPTNGLDIPTIDSLADAINEFNG---GVVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:COG1122 142 RVAIAgVLAME-PEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
391-571 |
1.15e-25 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 104.87 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 391 PVLAFDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYSQHSQD- 469
Cdd:COG4133 1 MMLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 470 ----QLDLTK---SALEFVRdkysnisqdfqFWRGQLG-------------RYGLTGEGQtVQMATLSEGQRSRVVFALL 529
Cdd:COG4133 78 aylgHADGLKpelTVRENLR-----------FWAALYGlradreaidealeAVGLAGLAD-LPVRQLSAGQKRRVALARL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 285811661 530 ALEQPNVLLLDEPTNGLDIPTIDSLADAINEF--NGG-VVVVSHD 571
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHlaRGGaVLLTTHQ 190
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
395-587 |
2.21e-25 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 104.09 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 395 FDDISFHYESNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS------RHTHV-----KLGVY 463
Cdd:cd03225 2 LKNLSFSYPDGARPAL-DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdgkdlTKLSLkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 464 SQHSQDQLdLTKSalefVRDkysnisqDFQFWRGQLG---------------RYGLTGEgQTVQMATLSEGQRSRVVFA- 527
Cdd:cd03225 81 FQNPDDQF-FGPT----VEE-------EVAFGLENLGlpeeeieerveealeLVGLEGL-RDRSPFTLSGGQKQRVAIAg 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 528 LLALeQPNVLLLDEPTNGLDIPTIDSLADAINEFNG---GVVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:cd03225 148 VLAM-DPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
392-571 |
7.94e-25 |
|
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: 103.97 E-value: 7.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 392 VLAFDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV---------------SRht 456
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaslsrrelAR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 457 hvKLGVYSQHSQDQLDLTksALEFVRdkysnisqdfqfwrgqLGRY----GLTGEG-----------QTVQMA------- 514
Cdd:COG1120 76 --RIAYVPQEPPAPFGLT--VRELVA----------------LGRYphlgLFGRPSaedreaveealERTGLEhladrpv 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 515 -TLSEGQRSRVVFA-LLAlEQPNVLLLDEPTNGLDIP----TIDSLADAINEFNGGVVVVSHD 571
Cdd:COG1120 136 dELSGGERQRVLIArALA-QEPPLLLLDEPTSHLDLAhqleVLELLRRLARERGRTVVMVLHD 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
82-305 |
2.50e-24 |
|
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: 102.24 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDI-----------------YLLD 144
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdgedvrkeprearrqigVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 145 EPAEPSELSALDYV-VTEAQHEL------KRIEDLVEKTILEdgpeselleplyermDSLDpdtfesraaiiliglgfnk 217
Cdd:COG4555 82 ERGLYDRLTVRENIrYFAELYGLfdeelkKRIEELIELLGLE---------------EFLD------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 218 ktilKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF---DRTLVLVSHSQDFLNGVCTNMI 294
Cdd:COG4555 128 ----RRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVV 203
|
250
....*....|.
gi 285811661 295 DMRAQKLTAYG 305
Cdd:COG4555 204 ILHKGKVVAQG 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
82-301 |
3.01e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 101.05 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATReypIPEHI-DIYLLDEPAepSELSALD---- 156
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADL---DPPTSgEIYLDGKPL--SAMPPPEwrrq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 157 --YVVTEAQhelkriedLVEKTILEDgpeseLLEPLYERMDSLDPDtfesRAAIILIGLGFNKKTILKKTKDMSGGWKMR 234
Cdd:COG4619 76 vaYVPQEPA--------LWGGTVRDN-----LPFPFQLRERKFDRE----RALELLERLGLPPDILDKPVERLSGGERQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 235 VALAKALFVKPTLLLLDDPTAHLDLE--ACV--WLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKL 301
Cdd:COG4619 139 LALIRALLLQPDVLLLDEPTSALDPEntRRVeeLLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
294-382 |
3.50e-24 |
|
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: 96.49 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 294 IDMRAQKLTAYGGNYDSYHKTRSELETNQMKQYNKQQEEIQHIKKFIASAGTYANLVKQAKSRQKILDKMEadgLVQPVV 373
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKME---RIEKPE 77
|
....*....
gi 285811661 374 PDKVfSFRF 382
Cdd:pfam12848 78 RDKP-KLRF 85
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
82-571 |
4.80e-24 |
|
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: 106.04 E-value: 4.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKAL-ATREYPIPEHIDIYLL---------DEPA---- 147
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrGMDQYEPTSGRIIYHValcekcgyvERPSkvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 148 ---------EPSELSALDYVVTEAQHELKRIEDLV--------EKTILEDGPESeLLEPLYERMDSLDpdtfesrAAIIL 210
Cdd:TIGR03269 81 pcpvcggtlEPEEVDFWNLSDKLRRRIRKRIAIMLqrtfalygDDTVLDNVLEA-LEEIGYEGKEAVG-------RAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 211 IGLGFNKKTILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVW----LEEYLKRFDRTLVLVSHSQDFL 286
Cdd:TIGR03269 153 IEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 287 NGVCTNMIdmraqkltayggnydsyhktrsELETNQMKQYNKQQEEIQhikKFIASAgtyanlvkqaksrqKILDKMEAD 366
Cdd:TIGR03269 233 EDLSDKAI----------------------WLENGEIKEEGTPDEVVA---VFMEGV--------------SEVEKECEV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 367 GLVQPVVPDKVFSFRFPQVERlpPPVLAFDDISFhyesnpseNLYEHLNFGvdmdsriaLVGPNGVGKSTLLKIMTGELT 446
Cdd:TIGR03269 274 EVGEPIIKVRNVSKRYISVDR--GVVKAVDNVSL--------EVKEGEIFG--------IVGTSGAGKTTLSKIIAGVLE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 447 PQSGRVsrhtHVKLGvysqhsQDQLDLTKSA----------LEFVRDKYS-------------NISQDFQFwrgQLGR-- 501
Cdd:TIGR03269 336 PTSGEV----NVRVG------DEWVDMTKPGpdgrgrakryIGILHQEYDlyphrtvldnlteAIGLELPD---ELARmk 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 502 --YGLTGEGQTVQMA---------TLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAI----NEFNGGVV 566
Cdd:TIGR03269 403 avITLKMVGFDEEKAeeildkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTFI 482
|
....*
gi 285811661 567 VVSHD 571
Cdd:TIGR03269 483 IVSHD 487
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
396-579 |
1.82e-23 |
|
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: 98.48 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 396 DDISFHYESNPSenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV-------SRHTHVKLGVY-SQHS 467
Cdd:cd03226 3 ENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpiKAKERRKSIGYvMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 468 QDQLdLTKSALEFVRDKYSNISQDFQFWRGQLGRYGLTGEgQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLD 547
Cdd:cd03226 81 DYQL-FTDSVREELLLGLKELDAGNEQAETVLKDLDLYAL-KERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190
....*....|....*....|....*....|....*
gi 285811661 548 IPTIDSLADAINEFNG---GVVVVSHDFRLLDKIA 579
Cdd:cd03226 159 YKNMERVGELIRELAAqgkAVIVITHDYEFLAKVC 193
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
425-571 |
8.14e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 98.26 E-value: 8.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 425 ALVGPNGVGKSTLLKIMTGELTPQSGRV-------SRHTHVKL----GVYSQHSQDQLDLTksALEFVRdkysnisqdfq 493
Cdd:COG4559 31 AIIGPNGAGKSTLLKLLTGELTPSSGEVrlngrplAAWSPWELarrrAVLPQHSSLAFPFT--VEEVVA----------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 494 fwrgqLGRYGLTGEG-----------QTVQMA--------TLSEGQRSRVVFA-LLA------LEQPNVLLLDEPTNGLD 547
Cdd:COG4559 98 -----LGRAPHGSSAaqdrqivrealALVGLAhlagrsyqTLSGGEQQRVQLArVLAqlwepvDGGPRWLFLDEPTSALD 172
|
170 180 190
....*....|....*....|....*....|.
gi 285811661 548 IP-------TIDSLADAinefNGGVVVVSHD 571
Cdd:COG4559 173 LAhqhavlrLARQLARR----GGGVVAVLHD 199
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
396-589 |
1.62e-22 |
|
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: 96.85 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 396 DDISFHYESNPSenlYEHLNFGVDmDSRI-ALVGPNGVGKSTLLKIMTGELTPQSGRVS----------RHTHVKLGVYS 464
Cdd:COG4555 5 ENLSKKYGKVPA---LKDVSFTAK-DGEItGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrkepREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 465 QhsQDQLDLTKSALEFVR--------------DKYSNISQDFQFWRGQLGRYGltgegqtvqmaTLSEGQRSRVVFALLA 530
Cdd:COG4555 81 D--ERGLYDRLTVRENIRyfaelyglfdeelkKRIEELIELLGLEEFLDRRVG-----------ELSTGMKKKVALARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 531 LEQPNVLLLDEPTNGLDIPTIDSLADAINEF---NGGVVVVSHDFRLLDKIAQDIFVVENKT 589
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGK 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
425-582 |
2.29e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 96.29 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 425 ALVGPNGVGKSTLLKIMTGELTPQSGRV----------SRHTHVKLGVYSQHSQDQLDLT-KSALEFVRdKYSNISQDFQ 493
Cdd:COG1131 30 GLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedvardPAEVRRRIGYVPQEPALYPDLTvRENLRFFA-RLYGLPRKEA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 494 FWRGQ--LGRYGLTGEGQTvQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGG---VVVV 568
Cdd:COG1131 109 RERIDelLELFGLTDAADR-KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEgktVLLS 187
|
170
....*....|....
gi 285811661 569 SHDFRLLDKIAQDI 582
Cdd:COG1131 188 THYLEEAERLCDRV 201
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
396-589 |
5.74e-22 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 93.27 E-value: 5.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 396 DDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGrvsrhtHVKLgvysqhsqDQLDLTK 475
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSG------EILL--------DGKDLAS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 476 -SALEFVRdKYSNISQdfqfwrgQLGRYGLTGEGQTvQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIP----T 550
Cdd:cd03214 66 lSPKELAR-KIAYVPQ-------ALELLGLAHLADR-PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAhqieL 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 285811661 551 IDSLADAINEFNGGVVVVSHDFRLLDKIAQDIFVVENKT 589
Cdd:cd03214 137 LELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
381-587 |
1.33e-21 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 98.68 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 381 RFPQVERLPP--PVLAFDDISFHYESNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV------ 452
Cdd:COG4987 320 TEPAEPAPAPggPSLELEDVSFRYPGAGRPVL-DGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvd 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 453 -------SRHTHVklGVYSQH-------------------SQDQLdltKSALEFVrdkysnisqdfqfwrgQLG------ 500
Cdd:COG4987 399 lrdldedDLRRRI--AVVPQRphlfdttlrenlrlarpdaTDEEL---WAALERV----------------GLGdwlaal 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 501 RYGL---TGEGQtvqmATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGG--VVVVSHDFRLL 575
Cdd:COG4987 458 PDGLdtwLGEGG----RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHRLAGL 533
|
250
....*....|..
gi 285811661 576 DKIAQdIFVVEN 587
Cdd:COG4987 534 ERMDR-ILVLED 544
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
393-587 |
1.50e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 92.96 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSrhthvklgvYSQHSQDQLD 472
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIY---------LDGKPLSAMP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 LTK-----------SAL--EFVRD------KYSNISQDFQFWRGQLGRYGLTGE--GQTVQmaTLSEGQRSRVVFALLAL 531
Cdd:COG4619 69 PPEwrrqvayvpqePALwgGTVRDnlpfpfQLRERKFDRERALELLERLGLPPDilDKPVE--RLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 532 EQPNVLLLDEPTNGLDIPTIDSLADAINEF----NGGVVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
383-587 |
1.72e-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: 99.14 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 383 PQVERLPPPVLA----FDDISFHYESNpSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSrhthv 458
Cdd:COG2274 460 EGRSKLSLPRLKgdieLENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL----- 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 459 klgvYsqhsqDQLDLTKSALEFVRDKYSNISQDFQFWRG------QLGRYGLT--------------------------- 505
Cdd:COG2274 534 ----I-----DGIDLRQIDPASLRRQIGVVLQDVFLFSGtireniTLGDPDATdeeiieaarlaglhdfiealpmgydtv 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 506 -GEGQtvqmATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGG--VVVVSHDFRLLdKIAQDI 582
Cdd:COG2274 605 vGEGG----SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAHRLSTI-RLADRI 679
|
....*
gi 285811661 583 FVVEN 587
Cdd:COG2274 680 IVLDK 684
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
83-300 |
5.95e-20 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 86.92 E-value: 5.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 83 KLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPipEHIDIYLLDEPAEPSELSALdyvvtea 162
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP--TSGEILIDGKDIAKLPLEEL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 163 qhelkriedlvektiledgpeselleplyermdsldpdtfesRAAIILIGlgfnkktilkktkDMSGGWKMRVALAKALF 242
Cdd:cd00267 72 ------------------------------------------RRRIGYVP-------------QLSGGQRQRVALARALL 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 243 VKPTLLLLDDPTAHLDLEACVWLEEYLKRF---DRTLVLVSHSQDFLNGVCTNMIDMRAQK 300
Cdd:cd00267 97 LNPDLLLLDEPTSGLDPASRERLLELLRELaeeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
91-311 |
6.39e-20 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 93.42 E-value: 6.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 91 FHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATrEYPiPEHIDIylldepaEPSELSALDYVvteAQ-HELKRI 169
Cdd:PRK15064 329 FDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG-ELE-PDSGTV-------KWSENANIGYY---AQdHAYDFE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 170 EDLvektiledgpesELLEPLYERMDSLDPDTFeSRAaiILIGLGFNKKTILKKTKDMSGGWKMRVALAKALFVKPTLLL 249
Cdd:PRK15064 397 NDL------------TLFDWMSQWRQEGDDEQA-VRG--TLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 250 LDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYGGNYDSY 311
Cdd:PRK15064 462 MDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
411-601 |
1.01e-19 |
|
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: 88.12 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 411 YEHLNFGVDMD-----SRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHthvklGVYSQHSQDQLDL------------ 473
Cdd:cd03297 8 KRLPDFTLKIDfdlneEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLN-----GTVLFDSRKKINLppqqrkiglvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 474 ---------TKSALEFVRDKYSNISQDFQFwRGQLGRYGLTGEGQTvQMATLSEGQRSRVVFALLALEQPNVLLLDEPTN 544
Cdd:cd03297 83 qyalfphlnVRENLAFGLKRKRNREDRISV-DELLDLLGLDHLLNR-YPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 545 GLDIPTIDSLADAINE----FNGGVVVVSHDFRLLDKIAQDIFVVEnktatrwDGSILQYK 601
Cdd:cd03297 161 ALDRALRLQLLPELKQikknLNIPVIFVTHDLSEAEYLADRIVVME-------DGRLQYIG 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
82-301 |
1.98e-19 |
|
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: 85.91 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYP------------------IPEHIDiYLL 143
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPdsgeikvlgkdikkepeeVKRRIG-YLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 144 DEPAEPSELSALDYVvteaqhelkriedlvektiledgpeselleplyermdsldpdtfesraaiiliglgfnkktilkk 223
Cdd:cd03230 80 EEPSLYENLTVRENL----------------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 224 tkDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF---DRTLVLVSHSQDFLNGVCTNMIDMRAQK 300
Cdd:cd03230 95 --KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGR 172
|
.
gi 285811661 301 L 301
Cdd:cd03230 173 I 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
339-571 |
2.75e-19 |
|
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: 91.27 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 339 FIASAGTYANLVKQAKSRQKILDKMEADGLVQPVVpdkvfsfrFPQVERLPP--PVLAFDDISFHYESNPS--ENLYEHL 414
Cdd:TIGR02868 287 FAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGS--------APAAGAVGLgkPTLELRDLSAGYPGAPPvlDGVSLDL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 415 NFGvdmdSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSrhthvkLGVYSQHSQDQLDLTKSALEFVRDKY---SNISQD 491
Cdd:TIGR02868 359 PPG----ERVAILGPSGSGKSTLLATLAGLLDPLQGEVT------LDGVPVSSLDQDEVRRRVSVCAQDAHlfdTTVREN 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 492 FQFWRG--------------QLGRY--GLTGEGQTV---QMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTID 552
Cdd:TIGR02868 429 LRLARPdatdeelwaalervGLADWlrALPDGLDTVlgeGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETAD 508
|
250 260
....*....|....*....|.
gi 285811661 553 SLADAINEFNGG--VVVVSHD 571
Cdd:TIGR02868 509 ELLEDLLAALSGrtVVLITHH 529
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
82-289 |
2.90e-19 |
|
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: 86.38 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALA------------------TREYPIPEHIdIYLL 143
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAgllppsagevlwngepirDAREDYRRRL-AYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 144 DEPAEPSELSALdyvvteaqhelkriedlvektiledgpesELLEpLYERMDSLDPDTFESRAAIILIGLGfnkKTILKK 223
Cdd:COG4133 82 HADGLKPELTVR-----------------------------ENLR-FWAALYGLRADREAIDEALEAVGLA---GLADLP 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 224 TKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF---DRTLVLVSHSQDFLNGV 289
Cdd:COG4133 129 VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA 197
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
390-587 |
4.08e-19 |
|
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: 90.97 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 390 PPVLAFDDISFHYEsnPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV-------------SRHT 456
Cdd:COG4988 334 PPSIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdldpaSWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 457 HVklGVYSQHSQ-------DQLDLTK---------------SALEFVRDkysnISQDFQFwrgQLGRYGltgegqtvqmA 514
Cdd:COG4988 412 QI--AWVPQNPYlfagtirENLRLGRpdasdeeleaaleaaGLDEFVAA----LPDGLDT---PLGEGG----------R 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285811661 515 TLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGG--VVVVSHDFRLLdKIAQDIFVVEN 587
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALL-AQADRILVLDD 546
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
82-331 |
5.01e-19 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 91.00 E-value: 5.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIylldepaepSELSALDYVvte 161
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGIKLGYF--- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 162 AQHELKRIEdlvektiledGPESELleplyERMDSLDPDTFESRAAIILIGLGFNKKTILKKTKDMSGGWKMRVALAKAL 241
Cdd:PRK10636 381 AQHQLEFLR----------ADESPL-----QHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIV 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 242 FVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYGGNYDSYHKTRSELETN 321
Cdd:PRK10636 446 WQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQ 525
|
250
....*....|
gi 285811661 322 QMKQYNKQQE 331
Cdd:PRK10636 526 ENQTDEAPKE 535
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
94-300 |
5.59e-19 |
|
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: 85.60 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 94 KVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIdiYLLDEPAEPSELSALDYVV------TEAQhelk 167
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEV--LVDGKDLTKLSLKELRRKVglvfqnPDDQ---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 168 riedLVEKTILED---GPESElleplyermdSLDPDTFESRAAIILIGLGFNKKTIlKKTKDMSGGWKMRVALAKALFVK 244
Cdd:cd03225 88 ----FFGPTVEEEvafGLENL----------GLPEEEIEERVEEALELVGLEGLRD-RSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 245 PTLLLLDDPTAHLDLEACVWLEEYLKRFDR---TLVLVSHSQDFLNGVCTNMIDMRAQK 300
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
390-570 |
6.81e-19 |
|
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: 86.29 E-value: 6.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 390 PPVLAFDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQS-----------GRVS----R 454
Cdd:COG1119 1 DPLLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYgndvrlfgerrGGEDvwelR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 455 HthvKLGVYSQHSQDQLDLTKSALEFVR-------DKYSNIS-QDFQFWRGQLGRYGLTGEGQTvQMATLSEGQRSRVvf 526
Cdd:COG1119 78 K---RIGLVSPALQLRFPRDETVLDVVLsgffdsiGLYREPTdEQRERARELLELLGLAHLADR-PFGTLSQGEQRRV-- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 285811661 527 aLLA---LEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGG----VVVVSH 570
Cdd:COG1119 152 -LIAralVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaptLVLVTH 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
410-570 |
7.46e-19 |
|
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: 85.24 E-value: 7.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 410 LYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS---RHTHVKLGVYSQ------HsQDQLDLTKSALEF 480
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlngGPLDFQRDSIARgllylgH-APGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 481 VRdKYSNISQDFQFWRGqLGRYGLTGEGQtVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAIN- 559
Cdd:cd03231 94 LR-FWHADHSDEQVEEA-LARVGLNGFED-RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAg 170
|
170
....*....|...
gi 285811661 560 --EFNGGVVVVSH 570
Cdd:cd03231 171 hcARGGMVVLTTH 183
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
417-571 |
9.00e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 86.36 E-value: 9.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 417 GVDMDSR----IALVGPNGVGKSTLLKIMTGELTPQSGRV---------------SRHthvkLGVYSQHSQDQLDLTksA 477
Cdd:PRK13548 20 DVSLTLRpgevVAILGPNGAGKSTLLRALSGELSPDSGEVrlngrpladwspaelARR----RAVLPQHSSLSFPFT--V 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 478 LEFVRdkysnisqdfqfwrgqLGRYGLTGEGQTVQ------MA-------------TLSEGQRSRVVFA-LLA-----LE 532
Cdd:PRK13548 94 EEVVA----------------MGRAPHGLSRAEDDalvaaaLAqvdlahlagrdypQLSGGEQQRVQLArVLAqlwepDG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 285811661 533 QPNVLLLDEPTNGLDI----PTIDSLADAINEFNGGVVVVSHD 571
Cdd:PRK13548 158 PPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD 200
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
82-281 |
2.09e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 84.73 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYP------------IPEHIDI-----YLLD 144
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPtsgevrvlgedvARDPAEVrrrigYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 145 EPAEPSELSALDYVVteaqhelkriedlvektiledgpesellepLYERMDSLDPDTFESRAAIIL--IGLGFNKKtilK 222
Cdd:COG1131 81 EPALYPDLTVRENLR------------------------------FFARLYGLPRKEARERIDELLelFGLTDAAD---R 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 223 KTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF---DRTLVLVSH 281
Cdd:COG1131 128 KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaeGKTVLLSTH 189
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
379-587 |
4.82e-18 |
|
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: 84.08 E-value: 4.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 379 SFRFPQVERLPPpvlAFDDISFHYESNpsenlyehlnfgvdmdSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS----- 453
Cdd:COG1124 8 SVSYGQGGRRVP---VLKDVSLEVAPG----------------ESFGLVGESGSGKSTLLRALAGLERPWSGEVTfdgrp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 454 --------------------------RHT---HVKLGVYSQHSQDQLDLTKSALEFVrdkysNISQDFqfwrgqLGRYgl 504
Cdd:COG1124 69 vtrrrrkafrrrvqmvfqdpyaslhpRHTvdrILAEPLRIHGLPDREERIAELLEQV-----GLPPSF------LDRY-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 505 tgegqtvqMATLSEGQRSRVVFA-LLALEqPNVLLLDEPTNGLDIPT----IDSLADAINEFNGGVVVVSHDFRLLDKIA 579
Cdd:COG1124 136 --------PHQLSGGQRQRVAIArALILE-PELLLLDEPTSALDVSVqaeiLNLLKDLREERGLTYLFVSHDLAVVAHLC 206
|
....*...
gi 285811661 580 QDIFVVEN 587
Cdd:COG1124 207 DRVAVMQN 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
82-305 |
6.63e-18 |
|
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: 83.15 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFH-GKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALA---TreypiPEHIDIYLLDEPAEPSELSALdy 157
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNgllK-----PTSGEVLVDGKDITKKNLREL-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 158 vvteaqheLKRI-------ED-LVEKTILED---GPEselleplyeRMDsLDPDTFESRA--AIILIGLgfnkKTILKK- 223
Cdd:COG1122 74 --------RRKVglvfqnpDDqLFAPTVEEDvafGPE---------NLG-LPREEIRERVeeALELVGL----EHLADRp 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 224 TKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR---TLVLVSHSQDFLNGVCTNMIDMRAQK 300
Cdd:COG1122 132 PHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGR 211
|
....*
gi 285811661 301 LTAYG 305
Cdd:COG1122 212 IVADG 216
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
389-597 |
8.88e-18 |
|
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: 83.11 E-value: 8.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 389 PPPVLAFDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVsrhtHVkLGvysqhsQ 468
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEI----LV-DG------Q 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 469 DQLDLTKSALEFVRDKYS----------------NIsqdfQFW----------------RGQLGRYGLTGEGQtvQM-AT 515
Cdd:COG1127 68 DITGLSEKELYELRRRIGmlfqggalfdsltvfeNV----AFPlrehtdlseaeirelvLEKLELVGLPGAAD--KMpSE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 516 LSEGQRSRVvfAL---LALEqPNVLLLDEPTNGLDiP----TIDSLADAIN-EFNGGVVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:COG1127 142 LSGGMRKRV--ALaraLALD-PEILLYDEPTAGLD-PitsaVIDELIRELRdELGLTSVVVTHDLDSAFAIADRVAVLAD 217
|
250
....*....|
gi 285811661 588 KTAtRWDGSI 597
Cdd:COG1127 218 GKI-IAEGTP 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
414-585 |
1.17e-17 |
|
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: 82.38 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 414 LNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS---------RHTHVK-LG-VYSQHSQDQLDLT-KSALEFV 481
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpwkrRKKFLRrIGvVFGQKTQLWWDLPvIDSFYLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 482 RDKYSNISQDFQFWRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEF 561
Cdd:cd03267 120 AAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEY 199
|
170 180
....*....|....*....|....*...
gi 285811661 562 N----GGVVVVSHDFRLLDKIAQDIFVV 585
Cdd:cd03267 200 NrergTTVLLTSHYMKDIEALARRVLVI 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
392-584 |
1.52e-17 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 82.17 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 392 VLAFDDISFHYESNPSEN-LYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHthvklgvysqhSQDQ 470
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD-----------GKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 471 LDLTKSALEFVRDKYSNISQD------------FQFWRGQLGRYGLTGEGQTVQMAT-------------------LSEG 519
Cdd:cd03257 70 LKLSRRLRKIRRKEIQMVFQDpmsslnprmtigEQIAEPLRIHGKLSKKEARKEAVLlllvgvglpeevlnrypheLSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 520 QRSRVVFAL-LALeQPNVLLLDEPTNGLDIPT----IDSLADAINEFNGGVVVVSHDFRLLDKIAQDIFV 584
Cdd:cd03257 150 QRQRVAIARaLAL-NPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVVAKIADRVAV 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
417-584 |
1.90e-17 |
|
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: 82.39 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 417 GVDMD----SRIALVGPNGVGKSTLLKIMTGELTPQSGRVS--------RHTH--VKLGV---YsQHSQDQLDLTksALE 479
Cdd:COG0411 22 DVSLEvergEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrditgLPPHriARLGIartF-QNPRLFPELT--VLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 480 FV------RDKYSNISQDFQFWRG-------------QLGRYGLTGEGQTvQMATLSEGQRSRVVFAL-LALEqPNVLLL 539
Cdd:COG0411 99 NVlvaahaRLGRGLLAALLRLPRArreereareraeeLLERVGLADRADE-PAGNLSYGQQRRLEIARaLATE-PKLLLL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 285811661 540 DEPTNGLDIPTIDSLADAI----NEFNGGVVVVSHDFRLLDKIAQDIFV 584
Cdd:COG0411 177 DEPAAGLNPEETEELAELIrrlrDERGITILLIEHDMDLVMGLADRIVV 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
83-305 |
2.48e-17 |
|
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: 80.17 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 83 KLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALAtREYPiPEHIDIYLLDEPAE---PSELSALDYVV 159
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA-GLLK-PSSGEILLDGKDLAslsPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 160 TEAQHELkRIEDLVEKTILEdgpeselleplyermdsldpdtfesraaiiliglgfnkktilkktkdMSGGWKMRVALAK 239
Cdd:cd03214 79 PQALELL-GLAHLADRPFNE-----------------------------------------------LSGGERQRVLLAR 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 240 ALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF----DRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYG 305
Cdd:cd03214 111 ALAQEPPILLLDEPTSHLDIAHQIELLELLRRLarerGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
393-587 |
2.80e-17 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 81.10 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSrhthvklgvYSQHSQDQLD 472
Cdd:cd03245 3 IEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVL---------LDGTDIRQLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 LTKsalefVRDKYSNISQDFQFWRGQL--------------------GRYGLT--------------GEGQtvqmATLSE 518
Cdd:cd03245 73 PAD-----LRRNIGYVPQDVTLFYGTLrdnitlgapladderilraaELAGVTdfvnkhpngldlqiGERG----RGLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 519 GQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGG--VVVVSHDFRLLDkIAQDIFVVEN 587
Cdd:cd03245 144 GQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLD-LVDRIIVMDS 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
82-298 |
3.04e-17 |
|
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: 79.92 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALAtreypipehidiyLLDEPAEpSELSALDYVVTE 161
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIA-------------GLEEPDS-GSILIDGEDLTD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 162 AQHELKRIEDLVeKTILEDGPesellepLYERMDSLDpdtfesraaIILIGLgfnkktilkktkdmSGGWKMRVALAKAL 241
Cdd:cd03229 67 LEDELPPLRRRI-GMVFQDFA-------LFPHLTVLE---------NIALGL--------------SGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 242 FVKPTLLLLDDPTAHLDLEACVWLEEYLK----RFDRTLVLVSHSQDFLNGVCTNMIDMRA 298
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKslqaQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
414-574 |
3.27e-17 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 80.16 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 414 LNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV---------------SRHTHVKLGVysQHSQDQLdltksal 478
Cdd:TIGR01166 11 LNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVlidgepldysrkgllERRQRVGLVF--QDPDDQL------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 479 eFvrdkYSNISQDFQFWRGQLG----------RYGLTG------EGQTVQMatLSEGQRSRVVFALLALEQPNVLLLDEP 542
Cdd:TIGR01166 82 -F----AADVDQDVAFGPLNLGlseaeverrvREALTAvgasglRERPTHC--LSGGEKKRVAIAGAVAMRPDVLLLDEP 154
|
170 180 190
....*....|....*....|....*....|....*
gi 285811661 543 TNGLDIPTIDSLADAINEFNG---GVVVVSHDFRL 574
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRRLRAegmTVVISTHDVDL 189
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
417-597 |
4.22e-17 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 81.01 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 417 GVDMDSR----IALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHvklgvysqhsqDQLDLTKSALEFVRDKYS------ 486
Cdd:cd03261 18 GVDLDVRrgeiLAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGE-----------DISGLSEAELYRLRRRMGmlfqsg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 487 ------NISQDFQFW----------------RGQLGRYGLTGEGQtvQM-ATLSEGQRSRVVFA-LLALEqPNVLLLDEP 542
Cdd:cd03261 87 alfdslTVFENVAFPlrehtrlseeeireivLEKLEAVGLRGAED--LYpAELSGGMKKRVALArALALD-PELLLYDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 543 TNGLDIPTIDSLADAIN----EFNGGVVVVSHDFRLLDKIAQDIFVVENKTaTRWDGSI 597
Cdd:cd03261 164 TAGLDPIASGVIDDLIRslkkELGLTSIMVTHDLDTAFAIADRIAVLYDGK-IVAEGTP 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
410-570 |
6.98e-17 |
|
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: 79.32 E-value: 6.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 410 LYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV---SRHTHVKLGVYSQHS-----QDQLDLTKSALEfv 481
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrwnGTPLAEQRDEPHENIlylghLPGLKPELSALE-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 482 rdkysnisqDFQFWRGQLG-----------RYGLTGEGQTVqMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPT 550
Cdd:TIGR01189 93 ---------NLHFWAAIHGgaqrtiedalaAVGLTGFEDLP-AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|...
gi 285811661 551 IDSLADAINEF---NGGVVVVSH 570
Cdd:TIGR01189 163 VALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
393-590 |
1.26e-16 |
|
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: 78.03 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNpSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRvsrhthVKLgvysqhsqDQLD 472
Cdd:cd03246 1 LEVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGR------VRL--------DGAD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 LTKSALEFVRDKYSNISQDFQFWRGqlgrygltgegqTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTID 552
Cdd:cd03246 66 ISQWDPNELGDHVGYLPQDDELFSG------------SIAENILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 285811661 553 SLADAINEFNGG---VVVVSHDFRLLdKIAQDIFVVENKTA 590
Cdd:cd03246 134 ALNQAIAALKAAgatRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
384-578 |
1.79e-16 |
|
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: 82.72 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 384 QVERLPPPVLAFDDISFHYESnpSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS---------- 453
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYPG--RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladad 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 454 -RHTHVKLGVYSQH-----------------------SQDQLDLTkSALEFVRDKYsnisqdfQFWRGQLGRYGltgegq 509
Cdd:TIGR02857 391 aDSWRDQIAWVPQHpflfagtiaenirlarpdasdaeIREALERA-GLDEFVAALP-------QGLDTPIGEGG------ 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 285811661 510 tvqmATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGG--VVVVSHD---FRLLDKI 578
Cdd:TIGR02857 457 ----AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRlalAALADRI 526
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
389-587 |
5.67e-16 |
|
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: 77.19 E-value: 5.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 389 PPPVLAFDDISFHYESNpsenlyehlnfgvdmdSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKL-------- 460
Cdd:cd03220 32 VGEFWALKDVSFEVPRG----------------ERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSllglgggf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 461 -------------GVYSQHSQDQLDltkSALEFVrdkysnisQDFqfwrGQLGRYgltgegQTVQMATLSEGQRSRVVFA 527
Cdd:cd03220 96 npeltgreniylnGRLLGLSRKEID---EKIDEI--------IEF----SELGDF------IDLPVKTYSSGMKARLAFA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 528 LLALEQPNVLLLDEPTNGLDIPTIDSLADAINEF---NGGVVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDAAFQEKCQRRLRELlkqGKTVILVSHDPSSIKRLCDRALVLEK 217
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
393-587 |
7.89e-16 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 81.07 E-value: 7.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSrhthvklgvysqhsQDQLD 472
Cdd:TIGR03375 464 IEFRNVSFAYPGQETPAL-DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVL--------------LDGVD 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 LTKSALEFVRDKYSNISQDFQFWRGQL--------------------GRYGLT--------------GEGQtvqmATLSE 518
Cdd:TIGR03375 529 IRQIDPADLRRNIGYVPQDPRLFYGTLrdnialgapyaddeeilraaELAGVTefvrrhpdgldmqiGERG----RSLSG 604
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 519 GQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGG--VVVVSHDFRLLDkIAQDIFVVEN 587
Cdd:TIGR03375 605 GQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGktLVLVTHRTSLLD-LVDRIIVMDN 674
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
410-582 |
1.06e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 80.38 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 410 LYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGR--------VSR-----HTHVKLGVYS------QHSQDQ 470
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRiiyeqdliVARlqqdpPRNVEGTVYDfvaegiEEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 471 LDLTKSALEFVRDKYS--NISQ--------DFQ-FWRGQ------LGRYGLTGEgqtVQMATLSEGQRSRVVFALLALEQ 533
Cdd:PRK11147 98 LKRYHDISHLVETDPSekNLNElaklqeqlDHHnLWQLEnrinevLAQLGLDPD---AALSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 285811661 534 PNVLLLDEPTNGLDIPTIDSLADAINEFNGGVVVVSHDFRLLDKIAQDI 582
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRI 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
424-575 |
1.12e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYSQ--HSQDQLDLTKSalEFVRDKYSNISQDFqfwrgqLGR 501
Cdd:PRK09544 33 LTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQklYLDTTLPLTVN--RFLRLRPGTKKEDI------LPA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 502 YGLTGEGQTVQ--MATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAIN----EFNGGVVVVSHDFRLL 575
Cdd:PRK09544 105 LKRVQAGHLIDapMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDqlrrELDCAVLMVSHDLHLV 184
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
393-587 |
1.25e-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: 75.04 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVsrhthvklgvysqhsqdQLD 472
Cdd:cd03247 1 LSINNVSFSYPEQEQQVL-KNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-----------------TLD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 --LTKSALEFVRDKYSNISQDFQFW----RGQLGRygltgegqtvqmaTLSEGQRSRVVFALLALEQPNVLLLDEPTNGL 546
Cdd:cd03247 63 gvPVSDLEKALSSLISVLNQRPYLFdttlRNNLGR-------------RFSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 285811661 547 DIPTIDSLADAINEF--NGGVVVVSHDFRLLDKiAQDIFVVEN 587
Cdd:cd03247 130 DPITERQLLSLIFEVlkDKTLIWITHHLTGIEH-MDKILFLEN 171
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
410-569 |
2.12e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 410 LYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRH-------THVKLGVYSQHsqdqLDLTKSALEfVR 482
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDggdiddpDVAEACHYLGH----RNAMKPALT-VA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 483 DkysNIsqdfQFWRGQLG-----------RYGLtGEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTI 551
Cdd:PRK13539 92 E---NL----EFWAAFLGgeeldiaaaleAVGL-APLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|
gi 285811661 552 DSLADAINEF--NGGVVVVS 569
Cdd:PRK13539 164 ALFAELIRAHlaQGGIVIAA 183
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
412-595 |
2.13e-15 |
|
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: 75.33 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 412 EHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSrhthvKLGVYSQHSQDQL-------------------- 471
Cdd:cd03268 17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT-----FDGKSYQKNIEALrrigalieapgfypnltare 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 472 DLTKSALEFvRDKYSNISQdfqfwrgQLGRYGLTGEGQtVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTI 551
Cdd:cd03268 92 NLRLLARLL-GIRKKRIDE-------VLDVVGLKDSAK-KKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 285811661 552 DSLADAI---NEFNGGVVVVSHDFRLLDKIAqDIFVVENKTATRWDG 595
Cdd:cd03268 163 KELRELIlslRDQGITVLISSHLLSEIQKVA-DRIGIINKGKLIEEG 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
414-584 |
2.52e-15 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 75.55 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 414 LNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV----------SRHTHVKLGV---YsQHSQDQLDLTksALEF 480
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeditglPPHEIARLGIgrtF-QIPRLFPELT--VLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 481 V------RDKYSNISQDFQFWRGQ--------LGRYGLTGEGQtVQMATLSEGQRSRVVFAL-LALEqPNVLLLDEPTNG 545
Cdd:cd03219 96 VmvaaqaRTGSGLLLARARREEREareraeelLERVGLADLAD-RPAGELSYGQQRRLEIARaLATD-PKLLLLDEPAAG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 285811661 546 LDIPTIDSLAD---AINEFNGGVVVVSHDFRLLDKIAQDIFV 584
Cdd:cd03219 174 LNPEETEELAElirELRERGITVLLVEHDMDVVMSLADRVTV 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
414-587 |
2.65e-15 |
|
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: 74.15 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 414 LNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHThvklgvysqhsQDQLDLTKSALEFvRDKYSNISQDFQ 493
Cdd:cd03229 19 VSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDG-----------EDLTDLEDELPPL-RRRIGMVFQDFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 494 FWRGqlgrygLTGEgQTVQMAtLSEGQRSRVVFA-LLALEqPNVLLLDEPTNGLDIPTIDSLADAINEFNGG----VVVV 568
Cdd:cd03229 87 LFPH------LTVL-ENIALG-LSGGQQQRVALArALAMD-PDVLLLDEPTSALDPITRREVRALLKSLQAQlgitVVLV 157
|
170
....*....|....*....
gi 285811661 569 SHDFRLLDKIAQDIFVVEN 587
Cdd:cd03229 158 THDLDEAARLADRVVVLRD 176
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
397-587 |
3.01e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 76.38 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 397 DISFHYESNpsENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV-----------SRHTHVKLGVYSQ 465
Cdd:PRK13652 8 DLCYSYSGS--KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepitkenIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 466 HSQDQLDLTksalefvrdkysNISQDFQFWRGQLGRYGLTGE---GQTVQMATLSE-----------GQRSRVVFA-LLA 530
Cdd:PRK13652 86 NPDDQIFSP------------TVEQDIAFGPINLGLDEETVAhrvSSALHMLGLEElrdrvphhlsgGEKKRVAIAgVIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 531 LEqPNVLLLDEPTNGLDIPTIDSLADAINEFN---GGVVVVS-HDFRLLDKIAQDIFVVEN 587
Cdd:PRK13652 154 ME-PQVLVLDEPTAGLDPQGVKELIDFLNDLPetyGMTVIFStHQLDLVPEMADYIYVMDK 213
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
416-571 |
3.08e-15 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 75.27 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 416 FGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV------SRHTHVKLGVYSQHSQDQLDLTKSALEFVRDKYSNI- 488
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVkvagasPGKGWRHIGYVPQRHEFAWDFPISVAHTVMSGRTGHi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 489 -------SQDFQFWRGQLGRYGLTgEGQTVQMATLSEGQRSRVVFA-LLALEqPNVLLLDEPTNGLDIPTIDSLADAINE 560
Cdd:TIGR03771 81 gwlrrpcVADFAAVRDALRRVGLT-ELADRPVGELSGGQRQRVLVArALATR-PSVLLLDEPFTGLDMPTQELLTELFIE 158
|
170
....*....|....
gi 285811661 561 FNG---GVVVVSHD 571
Cdd:TIGR03771 159 LAGagtAILMTTHD 172
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
103-306 |
4.61e-15 |
|
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: 75.14 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 103 ELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDEPAEPSELSAlDYVVTEAQHELKRIEDLVEKTILEdgp 182
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKA-DYEGTVRDLLSSITKDFYTHPYFK--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 183 eSELLEPLyeRMDSLdpdtfesraaiiliglgfnkktILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEAC 262
Cdd:cd03237 97 -TEIAKPL--QIEQI----------------------LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 285811661 263 VWLEEYLKRF----DRTLVLVSHsqDFLngvctnMIDMRAQKLTAYGG 306
Cdd:cd03237 152 LMASKVIRRFaennEKTAFVVEH--DII------MIDYLADRLIVFEG 191
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
393-579 |
6.42e-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: 74.05 E-value: 6.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPSENL-YEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRH------THVKLGVYSQ 465
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgepvtgPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 466 hsQDQL-------DLTKSALEFVRDKYSNISQDFQFWrgqLGRYGLTG-EGQTVqmATLSEGQRSRVVFA-LLALEqPNV 536
Cdd:cd03293 81 --QDALlpwltvlDNVALGLELQGVPKAEARERAEEL---LELVGLSGfENAYP--HQLSGGMRQRVALArALAVD-PDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 285811661 537 LLLDEPTNGLDIPT----IDSLADAINEFNGGVVVVSHD----FRLLDKIA 579
Cdd:cd03293 153 LLLDEPFSALDALTreqlQEELLDIWRETGKTVLLVTHDideaVFLADRVV 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
82-305 |
9.36e-15 |
|
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: 74.31 E-value: 9.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALAtREYPiPEHIDIYLLDEPAepSELSALD----- 156
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALA-GLLK-PSSGEVLLDGRDL--ASLSRRElarri 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 157 -YVVTEAQHELK-RIEDLVektiledgpeseLL--EPLYERMDSLDPDTFES-RAAIILIGL-GFNKKTILkktkDMSGG 230
Cdd:COG1120 78 aYVPQEPPAPFGlTVRELV------------ALgrYPHLGLFGRPSAEDREAvEEALERTGLeHLADRPVD----ELSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 231 WKMRVALAKALFVKPTLLLLDDPTAHLDL----EACVWLEEYLKRFDRTLVLVSHsqDfLN---GVCTNMIDMRAQKLTA 303
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLH--D-LNlaaRYADRLVLLKDGRIVA 218
|
..
gi 285811661 304 YG 305
Cdd:COG1120 219 QG 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
392-587 |
1.48e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 73.16 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 392 VLAFDDISFHYESNPsENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS---------RHTHV---- 458
Cdd:COG2884 1 MIRFENVSKRYPGGR-EAL-SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrlKRREIpylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 459 -KLG-VYsqhsQD-QL--DLT-----KSALEFVRDKYSNISQDFQFWrgqLGRYGLTGEGQtvQM-ATLSEGQRSRVVF- 526
Cdd:COG2884 79 rRIGvVF----QDfRLlpDRTvyenvALPLRVTGKSRKEIRRRVREV---LDLVGLSDKAK--ALpHELSGGEQQRVAIa 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285811661 527 -ALLAleQPNVLLLDEPTNGLDIPTIDSLADAINEFN-GG--VVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:COG2884 150 rALVN--RPELLLADEPTGNLDPETSWEIMELLEEINrRGttVLIATHDLELVDRMPKRVLELED 212
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
413-609 |
1.53e-14 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 74.73 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 413 HLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSG--RVSRHTHVK--------LGVYSQHSQDQLDLT-KSALEFV 481
Cdd:TIGR01188 11 GVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGtaRVAGYDVVReprkvrrsIGIVPQYASVDEDLTgRENLEMM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 482 RDKYsNISQDFQFWRGQ--LGRYGLtGEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAIN 559
Cdd:TIGR01188 91 GRLY-GLPKDEAEERAEelLELFEL-GEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 285811661 560 EFNGG---VVVVSHDFRLLDKIAQDIFVVeNKTATRWDGSILQYKNKLAKNVV 609
Cdd:TIGR01188 169 ALKEEgvtILLTTHYMEEADKLCDRIAII-DHGRIIAEGTPEELKRRLGKDTL 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
393-595 |
1.54e-14 |
|
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: 72.91 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPSenlyeHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHthvklGVYSQHSqDQLD 472
Cdd:cd03298 1 VRLDKIRFSYGEQPM-----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN-----GVDVTAA-PPAD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 LTKSALEFVRDKYSNIS-----------------QDFQFWRGQLGRYGLTGEGQTVQmATLSEGQRSRVVFALLALEQPN 535
Cdd:cd03298 70 RPVSMLFQENNLFAHLTveqnvglglspglkltaEDRQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 285811661 536 VLLLDEPTNGLDIPTIDSLADAINEFNG----GVVVVSHDFRLLDKIAQDIFVVENKTATrWDG 595
Cdd:cd03298 149 VLLLDEPFAALDPALRAEMLDLVLDLHAetkmTVLMVTHQPEDAKRLAQRVVFLDNGRIA-AQG 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
392-610 |
1.83e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.74 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 392 VLAFDDISFHYEsnPSEnlyehlnfgvdmdsRIALVGPNGVGKSTLLKIMTGELTPQSGRVS---------RHTHVK-LG 461
Cdd:COG4586 35 VEAVDDISFTIE--PGE--------------IVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvpfkrRKEFARrIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 462 -VYSQHSQDQLDLT-KSALEFVRDKYsNIS-QDFQFWRGQL-GRYGLtGEGQTVQMATLSEGQRSRVVFALLALEQPNVL 537
Cdd:COG4586 99 vVFGQRSQLWWDLPaIDSFRLLKAIY-RIPdAEYKKRLDELvELLDL-GELLDTPVRQLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 285811661 538 LLDEPTNGLDIPTIDSLADAINEFN--GGVVVV--SHDFRLLDKIAQDIFVVeNKTATRWDGSILQYKNKLAKNVVL 610
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYNreRGTTILltSHDMDDIEALCDRVIVI-DHGRIIYDGSLEELKERFGPYKTI 252
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
82-303 |
1.86e-14 |
|
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: 73.30 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLF----HGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALAtREYPiPEHIDIYLLDEPAEPSELSAL-- 155
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALA-GLER-PWSGEVTFDGRPVTRRRRKAFrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 156 -------DYvvTEAQHELKRIEDLvektiledgpeseLLEPLYERmdSLDPDTFESRAAIILIGLGfnkKTILKKTK-DM 227
Cdd:COG1124 80 rvqmvfqDP--YASLHPRHTVDRI-------------LAEPLRIH--GLPDREERIAELLEQVGLP---PSFLDRYPhQL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLDL--EACVW--LEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTA 303
Cdd:COG1124 140 SGGQRQRVAIARALILEPELLLLDEPTSALDVsvQAEILnlLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVE 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
393-587 |
1.87e-14 |
|
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: 73.03 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVsrhthvklgvysqhSQDQLD 472
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVL-RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRI--------------LIDGHD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 LTKSALEFVRDKYSNISQDFQFWRGQLG---RYGLTGEGQ-----TVQMA----------------------TLSEGQRS 522
Cdd:cd03251 66 VRDYTLASLRRQIGLVSQDVFLFNDTVAeniAYGRPGATReeveeAARAAnahefimelpegydtvigergvKLSGGQRQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 285811661 523 RVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEF--NGGVVVVSHdfRLLD-KIAQDIFVVEN 587
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAH--RLSTiENADRIVVLED 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
82-284 |
1.98e-14 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 72.55 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATreypipehidiylLDEPAEpSELSALDYVVTE 161
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAG-------------LERPDS-GEILIDGRDVTG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 162 AQHELKRI----EDL-------VEKTI-----LEDGPESELLEPLYERMDSLDPDTFESRaaiiliglgfnkktilkKTK 225
Cdd:cd03259 67 VPPERRNIgmvfQDYalfphltVAENIafglkLRGVPKAEIRARVRELLELVGLEGLLNR-----------------YPH 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 226 DMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKR----FDRTLVLVSHSQD 284
Cdd:cd03259 130 ELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKElqreLGITTIYVTHDQE 192
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
82-305 |
2.05e-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: 72.61 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRrYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDEPAEPSEL--------- 152
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLrrrigylpq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 153 -----------SALDYVVTeaqheLKRIEDLVEKTILEdgpesELLEplyermdsldpdtfesraaiiLIGLGFNKKtil 221
Cdd:cd03264 80 efgvypnftvrEFLDYIAW-----LKGIPSKEVKARVD-----EVLE---------------------LVNLGDRAK--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 222 KKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF--DRTLVLVSHSQDFLNGVCTNMIDMRAQ 299
Cdd:cd03264 126 KKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELgeDRIVILSTHIVEDVESLCNQVAVLNKG 205
|
....*.
gi 285811661 300 KLTAYG 305
Cdd:cd03264 206 KLVFEG 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
385-587 |
2.14e-14 |
|
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: 72.44 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 385 VERLPPPVLAFDDIsfhyesnpsenlyehlNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSG--RVSrhthvklgv 462
Cdd:cd03292 7 TKTYPNGTAALDGI----------------NISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGtiRVN--------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 463 ysqhSQDQLDLTKSALEFVRDKYSNISQDF-----------------------QFWRGQ----LGRYGLTGEGQTVQMAt 515
Cdd:cd03292 62 ----GQDVSDLRGRAIPYLRRKIGVVFQDFrllpdrnvyenvafalevtgvppREIRKRvpaaLELVGLSHKHRALPAE- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285811661 516 LSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFN--GGVVVVS-HDFRLLDKIAQDIFVVEN 587
Cdd:cd03292 137 LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkaGTTVVVAtHAKELVDTTRHRVIALER 211
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
412-562 |
3.44e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.10 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 412 EHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV-----------SRHTHVKLGVYSQHSQDQLDLTKSALeF 480
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaSKEVARRIGLLAQNATTPGDITVQEL-V 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 481 VRDKYSNiSQDFQFWR--------GQLGRYGLTG-EGQTVQmaTLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTI 551
Cdd:PRK10253 103 ARGRYPH-QPLFTRWRkedeeavtKAMQATGITHlADQSVD--TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
|
170
....*....|.
gi 285811661 552 DSLADAINEFN 562
Cdd:PRK10253 180 IDLLELLSELN 190
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
391-584 |
3.81e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 75.32 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 391 PVLAFDDISFHYESNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGeLTPQSGRVSRHTHV------------ 458
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRISGEVLLdgrdllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 459 ---KLGVYSQHSQDQLDLTKSALEfVRDKYSNISQDFQFWRGQ----LGRYGLTGEGQTvQMATLSEGQRSRVVFALLAL 531
Cdd:COG1123 81 rgrRIGMVFQDPMTQLNPVTVGDQ-IAEALENLGLSRAEARARvlelLEAVGLERRLDR-YPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 285811661 532 EQPNVLLLDEPTNGLDIPT----IDSLADAINEFNGGVVVVSHDFRLLDKIAQDIFV 584
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHDLGVVAEIADRVVV 215
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
393-574 |
4.37e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 75.20 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYEsnPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRvsrhthVKLGvysqhSQDQLD 472
Cdd:COG1132 340 IEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR------ILID-----GVDIRD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 LTKSALefvRDKYSNISQDFQFWRG------QLGRYGLT----------------------------GEGQTvqmaTLSE 518
Cdd:COG1132 407 LTLESL---RRQIGVVPQDTFLFSGtireniRYGRPDATdeeveeaakaaqahefiealpdgydtvvGERGV----NLSG 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 519 GQRSRVVFA--LLAleQPNVLLLDEPTNGLDIPTIDSLADAINEFNGG--VVVVSHdfRL 574
Cdd:COG1132 480 GQRQRIAIAraLLK--DPPILILDEATSALDTETEALIQEALERLMKGrtTIVIAH--RL 535
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
389-571 |
6.30e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 72.04 E-value: 6.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 389 PPPVLAFDDISFHYESNPSENL-YEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLG------ 461
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVTaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGpgpdrg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 462 -VYSQHS-------QDQLDLtksALEFV---RDKYSNISQDFqfwrgqLGRYGLTGEGQtvqmA---TLSEGQRSRVvfA 527
Cdd:COG1116 84 vVFQEPAllpwltvLDNVAL---GLELRgvpKAERRERAREL------LELVGLAGFED----AyphQLSGGMRQRV--A 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 285811661 528 L---LALEqPNVLLLDEPTNGLDIPTI----DSLADAINEFNGGVVVVSHD 571
Cdd:COG1116 149 IaraLAND-PEVLLMDEPFGALDALTRerlqDELLRLWQETGKTVLFVTHD 198
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
415-582 |
6.37e-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: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 415 NFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSrhthvkLGVYSQHSqdqldLTKSALEFVRDKYSNISQDFQ- 493
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL------IDGTDINK-----LKGKALRQLRRQIGMIFQQFNl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 494 -------------------FWRGQLGRY---------------GLtgEGQTVQMA-TLSEGQRSRVVFALLALEQPNVLL 538
Cdd:cd03256 90 ierlsvlenvlsgrlgrrsTWRSLFGLFpkeekqralaalervGL--LDKAYQRAdQLSGGQQQRVAIARALMQQPKLIL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 285811661 539 LDEPTNGLDIPT----IDSLADAINEFNGGVVVVSHDFRLLDKIAQDI 582
Cdd:cd03256 168 ADEPVASLDPASsrqvMDLLKRINREEGITVIVSLHQVDLAREYADRI 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
393-574 |
7.06e-14 |
|
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: 70.98 E-value: 7.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPSEN-LYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVsrhthVKLGvysqhsQDQL 471
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEV-----RVDG------TDIS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 472 DLTKSAL-EFVRDKYSNISQDF---------------QFWRGQ------------LGRYGLtGEGQTVQMATLSEGQRSR 523
Cdd:cd03255 70 KLSEKELaAFRRRHIGFVFQSFnllpdltalenvelpLLLAGVpkkerreraeelLERVGL-GDRLNHYPSELSGGQQQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 285811661 524 VVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNG----GVVVVSHDFRL 574
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeagtTIVVVTHDPEL 203
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
82-281 |
8.45e-14 |
|
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: 71.65 E-value: 8.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKaLATREYPIPEHIDIYLLDEP---AEPSEL-SALDY 157
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLS-LITGDLPPTYGNDVRLFGERrggEDVWELrKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 158 VVTEAQHELKRiEDLVEKTIL---EDGPEsellepLYERMDSLDpdtfESRAAIILIGLG---FNKKTIlkktKDMSGGW 231
Cdd:COG1119 83 VSPALQLRFPR-DETVLDVVLsgfFDSIG------LYREPTDEQ----RERARELLELLGlahLADRPF----GTLSQGE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 285811661 232 KMRVALAKALFVKPTLLLLDDPTAHLDLEACV----WLEEYLKRFDRTLVLVSH 281
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARElllaLLDKLAAEGAPTLVLVTH 201
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
29-282 |
9.31e-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: 73.93 E-value: 9.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 29 IRKLGRKKEAAAEESEVDAAAREIKMMKLQQDKDGLSDrVVTGVLSSLETSRD---IKLSSVSLlfhgkvliqdsglELN 105
Cdd:TIGR02868 294 AQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLG-KPTLELRDLSAGYPgapPVLDGVSL-------------DLP 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 106 YGRRYGLLGENGCGKSTFLKALaTREYPiPEHIDIYLLDEPA---EPSELSALDYVVTEAQHelkriedLVEKTILE--- 179
Cdd:TIGR02868 360 PGERVAILGPSGSGKSTLLATL-AGLLD-PLQGEVTLDGVPVsslDQDEVRRRVSVCAQDAH-------LFDTTVREnlr 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 180 ----DGPESELL---------EPLYERMDSLDPDTFESRAAIiliglgfnkktilkktkdmSGGWKMRVALAKALFVKPT 246
Cdd:TIGR02868 431 larpDATDEELWaalervglaDWLRALPDGLDTVLGEGGARL-------------------SGGERQRLALARALLADAP 491
|
250 260 270
....*....|....*....|....*....|....*...
gi 285811661 247 LLLLDDPTAHLDLEACVWLEEYLKRFD--RTLVLVSHS 282
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLEDLLAALsgRTVVLITHH 529
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
413-585 |
1.22e-13 |
|
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: 70.23 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 413 HLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV-----SRHTHVK-----LGVYSQHsqDQLDLTKSALEFVR 482
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingySIRTDRKaarqsLGYCPQF--DALFDELTVREHLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 483 -----------DKYSNISQDfqfwrgqLGRYGLTgEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTI 551
Cdd:cd03263 98 fyarlkglpksEIKEEVELL-------LRVLGLT-DKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASR 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 285811661 552 DSLADAINEFNGG--VVVVSHDFRLLDKIAQDIFVV 585
Cdd:cd03263 170 RAIWDLILEVRKGrsIILTTHSMDEAEALCDRIAIM 205
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
90-298 |
1.68e-13 |
|
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: 70.16 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 90 LFHGKVL--IQDSGLELNYGRRYGLLGENGCGKSTFLKALaTREYpIPE--HIDIYLLDEP-----AEPSELSAL----- 155
Cdd:COG4778 18 LQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCI-YGNY-LPDsgSILVRHDGGWvdlaqASPREILALrrrti 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 156 DYVvteAQ--HELKRI--EDLVEKTILEDGPE--------SELLEPLY--ERMDSLDPDTFesraaiiliglgfnkktil 221
Cdd:COG4778 96 GYV---SQflRVIPRVsaLDVVAEPLLERGVDreeararaRELLARLNlpERLWDLPPATF------------------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 222 kktkdmSGGWKMRVALAKALFVKPTLLLLDDPTAHLDL---EACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRA 298
Cdd:COG4778 154 ------SGGEQQRVNIARGFIADPPLLLLDEPTASLDAanrAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
416-587 |
1.68e-13 |
|
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: 70.16 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 416 FGVDMDSR----IALVGPNGVGKSTLLKIMTGELTPQSGRVSR----------HTHVKLGVySQHSQDQL---DLTksal 478
Cdd:cd03224 17 FGVSLTVPegeiVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrditglppHERARAGI-GYVPEGRRifpELT---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 479 efVRDkysNIsqdfqfwrgQLGRYGLTGEGQTVQMA------------------TLSEGQRSRVVFALLALEQPNVLLLD 540
Cdd:cd03224 92 --VEE---NL---------LLGAYARRRAKRKARLErvyelfprlkerrkqlagTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 285811661 541 EPTNGLDIPTIDSLADAINEFNGG---VVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEgvtILLVEQNARFALEIADRAYVLER 207
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
424-571 |
2.09e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 70.43 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVsrhtHVKLGVYSQHSQDQLDLTKSAL----------------EFVRDKYSN 487
Cdd:PRK11231 31 TALIGPNGCGKSTLLKCFARLLTPQSGTV----FLGDKPISMLSSRQLARRLALLpqhhltpegitvrelvAYGRSPWLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 488 isqdfqFWrgqlGRygLTGEG-----------QTVQMA-----TLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTI 551
Cdd:PRK11231 107 ------LW----GR--LSAEDnarvnqameqtRINHLAdrrltDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQ 174
|
170 180
....*....|....*....|...
gi 285811661 552 DSLADAINEFNGG---VVVVSHD 571
Cdd:PRK11231 175 VELMRLMRELNTQgktVVTVLHD 197
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
79-282 |
3.13e-13 |
|
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: 72.32 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 79 SRDIKLSSVSLLFHGK-VLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATreYPIPEHIDIYLLDEP-AEPSELSALD 156
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG--FVDPTEGSIAVNGVPlADADADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 157 YVVTEAQHELkriedLVEKTILEDgpeselleplyERMDSLDPDTFESRAAIILIGL---------GFNKKtILKKTKDM 227
Cdd:TIGR02857 397 QIAWVPQHPF-----LFAGTIAEN-----------IRLARPDASDAEIREALERAGLdefvaalpqGLDTP-IGEGGAGL 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF--DRTLVLVSHS 282
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHR 516
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
107-305 |
3.39e-13 |
|
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: 68.93 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 107 GRRYGLLGENGCGKSTFLKALATreypipehidiyLLDEPAEPSELSALDyVVTEAQHELKRIedlvekTILEDGpesel 186
Cdd:cd03266 31 GEVTGLLGPNGAGKTTTLRMLAG------------LLEPDAGFATVDGFD-VVKEPAEARRRL------GFVSDS----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 187 lEPLYERMDS------------LDPDTFESRAAIILIGLGFnKKTILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPT 254
Cdd:cd03266 87 -TGLYDRLTArenleyfaglygLKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 285811661 255 AHLDLEACVWLEEYLKRFDR---TLVLVSHSQDFLNGVCTNMIDMRAQKLTAYG 305
Cdd:cd03266 165 TGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
393-597 |
4.16e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 69.01 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYEsnpseNLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS----RHTH----------- 457
Cdd:COG3840 2 LRLDDLTYRYG-----DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILwngqDLTAlppaerpvsml 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 458 ---------------VKLGVysqhsQDQLDLTksalEFVRDKYSNIsqdfqfwrgqLGRYGLTGEGQTVQmATLSEGQRS 522
Cdd:COG3840 77 fqennlfphltvaqnIGLGL-----RPGLKLT----AEQRAQVEQA----------LERVGLAGLLDRLP-GQLSGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 523 RVVFALLALEQPNVLLLDEPTNGLDiPT-----IDSLADAINEFNGGVVVVSHDFRLLDKIAQDIFVVENKTATrWDGSI 597
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALD-PAlrqemLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIA-ADGPT 214
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
388-547 |
4.30e-13 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 72.04 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 388 LPPPV---LAFDDISFHYESNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS------RHTHV 458
Cdd:TIGR02204 330 LPVPLrgeIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILldgvdlRQLDP 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 459 KlgVYSQH----SQDQLDLTKSALEFVRdkYSN--------------------ISQDFQFWRGQLGRYGLtgegqtvqma 514
Cdd:TIGR02204 410 A--ELRARmalvPQDPVLFAASVMENIR--YGRpdatdeeveaaaraahahefISALPEGYDTYLGERGV---------- 475
|
170 180 190
....*....|....*....|....*....|...
gi 285811661 515 TLSEGQRSRVVFALLALEQPNVLLLDEPTNGLD 547
Cdd:TIGR02204 476 TLSGGQRQRIAIARAILKDAPILLLDEATSALD 508
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
82-283 |
4.58e-13 |
|
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: 68.80 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPipEHIDIYLLDEPAEPseLSALdyvvte 161
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETP--TSGEILLDGKDITN--LPPH------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 162 aqhelKRIEDLVEK--------TILEDgpeseLLEPLyeRMDSLDPDTFESRA--AIILIGL-GFNKKtilkKTKDMSGG 230
Cdd:cd03300 71 -----KRPVNTVFQnyalfphlTVFEN-----IAFGL--RLKKLPKAEIKERVaeALDLVQLeGYANR----KPSQLSGG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 285811661 231 WKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR----TLVLVSHSQ 283
Cdd:cd03300 135 QQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQ 191
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
111-305 |
7.22e-13 |
|
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: 68.30 E-value: 7.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 111 GLLGENGCGKSTFLKALATREYPipEHIDIYLLDEpaepselsaldYVVTEAQHELKRI----------EDLvekTILEd 180
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLTGELRP--TSGTAYINGY-----------SIRTDRKAARQSLgycpqfdalfDEL---TVRE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 181 gpeseLLEpLYERMDSLDPDTFESRAAIILIGLGFNKKtILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLE 260
Cdd:cd03263 95 -----HLR-FYARLKGLPKSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 285811661 261 A--CVW--LEEYLKrfDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYG 305
Cdd:cd03263 168 SrrAIWdlILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
82-305 |
8.74e-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: 67.92 E-value: 8.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGK----VLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYP-----IPEHIDIYLLDE------- 145
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPtsgsiIFDGKDLLKLSRrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 146 ------PAEPseLSALDYVVTeaqhelkrIEDLvektiledgpeseLLEPLYERMDSLDPDTFESRAAIILIGLGFNKKT 219
Cdd:cd03257 82 keiqmvFQDP--MSSLNPRMT--------IGEQ-------------IAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 220 ILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLD--LEACVwLEEYLK---RFDRTLVLVSHSQDFLNGVCTNMI 294
Cdd:cd03257 139 LNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDvsVQAQI-LDLLKKlqeELGLTLLFITHDLGVVAKIADRVA 217
|
250
....*....|.
gi 285811661 295 DMRAQKLTAYG 305
Cdd:cd03257 218 VMYAGKIVEEG 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
92-302 |
9.13e-13 |
|
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: 67.67 E-value: 9.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 92 HGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALA--TREYpipeHIDIYLLDEPAEPSE-LSALDYVVTEAQHELkr 168
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAglIKES----SGSILLNGKPIKAKErRKSIGYVMQDVDYQL-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 169 IEDLVEktiledgpesellEPLYERMDSLDPDtfESRAAIILIGLGFNKKTiLKKTKDMSGGWKMRVALAKALFVKPTLL 248
Cdd:cd03226 85 FTDSVR-------------EELLLGLKELDAG--NEQAETVLKDLDLYALK-ERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 285811661 249 LLDDPTAHLDLEA----CVWLEEyLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLT 302
Cdd:cd03226 149 IFDEPTSGLDYKNmervGELIRE-LAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
102-305 |
1.19e-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: 70.60 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 102 LELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDEPAEPSELSaldyvVTEAQHELKRIEDLVEKTILEdg 181
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPG-----PDGRGRAKRYIGILHQEYDLY-- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 182 PESELLEPLYERMdSLD-PDTFESRAAII-LIGLGFNKK---TILKKTKD-MSGGWKMRVALAKALFVKPTLLLLDDPTA 255
Cdd:TIGR03269 378 PHRTVLDNLTEAI-GLElPDELARMKAVItLKMVGFDEEkaeEILDKYPDeLSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 285811661 256 HLDLEACVWLEEYL----KRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYG 305
Cdd:TIGR03269 457 TMDPITKVDVTHSIlkarEEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
390-576 |
1.65e-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: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 390 PPVLAFDDISFHYESNPSENlyeHLNFGVDMD----SRIALVGPNGVGKSTLLKIMTGELTPQSGRVS------------ 453
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEV---TALRGVSLSieagEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdisslser 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 454 -----RHTHVklG-VYSQHsqdQL--DLTksALEFVR--DKYSNIS--QDFQFWRGQLGRYGLTG-EGQTVqmATLSEGQ 520
Cdd:COG1136 79 elarlRRRHI--GfVFQFF---NLlpELT--ALENVAlpLLLAGVSrkERRERARELLERVGLGDrLDHRP--SQLSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 521 RSRVVF--ALLAleQPNVLLLDEPTNGLDIPT----IDSLADAINEFNGGVVVVSHDFRLLD 576
Cdd:COG1136 150 QQRVAIarALVN--RPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPELAA 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
82-281 |
1.77e-12 |
|
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: 66.86 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALA-----------------TREYPIPEHIDIyLLD 144
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILglikpdsgeitfdgksyQKNIEALRRIGA-LIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 145 EPAEPSELSALDYVVTEAqhelkRIEDLVEKTIledgpeSELLEplyermdsldpdtfesraaiiLIGLGFNKKtilKKT 224
Cdd:cd03268 80 APGFYPNLTARENLRLLA-----RLLGIRKKRI------DEVLD---------------------VVGLKDSAK---KKV 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 225 KDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEY---LKRFDRTLVLVSH 281
Cdd:cd03268 125 KGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSH 184
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
393-570 |
1.92e-12 |
|
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: 65.64 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFhyeSNPSEN-LYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMtGELTP-QSGRVSRHTHVKLGVYSQHSQdq 470
Cdd:cd03223 1 IELENLSL---ATPDGRvLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPwGSGRIGMPEGEDLLFLPQRPY-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 471 ldLTKSALefvrdkysnisqdfqfwRGQLgRYGLtgegqtvqMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPT 550
Cdd:cd03223 75 --LPLGTL-----------------REQL-IYPW--------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180
....*....|....*....|
gi 285811661 551 IDSLADAINEFNGGVVVVSH 570
Cdd:cd03223 127 EDRLYQLLKELGITVISVGH 146
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
82-281 |
2.06e-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: 65.48 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSllFH----GKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALAtREYPiPEHIDIYLLDepaepselsaldy 157
Cdd:cd03228 1 IEFKNVS--FSypgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLL-RLYD-PTSGEILIDG------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 158 vvteaqHELKRIedlvektiledgpeselleplyermdsldpDTFESRAAIILIG---------LGFNkktILkktkdmS 228
Cdd:cd03228 64 ------VDLRDL------------------------------DLESLRKNIAYVPqdpflfsgtIREN---IL------S 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 285811661 229 GGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF--DRTLVLVSH 281
Cdd:cd03228 99 GGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALakGKTVIVIAH 153
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
417-587 |
2.24e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.10 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 417 GVDMDSR----IALVGPNGVGKSTLLKIMTGELTPQSGRVsrhthvklgvysqHSQDQLDLTKSALEFVRdKYSNISQD- 491
Cdd:PRK09536 21 GVDLSVRegslVGLVGPNGAGKTTLLRAINGTLTPTAGTV-------------LVAGDDVEALSARAASR-RVASVPQDt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 492 ---FQF------------WRGQLGRYGLTGE---------GQTVQMA-----TLSEGQRSRVVFA-LLALEQPnVLLLDE 541
Cdd:PRK09536 87 slsFEFdvrqvvemgrtpHRSRFDTWTETDRaaveramerTGVAQFAdrpvtSLSGGERQRVLLArALAQATP-VLLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 285811661 542 PTNGLDI----PTIDSLADAINEfNGGVVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:PRK09536 166 PTASLDInhqvRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLAD 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
396-579 |
2.31e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 68.63 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 396 DDISFHYesnPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS-------RHTHV---KLGVYSQ 465
Cdd:COG1118 6 RNISKRF---GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVlngrdlfTNLPPrerRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 466 HSqdqldltksALeF----VRDkysNISqdfqfwrgqlgrYGLTGEGQT--------------VQM--------ATLSEG 519
Cdd:COG1118 83 HY---------AL-FphmtVAE---NIA------------FGLRVRPPSkaeirarveellelVQLegladrypSQLSGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285811661 520 QRSRVvfAL---LALEqPNVLLLDEPTNGLDIptidSLADAI--------NEFNGGVVVVSHD----FRLLDKIA 579
Cdd:COG1118 138 QRQRV--ALaraLAVE-PEVLLLDEPFGALDA----KVRKELrrwlrrlhDELGGTTVFVTHDqeeaLELADRVV 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
392-585 |
2.59e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.34 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 392 VLAFDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHThvklgvysqhsqDQL 471
Cdd:PRK13638 1 MLATSDLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG------------KPL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 472 DLTKSALEFVRDK-------------YSNISQDFQFWRGQLG----------RYGLT------GEGQTVQmaTLSEGQRS 522
Cdd:PRK13638 66 DYSKRGLLALRQQvatvfqdpeqqifYTDIDSDIAFSLRNLGvpeaeitrrvDEALTlvdaqhFRHQPIQ--CLSHGQKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 523 RVVFALLALEQPNVLLLDEPTNGLD-------IPTIDSLADAINEfnggVVVVSHDFRLLDKIAQDIFVV 585
Cdd:PRK13638 144 RVAIAGALVLQARYLLLDEPTAGLDpagrtqmIAIIRRIVAQGNH----VIISSHDIDLIYEISDAVYVL 209
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
414-579 |
2.63e-12 |
|
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: 66.62 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 414 LNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGR--VSRHthvklgvysqhsqdqlDLTKSALEfVRDKYSNISQD 491
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatVAGH----------------DVVREPRE-VRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 492 FQFWRGQLGR---------YGLTG-----------------EGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNG 545
Cdd:cd03265 82 LSVDDELTGWenlyiharlYGVPGaerreridelldfvgllEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 285811661 546 LDIPTIDSLADAIN----EFNGGVVVVSHDF----RLLDKIA 579
Cdd:cd03265 162 LDPQTRAHVWEYIEklkeEFGMTILLTTHYMeeaeQLCDRVA 203
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
412-595 |
2.69e-12 |
|
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: 66.62 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 412 EHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSrhthvklgvysqhsQDQLDLTKSALEfVRDKYSNISQD 491
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT--------------VDGFDVVKEPAE-ARRRLGFVSDS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 492 FQFW-----RGQL----GRYGLTGEGQT-----------------VQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNG 545
Cdd:cd03266 87 TGLYdrltaRENLeyfaGLYGLKGDELTarleeladrlgmeelldRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 285811661 546 LDIPTIDSLADAINEFNGG---VVVVSHdfrLLDKIAQ--DIFVVENKTATRWDG 595
Cdd:cd03266 167 LDVMATRALREFIRQLRALgkcILFSTH---IMQEVERlcDRVVVLHRGRVVYEG 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
392-597 |
2.82e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.03 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 392 VLAFDDISFHyesnpsenlyehlnfgVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVK------LGVYSQ 465
Cdd:COG1134 39 FWALKDVSFE----------------VERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSallelgAGFHPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 466 HSQDQ--------LDLTKsalEFVRDKYSNIsQDFqfwrGQLGRYGLTgegqtvQMATLSEGQRSRVVFAL-LALEqPNV 536
Cdd:COG1134 103 LTGREniylngrlLGLSR---KEIDEKFDEI-VEF----AELGDFIDQ------PVKTYSSGMRARLAFAVaTAVD-PDI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 285811661 537 LLLDEPTNGLDIPTIDSLADAINEF---NGGVVVVSHDFRLLDKIAQDIFVVENKTAtRWDGSI 597
Cdd:COG1134 168 LLVDEVLAVGDAAFQKKCLARIRELresGRTVIFVSHSMGAVRRLCDRAIWLEKGRL-VMDGDP 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
410-570 |
2.96e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.98 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 410 LYEHLNFGV---DMdsrIALVGPNGVGKSTLLKIMTGELTPQSGRVS---------RHT-HVKL-------GVYSqhsqd 469
Cdd:PRK13538 16 LFSGLSFTLnagEL---VQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepirrqRDEyHQDLlylghqpGIKT----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 470 qlDLTksALEFVRdKYSNISQ---DFQFWRGqLGRYGLTGEgQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGL 546
Cdd:PRK13538 88 --ELT--ALENLR-FYQRLHGpgdDEALWEA-LAQVGLAGF-EDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|....*..
gi 285811661 547 DIPTIDSLADAINEF--NGGVVVV-SH 570
Cdd:PRK13538 161 DKQGVARLEALLAQHaeQGGMVILtTH 187
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
393-579 |
2.99e-12 |
|
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: 66.00 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS----RHTHV---------- 458
Cdd:cd03259 1 LELKGLSKTYGSVR---ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILidgrDVTGVpperrnigmv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 459 ---------------------KLGVYSQHSQDQLDLtksALEFVRDkysnisqdfqfwRGQLGRYgltgegqtvqMATLS 517
Cdd:cd03259 78 fqdyalfphltvaeniafglkLRGVPKAEIRARVRE---LLELVGL------------EGLLNRY----------PHELS 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 518 EGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSL----ADAINEFNGGVVVVSHD----FRLLDKIA 579
Cdd:cd03259 133 GGQQQRVALARALAREPSLLLLDEPLSALDAKLREELreelKELQRELGITTIYVTHDqeeaLALADRIA 202
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
376-588 |
3.21e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 69.37 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 376 KVFSF--RFPQVER----LPPPV---LAFDDISFHYESNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELT 446
Cdd:TIGR00958 453 KVFEYldRKPNIPLtgtlAPLNLeglIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQ 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 447 PQSGRV-------------SRHTHVKL-----GVYSQHSQDQL--DLTKSALEFVRD--KYSN----ISQDFQFWRGQLG 500
Cdd:TIGR00958 533 PTGGQVlldgvplvqydhhYLHRQVALvgqepVLFSGSVRENIayGLTDTPDEEIMAaaKAANahdfIMEFPNGYDTEVG 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 501 RYGltgegqtVQMatlSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGGVVVVSHDFRLLDKIAQ 580
Cdd:TIGR00958 613 EKG-------SQL---SGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQ 682
|
....*...
gi 285811661 581 DIFVVENK 588
Cdd:TIGR00958 683 ILVLKKGS 690
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
91-284 |
3.59e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 68.32 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 91 FHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDEPAEPSELSALDYVVteaQHELKRIE 170
Cdd:PRK11607 29 FDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMF---QSYALFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 171 DLVEKTIledgpesellePLYERMDSLDPDTFESRAAIILiGLGFNKKTILKKTKDMSGGWKMRVALAKALFVKPTLLLL 250
Cdd:PRK11607 106 MTVEQNI-----------AFGLKQDKLPKAEIASRVNEML-GLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 285811661 251 DDPTAHLD--LEACVWLE--EYLKRFDRTLVLVSHSQD 284
Cdd:PRK11607 174 DEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQE 211
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
81-305 |
4.02e-12 |
|
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: 69.02 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 81 DIKLSSVSLLFH-GKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALAtREYPiPEHIDIYLLDEPaepseLSALD--- 156
Cdd:COG4988 336 SIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL-GFLP-PYSGSILINGVD-----LSDLDpas 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 157 ------YVvteAQHELkriedLVEKTILE-------DGPESELLEPL-----YERMDSLdPDTFESRaaiilIGL-GFNk 217
Cdd:COG4988 409 wrrqiaWV---PQNPY-----LFAGTIREnlrlgrpDASDEELEAALeaaglDEFVAAL-PDGLDTP-----LGEgGRG- 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 218 ktilkktkdMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDL--EACVW--LEEYLKrfDRTLVLVSHSQDFLNgVCTNM 293
Cdd:COG4988 474 ---------LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAetEAEILqaLRRLAK--GRTVILITHRLALLA-QADRI 541
|
250
....*....|..
gi 285811661 294 IDMRAQKLTAYG 305
Cdd:COG4988 542 LVLDDGRIVEQG 553
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
102-281 |
4.07e-12 |
|
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: 69.02 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 102 LELNYGRRYGLLGENGCGKSTFLKALaTREYPiPEHIDIYLLDEPAE---PSELSALDYVVTEAQHelkriedLVEKTIL 178
Cdd:COG4987 356 LTLPPGERVAIVGPSGSGKSTLLALL-LRFLD-PQSGSITLGGVDLRdldEDDLRRRIAVVPQRPH-------LFDTTLR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 179 E-------DGPESEL--------LEPLYERMdsldPDTFESRaaiiLIGLGFNkktilkktkdMSGGWKMRVALAKALFV 243
Cdd:COG4987 427 EnlrlarpDATDEELwaalervgLGDWLAAL----PDGLDTW----LGEGGRR----------LSGGERRRLALARALLR 488
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 285811661 244 KPTLLLLDDPTAHLD--LEACVW--LEEYLKrfDRTLVLVSH 281
Cdd:COG4987 489 DAPILLLDEPTEGLDaaTEQALLadLLEALA--GRTVLLITH 528
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
390-570 |
4.08e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 390 PPVLAFDDISFhyeSNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTH-VKLGVYSQHSQ 468
Cdd:PRK13543 9 PPLLAAHALAF---SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtATRGDRSRFMA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 469 -----DQLDLTKSALEfvrdkysnisqDFQFWRGQLGRY------------GLTGEGQTVqMATLSEGQRSRVVFALLAL 531
Cdd:PRK13543 86 ylghlPGLKADLSTLE-----------NLHFLCGLHGRRakqmpgsalaivGLAGYEDTL-VRQLSAGQKKRLALARLWL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 285811661 532 EQPNVLLLDEPTNGLDIPTIDSLADAINEF---NGGVVVVSH 570
Cdd:PRK13543 154 SPAPLWLLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTH 195
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
424-586 |
4.73e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVSrhTHVKLGVYSQHSQDQLDLTksalefVRDKYSNISQDF--QFWRGQLGR 501
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--PELKISYKPQYIKPDYDGT------VEDLLRSITDDLgsSYYKSEIIK 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 502 -YGLTgEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAIN----EFNGGVVVVSHDFRLLD 576
Cdd:PRK13409 440 pLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRriaeEREATALVVDHDIYMID 518
|
170
....*....|
gi 285811661 577 KIAQDIFVVE 586
Cdd:PRK13409 519 YISDRLMVFE 528
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
393-587 |
4.85e-12 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 66.10 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYesNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVsrhthvklgvysqhSQDQLD 472
Cdd:cd03253 1 IEFENVTFAY--DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSI--------------LIDGQD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 LTKSALEFVRDKYSNISQDFQFWRGQLG---RYG-LTGEGQTVQMAT--------------------------LSEGQRS 522
Cdd:cd03253 65 IREVTLDSLRRAIGVVPQDTVLFNDTIGyniRYGrPDATDEEVIEAAkaaqihdkimrfpdgydtivgerglkLSGGEKQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 285811661 523 RVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGG--VVVVSHdfRLLDKIAQD-IFVVEN 587
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAH--RLSTIVNADkIIVLKD 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
82-282 |
5.96e-12 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 65.66 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEhidiylldEPAE------PSELSAL 155
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPG--------APDEgevlldGKDIYDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 156 DYVVTEaqheLKR-------IEDLVEKTILED---GPesellePLYERMDSLDPDTfESRAAIILIGLGFNKKTILKKTk 225
Cdd:cd03260 73 DVDVLE----LRRrvgmvfqKPNPFPGSIYDNvayGL------RLHGIKLKEELDE-RVEEALRKAALWDEVKDRLHAL- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 226 DMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF--DRTLVLVSHS 282
Cdd:cd03260 141 GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
111-305 |
6.25e-12 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 65.39 E-value: 6.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 111 GLLGENGCGKSTFLKALATREYPIPEHIDI--YLLDEPAE----PSELSALDYVVTEAQ---HeLKRIEDLVEKTiledg 181
Cdd:cd03297 27 GIFGASGAGKSTLLRCIAGLEKPDGGTIVLngTVLFDSRKkinlPPQQRKIGLVFQQYAlfpH-LNVRENLAFGL----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 182 peselleplyeRMDSLDPDTFESRAAIILIGLGfnkKTILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLD--- 258
Cdd:cd03297 101 -----------KRKRNREDRISVDELLDLLGLD---HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDral 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 285811661 259 -LEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYG 305
Cdd:cd03297 167 rLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
414-603 |
6.65e-12 |
|
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: 65.82 E-value: 6.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 414 LNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRhthvklgvysqhsqDQLDLT-----KSALEFVRDKYS-- 486
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL--------------NGKDITnlppeKRDISYVPQNYAlf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 487 ---NISQDFQFWRGQLGRYGLTGEGQTVQMA--------------TLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIP 549
Cdd:cd03299 84 phmTVYKNIAYGLKKRKVDKKEIERKVLEIAemlgidhllnrkpeTLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 285811661 550 T----IDSLADAINEFNGGVVVVSHDFrlldkiaQDIFVVENKTATRWDGSILQYKNK 603
Cdd:cd03299 164 TkeklREELKKIRKEFGVTVLHVTHDF-------EEAWALADKVAIMLNGKLIQVGKP 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
424-547 |
7.28e-12 |
|
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: 64.91 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVSRhthvklgvysqhsqDQLDLTKSALEFvRDKYSNISQDFQFW-------- 495
Cdd:cd03264 28 YGLLGPNGAGKTTLMRILATLTPPSSGTIRI--------------DGQDVLKQPQKL-RRRIGYLPQEFGVYpnftvref 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 496 -------------------RGQLGRYGLTGEGQTvQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLD 547
Cdd:cd03264 93 ldyiawlkgipskevkarvDEVLELVNLGDRAKK-KIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
334-587 |
7.77e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.93 E-value: 7.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 334 QHIKKFIASAgtyanlvkqaksrQKILDKMEADGLVQpvvpdkvfsFRFPQVERLPPPVLAFDDISFHYESNPSENLyEH 413
Cdd:PRK11160 302 QHLGQVIASA-------------RRINEITEQKPEVT---------FPTTSTAAADQVSLTLNNVSFTYPDQPQPVL-KG 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 414 LNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVsRHTHVKLGVYSQH---------SQ----------DQLDL- 473
Cdd:PRK11160 359 LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI-LLNGQPIADYSEAalrqaisvvSQrvhlfsatlrDNLLLa 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 474 ----TKSALEFVRDK--YSNISQDFQ---FWRGQLGRygltgegqtvqmaTLSEGQRSRVVFALLALEQPNVLLLDEPTN 544
Cdd:PRK11160 438 apnaSDEALIEVLQQvgLEKLLEDDKglnAWLGEGGR-------------QLSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 285811661 545 GLDIPTIDSLADAINEFNGG--VVVVSHDFRLLDKIAQdIFVVEN 587
Cdd:PRK11160 505 GLDAETERQILELLAEHAQNktVLMITHRLTGLEQFDR-ICVMDN 548
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
424-590 |
9.74e-12 |
|
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: 65.51 E-value: 9.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVSRHThVKLGVYSQHSQDQLDLTksalefVRDKYSNISQDF---QFWRGQ-- 498
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL-DTVSYKPQYIKADYEGT------VRDLLSSITKDFythPYFKTEia 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 499 --LGRYGLTGEgqtvQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEF----NGGVVVVSHDF 572
Cdd:cd03237 101 kpLQIEQILDR----EVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHDI 176
|
170
....*....|....*...
gi 285811661 573 RLLDKIAQDIFVVENKTA 590
Cdd:cd03237 177 IMIDYLADRLIVFEGEPS 194
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
94-281 |
1.20e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.48 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 94 KVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPipEHIDIYLLDEPaepseLSALDyvvTEAQHELKRIEDLV 173
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESP--SQGNVSWRGEP-----LAKLN---RAQRKAFRRDIQMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 174 ----------EKTILEDgpeseLLEPLyERMDSLDPDTFESRAAIILIGLGFNKKTILKKTKDMSGGWKMRVALAKALFV 243
Cdd:PRK10419 95 fqdsisavnpRKTVREI-----IREPL-RHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 285811661 244 KPTLLLLDDPTAHLDL----EACVWLEEYLKRFDRTLVLVSH 281
Cdd:PRK10419 169 EPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITH 210
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
395-586 |
1.36e-11 |
|
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: 64.87 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 395 FDDISFHYESNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVsrhthvklgvysqhSQDQLDLT 474
Cdd:cd03249 3 FKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEI--------------LLDGVDIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 475 KSALEFVRDKYSNISQDFQFWRGQLG---RYGLTGEGQTVQMA---------------------------TLSEGQRSRV 524
Cdd:cd03249 69 DLNLRWLRSQIGLVSQEPVLFDGTIAeniRYGKPDATDEEVEEaakkanihdfimslpdgydtlvgergsQLSGGQKQRI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 525 VFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGG--VVVVSHdfRLL-----DKIA--QDIFVVE 586
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGrtTIVIAH--RLStirnaDLIAvlQNGQVVE 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
395-586 |
1.38e-11 |
|
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: 64.41 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 395 FDDISFHYESNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV-----------SRHTHVKLGVY 463
Cdd:cd03248 14 FQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldgkpisqyeHKYLHSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 464 SQHS-------QDQLD--LTKSALEFVRDKYSNISQDFQFWRGQLGRYGLTGEgqtvQMATLSEGQRSRVVFALLALEQP 534
Cdd:cd03248 94 GQEPvlfarslQDNIAygLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGE----KGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 285811661 535 NVLLLDEPTNGLDIPTIDSLADAINEFNGG--VVVVSHDFRLLDKiAQDIFVVE 586
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERrtVLVIAHRLSTVER-ADQILVLD 222
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
77-291 |
1.53e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 77 ETSRDIK----LSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHI------DIYLLDEP 146
Cdd:PRK11147 311 EASRSGKivfeMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklEVAYFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 147 AEpselsALDyvvteaqhELKRIEDLV---EKTILEDGPESELLEPLyerMDSLdpdtfesraaiiliglgFNKKTILKK 223
Cdd:PRK11147 391 RA-----ELD--------PEKTVMDNLaegKQEVMVNGRPRHVLGYL---QDFL-----------------FHPKRAMTP 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 224 TKDMSGGWKMRVALAKaLFVKPT-LLLLDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCT 291
Cdd:PRK11147 438 VKALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVT 505
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
408-589 |
1.65e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 408 ENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGEL--TPQSGRVSrhthVKLGVYSQHSQ--DQLDLTKSALEFV-- 481
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVD----VPDNQFGREASliDAIGRKGDFKDAVel 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 482 --RDKYSnisqDFQFWRGqlgRYgltgegqtvqmATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLA---- 555
Cdd:COG2401 119 lnAVGLS----DAVLWLR---RF-----------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVArnlq 180
|
170 180 190
....*....|....*....|....*....|....
gi 285811661 556 DAINEFNGGVVVVSHDFRLLDKIAQDIFVVENKT 589
Cdd:COG2401 181 KLARRAGITLVVATHHYDVIDDLQPDLLIFVGYG 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
390-587 |
1.72e-11 |
|
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: 64.23 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 390 PPVLAFDDISFHYesNPSENLyehlnFGVDMD----SRIALVGPNGVGKSTLLKIMTGELTPQSGRVS--------RHTH 457
Cdd:COG0410 1 MPMLEVENLHAGY--GGIHVL-----HGVSLEveegEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgeditgLPPH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 458 --VKLGVySQHSQD-QL--DLTksalefVRDkysNIsqdfqfwrgQLGRYGLTGEGQTV------------------QMA 514
Cdd:COG0410 74 riARLGI-GYVPEGrRIfpSLT------VEE---NL---------LLGAYARRDRAEVRadlervyelfprlkerrrQRA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 515 -TLSEGQR-----SRvvfALLAleQPNVLLLDEPTNGLDIPTIDSLADAINEFNG---GVVVVSHDFRLLDKIAQDIFVV 585
Cdd:COG0410 135 gTLSGGEQqmlaiGR---ALMS--RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRegvTILLVEQNARFALEIADRAYVL 209
|
..
gi 285811661 586 EN 587
Cdd:COG0410 210 ER 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
97-305 |
1.91e-11 |
|
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: 64.15 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 97 IQDSGLELNYGRRYGLLGENGCGKSTFLKALAtREYpIPEH-------IDIYLLDepaePSELSA-LDYVVTEAQhelkr 168
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLA-GLY-KPTSgsvlldgTDIRQLD----PADLRRnIGYVPQDVT----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 169 iedLVEKTILE-------DGPESELLEPLyeRMDSLD------PDTFEsraaiILIG-LGFNkktilkktkdMSGGWKMR 234
Cdd:cd03245 89 ---LFYGTLRDnitlgapLADDERILRAA--ELAGVTdfvnkhPNGLD-----LQIGeRGRG----------LSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 235 VALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF--DRTLVLVSHSQDFLNgVCTNMIDMRAQKLTAYG 305
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
82-285 |
2.00e-11 |
|
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: 64.05 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHG----KVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYP-----IPEHIDIYLLDEpaepSEL 152
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPtsgevRVDGTDISKLSE----KEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 153 SAL-----DYVVTeaQHELkrIEDLvekTILEDgpeseLLEPLyeRMDSLDPDTFESRAAIILIGLGFNKKtILKKTKDM 227
Cdd:cd03255 77 AAFrrrhiGFVFQ--SFNL--LPDL---TALEN-----VELPL--LLAGVPKKERRERAEELLERVGLGDR-LNHYPSEL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEAC--VW--LEEYLKRFDRTLVLVSHSQDF 285
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGkeVMelLRELNKEAGTTIVVVTHDPEL 203
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
83-281 |
2.20e-11 |
|
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: 63.71 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 83 KLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALA---TreypiPEHIDIYLLDEPAEpSELSALDYVv 159
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILgllK-----PTSGSIRVFGKPLE-KERKRIGYV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 160 teAQHELK------RIEDLVektiledgpeselLEPLYERMDSLDPDTFESRAAII----LIGL-GFNKKTIlkktKDMS 228
Cdd:cd03235 74 --PQRRSIdrdfpiSVRDVV-------------LMGLYGHKGLFRRLSKADKAKVDealeRVGLsELADRQI----GELS 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 285811661 229 GGWKMRVALAKALFVKPTLLLLDDPTAHLDLEAC---VWLEEYLKRFDRTLVLVSH 281
Cdd:cd03235 135 GGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQediYELLRELRREGMTILVVTH 190
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
228-284 |
2.23e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 65.55 E-value: 2.23e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLD------LEAcvWLEEYLKRFDRTLVLVSHSQD 284
Cdd:COG1118 135 SGGQRQRVALARALAVEPEVLLLDEPFGALDakvrkeLRR--WLRRLHDELGGTTVFVTHDQE 195
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
412-587 |
2.37e-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: 63.45 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 412 EHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV----------SRHTHVKL----GVYSQHS-QDQL----- 471
Cdd:cd03269 17 DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdgkpldiaARNRIGYLpeerGLYPKMKvIDQLvylaq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 472 --DLTKS-ALEFVRDkysnisqdfqfWrgqLGRYGLtGEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDI 548
Cdd:cd03269 97 lkGLKKEeARRRIDE-----------W---LERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 285811661 549 PTIDSLADAINEFNGG---VVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:cd03269 162 VNVELLKDVIRELARAgktVILSTHQMELVEELCDRVLLLNK 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
99-284 |
3.05e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 64.75 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 99 DSGLELNYGRRYGLLGENGCGKSTFLkalatreypipEHIDIYLldEPAEPSeLSALDYVVTEA--QHELKRIEDLVekT 176
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLL-----------QHLNGLL--QPTEGK-VTVGDIVVSSTskQKEIKPVRKKV--G 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 177 ILEDGPESELLEPLYERMDSLDPDTF-------ESRAAIILIGLGFNKKTILKKTKDMSGGWKMRVALAKALFVKPTLLL 249
Cdd:PRK13643 88 VVFQFPESQLFEETVLKDVAFGPQNFgipkekaEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 285811661 250 LDDPTAHLDLEACVwleEYLKRFD------RTLVLVSHSQD 284
Cdd:PRK13643 168 LDEPTAGLDPKARI---EMMQLFEsihqsgQTVVLVTHLMD 205
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
82-282 |
3.63e-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: 63.96 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGK----VLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATreypipehidiylLDEPAEpSELSALDY 157
Cdd:COG1116 8 LELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG-------------LEKPTS-GEVLVDGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 158 VVTEAQHEL------------KRIEDLVEktiledgpeselLePLyeRMDSLDPDTFESRA--AIILIGL-GFNKKtilk 222
Cdd:COG1116 74 PVTGPGPDRgvvfqepallpwLTVLDNVA------------L-GL--ELRGVPKAERRERAreLLELVGLaGFEDA---- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285811661 223 KTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLD------LEAcvWLEEYLKRFDRTLVLVSHS 282
Cdd:COG1116 135 YPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDaltrerLQD--ELLRLWQETGKTVLFVTHD 198
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
414-607 |
3.72e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.99 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 414 LNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS-----------RHTHVKLGVYSQHSQDQLdltksaleFVr 482
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvmgrevnaeneKWVRSKVGLVFQDPDDQV--------FS- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 483 dkySNISQDFQFWRGQLgryGLTGEG---------QTVQMAT--------LSEGQRSRVVFA-LLALEqPNVLLLDEPTN 544
Cdd:PRK13647 95 ---STVWDDVAFGPVNM---GLDKDEverrveealKAVRMWDfrdkppyhLSYGQKKRVAIAgVLAMD-PDVIVLDEPMA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 285811661 545 GLDIPTIDSLADAINEFNGG---VVVVSHDFRLLDKIAQDIFVV-ENKTATRWDGSILQYKNKLAKN 607
Cdd:PRK13647 168 YLDPRGQETLMEILDRLHNQgktVIVATHDVDLAAEWADQVIVLkEGRVLAEGDKSLLTDEDIVEQA 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
391-582 |
4.22e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.30 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 391 PVLAFDDISFHY-ESNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVsrhthvklgVYSQHSQD 469
Cdd:PRK11629 4 ILLQCDNLCKRYqEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV---------IFNGQPMS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 470 QL------DLTKSALEFVRdKYSNISQDF---------------------QFWRGQLGRYGLTGEGQTvQMATLSEGQRS 522
Cdd:PRK11629 75 KLssaakaELRNQKLGFIY-QFHHLLPDFtalenvamplligkkkpaeinSRALEMLAAVGLEHRANH-RPSELSGGERQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 285811661 523 RVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFN----GGVVVVSHDFRLLDKIAQDI 582
Cdd:PRK11629 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHDLQLAKRMSRQL 216
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
54-281 |
4.25e-11 |
|
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: 66.01 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 54 MMKLQQDKDGLSDRVVTGVLSSletsrDIKLSSVSllF----HGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALAt 129
Cdd:COG2274 451 ILDLPPEREEGRSKLSLPRLKG-----DIELENVS--FrypgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 130 REYPiPEH-------IDIYLLDepaePSEL-SALDYVVTEAQhelkriedLVEKTILEDgpesellepLyeRMDSLDPDT 201
Cdd:COG2274 523 GLYE-PTSgrilidgIDLRQID----PASLrRQIGVVLQDVF--------LFSGTIREN---------I--TLGDPDATD 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 202 FESRAAIILIGL---------GFNkkTILKKT-KDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLD--LEACVWleEYL 269
Cdd:COG2274 579 EEIIEAARLAGLhdfiealpmGYD--TVVGEGgSNLSGGQRQRLAIARALLRNPRILILDEATSALDaeTEAIIL--ENL 654
|
250
....*....|....
gi 285811661 270 KRF--DRTLVLVSH 281
Cdd:COG2274 655 RRLlkGRTVIIIAH 668
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
391-575 |
4.83e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.41 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 391 PVLAFDDISFhyESNPSENLyehlnfgvdmdsriALVGPNGVGKSTLLKIMTGELTPQSGRVS----------------- 453
Cdd:PRK11701 18 PRKGCRDVSF--DLYPGEVL--------------GIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdgqlrdlyalsea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 454 --RHTH-VKLGVYSQHSQDQLDLTKSA-------LEFVRDK-YSNISQDFQFWrgqLGRYGLTGEGQTVQMATLSEGQRS 522
Cdd:PRK11701 82 erRRLLrTEWGFVHQHPRDGLRMQVSAggnigerLMAVGARhYGDIRATAGDW---LERVEIDAARIDDLPTTFSGGMQQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 523 RVVFALLALEQPNVLLLDEPTNGLDIPT----IDSLADAINEFNGGVVVVSHDF---RLL 575
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVqarlLDLLRGLVRELGLAVVIVTHDLavaRLL 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
410-596 |
5.22e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.06 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 410 LYEHL----NFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV----SRHTH-------VKL-----GVYSQHSQD 469
Cdd:PRK10771 10 LYHHLpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngQDHTTtppsrrpVSMlfqenNLFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 470 Q---------LDLTKSALEFVRDKYSNISQDFQFWRgqlgrygLTGEgqtvqmatLSEGQRSRVVFA-LLALEQPnVLLL 539
Cdd:PRK10771 90 QniglglnpgLKLNAAQREKLHAIARQMGIEDLLAR-------LPGQ--------LSGGQRQRVALArCLVREQP-ILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 540 DEPTNGLDiPT-----IDSLADAINEFNGGVVVVSHDFRLLDKIA-QDIFVVENKTAtrWDGS 596
Cdd:PRK10771 154 DEPFSALD-PAlrqemLTLVSQVCQERQLTLLMVSHSLEDAARIApRSLVVADGRIA--WDGP 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
82-281 |
5.22e-11 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 63.18 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALAtREYPiPEHIDIYLLDEPAEPSE---------- 151
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIL-GLLP-PTSGTVRLFGKPPRRARrrigyvpqra 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 152 -------LSALDYVVTEAQHEL-------KRIEDLVEKTIledgpeselleplyERMDSLDpdtFESRaaiiLIGlgfnk 217
Cdd:COG1121 85 evdwdfpITVRDVVLMGRYGRRglfrrpsRADREAVDEAL--------------ERVGLED---LADR----PIG----- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 285811661 218 ktilkktkDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF---DRTLVLVSH 281
Cdd:COG1121 139 --------ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrreGKTILVVTH 197
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
425-571 |
5.44e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.18 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 425 ALVGPNGVGKSTLLKIMTGELTPQSGRVS------RHTHV-----KLGVYSQHSQDQLDLTksalefVRDKYSnisqdfq 493
Cdd:COG4604 31 ALIGPNGAGKSTLLSMISRLLPPDSGEVLvdgldvATTPSrelakRLAILRQENHINSRLT------VRELVA------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 494 fwrgqLGRY----G-LTGEGQT-VQMA---------------TLSEGQRSRvvfALLAL---EQPNVLLLDEPTNGLDI- 548
Cdd:COG4604 98 -----FGRFpyskGrLTAEDREiIDEAiayldledladryldELSGGQRQR---AFIAMvlaQDTDYVLLDEPLNNLDMk 169
|
170 180
....*....|....*....|....*....
gi 285811661 549 ------PTIDSLADainEFNGGVVVVSHD 571
Cdd:COG4604 170 hsvqmmKLLRRLAD---ELGKTVVIVLHD 195
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
390-584 |
1.03e-10 |
|
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: 60.52 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 390 PPVLAFDDISFHYESNpsenlyEHLnfgvdmdsriALVGPNGVGKSTLLKIMTGELTPQSGRVsrhthvklgvysqhsqd 469
Cdd:cd03216 11 GGVKALDGVSLSVRRG------EVH----------ALLGENGAGKSTLMKILSGLYKPDSGEI----------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 470 qldltksalefvrdkysnisqdfqFWRGQLGRYGLTGEGQTVQMAT---LSEGQRSRVVFALLALEQPNVLLLDEPTNGL 546
Cdd:cd03216 58 ------------------------LVDGKEVSFASPRDARRAGIAMvyqLSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 285811661 547 DIPTIDSLADAINEF--NG-GVVVVSHDFRLLDKIAQDIFV 584
Cdd:cd03216 114 TPAEVERLFKVIRRLraQGvAVIFISHRLDEVFEIADRVTV 154
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
424-578 |
1.05e-10 |
|
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: 61.41 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPqsgrvsrhTHVKLGVYSQHSQDQLDLTKSALEFVRdkysnisQDFQFwrgqLGRyg 503
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALAGRRTG--------LGVSGEVLINGRPLDKRSFRKIIGYVP-------QDDIL----HPT-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 504 LTGEgQTVQMAT----LSEGQRSRVVFALLALEQPNVLLLDEPTNGLD-------IPTIDSLADAinefNGGVVVVSH-- 570
Cdd:cd03213 97 LTVR-ETLMFAAklrgLSGGERKRVSIALELVSNPSLLFLDEPTSGLDsssalqvMSLLRRLADT----GRTIICSIHqp 171
|
170
....*....|.
gi 285811661 571 ---DFRLLDKI 578
Cdd:cd03213 172 sseIFELFDKL 182
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
423-572 |
1.13e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.17 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 423 RIALVGPNGVGKSTLLKIMTGeLTPQSGRV-------SRHTHVKLGVY-SQHSQDQ-----------LDL---TKSALEF 480
Cdd:COG4138 24 LIHLIGPNGAGKSTLLARMAG-LLPGQGEIllngrplSDWSAAELARHrAYLSQQQsppfampvfqyLALhqpAGASSEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 481 VRDKYSNISQDFQFwRGQLGRygltgegqtvQMATLSEG--QRSRVVFALLAL-----EQPNVLLLDEPTNGLDIP---T 550
Cdd:COG4138 103 VEQLLAQLAEALGL-EDKLSR----------PLTQLSGGewQRVRLAAVLLQVwptinPEGQLLLLDEPMNSLDVAqqaA 171
|
170 180
....*....|....*....|..
gi 285811661 551 IDSLADAINEFNGGVVVVSHDF 572
Cdd:COG4138 172 LDRLLRELCQQGITVVMSSHDL 193
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
413-589 |
1.18e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 62.31 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 413 HLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSG---------------RVSRH------THVKLG---------V 462
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGtillrgqhieglpghQIARMgvvrtfQHVRLFremtvienlL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 463 YSQHSQDQLDLTKSALE---FVRDKYSNISQDfQFWrgqLGRYGLTgEGQTVQMATLSEGQRSRVVFALLALEQPNVLLL 539
Cdd:PRK11300 103 VAQHQQLKTGLFSGLLKtpaFRRAESEALDRA-ATW---LERVGLL-EHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 285811661 540 DEPTNGLDIPTIDSLADAI----NEFNGGVVVVSHDFRLLDKIAQDIFVVENKT 589
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIaelrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
389-577 |
1.63e-10 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 61.30 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 389 PPPVLAFDDISFHYESNPSE-NLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS-------------- 453
Cdd:COG4181 5 SAPIIELRGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRlagqdlfaldedar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 454 ---RHTHVklGVYSQHSqdQLDLTKSALEFV---------RDkysnisqDFQFWRGQLGRYGLtGEGQTVQMATLSEGQR 521
Cdd:COG4181 85 arlRARHV--GFVFQSF--QLLPTLTALENVmlplelagrRD-------ARARARALLERVGL-GHRLDHYPAQLSGGEQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 522 SRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNG--GV--VVVSHDFRLLDK 577
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRerGTtlVLVTHDPALAAR 212
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
414-571 |
1.69e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 414 LNFGVDMDSRIALVGPNGVGKSTLLKIMTGeLTPQSGRV-------SRHTHVKLGVYSQH-SQDQ-----------LDL- 473
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIqfagqplEAWSAAELARHRAYlSQQQtppfampvfqyLTLh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 474 --TKSALEFVRDKYSNISQDFQFwRGQLGRygltgegqTVQmaTLSEG--QRSRVVFALLALE---QPN--VLLLDEPTN 544
Cdd:PRK03695 94 qpDKTRTEAVASALNEVAEALGL-DDKLGR--------SVN--QLSGGewQRVRLAAVVLQVWpdiNPAgqLLLLDEPMN 162
|
170 180 190
....*....|....*....|....*....|
gi 285811661 545 GLDIP---TIDSLADAINEFNGGVVVVSHD 571
Cdd:PRK03695 163 SLDVAqqaALDRLLSELCQQGIAVVMSSHD 192
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
82-284 |
1.74e-10 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 61.59 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPipEHIDIYLLDEPAepSELSALDYVVTE 161
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERP--DSGTILFGGEDA--TDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 162 A-QH-ELKR---IED-----LVEKTILEDGPESELLEPLYERMDSLDPDTFESRAAiiliglgfnkktilkktKDMSGGW 231
Cdd:cd03296 79 VfQHyALFRhmtVFDnvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYP-----------------AQLSGGQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 285811661 232 KMRVALAKALFVKPTLLLLDDPTAHLDL----EACVWLEEYLKRFDRTLVLVSHSQD 284
Cdd:cd03296 142 RQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQE 198
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
391-588 |
1.95e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 61.69 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 391 PVLAFDDISFHYESNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVsrhthvklgVYSQHSQDQ 470
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI---------FYNNQAITD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 471 LDLTKsalefVRDKYSNISQ--DFQFwRGQLGRY----GLtgEGQTV------------------------QMATLSEGQ 520
Cdd:PRK13648 76 DNFEK-----LRKHIGIVFQnpDNQF-VGSIVKYdvafGL--ENHAVpydemhrrvsealkqvdmleradyEPNALSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 521 RSRVVFA-LLALeQPNVLLLDEPTNGLDIPTIDSLADAINEF----NGGVVVVSHDfrLLDKIAQDIFVVENK 588
Cdd:PRK13648 148 KQRVAIAgVLAL-NPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITHD--LSEAMEADHVIVMNK 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
82-284 |
2.08e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.10 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLF-----HGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLkalatreypipEHIDIYLldepaEPSELS-AL 155
Cdd:PRK13646 3 IRFDNVSYTYqkgtpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLI-----------QNINALL-----KPTTGTvTV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 156 DYVVTEAQHELKRIEDLVEKT-ILEDGPESELLEPLYERMDSLDPDTF-------ESRAAIILIGLGFNKKTILKKTKDM 227
Cdd:PRK13646 67 DDITITHKTKDKYIRPVRKRIgMVFQFPESQLFEDTVEREIIFGPKNFkmnldevKNYAHRLLMDLGFSRDVMSQSPFQM 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF----DRTLVLVSHSQD 284
Cdd:PRK13646 147 SGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqtdeNKTIILVSHDMN 207
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
228-281 |
2.37e-10 |
|
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: 59.54 E-value: 2.37e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFD---RTLVLVSH 281
Cdd:cd03246 98 SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAH 154
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
94-284 |
2.38e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.99 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 94 KVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHI---DIYLLDEPAEPSEL-SALDYVVTEAQHELkrI 169
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidGVDITDKKVKLSDIrKKVGLVFQYPEYQL--F 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 170 EDLVEKTIlEDGP------ESELLEPLYERMD--SLDPDTFESRAAIiliglgfnkktilkktkDMSGGWKMRVALAKAL 241
Cdd:PRK13637 98 EETIEKDI-AFGPinlglsEEEIENRVKRAMNivGLDYEDYKDKSPF-----------------ELSGGQKRRVAIAGVV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 285811661 242 FVKPTLLLLDDPTAHLDLEAcvwLEEYL-------KRFDRTLVLVSHSQD 284
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKG---RDEILnkikelhKEYNMTIILVSHSME 206
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
392-579 |
2.57e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.67 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 392 VLAFDDISFHYESNP---SENLYEhLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV----------SRHTHV 458
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfaSRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvsstSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 459 K-----LGVYSQHSQDQLdLTKSALEFVRDKYSN--ISQDF--QFWRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFALL 529
Cdd:PRK13643 80 KpvrkkVGVVFQFPESQL-FEETVLKDVAFGPQNfgIPKEKaeKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 285811661 530 ALEQPNVLLLDEPTNGLDIPT---IDSLADAINEFNGGVVVVSHdfrLLDKIA 579
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH---LMDDVA 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
82-281 |
2.74e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.16 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATreYPIPEHIDIYLLDEPAEPSELSALDYVVTE 161
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILG--MTSPDAGKITVLGVPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 162 AQHELKRIEDLVEKTILEDGPeselleplYERMDsldpdTFESRAAI-ILIGLGFNKKTILKKTKDMSGGWKMRVALAKA 240
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGR--------YFGMS-----TREIEAVIpSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 285811661 241 LFVKPTLLLLDDPTAHLDLEA--CVW--LEEYLKRfDRTLVLVSH 281
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHArhLIWerLRSLLAR-GKTILLTTH 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
389-579 |
4.09e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 61.65 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 389 PPPVLAFDDISFHYESNPSenLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS----RHTHVK----- 459
Cdd:COG3842 2 AMPALELENVSKRYGDVTA--L-DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILldgrDVTGLPpekrn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 460 LGVYSQHSqdqldltksALeF----VRDkysNIsqdfqfwrgqlgRYGLTGEG--------------QTVQMA------- 514
Cdd:COG3842 79 VGMVFQDY---------AL-FphltVAE---NV------------AFGLRMRGvpkaeirarvaellELVGLEgladryp 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 285811661 515 -TLSEGQRSRVvfAL---LALEqPNVLLLDEPTNGLDIPTIDSLADAI----NEFNGGVVVVSHD----FRLLDKIA 579
Cdd:COG3842 134 hQLSGGQQQRV--ALaraLAPE-PRVLLLDEPLSALDAKLREEMREELrrlqRELGITFIYVTHDqeeaLALADRIA 207
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
425-609 |
4.50e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.89 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 425 ALVGPNGVGKSTLLKIMTGELTPQSGRVS------RHTHVKL--------GVYSQHS-QDQL-------DLTKSAlefvr 482
Cdd:COG4152 31 GLLGPNGAGKTTTIRIILGILAPDSGEVLwdgeplDPEDRRRigylpeerGLYPKMKvGEQLvylarlkGLSKAE----- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 483 dkysnISQDFQFWrgqLGRYGLTG-EGQTVQmaTLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEF 561
Cdd:COG4152 106 -----AKRRADEW---LERLGLGDrANKKVE--ELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIREL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 285811661 562 -NGGVVVV--SHDFRLLDKIAQDIFVVeNKTATRWDGSILQYKNKLAKNVV 609
Cdd:COG4152 176 aAKGTTVIfsSHQMELVEELCDRIVII-NKGRKVLSGSVDEIRRQFGRNTL 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
82-298 |
4.52e-10 |
|
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: 60.27 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLF-HGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATreypipehidiylLDEPAEpSELSALDYVVT 160
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNG-------------LVEPTS-GSVLIDGTDIN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 161 EAQH-ELKRIED----------LVEK-TILED---G--PESELLEPLYERMDSLDpdtfESRAAIILIGLGFNKKtILKK 223
Cdd:cd03256 67 KLKGkALRQLRRqigmifqqfnLIERlSVLENvlsGrlGRRSTWRSLFGLFPKEE----KQRALAALERVGLLDK-AYQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 224 TKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKR----FDRTLVLVSHSQDFLNGVCTNMIDMRA 298
Cdd:cd03256 142 ADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRinreEGITVIVSLHQVDLAREYADRIVGLKD 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
424-586 |
5.29e-10 |
|
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: 62.11 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVsrHTHVKLGVYSQHSQDQLDLTksalefVRDK-YSNISQDFQ--FWRGQLG 500
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDGT------VEEFlRSANTDDFGssYYKTEII 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 501 R-YGLTGEGQTvQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEF----NGGVVVVSHDFRLL 575
Cdd:COG1245 441 KpLGLEKLLDK-NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaenrGKTAMVVDHDIYLI 519
|
170
....*....|.
gi 285811661 576 DKIAQDIFVVE 586
Cdd:COG1245 520 DYISDRLMVFE 530
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
378-579 |
5.43e-10 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 61.98 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 378 FSFRFPQVeRLPPP--VLAFDDISFhyeSNPSENLY--EHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVs 453
Cdd:TIGR01842 301 YPSRDPAM-PLPEPegHLSVENVTI---VPPGGKKPtlRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 454 rhthvKLGVYSQHSQDQLDLTKSAlefvrdKYsnISQDFQFWRGQLG----RYGLTGEGQTVQMA--------------- 514
Cdd:TIGR01842 376 -----RLDGADLKQWDRETFGKHI------GY--LPQDVELFPGTVAeniaRFGENADPEKIIEAaklagvhelilrlpd 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 515 -----------TLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFN---GGVVVVSHDFRLL---DK 577
Cdd:TIGR01842 443 gydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITHRPSLLgcvDK 522
|
..
gi 285811661 578 IA 579
Cdd:TIGR01842 523 IL 524
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
81-284 |
5.74e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 61.27 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 81 DIKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALA--TReypiPEHIDIYLLDEP--AEPSE----- 151
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAgfET----PDSGRILLDGRDvtGLPPEkrnvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 152 -----------LSALDYV--------VTEAQhelkrIEDLVEktiledgpesELLEplyermdsldpdtfesraaiiLIG 212
Cdd:COG3842 81 mvfqdyalfphLTVAENVafglrmrgVPKAE-----IRARVA----------ELLE---------------------LVG 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 285811661 213 L-GFNKKtilkKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDL----EACVWLEEYLKRFDRTLVLVSHSQD 284
Cdd:COG3842 125 LeGLADR----YPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAklreEMREELRRLQRELGITFIYVTHDQE 197
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
383-547 |
6.92e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 61.00 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 383 PQVERLPPPVLAFDDISFHYESNPSENlyeHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS--------- 453
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKAVVN---GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvpar 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 454 -RHTHVKLGVYSQHsqDQLDLTKSALE--FVRDKYSNIS-QDFQFWRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFALL 529
Cdd:PRK13536 109 aRLARARIGVVPQF--DNLDLEFTVREnlLVFGRYFGMStREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170
....*....|....*...
gi 285811661 530 ALEQPNVLLLDEPTNGLD 547
Cdd:PRK13536 187 LINDPQLLILDEPTTGLD 204
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
388-590 |
7.07e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 60.25 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 388 LPPPVLAFDDISFHYeSNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV---------SRHTHV 458
Cdd:PRK13636 1 MEDYILKVEELNYNY-SDGTHAL-KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidySRKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 459 KL----GVYSQHSQDQL-------DLTKSALEF------VRDKYSNIsqdfqfwrgqLGRYGLTGEGQTVQMAtLSEGQR 521
Cdd:PRK13636 79 KLresvGMVFQDPDNQLfsasvyqDVSFGAVNLklpedeVRKRVDNA----------LKRTGIEHLKDKPTHC-LSFGQK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 522 SRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGG----VVVVSHDFRLLDKIAQDIFVVENKTA 590
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElgltIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
82-282 |
7.87e-10 |
|
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: 59.02 E-value: 7.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGK----VLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPipEHIDIYLLDEP-AEPSelSALD 156
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERP--TSGEVLVDGEPvTGPG--PDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 157 YVVTeaQHELkriedLVEKTILE---------DGPESELLEplyermdsldpdtfESRAAIILIGL-GFNKKTIlkktKD 226
Cdd:cd03293 77 YVFQ--QDAL-----LPWLTVLDnvalglelqGVPKAEARE--------------RAEELLELVGLsGFENAYP----HQ 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLD----LEACVWLEEYLKRFDRTLVLVSHS 282
Cdd:cd03293 132 LSGGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHD 191
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
82-281 |
8.24e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.59 E-value: 8.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPipEHIDIYLLDEPaepselsaldyVVTE 161
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHP--DAGSISLCGEP-----------VPSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 162 AQHELKRIEdlvektiledgpesellepLYERMDSLDPDtFESRAAIILIG--LGFNKKTILK----------------- 222
Cdd:PRK13537 75 ARHARQRVG-------------------VVPQFDNLDPD-FTVRENLLVFGryFGLSAAAARAlvppllefaklenkada 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 223 KTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEA--CVW--LEEYLKRfDRTLVLVSH 281
Cdd:PRK13537 135 KVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQArhLMWerLRSLLAR-GKTILLTTH 196
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
102-303 |
9.54e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 58.90 E-value: 9.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 102 LELNYGRRYGLLGENGCGKSTFLKALAtreypipehidiyLLDEPAEPS------ELSALDyvvtEAQ------------ 163
Cdd:COG1136 29 LSIEAGEFVAIVGPSGSGKSTLLNILG-------------GLDRPTSGEvlidgqDISSLS----ERElarlrrrhigfv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 164 ---HELkrIEDLvekTILEDgpeseLLEPLyeRMDSLDPDTFESRAAIIL--IGLGfNKKTilKKTKDMSGGWKMRVALA 238
Cdd:COG1136 92 fqfFNL--LPEL---TALEN-----VALPL--LLAGVSRKERRERARELLerVGLG-DRLD--HRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 239 KALFVKPTLLLLDDPTAHLDLEAC--VW--LEEYLKRFDRTLVLVSHSQDFLNgVCTNMIDMRAQKLTA 303
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGeeVLelLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVS 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
82-284 |
9.72e-10 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 58.81 E-value: 9.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREypIPEHIDIYLLDEpaepselsaldyVVTE 161
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE--EPTSGRIYIGGR------------DVTD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 162 AQHElKRIEDLV--------EKTILEDgpeseLLEPLyeRMDSLDPDTFESR----AAIILIGLGFNKKTilkktKDMSG 229
Cdd:cd03301 67 LPPK-DRDIAMVfqnyalypHMTVYDN-----IAFGL--KLRKVPKDEIDERvrevAELLQIEHLLDRKP-----KQLSG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 230 GWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR----TLVLVSHSQD 284
Cdd:cd03301 134 GQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlgtTTIYVTHDQV 192
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
84-281 |
9.78e-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: 9.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 84 LSSVSLLFHGK----VLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPipehidiylldepaEPSELSALDYVV 159
Cdd:cd03267 20 IGSLKSLFKRKyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQP--------------TSGEVRVAGLVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 160 TEAQHELKRIEDLV--EKTILE-DGPESELLEpLYERMDSLDPDTFESRAAII--LIGLGfnkkTILKK-TKDMSGGWKM 233
Cdd:cd03267 86 WKRRKKFLRRIGVVfgQKTQLWwDLPVIDSFY-LLAAIYDLPPARFKKRLDELseLLDLE----ELLDTpVRQLSLGQRM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 285811661 234 RVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR----TLVLVSH 281
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRergtTVLLTSH 212
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
94-547 |
1.06e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.18 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 94 KVLIQDSgLELNYGRRYGLLGENGCGKSTFLKALAtreypipehidiylldepaepSELSALDyvvTEAQHELKRIEDL- 172
Cdd:PRK10938 17 KTLQLPS-LTLNAGDSWAFVGANGSGKSALARALA---------------------GELPLLS---GERQSQFSHITRLs 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 173 VEKtiledgpESELLEPLYER----MDSLDPDTFESRAA-IILIGLG-----------FNKKTIL-KKTKDMSGGWKMRV 235
Cdd:PRK10938 72 FEQ-------LQKLVSDEWQRnntdMLSPGEDDTGRTTAeIIQDEVKdparceqlaqqFGITALLdRRFKYLSTGETRKT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 236 ALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR---TLVLVshsqdfLNgvctnmidmraqkltayggnydsyh 312
Cdd:PRK10938 145 LLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLV------LN------------------------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 313 ktrseletnqmkqynkqqeEIQHIKKFIASAGTYAN--LVKQAKsRQKILdkmeADGLVQPV----------VPDkvfSF 380
Cdd:PRK10938 194 -------------------RFDEIPDFVQFAGVLADctLAETGE-REEIL----QQALVAQLahseqlegvqLPE---PD 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 381 RFPQVERLPP--PVLAFDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGElTPQS--------G 450
Cdd:PRK10938 247 EPSARHALPAnePRIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQGysndltlfG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 451 R----------VSRHthvkLGVYSqhSQDQLDLTKSALefVRDK-----------YSNISQDFQFWRGQ-LGRYGLTGEG 508
Cdd:PRK10938 323 RrrgsgetiwdIKKH----IGYVS--SSLHLDYRVSTS--VRNVilsgffdsigiYQAVSDRQQKLAQQwLDILGIDKRT 394
|
490 500 510
....*....|....*....|....*....|....*....
gi 285811661 509 QTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLD 547
Cdd:PRK10938 395 ADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
393-578 |
1.12e-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: 58.58 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSrhthvklgvysqhsQDQLD 472
Cdd:cd03369 7 IEVENLSVRYAPDLPPVL-KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE--------------IDGID 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 LTKSALEFVRDKYSNISQDFQFW----RGQLGRYGLTGEGQTVQM-------ATLSEGQRSRVVFALLALEQPNVLLLDE 541
Cdd:cd03369 72 ISTIPLEDLRSSLTIIPQDPTLFsgtiRSNLDPFDEYSDEEIYGAlrvseggLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 285811661 542 PTNGLDIPTIDSLADAINE-FNGG-VVVVSHDFRLL---DKI 578
Cdd:cd03369 152 ATASIDYATDALIQKTIREeFTNStILTIAHRLRTIidyDKI 193
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
102-281 |
1.19e-09 |
|
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: 58.54 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 102 LELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDEPAEPSELSA-LDYVVTE--AQHELKRIEDLVEKTIL 178
Cdd:cd03265 21 FRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRrIGIVFQDlsVDDELTGWENLYIHARL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 179 EDGPESELleplYERMDSLdpdtfesraaIILIGLGFNKKTILKKtkdMSGGWKMRVALAKALFVKPTLLLLDDPTAHLD 258
Cdd:cd03265 101 YGVPGAER----RERIDEL----------LDFVGLLEAADRLVKT---YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180
....*....|....*....|....*..
gi 285811661 259 LEA--CVW--LEEYLKRFDRTLVLVSH 281
Cdd:cd03265 164 PQTraHVWeyIEKLKEEFGMTILLTTH 190
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
425-581 |
1.31e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.93 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 425 ALVGPNGVGKSTLLKIMTG--ELTPQSGRV----------SRHTHVKLGV----------------------YSQHSQDQ 470
Cdd:COG0396 30 AIMGPNGSGKSTLAKVLMGhpKYEVTSGSIlldgedilelSPDERARAGIflafqypveipgvsvsnflrtaLNARRGEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 471 LDLTKsALEFVRDKYS--NISQDFqfwrgqLGRYglTGEGqtvqmatLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDI 548
Cdd:COG0396 110 LSARE-FLKLLKEKMKelGLDEDF------LDRY--VNEG-------FSGGEKKRNEILQMLLLEPKLAILDETDSGLDI 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 285811661 549 PTIDSLADAINEF---NGGVVVVSHDFRLLDKIAQD 581
Cdd:COG0396 174 DALRIVAEGVNKLrspDRGILIITHYQRILDYIKPD 209
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
391-547 |
1.33e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 59.23 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 391 PVLAFDDISFHYESNpSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGrvsrhtHVKLgvysqhsqDQ 470
Cdd:PRK13632 6 VMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSG------EIKI--------DG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 471 LDLTKSALEFVRDKYSNISQ--DFQFwrgqlgrYGLTGE------------------------GQTVQM--------ATL 516
Cdd:PRK13632 71 ITISKENLKEIRKKIGIIFQnpDNQF-------IGATVEddiafglenkkvppkkmkdiiddlAKKVGMedyldkepQNL 143
|
170 180 190
....*....|....*....|....*....|..
gi 285811661 517 SEGQRSRVVFA-LLALEqPNVLLLDEPTNGLD 547
Cdd:PRK13632 144 SGGQKQRVAIAsVLALN-PEIIIFDESTSMLD 174
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
393-547 |
1.34e-09 |
|
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: 59.04 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV-----------SRHTHVKLG 461
Cdd:cd03252 1 ITFEHVRFRYKPDGPVIL-DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 462 VYSQHS-------QDQLDLTKSALEFVRDKY-SNISQDFQFWRG-QLGRYGLTGEgqtvQMATLSEGQRSRVVFALLALE 532
Cdd:cd03252 80 VVLQENvlfnrsiRDNIALADPGMSMERVIEaAKLAGAHDFISElPEGYDTIVGE----QGAGLSGGQRQRIAIARALIH 155
|
170
....*....|....*
gi 285811661 533 QPNVLLLDEPTNGLD 547
Cdd:cd03252 156 NPRILIFDEATSALD 170
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
77-281 |
1.36e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.98 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 77 ETSRDIKLSSVSLLF-HGKVLIQDSGLELNYGRRygLL--GENGCGKSTFLKALA------TREYPIPEHIDIYLLdePA 147
Cdd:COG4178 358 SEDGALALEDLTLRTpDGRPLLEDLSLSLKPGER--LLitGPSGSGKSTLLRAIAglwpygSGRIARPAGARVLFL--PQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 148 EP-----SELSALDYVVTEAQHELKRIEDLVEKTILEDgpesellepLYERMDSldpdtfESRAAIILiglgfnkktilk 222
Cdd:COG4178 434 RPylplgTLREALLYPATAEAFSDAELREALEAVGLGH---------LAERLDE------EADWDQVL------------ 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 223 ktkdmSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKR--FDRTLVLVSH 281
Cdd:COG4178 487 -----SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH 542
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
425-581 |
1.44e-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: 57.92 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 425 ALVGPNGVGKSTLLKIMTG--ELTPQSGRV----------SRHTHVKLGVY--SQHSQDQLDLTKSalEFVRDkysnisq 490
Cdd:cd03217 30 ALMGPNGSGKSTLAKTIMGhpKYEVTEGEIlfkgeditdlPPEERARLGIFlaFQYPPEIPGVKNA--DFLRY------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 491 dfqfwrgqlgryglTGEGqtvqmatLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEF---NGGVVV 567
Cdd:cd03217 101 --------------VNEG-------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreeGKSVLI 159
|
170
....*....|....
gi 285811661 568 VSHDFRLLDKIAQD 581
Cdd:cd03217 160 ITHYQRLLDYIKPD 173
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
111-306 |
1.63e-09 |
|
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: 60.57 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 111 GLLGENGCGKSTFLKALATREYP----IPEHIDI-YlldepaEPSELSAlDYVVTeaqhelkrIEDLVEKTILEDGPES- 184
Cdd:COG1245 370 GIVGPNGIGKTTFAKILAGVLKPdegeVDEDLKIsY------KPQYISP-DYDGT--------VEEFLRSANTDDFGSSy 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 185 ---ELLEPLyermdSLDPdtfesraaiiliglgfnkktIL-KKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLE 260
Cdd:COG1245 435 yktEIIKPL-----GLEK--------------------LLdKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 285811661 261 ACVWLEEYLKRF----DRTLVLVSHsqDFLngvctnMIDMRAQKLTAYGG 306
Cdd:COG1245 490 QRLAVAKAIRRFaenrGKTAMVVDH--DIY------LIDYISDRLMVFEG 531
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
395-570 |
1.71e-09 |
|
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: 58.39 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 395 FDDISFHYesNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRvsrhthVKLGvysqhSQDQLDLT 474
Cdd:cd03254 5 FENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQ------ILID-----GIDIRDIS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 475 KSALefvRDKYSNISQDFQFWRG------QLGRYGLTGE-----GQTVQM-------------------ATLSEGQRSRV 524
Cdd:cd03254 72 RKSL---RSMIGVVLQDTFLFSGtimeniRLGRPNATDEevieaAKEAGAhdfimklpngydtvlgengGNLSQGERQLL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 285811661 525 VFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGG--VVVVSH 570
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGrtSIIIAH 196
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
388-547 |
1.76e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.43 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 388 LPPPVLAFDDISFHYESnpsENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS----------RHTH 457
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGD---KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsraRHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 458 VKLGVYSQHSQDQLDLTKSALEFVRDKYSNIS-QDFQFWRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFALLALEQPNV 536
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSaAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170
....*....|.
gi 285811661 537 LLLDEPTNGLD 547
Cdd:PRK13537 160 LVLDEPTTGLD 170
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
391-588 |
1.85e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 58.87 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 391 PVLAFDDISFHYESNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVsrhthvKLGvysqhsqdQ 470
Cdd:PRK13635 4 EIIRVEHISFRYPDAATYAL-KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI------TVG--------G 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 471 LDLTKSALEFVRDKYSNISQ--DFQFwrgqLGR-------YGLTGEG--------------QTVQM--------ATLSEG 519
Cdd:PRK13635 69 MVLSEETVWDVRRQVGMVFQnpDNQF----VGAtvqddvaFGLENIGvpreemvervdqalRQVGMedflnrepHRLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 520 QRSRVVFA-LLALeQPNVLLLDEPTNGLD-------IPTIDSLADainefNGGVVVVS--HDfrlLDKIAQ-DIFVVENK 588
Cdd:PRK13635 145 QKQRVAIAgVLAL-QPDIIILDEATSMLDprgrrevLETVRQLKE-----QKGITVLSitHD---LDEAAQaDRVIVMNK 215
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
102-305 |
2.10e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 58.44 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 102 LELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHI-----DIYLL---DEPAEPSELSALDYVVTEAQHELKRIEDLV 173
Cdd:PRK10619 26 LQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqTINLVrdkDGQLKVADKNQLRLLRTRLTMVFQHFNLWS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 174 EKTILEDGPESELleplyeRMDSLDPDTFESRAAIILIGLGFNKKTILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDP 253
Cdd:PRK10619 106 HMTVLENVMEAPI------QVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 285811661 254 TAHLDLE---ACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYG 305
Cdd:PRK10619 180 TSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
412-584 |
2.23e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 58.91 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 412 EHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS-------------RHTHVKLGVYSQHSQDQL------- 471
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIidgvditdkkvklSDIRKKVGLVFQYPEYQLfeetiek 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 472 -----------------DLTKSALEFVRDKYSNISQDFQFwrgqlgrygltgegqtvqmaTLSEGQRSRVVFA-LLALEq 533
Cdd:PRK13637 104 diafgpinlglseeeieNRVKRAMNIVGLDYEDYKDKSPF--------------------ELSGGQKRRVAIAgVVAME- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 285811661 534 PNVLLLDEPTNGLDIPTIDSLADAI----NEFNGGVVVVSHDFRLLDKIAQDIFV 584
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIkelhKEYNMTIILVSHSMEDVAKLADRIIV 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
82-284 |
2.34e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.94 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKV-----LIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDE----PAEPSEL 152
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 153 SALDYVVTEAQH-ELKRIED---------------LVEKTILED---GPESElleplyermdSLDPDTFESRAA--IILI 211
Cdd:PRK13651 83 VLEKLVIQKTRFkKIKKIKEirrrvgvvfqfaeyqLFEQTIEKDiifGPVSM----------GVSKEEAKKRAAkyIELV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 212 GLgfnKKTILKKTK-DMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEAcvwLEEYLKRFD------RTLVLVSHSQD 284
Cdd:PRK13651 153 GL---DESYLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQG---VKEILEIFDnlnkqgKTIILVTHDLD 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
395-547 |
2.38e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.88 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 395 FDDISFHYESN-PSEN--LYeHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHV------------- 458
Cdd:PRK13634 5 FQKVEHRYQYKtPFERraLY-DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkpl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 459 --KLGVYSQHSQDQL-------DLTKSALEFvrdkysNISQD--FQFWRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFA 527
Cdd:PRK13634 84 rkKVGIVFQFPEHQLfeetvekDICFGPMNF------GVSEEdaKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIA 157
|
170 180
....*....|....*....|.
gi 285811661 528 -LLALEqPNVLLLDEPTNGLD 547
Cdd:PRK13634 158 gVLAME-PEVLVLDEPTAGLD 177
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
425-579 |
2.64e-09 |
|
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: 57.96 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 425 ALVGPNGVGKSTLLKIMTG-----ELTPQSGRVSrhthvklgvysQHSQDQLDLTKSALEfVRDK--------------- 484
Cdd:cd03260 30 ALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVL-----------LDGKDIYDLDVDVLE-LRRRvgmvfqkpnpfpgsi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 485 YSNIS---QDFQFWRGQ---------LGRYGLTGEGQTVQMAT-LSEGQRSRVVFA-LLALEqPNVLLLDEPTNGLDIPT 550
Cdd:cd03260 98 YDNVAyglRLHGIKLKEelderveeaLRKAALWDEVKDRLHALgLSGGQQQRLCLArALANE-PEVLLLDEPTSALDPIS 176
|
170 180 190
....*....|....*....|....*....|....*
gi 285811661 551 IDSLADAINEFNG--GVVVVSHDF----RLLDKIA 579
Cdd:cd03260 177 TAKIEELIAELKKeyTIVIVTHNMqqaaRVADRTA 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
393-571 |
2.69e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 57.49 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQ---SGRV----SRHTHV-----KL 460
Cdd:COG4136 2 LSLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVllngRRLTALpaeqrRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 461 GVysqhsqdqldLTKSALEFvrdKYSNISQDFQF------WRGQ--------LGRYGLTG-EGQTVqmATLSEGQRSRV- 524
Cdd:COG4136 79 GI----------LFQDDLLF---PHLSVGENLAFalpptiGRAQrrarveqaLEEAGLAGfADRDP--ATLSGGQRARVa 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 285811661 525 -VFALLAleQPNVLLLDEPTNGLDIPTIDSLA----DAINEFNGGVVVVSHD 571
Cdd:COG4136 144 lLRALLA--EPRALLLDEPFSKLDAALRAQFRefvfEQIRQRGIPALLVTHD 193
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
414-587 |
2.75e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.55 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 414 LNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS-------------RHTHVKLGVYSQHSQDQLdltksaleF 480
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLikgepikydkkslLEVRKTVGIVFQNPDDQL--------F 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 481 VrdkySNISQDFQFWRGQLG---------------RYGLTGEGQTVQMAtLSEGQRSRVVFALLALEQPNVLLLDEPTNG 545
Cdd:PRK13639 93 A----PTVEEDVAFGPLNLGlskeevekrvkealkAVGMEGFENKPPHH-LSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 285811661 546 LDIPTIDSLADAINEFN--GGVVVVS-HDFRLLDKIAQDIFVVEN 587
Cdd:PRK13639 168 LDPMGASQIMKLLYDLNkeGITIIIStHDVDLVPVYADKVYVMSD 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
97-284 |
2.99e-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: 57.86 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 97 IQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPipEHIDIYL----LDEPAEPSELSALDYVVTEAQHELKRIEdL 172
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQP--TSGGVILegkqITEPGPDRMVVFQNYSLLPWLTVRENIA-L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 173 VEKTILEDGPESELLEPLYERMDsldpdtfesraaiiLIGLGfnkKTILKKTKDMSGGWKMRVALAKALFVKPTLLLLDD 252
Cdd:TIGR01184 78 AVDRVLPDLSKSERRAIVEEHIA--------------LVGLT---EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 285811661 253 PTAHLDLEACVWLEEYLKRFDR----TLVLVSHSQD 284
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQIWEehrvTVLMVTHDVD 176
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
77-305 |
3.05e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.07 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 77 ETSRDIKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIdiYLLDEPAEpselsalD 156
Cdd:PRK10253 3 ESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV--WLDGEHIQ-------H 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 157 YVVTEAQhelKRIEDLVEK-TILEDGPESELL-------EPLYERMDSLDPDTFESraAIILIGLgfnKKTILKKTKDMS 228
Cdd:PRK10253 74 YASKEVA---RRIGLLAQNaTTPGDITVQELVargryphQPLFTRWRKEDEEAVTK--AMQATGI---THLADQSVDTLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 229 GGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR----TLVLVSHSqdfLNGVC---TNMIDMRAQKL 301
Cdd:PRK10253 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNRekgyTLAAVLHD---LNQACryaSHLIALREGKI 222
|
....
gi 285811661 302 TAYG 305
Cdd:PRK10253 223 VAQG 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
390-578 |
3.24e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.54 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 390 PPVLAFDDISFhyESNPSEnlyEHlnfgvdmdsriALVGPNGVGKSTLLKIMTGELTPQSGRVS------RHTHVK---- 459
Cdd:PRK11288 15 PGVKALDDISF--DCRAGQ---VH-----------ALMGENGAGKSTLLKILSGNYQPDAGSILidgqemRFASTTaala 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 460 LGVYSQHSQDQL--DLT----------KSALEFVRDKYSNisqdfQFWRGQLGRYGLTGEGQTvQMATLSEGQRSRVVFA 527
Cdd:PRK11288 79 AGVAIIYQELHLvpEMTvaenlylgqlPHKGGIVNRRLLN-----YEAREQLEHLGVDIDPDT-PLKYLSIGQRQMVEIA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 285811661 528 LLALEQPNVLLLDEPTNGLDIPTIDSLADAINEF--NGGVVV-VSHD----FRLLDKI 578
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSAREIEQLFRVIRELraEGRVILyVSHRmeeiFALCDAI 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
373-560 |
3.57e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 59.59 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 373 VPDKVFSFRFPQVERLPPPV---LAFDDISFHYEsNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQS 449
Cdd:PRK13657 312 VEDAVPDVRDPPGAIDLGRVkgaVEFDDVSFSYD-NSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 450 GRVS--------------RHThvkLGVYSQHS-------QDQLDLTK---------------SALEFVRDKysniSQDFQ 493
Cdd:PRK13657 390 GRILidgtdirtvtraslRRN---IAVVFQDAglfnrsiEDNIRVGRpdatdeemraaaeraQAHDFIERK----PDGYD 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 285811661 494 FWRGQLGRygltgegqtvqmaTLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINE 560
Cdd:PRK13657 463 TVVGERGR-------------QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDE 516
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
424-603 |
3.80e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 57.72 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTpqsGRVSRHTHVKLGVYSQHSQDQL--DLTKSalefvRDKYSNISQDFQ-------- 493
Cdd:PRK09984 33 VALLGPSGSGKSTLLRHLSGLIT---GDKSAGSHIELLGRTVQREGRLarDIRKS-----RANTGYIFQQFNlvnrlsvl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 494 ------------FWR----------GQLGRYGLTGEGQT----VQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLD 547
Cdd:PRK09984 105 envligalgstpFWRtcfswftreqKQRALQALTRVGMVhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285811661 548 IPT----IDSLADaINEFNGGVVVVShdfrlLDKIAQDIFVVENKTATR-----WDGSILQYKNK 603
Cdd:PRK09984 185 PESarivMDTLRD-INQNDGITVVVT-----LHQVDYALRYCERIVALRqghvfYDGSSQQFDNE 243
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
393-587 |
4.79e-09 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 56.79 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPSEnlyehLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSG--RVSRHTHVKLGVYSQhsqdq 470
Cdd:TIGR01277 1 LALDKVRYEYEHLPME-----FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGsiKVNDQSHTGLAPYQR----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 471 ldlTKSALEFVRDKYSNISQDFQFWRGQLGRYGLTGEGQ--TVQMA--------------TLSEGQRSRVVFALLALEQP 534
Cdd:TIGR01277 71 ---PVSMLFQENNLFAHLTVRQNIGLGLHPGLKLNAEQQekVVDAAqqvgiadyldrlpeQLSGGQRQRVALARCLVRPN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 535 NVLLLDEPTNGLD-------IPTIDSLADainEFNGGVVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:TIGR01277 148 PILLLDEPFSALDpllreemLALVKQLCS---ERQRTLLMVTHHLSDARAIASQIAVVSQ 204
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
391-571 |
5.00e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.03 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 391 PVLAFDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV----SRHTHVKLGVYSQh 466
Cdd:PRK10247 6 PLLQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegEDISTLKPEIYRQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 467 sQDQLDLTKSAL--EFVRD------KYSNISQDFQFWRGQLGRYGLTGEGQTVQMATLSEGQRSRVvfALLALEQ--PNV 536
Cdd:PRK10247 82 -QVSYCAQTPTLfgDTVYDnlifpwQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRI--SLIRNLQfmPKV 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 285811661 537 LLLDEPTNGLDIPTIDSLADAINEFNG----GVVVVSHD 571
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVReqniAVLWVTHD 197
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
222-315 |
5.35e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 222 KKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQ-K 300
Cdd:PRK11819 441 KKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDsQ 520
|
90
....*....|....*
gi 285811661 301 LTAYGGNYDSYHKTR 315
Cdd:PRK11819 521 VEWFEGNFQEYEEDK 535
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
97-305 |
6.43e-09 |
|
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: 56.39 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 97 IQDSGLELNYGRRYGLLGENGCGKSTFLKALAtREYPiPEHIDIYLLDEPAEP--------SELSALDYV---------- 158
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLA-GIYP-PDSGTVTVRGRVSSLlglgggfnPELTGRENIylngrllgls 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 159 VTEAQHELKRIEDLvektiledgpeSELLEPLYERMdsldpdtfesraaiiliglgfnkktilkktKDMSGGWKMRVALA 238
Cdd:cd03220 116 RKEIDEKIDEIIEF-----------SELGDFIDLPV------------------------------KTYSSGMKARLAFA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 239 KALFVKPTLLLLDDPTAHLDL---EACV-WLEEYLKRfDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYG 305
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDAafqEKCQrRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
414-582 |
6.55e-09 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 56.38 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 414 LNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVklgvysqhsqdqLDLTKSALEFVRDKYSNISQDFQ 493
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLK------------LTDDKKNINELRQKVGMVFQQFN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 494 FW----------------RGQ------------LGRYGLTgEGQTVQMATLSEGQRSRVVFA-LLALeQPNVLLLDEPTN 544
Cdd:cd03262 87 LFphltvlenitlapikvKGMskaeaeeralelLEKVGLA-DKADAYPAQLSGGQQQRVAIArALAM-NPKVMLFDEPTS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 285811661 545 GLDIPTIDSLADAINEF---NGGVVVVSHDFRLLDKIAQDI 582
Cdd:cd03262 165 ALDPELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRV 205
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
227-305 |
6.74e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.96 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDL----EACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLT 302
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
...
gi 285811661 303 AYG 305
Cdd:PRK11144 209 AFG 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
395-586 |
7.38e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.10 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 395 FDDISFHYES-NPSEnlYE---HLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS---------------RH 455
Cdd:PRK13646 5 FDNVSYTYQKgTPYE--HQaihDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTvdditithktkdkyiRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 456 THVKLGVYSQHSQDQL--DLTKSALEF-----------VRDKYSNISQDFQFWRGQLgrygltgEGQTVQMatlSEGQ-R 521
Cdd:PRK13646 83 VRKRIGMVFQFPESQLfeDTVEREIIFgpknfkmnldeVKNYAHRLLMDLGFSRDVM-------SQSPFQM---SGGQmR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 522 SRVVFALLALEqPNVLLLDEPTNGLDIPTIDSLADAINEF----NGGVVVVSHDFRLLDKIAQDIFVVE 586
Cdd:PRK13646 153 KIAIVSILAMN-PDIIVLDEPTAGLDPQSKRQVMRLLKSLqtdeNKTIILVSHDMNEVARYADEVIVMK 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
84-327 |
9.01e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.42 E-value: 9.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 84 LSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIyllD-EPAEPSELSALDYVVTEA 162
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI---DgEDVTHRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 163 QHEL---KRIEDLVEKTILEDG-PESELLEPLYERMDSLDPDTFESRAaiiliglgfnkktilkkTKDMSGGWKMRVALA 238
Cdd:PRK11432 86 SYALfphMSLGENVGYGLKMLGvPKEERKQRVKEALELVDLAGFEDRY-----------------VDQISGGQQQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 239 KALFVKPTLLLLDDPTAHLDL-------EAcvwLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYGGNYDSY 311
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDAnlrrsmrEK---IRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY 225
|
250
....*....|....*.
gi 285811661 312 HKTRSELETNQMKQYN 327
Cdd:PRK11432 226 RQPASRFMASFMGDAN 241
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
393-579 |
1.02e-08 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 56.15 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESnpSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV-------SRHTHVKL----- 460
Cdd:cd03295 1 IEFENVTKRYGG--GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgediREQDPVELrrkig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 461 ------GVYSQHSQDQ-----LDLTKSALEFVRDKYSNISQDFQFWRGQL-GRYGltgegqtvqmATLSEGQRSRV-VFA 527
Cdd:cd03295 79 yviqqiGLFPHMTVEEnialvPKLLKWPKEKIRERADELLALVGLDPAEFaDRYP----------HELSGGQQQRVgVAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 528 LLALEqPNVLLLDEPTNGLDIPTIDSLADAI----NEFNGGVVVVSHD----FRLLDKIA 579
Cdd:cd03295 149 ALAAD-PPLLLMDEPFGALDPITRDQLQEEFkrlqQELGKTIVFVTHDideaFRLADRIA 207
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
84-306 |
1.10e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.33 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 84 LSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALAtREYPiPEHIDIYLLDEPAEPSELSALDYVVTEAQ 163
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLG-RHQP-PSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 164 HELKRIEDLVEKTILEDG--PESELLeplyERMDSLDPDTFESraAIILIGLgfnkKTILKKTKD-MSGGWKMRVALAKA 240
Cdd:PRK10575 92 QQLPAAEGMTVRELVAIGryPWHGAL----GRFGAADREKVEE--AISLVGL----KPLAHRLVDsLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 241 LFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR----TLVLVSHSQDFLNGVCTNMIDMRAQKLTAYGG 306
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQerglTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
112-286 |
1.29e-08 |
|
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: 55.80 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 112 LLGENGCGKSTFLKALATREYPIPE--HIDIYLLDEPAEPSELSALDYVVTEAQHELKRIEDLVEKTILEDGPESELLEP 189
Cdd:cd03290 32 IVGQVGCGKSSLLLAILGEMQTLEGkvHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 190 LYERMDSLDPDtfesraaIILIGLGfNKKTILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLE--- 266
Cdd:cd03290 112 AVTDACSLQPD-------IDLLPFG-DQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqeg 183
|
170 180
....*....|....*....|..
gi 285811661 267 --EYLKRFDRTLVLVSHSQDFL 286
Cdd:cd03290 184 ilKFLQDDKRTLVLVTHKLQYL 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
392-587 |
1.29e-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: 55.67 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 392 VLAFDDISFHyesnpsenLYEHLNFGVdmdsrialVGPNGVGKSTLLKIMTGELTPQSGRVsrhtHVklgvysqHSQDQL 471
Cdd:cd03258 18 VTALKDVSLS--------VPKGEIFGI--------IGRSGAGKSTLIRCINGLERPTSGSV----LV-------DGTDLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 472 DLTKSALEFVRDKYSNISQDFQ-FWRG----------QLGRY----------------GLTGEGQTVQmATLSEGQRSRV 524
Cdd:cd03258 71 LLSGKELRKARRRIGMIFQHFNlLSSRtvfenvalplEIAGVpkaeieervlellelvGLEDKADAYP-AQLSGGQKQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 285811661 525 VFA-LLALEqPNVLLLDEPTNGLDIPTIDS----LADAINEFNGGVVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:cd03258 150 GIArALANN-PKVLLCDEATSALDPETTQSilalLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
227-281 |
1.32e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.81 E-value: 1.32e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTLVLVSH 281
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
417-571 |
1.43e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.91 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 417 GVDMDSR----IALVGPNGVGKSTLLKIMTGELTPQSGRVsrhthvKLGVYSQHSQDQLDLTKSALEFVRDKYSNISQDF 492
Cdd:PRK11264 21 GIDLEVKpgevVAIIGPSGSGKTTLLRCINLLEQPEAGTI------RVGDITIDTARSLSQQKGLIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 493 QFW----------------------------RGQLGRYGLTGEgQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTN 544
Cdd:PRK11264 95 NLFphrtvleniiegpvivkgepkeeataraRELLAKVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190
....*....|....*....|....*....|....
gi 285811661 545 GLD-------IPTIDSLAdainEFNGGVVVVSHD 571
Cdd:PRK11264 174 ALDpelvgevLNTIRQLA----QEKRTMVIVTHE 203
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
424-586 |
1.44e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.50 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRvsrhthvklgvysqhsqDQLDLTKSALEfvrdkysnisqdfqfwrgqlgryg 503
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDN-----------------DEWDGITPVYK------------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 504 ltgegqtVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEF----NGGVVVVSHDFRLLDKIA 579
Cdd:cd03222 67 -------PQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLS 139
|
....*..
gi 285811661 580 QDIFVVE 586
Cdd:cd03222 140 DRIHVFE 146
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
393-585 |
1.45e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.81 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNpsENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV-------SRHTHVKL--GVy 463
Cdd:PRK10790 341 IDIDNVSFAYRDD--NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldgrplSSLSHSVLrqGV- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 464 SQHSQDQLDLTKSALEFV---RDkysnISQDfQFWRG----QL---------GRYGLTGEgqtvQMATLSEGQRSRVVFA 527
Cdd:PRK10790 418 AMVQQDPVVLADTFLANVtlgRD----ISEE-QVWQAletvQLaelarslpdGLYTPLGE----QGNNLSVGQKQLLALA 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 528 LLALEQPNVLLLDEPTNGLDIPTIDSLADAINEF--NGGVVVVSHdfRLLDKIAQDIFVV 585
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAH--RLSTIVEADTILV 546
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
82-290 |
1.49e-08 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 55.52 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALaTREYPiPEHIDIYLLDE---------------- 145
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLI-SGFLR-PTSGSVLFDGEditglppheiarlgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 146 -----PAEPSELSALDYVVTEAQHELKRiedlvekTILEDGPESELLEpLYER-MDSLDpdtfesraaiiLIGLGFNKKT 219
Cdd:cd03219 79 rtfqiPRLFPELTVLENVMVAAQARTGS-------GLLLARARREERE-ARERaEELLE-----------RVGLADLADR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285811661 220 IlkkTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLE----ACVWLEEyLKRFDRTLVLVSHSQDFLNGVC 290
Cdd:cd03219 140 P---AGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeteeLAELIRE-LRERGITVLLVEHDMDVVMSLA 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
426-587 |
1.69e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.79 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 426 LVGPNGVGKSTLLKIMTGELTPQSGRVSRhthvklgvysqhSQDQLDLTK----SALEFVRDKYSNISQDFQFW------ 495
Cdd:PRK11124 33 LLGPSGAGKSSLLRVLNLLEMPRSGTLNI------------AGNHFDFSKtpsdKAIRELRRNVGMVFQQYNLWphltvq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 496 ----------------------RGQLGRYGLTGEGQTVQMaTLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDiPTIDS 553
Cdd:PRK11124 101 qnlieapcrvlglskdqalaraEKLLERLRLKPYADRFPL-HLSGGQQQRVAIARALMMEPQVLLFDEPTAALD-PEITA 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 285811661 554 -LADAINEFNG-GV--VVVSHDFRLLDKIAQDIFVVEN 587
Cdd:PRK11124 179 qIVSIIRELAEtGItqVIVTHEVEVARKTASRVVYMEN 216
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
82-305 |
1.69e-08 |
|
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: 55.76 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALA--TReypiPEHIDIYLLDEpaepsELSALDyvv 159
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIglLR----PDSGEILVDGQ-----DITGLS--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 160 teaQHELKRIE--------------DLvekTILEDgpeseLLEPLYERMDsLDPDTFESRAAIIL--IGLgfnKKTILKK 223
Cdd:COG1127 74 ---EKELYELRrrigmlfqggalfdSL---TVFEN-----VAFPLREHTD-LSEAEIRELVLEKLelVGL---PGAADKM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 224 TKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYL----KRFDRTLVLVSHSQDFLNGVCTNMIDMRAQ 299
Cdd:COG1127 139 PSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIrelrDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
....*.
gi 285811661 300 KLTAYG 305
Cdd:COG1127 219 KIIAEG 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
82-282 |
1.74e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.81 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALaTREYPIPEHIDIylldepaePSELSALDYVVTE 161
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRV--------EGRVEFFNQNIYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 162 AQHELKRIEDLVEKTIledgPESELLE-PLYERMD------------SLDpDTFES--RAAIILIGLgfnKKTILKKTKD 226
Cdd:PRK14258 79 RRVNLNRLRRQVSMVH----PKPNLFPmSVYDNVAygvkivgwrpklEID-DIVESalKDADLWDEI---KHKIHKSALD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLK----RFDRTLVLVSHS 282
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslrlRSELTMVIVSHN 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
82-258 |
1.84e-08 |
|
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: 55.20 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALAtREYPiPEHIDIYLLDEPaePSELSAldyvvTE 161
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIV-GLLR-PDSGEVLIDGED--ISGLSE-----AE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 162 AQHELKRI----------EDLvekTILEDgpeseLLEPLYERMDsLDPDTFESRAAIIL--IGLgfnKKTILKKTKDMSG 229
Cdd:cd03261 72 LYRLRRRMgmlfqsgalfDSL---TVFEN-----VAFPLREHTR-LSEEEIREIVLEKLeaVGL---RGAEDLYPAELSG 139
|
170 180
....*....|....*....|....*....
gi 285811661 230 GWKMRVALAKALFVKPTLLLLDDPTAHLD 258
Cdd:cd03261 140 GMKKRVALARALALDPELLLYDEPTAGLD 168
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
111-301 |
1.92e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 111 GLLGENGCGKSTFLKALATREYPIPEHIDI-----YlldepaEPSELSAlDYVVTeaqhelkrIEDLVEK--TILEDGP- 182
Cdd:PRK13409 369 GIVGPNGIGKTTFAKLLAGVLKPDEGEVDPelkisY------KPQYIKP-DYDGT--------VEDLLRSitDDLGSSYy 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 183 ESELLEPLyermdSLDPdtfesraaiiliglgfnkktIL-KKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEA 261
Cdd:PRK13409 434 KSEIIKPL-----QLER--------------------LLdKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 285811661 262 CVWLEEYLKRF----DRTLVLVSHsqDFLngvctnMIDMRAQKL 301
Cdd:PRK13409 489 RLAVAKAIRRIaeerEATALVVDH--DIY------MIDYISDRL 524
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
94-287 |
2.00e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.96 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 94 KVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDEPAePSELSALDYVVteaqhelkRIEDLV 173
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQF-GREASLIDAIG--------RKGDFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 174 EKTiledgpesELLeplyermdsldpdtfeSRAaiiliGLGFNKkTILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDP 253
Cdd:COG2401 114 DAV--------ELL----------------NAV-----GLSDAV-LWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 285811661 254 TAHLDLE-----ACVWLEEyLKRFDRTLVLVSHSQDFLN 287
Cdd:COG2401 164 CSHLDRQtakrvARNLQKL-ARRAGITLVVATHHYDVID 201
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
82-305 |
2.20e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 54.59 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALaTREYPiPEHIDIYLLDEPAEPSELSALDYVVTE 161
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMI-LGIIL-PDSGEVLFDGKPLDIAARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 162 A--QHELKRIEDLVEKTILEDGPESELLEPLYERMDSLDPDTFESraaiiliglgfnkktilKKTKDMSGGWKMRVALAK 239
Cdd:cd03269 79 RglYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYAN-----------------KRVEELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 240 ALFVKPTLLLLDDPTAHLD-LEACVWLEEY--LKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYG 305
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDpVNVELLKDVIreLARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
392-598 |
2.28e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.58 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 392 VLAFDDISFHYESNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHThvklgvysqhsQDQL 471
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPAL-NDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKIT-----------VDGI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 472 DLTKSALEFVRDKYSNISQ--DFQFWRGQLG---RYGLTGEG----------------------QTVQMATLSEGQRSRV 524
Cdd:PRK13640 73 TLTAKTVWDIREKVGIVFQnpDNQFVGATVGddvAFGLENRAvprpemikivrdvladvgmldyIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 525 VFA-LLALEqPNVLLLDEPTNGLDiPT-----IDSLADAINEFNGGVVVVSHDfrlLDK--IAQDIFVVEnktatrwDGS 596
Cdd:PRK13640 153 AIAgILAVE-PKIIILDESTSMLD-PAgkeqiLKLIRKLKKKNNLTVISITHD---IDEanMADQVLVLD-------DGK 220
|
..
gi 285811661 597 IL 598
Cdd:PRK13640 221 LL 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
82-281 |
2.69e-08 |
|
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: 53.59 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATrEYPiPEHIDIYLLDEPAEPSelsaldyvvte 161
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSG-LYK-PDSGEILVDGKEVSFA----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 162 aqhelkriedlvektiledgpeselleplyermdsldpDTFESRAAiiliGLGfnkkTILKktkdMSGGWKMRVALAKAL 241
Cdd:cd03216 68 --------------------------------------SPRDARRA----GIA----MVYQ----LSVGERQMVEIARAL 97
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 285811661 242 FVKPTLLLLDDPTAHLDLEACVWLEEYLKRF---DRTLVLVSH 281
Cdd:cd03216 98 ARNARLLILDEPTAALTPAEVERLFKVIRRLraqGVAVIFISH 140
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
227-284 |
2.83e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.86 E-value: 2.83e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLD----LEACVWLEEYLKRFDRTLVLVSHSQD 284
Cdd:PRK10851 137 LSGGQKQRVALARALAVEPQILLLDEPFGALDaqvrKELRRWLRQLHEELKFTSVFVTHDQE 198
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
101-305 |
3.56e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.01 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 101 GLELNYGRR--YGLLGENGCGKSTFLKALATreypipehidiylLDEPAEPSEL---SALDYvvteAQHELKRIEDLVeK 175
Cdd:PRK13638 19 GLNLDFSLSpvTGLVGANGCGKSTLFMNLSG-------------LLRPQKGAVLwqgKPLDY----SKRGLLALRQQV-A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 176 TILEDgPESELLeplYERMDSldpdtfesRAAIILIGLGFNKKTILKKTKD-----------------MSGGWKMRVALA 238
Cdd:PRK13638 81 TVFQD-PEQQIF---YTDIDS--------DIAFSLRNLGVPEAEITRRVDEaltlvdaqhfrhqpiqcLSHGQKKRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 239 KALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF---DRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYG 305
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvaqGNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
394-555 |
3.59e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.79 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 394 AFDDISFhyeSNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV-----------SRHTHVKLGV 462
Cdd:PRK10575 13 ALRNVSF---RVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleswsSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 463 YSQHSQDQLDLTKSALEFVrDKYSnisqdfqfWRGQLGRYGLTgEGQTVQMA---------------TLSEGQRSRVVFA 527
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVAI-GRYP--------WHGALGRFGAA-DREKVEEAislvglkplahrlvdSLSGGERQRAWIA 159
|
170 180
....*....|....*....|....*....
gi 285811661 528 LLALEQPNVLLLDEPTNGLDIP-TIDSLA 555
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAhQVDVLA 188
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
82-282 |
3.77e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.99 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLF-HGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDEpAEPSELSALDYVV- 159
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDT-GDFSKLQGIRKLVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 160 -----TEAQhelkriedLVEKTILED---GPESELLEP--LYERMDSldpdtfesraAIILIGLGfnkKTILKKTKDMSG 229
Cdd:PRK13644 81 ivfqnPETQ--------FVGRTVEEDlafGPENLCLPPieIRKRVDR----------ALAEIGLE---KYRHRSPKTLSG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 285811661 230 GWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR---TLVLVSHS 282
Cdd:PRK13644 140 GQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkgkTIVYITHN 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
82-283 |
3.98e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 55.72 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREypIPEHIDIYLLDE-----PAEPSelsald 156
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFE--TPDSGRIMLDGQdithvPAENR------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 157 YVVTEAQH-----ELKRIEDLVEKTILEDGPESELLEPLYE--RMDSLdpdtfESRAAiiliglgfnkktilKKTKDMSG 229
Cdd:PRK09452 87 HVNTVFQSyalfpHMTVFENVAFGLRMQKTPAAEITPRVMEalRMVQL-----EEFAQ--------------RKPHQLSG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 285811661 230 GWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTL----VLVSHSQ 283
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQ 205
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
82-326 |
4.02e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 54.63 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDI--YLLDEPAEPSElsaldyvv 159
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIagHQFDFSQKPSE-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 160 tEAQHELKRIEDLVEK--------TILEDgpeseLLE-PLyeRMDSLDPDTFESRAAIILIGLGFNKKTilkktkD---- 226
Cdd:COG4161 75 -KAIRLLRQKVGMVFQqynlwphlTVMEN-----LIEaPC--KVLGLSKEQAREKAMKLLARLRLTDKA------Drfpl 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 227 -MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR---TLVLVSHSQDFLNGVCTNMIDMRAQKLT 302
Cdd:COG4161 141 hLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIVTHEVEFARKVASQVVYMEKGRII 220
|
250 260
....*....|....*....|....
gi 285811661 303 AYGgnyDSYHKTRSelETNQMKQY 326
Cdd:COG4161 221 EQG---DASHFTQP--QTEAFAHY 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
222-284 |
4.15e-08 |
|
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: 54.26 E-value: 4.15e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 285811661 222 KKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKR----FDRTLVLVSHSQD 284
Cdd:cd03299 125 RKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKirkeFGVTVLHVTHDFE 191
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
226-306 |
4.16e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 54.33 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 226 DMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEAcvwLEEYLKRFDR------TLVLVSHSQDFLNGVCTNMIDMRAQ 299
Cdd:PRK09493 136 ELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL---RHEVLKVMQDlaeegmTMVIVTHEIGFAEKVASRLIFIDKG 212
|
....*..
gi 285811661 300 KLTAYGG 306
Cdd:PRK09493 213 RIAEDGD 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
90-284 |
4.63e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.03 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 90 LFHGKVLIQDsglelnyGRRYGLLGENGCGKSTFLkalatreypipEHIDIYLldepaEPSE--LSALDYVVTeAQHELK 167
Cdd:PRK13634 23 LYDVNVSIPS-------GSYVAIIGHTGSGKSTLL-----------QHLNGLL-----QPTSgtVTIGERVIT-AGKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 168 RIEDLVEKT-ILEDGPESELLEPLYERMDSLDPDTF---------ESRAAIILIGLGfnkKTILKKTK-DMSGGWKMRVA 236
Cdd:PRK13634 79 KLKPLRKKVgIVFQFPEHQLFEETVEKDICFGPMNFgvseedakqKAREMIELVGLP---EELLARSPfELSGGQMRRVA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 285811661 237 LAKALFVKPTLLLLDDPTAHLD----LEACVWLEEYLKRFDRTLVLVSHSQD 284
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVLVTHSME 207
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
96-281 |
6.05e-08 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 53.63 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 96 LIQDSGLELNYGRRYGLLGENGCGKSTFLkALATREYPiPEHIDIYLLDEPAEPSELSALDYVVTEAQHElkriEDLVEK 175
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVV-ALLENFYQ-PQGGQVLLDGKPISQYEHKYLHSKVSLVGQE----PVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 176 TILED---GPESELLEPLYERMDSLDPDTFesraaIILIGLGFNKKTIlKKTKDMSGGWKMRVALAKALFVKPTLLLLDD 252
Cdd:cd03248 103 SLQDNiayGLQSCSFECVKEAAQKAHAHSF-----ISELASGYDTEVG-EKGSQLSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190
....*....|....*....|....*....|.
gi 285811661 253 PTAHLDLEACVWLEEYLKRF--DRTLVLVSH 281
Cdd:cd03248 177 ATSALDAESEQQVQQALYDWpeRRTVLVIAH 207
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
397-570 |
6.19e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 397 DISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSrhthvklgVYSQHSQDQLDLTKS 476
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIL--------FERQSIKKDLCTYQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 477 ALEFVRDKY---------SNISQDFQFWRGQLGRYGLT-----GEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEP 542
Cdd:PRK13540 75 QLCFVGHRSginpyltlrENCLYDIHFSPGAVGITELCrlfslEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 285811661 543 TNGLDIPTIDSLADAINEF---NGGVVVVSH 570
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHrakGGAVLLTSH 185
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
414-586 |
6.35e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.45 E-value: 6.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 414 LNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS---------------RHTHVKLGVYSQHSQDQLdLTKSAL 478
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagyhitpetgnknlKKLRKKVSLVFQFPEAQL-FENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 479 EFVRDKYSNISQDFQFWRGQ----LGRYGLTGEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSL 554
Cdd:PRK13641 105 KDVEFGPKNFGFSEDEAKEKalkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEM 184
|
170 180 190
....*....|....*....|....*....|....*
gi 285811661 555 ADAINEFNGG---VVVVSHDFRLLDKIAQDIFVVE 586
Cdd:PRK13641 185 MQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLE 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
424-585 |
6.44e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVSR----------------HTHVKlGVY------SQHSQ--DQL-------- 471
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDYEEepswdevlkrfrgtelQNYFK-KLYngeikvVHKPQyvDLIpkvfkgkv 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 472 -DLTKSALEfvRDKYSNISQDFQFwRGQLGRygltgegqtvQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPT 550
Cdd:PRK13409 181 rELLKKVDE--RGKLDEVVERLGL-ENILDR----------DISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170 180 190
....*....|....*....|....*....|....*..
gi 285811661 551 IDSLADAINEFNGG--VVVVSHDFRLLDKIAQDIFVV 585
Cdd:PRK13409 248 RLNVARLIRELAEGkyVLVVEHDLAVLDYLADNVHIA 284
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
412-547 |
6.57e-08 |
|
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: 53.88 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 412 EHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV------SRHTHVK---LGVYSQHSQDQLDLT-------- 474
Cdd:cd03296 19 DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedATDVPVQernVGFVFQHYALFRHMTvfdnvafg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 475 ---------KSALEfVRDKYSNISQDFQF-WRGQlgRYGltgegqtvqmATLSEGQRSRVVFA-LLALEqPNVLLLDEPT 543
Cdd:cd03296 99 lrvkprserPPEAE-IRAKVHELLKLVQLdWLAD--RYP----------AQLSGGQRQRVALArALAVE-PKVLLLDEPF 164
|
....
gi 285811661 544 NGLD 547
Cdd:cd03296 165 GALD 168
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
94-281 |
6.68e-08 |
|
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: 52.70 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 94 KVLIQDSGLELNYGRRYGLLGENGCGKSTFLKaLATREYPiPEHIDIYLLDEPAEPSE--LSALDYVVTEAQHelkried 171
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQ-LLTGDLK-PQQGEITLDGVPVSDLEkaLSSLISVLNQRPY------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 172 LVEKTILEDgpeselleplyermdsldpdtfesraaiilIGLGFnkktilkktkdmSGGWKMRVALAKALFVKPTLLLLD 251
Cdd:cd03247 86 LFDTTLRNN------------------------------LGRRF------------SGGERQRLALARILLQDAPIVLLD 123
|
170 180 190
....*....|....*....|....*....|....
gi 285811661 252 DPTAHLD----LEACVWLEEYLKrfDRTLVLVSH 281
Cdd:cd03247 124 EPTVGLDpiteRQLLSLIFEVLK--DKTLIWITH 155
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
393-607 |
6.97e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.41 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSrhthvklgvysqhsQDQLD 472
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPAL-RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIL--------------LDGHD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 LTKSALEFVRDKYSNISQDF-----------------QFWRGQLGR---------------YGL---TGEGQtvqmATLS 517
Cdd:PRK11176 407 LRDYTLASLRNQVALVSQNVhlfndtianniayarteQYSREQIEEaarmayamdfinkmdNGLdtvIGENG----VLLS 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 518 EGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEF--NGGVVVVSHDFRLLDKiAQDIFVVEnktatrwDG 595
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELqkNRTSLVIAHRLSTIEK-ADEILVVE-------DG 554
|
250
....*....|....*
gi 285811661 596 SILQYKNK---LAKN 607
Cdd:PRK11176 555 EIVERGTHaelLAQN 569
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
393-579 |
7.59e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.98 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYES-NPSENlyeHLNFGVDMD----SRIALVGPNGVGKSTLLKIMTGELTPQSGRVS-------------- 453
Cdd:PRK13649 3 INLQNVSYTYQAgTPFEG---RALFDVNLTiedgSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitstsknkd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 454 -RHTHVKLGVYSQHSQDQLdLTKSALEFVRDKYSN--ISQD--FQFWRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFA- 527
Cdd:PRK13649 80 iKQIRKKVGLVFQFPESQL-FEETVLKDVAFGPQNfgVSQEeaEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAg 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 285811661 528 LLALEqPNVLLLDEPTNGLDIPTIDSLADAINEFNGG---VVVVSHdfrLLDKIA 579
Cdd:PRK13649 159 ILAME-PKILVLDEPTAGLDPKGRKELMTLFKKLHQSgmtIVLVTH---LMDDVA 209
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
82-301 |
7.96e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.06 E-value: 7.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGL-----ELNYGRRYGLLGENGCGKSTFLkalatreypipEHIDIYLLdepaePS--ELSA 154
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLdnisfELEEGSFVALVGHTGSGKSTLM-----------QHFNALLK-----PSsgTITI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 155 LDYVVTeAQHELKRIEDLVEKTILE-DGPESELLEPLYERMDSLDPDTF-------ESRAAIILIGLGFNKKTILKKTKD 226
Cdd:PRK13641 67 AGYHIT-PETGNKNLKKLRKKVSLVfQFPEAQLFENTVLKDVEFGPKNFgfsedeaKEKALKWLKKVGLSEDLISKSPFE 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR---TLVLVSHSQDFLNGVCTNMIDMRAQKL 301
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
393-541 |
7.96e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.36 E-value: 7.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESN-----PsenlyehLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV----------SRHTH 457
Cdd:PRK10522 323 LELRNVTFAYQDNgfsvgP-------INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIlldgkpvtaeQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 458 VKL--GVYSQ-HSQDQLdLTKsalefvrDKYSNISQDFQFWRGQLG-RYGLTGEGQTVQMATLSEGQRSRVVFALLALEQ 533
Cdd:PRK10522 396 RKLfsAVFTDfHLFDQL-LGP-------EGKPANPALVEKWLERLKmAHKLELEDGRISNLKLSKGQKKRLALLLALAEE 467
|
....*...
gi 285811661 534 PNVLLLDE 541
Cdd:PRK10522 468 RDILLLDE 475
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
82-284 |
8.02e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 54.85 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALatREYPIPEHIDIYLLDEPAEPSELSALDYVVTE 161
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAI--NGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 162 AQHELKRIEDLVEKTILEDGPEsellePLYERMDSLDP-DTFESRAAIILIGLG-FNKKTIlkktKDMSGGWKMRVALAK 239
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGRT-----PHRSRFDTWTEtDRAAVERAMERTGVAqFADRPV----TSLSGGERQRVLLAR 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 285811661 240 ALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF---DRTLVLVSHSQD 284
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLvddGKTAVAAIHDLD 200
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
426-585 |
8.54e-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: 53.52 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 426 LVGPNGVGKSTLLKIMTGELTPQSGRVS------------------------RHTHVKLGVYSQHSqDQL---------D 472
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildefrgselqnyftklLEGDVKVIVKPQYV-DLIpkavkgkvgE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 LTKSALEfvRDKYSNISQDFQFwRGQLGRygltgegqtvQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTID 552
Cdd:cd03236 110 LLKKKDE--RGKLDELVDQLEL-RHVLDR----------NIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 285811661 553 SLADAINEFN---GGVVVVSHDFRLLDKIAQDIFVV 585
Cdd:cd03236 177 NAARLIRELAeddNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
82-285 |
8.76e-08 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 52.92 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDEPAEPSELSALD-YVVT 160
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 161 EAQHElkrieDLVE-KTILEDgpeseLLEPLYERMdSLDPDTFESRAAIIL--IGLgFNKKTilKKTKDMSGGWKMRVAL 237
Cdd:cd03262 81 VFQQF-----NLFPhLTVLEN-----ITLAPIKVK-GMSKAEAEERALELLekVGL-ADKAD--AYPAQLSGGQQQRVAI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 285811661 238 AKALFVKPTLLLLDDPTAHLDLEacvWLEEYLK------RFDRTLVLVSHSQDF 285
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPE---LVGEVLDvmkdlaEEGMTMVVVTHEMGF 197
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
81-305 |
8.89e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 53.48 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 81 DIKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALAtrEYPIPEHIDIYLLDEPAepSELSALDYVVT 160
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA--RLLTPQSGTVFLGDKPI--SMLSSRQLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 161 EA---QHELKRiEDLVEKTILEDGPESELlePLYERMDSLDPDtfesraaiiLIGLGFNKKTIL----KKTKDMSGGWKM 233
Cdd:PRK11231 78 LAllpQHHLTP-EGITVRELVAYGRSPWL--SLWGRLSAEDNA---------RVNQAMEQTRINhladRRLTDLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 285811661 234 RVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFD---RTLVLVSHSqdfLNGV---CTNMIDMRAQKLTAYG 305
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNtqgKTVVTVLHD---LNQAsryCDHLVVLANGHVMAQG 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
91-296 |
1.29e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.22 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 91 FHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDEPAEPSelsaldyvVTEAQHELKRIE 170
Cdd:PRK11264 13 FHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARS--------LSQQKGLIRQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 171 DLV-----------EKTILEDGPESellePLYERMDSLDPDTFESRAAIILIGLGFNKKTILKKtkdMSGGWKMRVALAK 239
Cdd:PRK11264 85 QHVgfvfqnfnlfpHRTVLENIIEG----PVIVKGEPKEEATARARELLAKVGLAGKETSYPRR---LSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 240 ALFVKPTLLLLDDPTAHLDLEAcvwLEEYLKRF------DRTLVLVSHSQDFLNGVCTNMIDM 296
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPEL---VGEVLNTIrqlaqeKRTMVIVTHEMSFARDVADRAIFM 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
424-590 |
1.34e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 54.67 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTP----QSGRVSRHTHVKLGVYSQHS----QDQLDL----TKSALEF---VRDKySNI 488
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNALAFRSPKgvkgSGSVLLNGMPIDAKEMRAISayvqQDDLFIptltVREHLMFqahLRMP-RRV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 489 SQDFQFWRGQ--LGRYGLTGEGQTV-----QMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLD-------IPTIDSL 554
Cdd:TIGR00955 133 TKKEKRERVDevLQALGLRKCANTRigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDsfmaysvVQVLKGL 212
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 285811661 555 ADainefNGGVVVV------SHDFRLLDKIaqdIFVVENKTA 590
Cdd:TIGR00955 213 AQ-----KGKTIICtihqpsSELFELFDKI---ILMAEGRVA 246
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
424-579 |
1.35e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.22 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVSRhthvklgvysqhsqdqLDLTKSALEfvrdkysnisQDFQFWRGQLGRYG 503
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGVIY----------------IDGEDILEE----------VLDQLLLIIVGGKK 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 504 LTGEGqtvqmatlseGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAIN---------EFNGGVVVVSHDFRL 574
Cdd:smart00382 59 ASGSG----------ELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllllksEKNLTVILTTNDEKD 128
|
....*
gi 285811661 575 LDKIA 579
Cdd:smart00382 129 LGPAL 133
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
425-587 |
1.42e-07 |
|
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: 51.59 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 425 ALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYSqhsqdqldltksalefvrdkySNISQDFQFWRGQlgrygl 504
Cdd:cd03227 25 IITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIV---------------------AAVSAELIFTRLQ------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 505 tgegqtvqmatLSEGQRSRVVFAL---LALEQPNVL-LLDEPTNGLDIPTIDSLADAINEFNGG---VVVVSHD---FRL 574
Cdd:cd03227 78 -----------LSGGEKELSALALilaLASLKPRPLyILDEIDRGLDPRDGQALAEAILEHLVKgaqVIVITHLpelAEL 146
|
170
....*....|...
gi 285811661 575 LDKIAQDIFVVEN 587
Cdd:cd03227 147 ADKLIHIKKVITG 159
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
227-326 |
1.59e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 52.71 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLE---ACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTA 303
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEitaQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
90 100
....*....|....*....|...
gi 285811661 304 YGgnyDSYHKTRSelETNQMKQY 326
Cdd:PRK11124 222 QG---DASCFTQP--QTEAFKNY 239
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
410-588 |
1.75e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.85 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 410 LYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRhthvklgvysqHSQDQLDLTKSALEFVRDKYSNIS 489
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILF-----------DGENIPAMSRSRLYTVRKRMSMLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 490 Q------DFQFWRG----------------------QLGRYGLTGEGQtVQMATLSEGQRSRVVFA-LLALEqPNVLLLD 540
Cdd:PRK11831 91 QsgalftDMNVFDNvayplrehtqlpapllhstvmmKLEAVGLRGAAK-LMPSELSGGMARRAALArAIALE-PDLIMFD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 285811661 541 EPTNGLDIPTIDSLADAINEFNG--GV--VVVSHDFRLLDKIAQDIFVVENK 588
Cdd:PRK11831 169 EPFVGQDPITMGVLVKLISELNSalGVtcVVVSHDVPEVLSIADHAYIVADK 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
227-281 |
1.93e-07 |
|
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: 52.44 E-value: 1.93e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLD-------LEAcvwLEEYLKRFDRTLVLVSH 281
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDaatgeqiIDL---LFELNRERGTTLVLVTH 205
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
424-585 |
1.93e-07 |
|
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: 54.02 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVSR----------------HTHVKlGVY------SQHSQ--DQL-------- 471
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEepswdevlkrfrgtelQDYFK-KLAngeikvAHKPQyvDLIpkvfkgtv 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 472 -DLTKSALEfvRDKYSNISQDFQFwRGQLGRYgltgegqtvqMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPT 550
Cdd:COG1245 181 rELLEKVDE--RGKLDELAEKLGL-ENILDRD----------ISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180 190
....*....|....*....|....*....|....*...
gi 285811661 551 IDSLADAINEF---NGGVVVVSHDFRLLDKIAQDIFVV 585
Cdd:COG1245 248 RLNVARLIRELaeeGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
79-354 |
2.11e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 52.70 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 79 SRDIKLSSVSLLFHGKV-----LIQDSGLELNYGRRYGLLGENGCGKSTFLKAlaTREYPIpehidiylldepAEPSELS 153
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQL--TNGLII------------SETGQTI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 154 ALDYVVTEAQHELKRIEDL-VEKTILEDGPESELLEplyermdsldpDTFESRAAIILIGLGFNKKTILKKTKDM----- 227
Cdd:PRK13645 70 VGDYAIPANLKKIKEVKRLrKEIGLVFQFPEYQLFQ-----------ETIEKDIAFGPVNLGENKQEAYKKVPELlklvq 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 228 -------------SGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEAcvwLEEYLKRFDR-------TLVLVSHSQDFLN 287
Cdd:PRK13645 139 lpedyvkrspfelSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG---EEDFINLFERlnkeykkRIIMVTHNMDQVL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 288 GVCTNMIDMRAQKLTAYGGNYDSYHK----TRSELETNQMKQ--YNKQQEEIQHIKKFIASAGTYANLVKQAK 354
Cdd:PRK13645 216 RIADEVIVMHEGKVISIGSPFEIFSNqellTKIEIDPPKLYQlmYKLKNKGIDLLNKNIRTIEEFAKELAKVL 288
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
393-547 |
2.92e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 52.01 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPSenlYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS------RHTHVKLGVYSQH 466
Cdd:PRK11248 2 LQISHLYADYGGKPA---LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITldgkpvEGPGAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 467 S-----QDQLDLTKSALEFV---RDKYSNISQDFqfwrgqLGRYGLTGEGQTvQMATLSEGQRSRVVFALLALEQPNVLL 538
Cdd:PRK11248 79 EgllpwRNVQDNVAFGLQLAgveKMQRLEIAHQM------LKKVGLEGAEKR-YIWQLSGGQRQRVGIARALAANPQLLL 151
|
....*....
gi 285811661 539 LDEPTNGLD 547
Cdd:PRK11248 152 LDEPFGALD 160
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
82-259 |
3.13e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 52.08 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALAtrEYPIPEHIDIYLLDEPAE---PSEL------ 152
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS--GELSPDSGEVRLNGRPLAdwsPAELarrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 153 ----SALDY------VV-------TEAQHELKRIEDLVektiledgpeselleplyerMDSLDPDTFESRAAIILiglgf 215
Cdd:PRK13548 81 lpqhSSLSFpftveeVVamgraphGLSRAEDDALVAAA--------------------LAQVDLAHLAGRDYPQL----- 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 285811661 216 nkktilkktkdmSGGWKMRVALAKAL------FVKPTLLLLDDPTAHLDL 259
Cdd:PRK13548 136 ------------SGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDL 173
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
112-287 |
3.51e-07 |
|
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: 51.25 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 112 LLGENGCGKSTFLKALATREYPIPEHIDIylldepaEPSELSALdyvvteaqhELKRIEDLVEK--TILEDgpeSELLEP 189
Cdd:cd03292 32 LVGPSGAGKSTLLKLIYKEELPTSGTIRV-------NGQDVSDL---------RGRAIPYLRRKigVVFQD---FRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 190 L--YE------RMDSLDPDTFESR--AAIILIGLGFNKKTIlkkTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDL 259
Cdd:cd03292 93 RnvYEnvafalEVTGVPPREIRKRvpAALELVGLSHKHRAL---PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190
....*....|....*....|....*....|.
gi 285811661 260 EACVWLEEYLKRFDR---TLVLVSHSQDFLN 287
Cdd:cd03292 170 DTTWEIMNLLKKINKagtTVVVATHAKELVD 200
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
226-282 |
3.57e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.77 E-value: 3.57e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 226 DMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF--DRTLVLVSHS 282
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTHS 207
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
425-587 |
4.07e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.57 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 425 ALVGPNGVGKSTLLKIMTG-------------------ELTP----QSG------------RVSRHTHVKLGVYSQHSQD 469
Cdd:CHL00131 37 AIMGPNGSGKSTLSKVIAGhpaykilegdilfkgesilDLEPeeraHLGiflafqypieipGVSNADFLRLAYNSKRKFQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 470 QLDlTKSALEF---VRDKYSNISQDFQFwrgqLGRYglTGEGqtvqmatLSEGQRSRVVFALLALEQPNVLLLDEPTNGL 546
Cdd:CHL00131 117 GLP-ELDPLEFleiINEKLKLVGMDPSF----LSRN--VNEG-------FSGGEKKRNEILQMALLDSELAILDETDSGL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 285811661 547 DIPTIDSLADAINEF---NGGVVVVSHDFRLLDKIAQD-IFVVEN 587
Cdd:CHL00131 183 DIDALKIIAEGINKLmtsENSIILITHYQRLLDYIKPDyVHVMQN 227
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
425-587 |
4.35e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 50.68 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 425 ALVGPNGVGKSTLLK----IMTGELTPQSGRVSRHTHVklgVYSQHSQDQLDLTksaLEFVRDKYSNISQDFQFWRGQLg 500
Cdd:cd03240 26 LIVGQNGAGKTTIIEalkyALTGELPPNSKGGAHDPKL---IREGEVRAQVKLA---FENANGKKYTITRSLAILENVI- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 501 rYGLTGEGQT--VQM-ATLSEGQRsrVVFAL---LALEQP-----NVLLLDEPTNGLDIPTID-SLADAINEFNGG---- 564
Cdd:cd03240 99 -FCHQGESNWplLDMrGRCSGGEK--VLASLiirLALAETfgsncGILALDEPTTNLDEENIEeSLAEIIEERKSQknfq 175
|
170 180
....*....|....*....|...
gi 285811661 565 VVVVSHDFRLLDKiAQDIFVVEN 587
Cdd:cd03240 176 LIVITHDEELVDA-ADHIYRVEK 197
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
393-587 |
4.57e-07 |
|
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: 50.55 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPSENLY--EHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVklGVYSQHSQDQ 470
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--AYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 471 LDLTKS----ALEFVRDKYSNI------SQDFQFWRGQLgrygLT--GEGQTvqmaTLSEGQRSRVVFALLALEQPNVLL 538
Cdd:cd03250 79 NGTIREnilfGKPFDEERYEKVikacalEPDLEILPDGD----LTeiGEKGI----NLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 285811661 539 LDEPTNGLDIPTIDSLAD-AINEF---NGGVVVVSHDFRLLDKiAQDIFVVEN 587
Cdd:cd03250 151 LDDPLSAVDAHVGRHIFEnCILGLllnNKTRILVTHQLQLLPH-ADQIVVLDN 202
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
82-315 |
4.67e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.55 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALA---TREYPIPEHIDiyLLDEPAEPSELSALDYV 158
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSgliTGDKSAGSHIE--LLGRTVQREGRLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 159 VTEAQHE-LKRIEDLVEK-TILEDGPESEL-LEPLYERMDSLDPDTFESRAAIILIGLGFnKKTILKKTKDMSGGWKMRV 235
Cdd:PRK09984 83 KSRANTGyIFQQFNLVNRlSVLENVLIGALgSTPFWRTCFSWFTREQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 236 ALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR----TLVLVSHSQDFLNGVCTNMIDMRaQKLTAYGGNYDSY 311
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVALR-QGHVFYDGSSQQF 240
|
....
gi 285811661 312 HKTR 315
Cdd:PRK09984 241 DNER 244
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
417-577 |
4.69e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.03 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 417 GVDMDSRIA----LVGPNGVGKSTLLKIMTGELTPQSGRVsrhthvklgVYSQHsqDQLDLTKSALEFVRDKYSNISQDF 492
Cdd:PRK10908 20 GVTFHMRPGemafLTGHSGAGKSTLLKLICGIERPSAGKI---------WFSGH--DITRLKNREVPFLRRQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 493 QFW---------------------------RGQLGRYGLTGEGQTVQMaTLSEGQRSRVVFALLALEQPNVLLLDEPTNG 545
Cdd:PRK10908 89 HLLmdrtvydnvaipliiagasgddirrrvSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 285811661 546 LDiptiDSLADAI----NEFNG-GVVVV--SHDFRLLDK 577
Cdd:PRK10908 168 LD----DALSEGIlrlfEEFNRvGVTVLmaTHDIGLISR 202
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
393-588 |
4.78e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV---SRHT---------HVKL 460
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiinDSHNlkdinlkwwRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 461 GVYsqhSQDQLDLTKSA-------------LEFVRDKY---SNISQDFQFWR--------GQLG---------------- 500
Cdd:PTZ00265 463 GVV---SQDPLLFSNSIknnikyslyslkdLEALSNYYnedGNDSQENKNKRnscrakcaGDLNdmsnttdsneliemrk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 501 RYGLTGEGQTVQM-------------------------ATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLA 555
Cdd:PTZ00265 540 NYQTIKDSEVVDVskkvlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260 270
....*....|....*....|....*....|....*..
gi 285811661 556 DAINEFNGG----VVVVSHDFRLLdKIAQDIFVVENK 588
Cdd:PTZ00265 620 KTINNLKGNenriTIIIAHRLSTI-RYANTIFVLSNR 655
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
425-592 |
5.09e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 425 ALVGPNGVGKSTLLKIMTGELTPQSG-RVSRHTHVKLGVYSQH----------------SQDQLDLTKSALEFVRDKYSN 487
Cdd:PRK10938 33 AFVGANGSGKSALARALAGELPLLSGeRQSQFSHITRLSFEQLqklvsdewqrnntdmlSPGEDDTGRTTAEIIQDEVKD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 488 iSQDFQFWRGQLGRYGLTGEgqtvQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGG--- 564
Cdd:PRK10938 113 -PARCEQLAQQFGITALLDR----RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSgit 187
|
170 180
....*....|....*....|....*...
gi 285811661 565 VVVVSHDFRLLDKIAQDIFVVENKTATR 592
Cdd:PRK10938 188 LVLVLNRFDEIPDFVQFAGVLADCTLAE 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
424-571 |
5.16e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.22 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVsrhthvklgvysqhsqdqldLTKSA-LEFVRDKYSNISQDFQF--WRGQLG 500
Cdd:PRK11247 41 VAVVGRSGCGKSTLLRLLAGLETPSAGEL--------------------LAGTApLAEAREDTRLMFQDARLlpWKKVID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 501 RYGLTGEGQ----------TVQM--------ATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAI---- 558
Cdd:PRK11247 101 NVGLGLKGQwrdaalqalaAVGLadranewpAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIeslw 180
|
170
....*....|...
gi 285811661 559 NEFNGGVVVVSHD 571
Cdd:PRK11247 181 QQHGFTVLLVTHD 193
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
228-284 |
5.22e-07 |
|
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: 52.03 E-value: 5.22e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTL----VLVSHSQD 284
Cdd:COG4148 135 SGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELdipiLYVSHSLD 195
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
228-287 |
5.57e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 50.82 E-value: 5.57e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR---TLVLVSHSQDFLN 287
Cdd:COG2884 139 SGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRrgtTVLIATHDLELVD 201
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
424-547 |
5.65e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 52.01 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHvklGVYSQHSQDQldltksALEFVRDKYS-----NISQDFQFWRGQ 498
Cdd:PRK10851 31 VALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSRLHARDR------KVGFVFQHYAlfrhmTVFDNIAFGLTV 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 285811661 499 LGR----------YGLTGEGQTVQM--------ATLSEGQRSRVVFA-LLALEqPNVLLLDEPTNGLD 547
Cdd:PRK10851 102 LPRrerpnaaaikAKVTQLLEMVQLahladrypAQLSGGQKQRVALArALAVE-PQILLLDEPFGALD 168
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
414-547 |
7.81e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.15 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 414 LNFGVDMDSRIALVGPNGVGKSTLLKIMTG----------------ELTPQSGR-----VSRHTH---------VKLGvY 463
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkingielrELDPESWRkhlswVGQNPQlphgtlrdnVLLG-N 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 464 SQHSQDQLD--LTKS-ALEFVRdkysnisqdfqfwRGQLGRYGLTGEgqtvQMATLSEGQRSRVVFALLALEQPNVLLLD 540
Cdd:PRK11174 448 PDASDEQLQqaLENAwVSEFLP-------------LLPQGLDTPIGD----QAAGLSVGQAQRLALARALLQPCQLLLLD 510
|
....*..
gi 285811661 541 EPTNGLD 547
Cdd:PRK11174 511 EPTASLD 517
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
82-284 |
7.91e-07 |
|
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: 50.76 E-value: 7.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLF-HGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKaLATR--EypiPEHIDIYLLDEPA---EPSELS-A 154
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMK-MINRliE---PTSGEIFIDGEDIreqDPVELRrK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 155 LDYVVTEA---QHelKRIED---LVEKtiLEDGPESELLEPLYE--RMDSLDPDTFESRAAiiliglgfnkktilkktKD 226
Cdd:cd03295 77 IGYVIQQIglfPH--MTVEEniaLVPK--LLKWPKEKIRERADEllALVGLDPAEFADRYP-----------------HE 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR----TLVLVSHSQD 284
Cdd:cd03295 136 LSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelgkTIVFVTHDID 197
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
416-550 |
8.08e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.04 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 416 FGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS-------RHTHVKLGVYSQHSQdQLDLTKSALefVRD----- 483
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqptrQALQKNLVAYVPQSE-EVDWSFPVL--VEDvvmmg 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 285811661 484 KYSNI-------SQDFQFWRGQLGRYGLTgEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPT 550
Cdd:PRK15056 105 RYGHMgwlrrakKRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
94-281 |
8.30e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.86 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 94 KVLIQDSGLELNYGRRYGLLGENGCGKSTFLKalatreypipeHIDIYLLdepaePSE----LSALDYVVTEAQHELKRI 169
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAK-----------HMNALLI-----PSEgkvyVDGLDTSDEENLWDIRNK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 170 EDLVEK--------TILED----GPESELLEP--LYERMD-SLdpdtfesraaiiliglgfnKKTILKKTKD-----MSG 229
Cdd:PRK13633 87 AGMVFQnpdnqivaTIVEEdvafGPENLGIPPeeIRERVDeSL-------------------KKVGMYEYRRhaphlLSG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 285811661 230 GWKMRVALAKALFVKPTLLLLDDPTAHLD----LEACVWLEEYLKRFDRTLVLVSH 281
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
102-305 |
8.71e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.47 E-value: 8.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 102 LELNYGRRYGLLGENGCGKSTFLKALAtreypipehidiylldepaepselsaldyvvteaqhelkRIEDLVEKTILEDG 181
Cdd:COG1134 47 FEVERGESVGIIGRNGAGKSTLLKLIA---------------------------------------GILEPTSGRVEVNG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 182 PESELLEPlyerMDSLDPDtFESRAAIILIG--LGFNKKTILKKTK------------DM-----SGGWKMRVALAKALF 242
Cdd:COG1134 88 RVSALLEL----GAGFHPE-LTGRENIYLNGrlLGLSRKEIDEKFDeivefaelgdfiDQpvktySSGMRARLAFAVATA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285811661 243 VKPTLLLLDdptahldlEA-----------CV-WLEEYLKRfDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYG 305
Cdd:COG1134 163 VDPDILLVD--------EVlavgdaafqkkCLaRIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDG 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
82-258 |
8.72e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.47 E-value: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATreYPIPEHIDIYLLDEPAE-PSelsALDYVVT 160
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAG--FVPYQHGSITLDGKPVEgPG---AERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 161 eaQHE----LKRIEDLVEKTILEDGPESElleplyERMDSldpdtfeSRAAIILIGL-GFNKKTILKktkdMSGGWKMRV 235
Cdd:PRK11248 77 --QNEgllpWRNVQDNVAFGLQLAGVEKM------QRLEI-------AHQMLKKVGLeGAEKRYIWQ----LSGGQRQRV 137
|
170 180
....*....|....*....|...
gi 285811661 236 ALAKALFVKPTLLLLDDPTAHLD 258
Cdd:PRK11248 138 GIARALAANPQLLLLDEPFGALD 160
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
397-571 |
9.06e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 50.86 E-value: 9.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 397 DISFHYESN-PSE-NLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV------SRHTHVKLGVYSQHSQ 468
Cdd:PRK13651 7 NIVKIFNKKlPTElKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdEKNKKKTKEKEKVLEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 469 DQLDLTKS-ALEFVRDKYSNISQDFQFWRGQLGR--------YGLTGEGQTVQMA-----------------------TL 516
Cdd:PRK13651 87 LVIQKTRFkKIKKIKEIRRRVGVVFQFAEYQLFEqtiekdiiFGPVSMGVSKEEAkkraakyielvgldesylqrspfEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 517 SEGQRSRVVFA-LLALEqPNVLLLDEPTNGLD---IPTIDSLADAINEFNGGVVVVSHD 571
Cdd:PRK13651 167 SGGQKRRVALAgILAME-PDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
82-309 |
9.62e-07 |
|
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: 50.27 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGK----VLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYP-----IPEHIDIYLLDEPAepsel 152
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPtsgsvLVDGTDLTLLSGKE----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 153 saldyvVTEAQHELKRIED----LVEKTILEDgpeseLLEPLyeRMDSLDPDTFESRAA--IILIGLGfNKKTilKKTKD 226
Cdd:cd03258 77 ------LRKARRRIGMIFQhfnlLSSRTVFEN-----VALPL--EIAGVPKAEIEERVLelLELVGLE-DKAD--AYPAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLK----RFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLT 302
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRdinrELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
....*..
gi 285811661 303 AYGGNYD 309
Cdd:cd03258 221 EEGTVEE 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
228-314 |
9.95e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.88 E-value: 9.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLDL----EACVWLEEyLKR-FDRTLVLVSHSQDFLNGVCTNMIDMRAQKLT 302
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqaQIMTLLNE-LKReFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 241
|
90
....*....|...
gi 285811661 303 AYGGNYDS-YHKT 314
Cdd:PRK09473 242 EYGNARDVfYQPS 254
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
395-561 |
9.95e-07 |
|
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: 50.18 E-value: 9.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 395 FDDISFHYESNPSENLyEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVsrhthvklgvysqhSQDQLDLT 474
Cdd:cd03244 5 FKNVSLRYRPNLPPVL-KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSI--------------LIDGVDIS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 475 KSALEFVRDKYSNISQDFQFWRGQLgRYGLTGEGQ-----------TVQM-------------------ATLSEGQRSRV 524
Cdd:cd03244 70 KIGLHDLRSRISIIPQDPVLFSGTI-RSNLDPFGEysdeelwqaleRVGLkefveslpggldtvveeggENLSVGQRQLL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 285811661 525 VFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEF 561
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIREA 185
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
91-281 |
1.01e-06 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 49.54 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 91 FHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDEPAepselsaldYVVteaQH-ELKR- 168
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVA---------YVP---QRsEVPDs 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 169 ----IEDLVEKTiledgpesellepLYERMDSLDPDTFESRAAII----LIGL-GFNKKTIlkktKDMSGGWKMRVALAK 239
Cdd:NF040873 70 lpltVRDLVAMG-------------RWARRGLWRRLTRDDRAAVDdaleRVGLaDLAGRQL----GELSGGQRQRALLAQ 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 285811661 240 ALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF---DRTLVLVSH 281
Cdd:NF040873 133 GLAQEADLLLLDEPTTGLDAESRERIIALLAEEharGATVVVVTH 177
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
77-282 |
1.07e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.16 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 77 ETSRDIKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPE-----------HiDIY---- 141
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEvtitgsivyngH-NIYsprt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 142 -----------LLDEPaEPSELSALDYVVTEAqhelkRIEDLVEKTILEDGPESELleplyermdsldpdtfesRAAiil 210
Cdd:PRK14239 80 dtvdlrkeigmVFQQP-NPFPMSIYENVVYGL-----RLKGIKDKQVLDEAVEKSL------------------KGA--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 211 iglgfnkkTILKKTKD--------MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEE--YLKRFDRTLVLVS 280
Cdd:PRK14239 133 --------SIWDEVKDrlhdsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEEtlLGLKDDYTMLLVT 204
|
..
gi 285811661 281 HS 282
Cdd:PRK14239 205 RS 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
82-258 |
1.09e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.56 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHG-KVLiQDSGLELNYGRRYGLLGENGCGKSTFLKALATrEYPiPEHIDIYLLDEPAEPSelSALDyvvt 160
Cdd:COG1129 5 LEMRGISKSFGGvKAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSG-VYQ-PDSGEILLDGEPVRFR--SPRD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 161 eAQH--------ELKRIEDLvekTILED---GpeselLEPLyeRMDSLDPDTFESRAAIIL--IGLGFNKKTILkktKDM 227
Cdd:COG1129 76 -AQAagiaiihqELNLVPNL---SVAENiflG-----REPR--RGGLIDWRAMRRRARELLarLGLDIDPDTPV---GDL 141
|
170 180 190
....*....|....*....|....*....|.
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLD 258
Cdd:COG1129 142 SVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
424-571 |
1.20e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 50.35 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYSQHSQDQLdLTKSALEFVRDKYSNISQDFQFWRGQ----- 498
Cdd:PRK10619 34 ISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKV-ADKNQLRLLRTRLTMVFQHFNLWSHMtvlen 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 499 -----------------------LGRYGLTGEGQTVQMATLSEGQRSRVVFA-LLALEqPNVLLLDEPTNGLD---IPTI 551
Cdd:PRK10619 113 vmeapiqvlglskqeareravkyLAKVGIDERAQGKYPVHLSGGQQQRVSIArALAME-PEVLLFDEPTSALDpelVGEV 191
|
170 180
....*....|....*....|
gi 285811661 552 DSLADAINEFNGGVVVVSHD 571
Cdd:PRK10619 192 LRIMQQLAEEGKTMVVVTHE 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
227-281 |
1.25e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.30 E-value: 1.25e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEY---LKRfDRTLVLVSH 281
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLfleLKK-DMTIVLVTH 203
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
93-287 |
1.28e-06 |
|
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: 49.45 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 93 GKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDE---PAEPSELSALDyvVTEAQHELKRI 169
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEditDLPPEERARLG--IFLAFQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 170 EDLVEKTILEDgpeselleplyermdsldpdtfesraaiilIGLGFnkktilkktkdmSGGWKMRVALAKALFVKPTLLL 249
Cdd:cd03217 90 PGVKNADFLRY------------------------------VNEGF------------SGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 285811661 250 LDDPTAHLDLEACVWLEE---YLKRFDRTLVLVSHSQDFLN 287
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEvinKLREEGKSVLIITHYQRLLD 168
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
228-281 |
1.29e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 51.32 E-value: 1.29e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF--DRTLVLVSH 281
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLmkGRTTIVIAH 533
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
110-309 |
1.30e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 50.62 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 110 YGLLGENGCGKSTFL---KALATREYPIPEHIDIYLLDEPAEPSELsalDYVVTEAQHELKRIEDLVekTILEDGPESEL 186
Cdd:PRK13631 55 YFIIGNSGSGKSTLVthfNGLIKSKYGTIQVGDIYIGDKKNNHELI---TNPYSKKIKNFKELRRRV--SMVFQFPEYQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 187 LEPLYERMDSLDP-----DTFESR--AAIILIGLGFNKKTILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDL 259
Cdd:PRK13631 130 FKDTIEKDIMFGPvalgvKKSEAKklAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDP 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 285811661 260 EACVWLEEYL---KRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYGGNYD 309
Cdd:PRK13631 210 KGEHEMMQLIldaKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYE 262
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
397-579 |
1.45e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 50.12 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 397 DISFHYESNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSrhthvklgvysqhsQDQLDLTKS 476
Cdd:PRK13650 9 NLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII--------------IDGDLLTEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 477 ALEFVRDKYSNISQ--DFQFWRGQLG---RYGLTGEG--------------QTVQM--------ATLSEGQRSRVVFALL 529
Cdd:PRK13650 75 NVWDIRHKIGMVFQnpDNQFVGATVEddvAFGLENKGipheemkervnealELVGMqdfkerepARLSGGQKQRVAIAGA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 285811661 530 ALEQPNVLLLDEPTNGLD-------IPTIDSLADainEFNGGVVVVSHDfrlLDKIA 579
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDpegrlelIKTIKGIRD---DYQMTVISITHD---LDEVA 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
93-281 |
1.48e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.49 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 93 GKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHI-----DIYLLDEPAEPSELSALDYVVTEaqHELk 167
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghDITRLKNREVPFLRRQIGMIFQD--HHL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 168 riedLVEKTILEDgpeseLLEPLYERMDSLDPDTFESRAAIILIGLgfnkktiLKKTKD----MSGGWKMRVALAKALFV 243
Cdd:PRK10908 91 ----LMDRTVYDN-----VAIPLIIAGASGDDIRRRVSAALDKVGL-------LDKAKNfpiqLSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 285811661 244 KPTLLLLDDPTAHLD---LEACVWLEEYLKRFDRTLVLVSH 281
Cdd:PRK10908 155 KPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATH 195
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
222-306 |
1.71e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.85 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 222 KKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLD----LEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMR 297
Cdd:PRK13636 137 KPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMK 216
|
....*....
gi 285811661 298 AQKLTAYGG 306
Cdd:PRK13636 217 EGRVILQGN 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
84-281 |
1.74e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 49.68 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 84 LSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATreypipehidiylLDEPAEpSELSALDYVVTEAQ 163
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-------------LETPSA-GELLAGTAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 164 HELKRIEDlvektiledgpESELLePLYERMDSLD--------PDTFESRAAIiliGLGfnkktilKKTKD----MSGGW 231
Cdd:PRK11247 81 EDTRLMFQ-----------DARLL-PWKKVIDNVGlglkgqwrDAALQALAAV---GLA-------DRANEwpaaLSGGQ 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 285811661 232 KMRVALAKALFVKPTLLLLDDPTAHLD----LEACVWLEEYLKRFDRTLVLVSH 281
Cdd:PRK11247 139 KQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTH 192
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
102-281 |
1.79e-06 |
|
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: 49.46 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 102 LELNYGRRYGLLGENGCGKSTFLKaLATREY-PIPEHIdiyLLDEpaepselsalDYVVTEAQHELKRIEDLVEK----- 175
Cdd:cd03249 24 LTIPPGKTVALVGSSGCGKSTVVS-LLERFYdPTSGEI---LLDG----------VDIRDLNLRWLRSQIGLVSQepvlf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 176 --TILE-------DGPESELLEP-----LYERMDSLdPDTFESraaiiLIGlgfnkktilKKTKDMSGGWKMRVALAKAL 241
Cdd:cd03249 90 dgTIAEnirygkpDATDEEVEEAakkanIHDFIMSL-PDGYDT-----LVG---------ERGSQLSGGQKQRIAIARAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 285811661 242 FVKPTLLLLDDPTAHLDLEACVWLEEYLKRF--DRTLVLVSH 281
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAH 196
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
91-284 |
2.01e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.74 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 91 FHGKVLIqDSGLELNYGRRYGLLGENGCGKSTFLKalatreypipehidiyLLDEPAEPSELSAL-DYVVTEAQHELKRI 169
Cdd:PRK13649 18 FEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQ----------------LLNGLHVPTQGSVRvDDTLITSTSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 170 EDLVEKTILE-DGPESELLEPLYERMDSLDPDTF-------ESRAAIILIGLGFNKKTILKKTKDMSGGWKMRVALAKAL 241
Cdd:PRK13649 81 KQIRKKVGLVfQFPESQLFEETVLKDVAFGPQNFgvsqeeaEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 285811661 242 FVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR---TLVLVSHSQD 284
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsgmTIVLVTHLMD 206
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
101-307 |
2.01e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 49.73 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 101 GLELNY--GRRYGLLGENGCGKSTFLKalatreypipeHID-IYLldepAEPSELSALDYVVTEA-QHELKRIEDLV--- 173
Cdd:PRK13647 23 GLSLSIpeGSKTALLGPNGAGKSTLLL-----------HLNgIYL----PQRGRVKVMGREVNAEnEKWVRSKVGLVfqd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 174 ------EKTILED---GPESElleplyermdSLDPDTFESRAAIILIGLGFnKKTILKKTKDMSGGWKMRVALAKALFVK 244
Cdd:PRK13647 88 pddqvfSSTVWDDvafGPVNM----------GLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285811661 245 PTLLLLDDPTAHLDLEACVWLEEYLKRFDR---TLVLVSHSQDFLNGVCTNMIDMRAQKLTAYGGN 307
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNqgkTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
424-547 |
2.21e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 49.31 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVsrhthvklgvysqhSQDQLDLTKSAlEFVRDKYsnISQDFQ---------- 493
Cdd:COG1101 35 VTVIGSNGAGKSTLLNAIAGSLPPDSGSI--------------LIDGKDVTKLP-EYKRAKY--IGRVFQdpmmgtapsm 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 494 ----------------------------FWRGQLGRYGLTGEGQ-TVQMATLSEGQRSRVvfALL--ALEQPNVLLLDEP 542
Cdd:COG1101 98 tieenlalayrrgkrrglrrgltkkrreLFRELLATLGLGLENRlDTKVGLLSGGQRQAL--SLLmaTLTKPKLLLLDEH 175
|
....*
gi 285811661 543 TNGLD 547
Cdd:COG1101 176 TAALD 180
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
516-587 |
2.70e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.09 E-value: 2.70e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285811661 516 LSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPT----IDSLADAINEFNGGVVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVqaqiLQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQN 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
84-318 |
2.73e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 49.28 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 84 LSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHI-----------DIYLLD-------- 144
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIkvdgkvlyfgkDIFQIDaiklrkev 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 145 -----EPAEPSELSALDYVV----TEAQHELKRIEDLVEKTILEDGpeseLLEPLYERMDSldpdtfesraaiiliglgf 215
Cdd:PRK14246 93 gmvfqQPNPFPHLSIYDNIAyplkSHGIKEKREIKKIVEECLRKVG----LWKEVYDRLNS------------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 216 nkktilkKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR--TLVLVSHSQDFLNGVCTNM 293
Cdd:PRK14246 150 -------PASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYV 222
|
250 260
....*....|....*....|....*
gi 285811661 294 IDMRAQKLTAYGGNYDSYHKTRSEL 318
Cdd:PRK14246 223 AFLYNGELVEWGSSNEIFTSPKNEL 247
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
109-305 |
2.81e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.42 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 109 RYGLLGENGCGKSTFLKalatreypipeHIDIYLldEPAEPSELSALDYVVTEAQHELKRIEDLVEKTiledgPESELLE 188
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFR-----------HFNGIL--KPTSGSVLIRGEPITKENIREVRKFVGLVFQN-----PDDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 189 PLYERMDS-------LDPDTFESRAAIILIGLGFnKKTILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLD--- 258
Cdd:PRK13652 94 PTVEQDIAfgpinlgLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqg 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 285811661 259 -LEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYG 305
Cdd:PRK13652 173 vKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
425-598 |
2.88e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 425 ALVGPNGVGKSTLLKIMTGELT----PQSGRVSrhTHVKLGVYSQHSQDQLDLTK---------------SALEFV---R 482
Cdd:PRK13547 31 ALLGRNGAGKSTLLKALAGDLTgggaPRGARVT--GDVTLNGEPLAAIDAPRLARlravlpqaaqpafafSAREIVllgR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 483 DKYSNISQDFQFWRGQLGRYGLTGEGQTVQMA----TLSEGQRSRVVFALL---------ALEQPNVLLLDEPTNGLDIP 549
Cdd:PRK13547 109 YPHARRAGALTHRDGEIAWQALALAGATALVGrdvtTLSGGELARVQFARVlaqlwpphdAAQPPRYLLLDEPTAALDLA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 285811661 550 ----TIDSLADAINEFNGGVVVVSHDFRLLDKIAQDIfvvenktATRWDGSIL 598
Cdd:PRK13547 189 hqhrLLDTVRRLARDWNLGVLAIVHDPNLAARHADRI-------AMLADGAIV 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
82-281 |
2.97e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.96 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATreypipehidiylldepaepseLSALDYVVTE 161
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLG----------------------LVAPDEGVIK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 162 AQHELkRIEDLVEKTILEdgpesELLEPLYERMDSLDPDTfesRAAIILIGLGFNK--KTILKKTKDMSGGWKMRVALAK 239
Cdd:PRK09544 63 RNGKL-RIGYVPQKLYLD-----TTLPLTVNRFLRLRPGT---KKEDILPALKRVQagHLIDAPMQKLSGGETQRVLLAR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 285811661 240 ALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTL----VLVSH 281
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcavLMVSH 179
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
386-586 |
3.65e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 49.08 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 386 ERLPPPVLAFDDISFHYESNpseNLYehlnfgvdmdsriALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYSQ 465
Cdd:PRK13631 33 EKQENELVALNNISYTFEKN---KIY-------------FIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 466 HSQDQLDLTKSALEFVRDKySNISQDFQFWRGQLGR--------YGLTGEGQTVQMAT---------------------- 515
Cdd:PRK13631 97 HELITNPYSKKIKNFKELR-RRVSMVFQFPEYQLFKdtiekdimFGPVALGVKKSEAKklakfylnkmglddsylerspf 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285811661 516 -LSEGQRSRVVFA-LLALeQPNVLLLDEPTNGLDIPTIDSLADAINEF---NGGVVVVSHDFRLLDKIAQDIFVVE 586
Cdd:PRK13631 176 gLSGGQKRRVAIAgILAI-QPEILIFDEPTAGLDPKGEHEMMQLILDAkanNKTVFVITHTMEHVLEVADEVIVMD 250
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
82-290 |
4.43e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.40 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDEPAEPSELSALDYVVTE 161
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 162 AQhELKRIEDLvekTILEDGPESELLEPLYERMDSLDPDTFESRAAIILIGLGFnKKTILKKTKDMSGGWKMRVALAKAL 241
Cdd:PRK09700 86 YQ-ELSVIDEL---TVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGL-KVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 285811661 242 FVKPTLLLLDDPTAHL---DLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVC 290
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRIC 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
391-547 |
4.61e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.23 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 391 PVLAFDDISFHYesnpseNLYEHLNfGVDMD----SRIALVGPNGVGKSTLLKIMT--GELTPQ---SGRVSRHTHvklG 461
Cdd:PRK14239 4 PILQVSDLSVYY------NKKKALN-SVSLDfypnEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGH---N 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 462 VYSQHSqDQLDLTK-------SALEFVRDKYSNISqdfqfwrgqlgrYGLTGEG------------QTVQMAT------- 515
Cdd:PRK14239 74 IYSPRT-DTVDLRKeigmvfqQPNPFPMSIYENVV------------YGLRLKGikdkqvldeaveKSLKGASiwdevkd 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 285811661 516 --------LSEGQRSRVVFALLALEQPNVLLLDEPTNGLD 547
Cdd:PRK14239 141 rlhdsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
96-258 |
4.81e-06 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 48.04 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 96 LIQDSGLELNYGRRYGLLGENGCGKSTFLKALATReypIPEHI----DIYLLDEPAEPSE-LSALDYVvteAQHElkrie 170
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR---VEGGGttsgQILFNGQPRKPDQfQKCVAYV---RQDD----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 171 DLVEK-TILEDGPESELLePLYERMDS-----LDPDTFESRAAIILIGLgfnkktilKKTKDMSGGWKMRVALAKALFVK 244
Cdd:cd03234 91 ILLPGlTVRETLTYTAIL-RLPRKSSDairkkRVEDVLLRDLALTRIGG--------NLVKGISGGERRRVSIAVQLLWD 161
|
170
....*....|....
gi 285811661 245 PTLLLLDDPTAHLD 258
Cdd:cd03234 162 PKVLILDEPTSGLD 175
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
84-309 |
5.77e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.79 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 84 LSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIdiylLDEPAEPSELSALDY---VVT 160
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL----LFEGEDISTLKPEIYrqqVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 161 EAQhelkriedlvEKTILEDGPESELLEPLYERMDSLDPDTFesRAAIILIGLgfnKKTILKKT-KDMSGGWKMRVALAK 239
Cdd:PRK10247 86 CAQ----------TPTLFGDTVYDNLIFPWQIRNQQPDPAIF--LDDLERFAL---PDTILTKNiAELSGGEKQRISLIR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 285811661 240 ALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR----TLVLVSHSQDFLNGvCTNMIdmraqKLTAYGGNYD 309
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVReqniAVLWVTHDKDEINH-ADKVI-----TLQPHAGEMQ 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
102-258 |
5.83e-06 |
|
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: 49.30 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 102 LELNYGRRYGLLGENGCGKSTFLKALAtREypIPEHIDIYLLDEPaepseLSALDyvvTEAQHELKR------------- 168
Cdd:COG4172 307 LTLRRGETLGLVGESGSGKSTLGLALL-RL--IPSEGEIRFDGQD-----LDGLS---RRALRPLRRrmqvvfqdpfgsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 169 -----IEDLVEktiledgpesellEPLYERMDSLDPDTFESRAAIILIGLGFNKKTILKKTKDMSGGWKMRVALAKALFV 243
Cdd:COG4172 376 sprmtVGQIIA-------------EGLRVHGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALIL 442
|
170
....*....|....*
gi 285811661 244 KPTLLLLDDPTAHLD 258
Cdd:COG4172 443 EPKLLVLDEPTSALD 457
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
410-570 |
7.13e-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: 48.98 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 410 LYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMtGELTP-QSGRVSRHTHVKLGVYSQHS-------QDQLDLTKSALEFV 481
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPvYGGRLTKPAKGKLFYVPQRPymtlgtlRDQIIYPDSSEDMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 482 RDKYSNISQDFQFWRGQLGrYGLTGEG--QTVQ--MATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADA 557
Cdd:TIGR00954 546 RRGLSDKDLEQILDNVQLT-HILEREGgwSAVQdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL 624
|
170
....*....|...
gi 285811661 558 INEFNGGVVVVSH 570
Cdd:TIGR00954 625 CREFGITLFSVSH 637
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
82-258 |
7.88e-06 |
|
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: 47.10 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDsgLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLD-EPAEPSelsalDYVVT 160
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFD--LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDvTAAPPA-----DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 161 EAQHELKRIEDL-VEKTI-LEDGPESELLEPLYERMDSldpdtfesraaiILIGLGFNKKtILKKTKDMSGGWKMRVALA 238
Cdd:cd03298 74 MLFQENNLFAHLtVEQNVgLGLSPGLKLTAEDRQAIEV------------ALARVGLAGL-EKRLPGELSGGERQRVALA 140
|
170 180
....*....|....*....|
gi 285811661 239 KALFVKPTLLLLDDPTAHLD 258
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALD 160
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
81-283 |
8.32e-06 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 48.15 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 81 DIKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALAtreypipEHID---IYLLDEPA---EPSE--- 151
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAg-----lEDPTsgeILIGGRDVtdlPPKDrni 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 152 ------------LSALDYV--------VTEAQHElKRIEDLVEktILEdgpeselLEPLYERmdsldpdtfesraaiili 211
Cdd:COG3839 78 amvfqsyalyphMTVYENIafplklrkVPKAEID-RRVREAAE--LLG-------LEDLLDR------------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 212 glgfnkktilkKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLD--------LEacvwLEEYLKRFDRTLVLVSHSQ 283
Cdd:COG3839 130 -----------KPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrvemrAE----IKRLHRRLGTTTIYVTHDQ 194
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
225-328 |
8.62e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 225 KDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYL----KRFDRTLVLVSHSQDFLNgvctnmidmRAQK 300
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKADKTIITIAHRIASIK---------RSDK 1427
|
90 100 110
....*....|....*....|....*....|...
gi 285811661 301 LTAYG-----GNYDSYHKTRSELETNQMKQYNK 328
Cdd:PTZ00265 1428 IVVFNnpdrtGSFVQAHGTHEELLSVQDGVYKK 1460
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
82-287 |
8.67e-06 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 46.38 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLF-HGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALA------TREYPIPEHIDIYLLdePAEPselsa 154
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAglwpwgSGRIGMPEGEDLLFL--PQRP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 155 ldYVvteaqhelkriedlvektiledgPESELLEPL-YERMDSLdpdtfesraaiiliglgfnkktilkktkdmSGGWKM 233
Cdd:cd03223 74 --YL-----------------------PLGTLREQLiYPWDDVL------------------------------SGGEQQ 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 285811661 234 RVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLN 287
Cdd:cd03223 99 RLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWK 152
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
396-570 |
9.98e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.77 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 396 DDISFHYESNPSEN---LYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV-------SRHTHV-----KL 460
Cdd:PRK13633 8 KNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtSDEENLwdirnKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 461 GVYSQHSQDQLDLTKsalefvrdkysnISQDFQFWRGQLG------RYGLTGEGQTVQMAT--------LSEGQRSRVVF 526
Cdd:PRK13633 88 GMVFQNPDNQIVATI------------VEEDVAFGPENLGippeeiRERVDESLKKVGMYEyrrhaphlLSGGQKQRVAI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 285811661 527 A-LLALeQPNVLLLDEPTNGLDIPTIDSLADAINEFNG----GVVVVSH 570
Cdd:PRK13633 156 AgILAM-RPECIIFDEPTAMLDPSGRREVVNTIKELNKkygiTIILITH 203
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
516-579 |
1.08e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 46.27 E-value: 1.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 516 LSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEF---NGGVVVVSHD----FRLLDKIA 579
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELadaGKAVLLISSEldelLGLCDRIL 175
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
227-286 |
1.13e-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: 46.69 E-value: 1.13e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYL----KRFDRTLVLVSHSQDFL 286
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCilglLLNNKTRILVTHQLQLL 191
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
397-547 |
1.13e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 397 DISFHYESNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIM------------------TGELTPQSGR------- 451
Cdd:PTZ00265 1170 DVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehTNDMTNEQDYqgdeeqn 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 452 -----VSRHTHVKLGVYSQHSQ----------DQLDLTKSALEFVRDKYSNISQDFQFWRG------QLGRYGLTGEG-- 508
Cdd:PTZ00265 1250 vgmknVNEFSLTKEGGSGEDSTvfknsgkillDGVDICDYNLKDLRNLFSIVSQEPMLFNMsiyeniKFGKEDATREDvk 1329
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 509 QTVQMA----------------------TLSEGQRSRVVFALLALEQPNVLLLDEPTNGLD 547
Cdd:PTZ00265 1330 RACKFAaidefieslpnkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
393-579 |
1.24e-05 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 47.76 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 393 LAFDDISFHYESnpsenlYEHLNfGVDMD----SRIALVGPNGVGKSTLLKIMTGELTPQSGRVSrhthvkLGvysqhSQ 468
Cdd:COG3839 4 LELENVSKSYGG------VEALK-DIDLDiedgEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIL------IG-----GR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 469 DQLDLTksalefVRDKysNISQDFQFW--------RGQLGrYGLTGEG--------------QTVQM--------ATLSE 518
Cdd:COG3839 66 DVTDLP------PKDR--NIAMVFQSYalyphmtvYENIA-FPLKLRKvpkaeidrrvreaaELLGLedlldrkpKQLSG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 519 GQRSRVvfAL---LALEqPNVLLLDEPTNGLD----IPTIDSLADAINEFNGGVVVVSHD----FRLLDKIA 579
Cdd:COG3839 137 GQRQRV--ALgraLVRE-PKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHDqveaMTLADRIA 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
516-587 |
1.29e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 48.14 E-value: 1.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 285811661 516 LSEGQRSRVVFAL-LALEqPNVLLLDEPTNGLDIpTI-----DSLADAINEFNGGVVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:COG4172 157 LSGGQRQRVMIAMaLANE-PDLLIADEPTTALDV-TVqaqilDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQ 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
390-452 |
1.36e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.09 E-value: 1.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285811661 390 PPVLAFDDISFHyesnpsenLYE---HlnfgvdmdsriALVGPNGVGKSTLLKIMTGELTPQSGRV 452
Cdd:COG1129 15 GGVKALDGVSLE--------LRPgevH-----------ALLGENGAGKSTLMKILSGVYQPDSGEI 61
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
424-586 |
1.49e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.12 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYSQHSQDQLDLTKSaLEFVRDKYSNISQDFQFWRGQLGRYG 503
Cdd:PRK13546 53 IGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGIEN-IEFKMLCMGFKRKEIKAMTPKIIEFS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 504 LTGEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEF---NGGVVVVSHDFRLLDKIAQ 580
Cdd:PRK13546 132 ELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFkeqNKTIFFVSHNLGQVRQFCT 211
|
....*.
gi 285811661 581 DIFVVE 586
Cdd:PRK13546 212 KIAWIE 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
93-281 |
1.66e-05 |
|
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: 46.71 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 93 GKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKaLATREYPiPEH----IDIYLLdEPAEPSELSA-LDYVVTEAQhelk 167
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTK-LIQRFYV-PENgrvlVDGHDL-ALADPAWLRRqVGVVLQENV---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 168 riedLVEKTILED---GPESELLEPLYERMDSLDPDTFesraaIILIGLGFNkkTIL-KKTKDMSGGWKMRVALAKALFV 243
Cdd:cd03252 87 ----LFNRSIRDNialADPGMSMERVIEAAKLAGAHDF-----ISELPEGYD--TIVgEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 285811661 244 KPTLLLLDDPTAHLDLEACVWLEEYLKRF--DRTLVLVSH 281
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAH 195
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
424-598 |
1.74e-05 |
|
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: 46.38 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRV------------SRHTHVKLGVYSQHSQDQLDLT-----KSALEFVRDKYS 486
Cdd:cd03218 29 VGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklpmHKRARLGIGYLPQEASIFRKLTveeniLAVLEIRGLSKK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 487 NISQ-------DFQF--WRGQLGrygltgegqtvqmATLSEGQRSRVVFA-LLALeQPNVLLLDEPTNGLD---IPTIDS 553
Cdd:cd03218 109 EREEkleelleEFHIthLRKSKA-------------SSLSGGERRRVEIArALAT-NPKFLLLDEPFAGVDpiaVQDIQK 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 285811661 554 LADAINEFNGGVVVVSHDFRLLDKIAQDIFVVenktatrWDGSIL 598
Cdd:cd03218 175 IIKILKDRGIGVLITDHNVRETLSITDRAYII-------YEGKVL 212
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
390-452 |
1.81e-05 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 47.89 E-value: 1.81e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 390 PPVLAFDDISFHYEsnPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV 452
Cdd:COG5265 355 GGEVRFENVSFGYD--PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRI 415
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
112-281 |
2.42e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.93 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 112 LLGENGCGKSTFLKALATREYPipEHIDIYLLDEPaepseLSALDyvvtEAQHELKRIED---------LVEK-TILEDG 181
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDG--SSGEVSLVGQP-----LHQMD----EEARAKLRAKHvgfvfqsfmLIPTlNALENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 182 PESELLEPLYERMDsldpdtfESRAAIILIGLGFNKKtILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEA 261
Cdd:PRK10584 110 ELPALLRGESSRQS-------RNGAKALLEQLGLGKR-LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180
....*....|....*....|....
gi 285811661 262 CVWLEEYL----KRFDRTLVLVSH 281
Cdd:PRK10584 182 GDKIADLLfslnREHGTTLILVTH 205
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
225-262 |
2.48e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 45.64 E-value: 2.48e-05
10 20 30
....*....|....*....|....*....|....*...
gi 285811661 225 KDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEAC 262
Cdd:PRK13539 126 GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
424-587 |
2.64e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 46.22 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVS-----------------RHThVKLgVYsQHSQDQLDLTKSALEFVRD--- 483
Cdd:PRK10419 41 VALLGRSGCGKSTLARLLVGLESPSQGNVSwrgeplaklnraqrkafRRD-IQM-VF-QDSISAVNPRKTVREIIREplr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 484 KYSNISQDFQFWRGQ--LGRYGLTGEGQTVQMATLSEGQRSRVVFA-LLALEqPNVLLLDEPTNGLDI----PTIDSLAD 556
Cdd:PRK10419 118 HLLSLDKAERLARASemLRAVDLDDSVLDKRPPQLSGGQLQRVCLArALAVE-PKLLILDEAVSNLDLvlqaGVIRLLKK 196
|
170 180 190
....*....|....*....|....*....|.
gi 285811661 557 AINEFNGGVVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:PRK10419 197 LQQQFGTACLFITHDLRLVERFCQRVMVMDN 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
222-283 |
3.06e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 46.56 E-value: 3.06e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285811661 222 KKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLD----LEACVWLEEYLKRFDRTLVLVSHSQ 283
Cdd:PRK11000 129 RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRLGRTMIYVTHDQ 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
424-579 |
3.20e-05 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 45.72 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQ---SGRV-------SRHT------HVK--------LGVY-SQHSQDQLDLTKSAL 478
Cdd:cd03234 36 MAILGSSGSGKTTLLDAISGRVEGGgttSGQIlfngqprKPDQfqkcvaYVRqddillpgLTVReTLTYTAILRLPRKSS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 479 EFVRDKYSNISQdfqfwrgqLGRYGLTGEGQTVqMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLD-------IPTI 551
Cdd:cd03234 116 DAIRKKRVEDVL--------LRDLALTRIGGNL-VKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDsftalnlVSTL 186
|
170 180 190
....*....|....*....|....*....|...
gi 285811661 552 DSLAdainEFNGGVVVVSHD-----FRLLDKIA 579
Cdd:cd03234 187 SQLA----RRNRIVILTIHQprsdlFRLFDRIL 215
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
478-586 |
3.45e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 46.46 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 478 LEFVRDKYSNIsQDFQFWRGQLGRYGLT----GEGQTVQMATLSEGQRsrVVFALLAL----EQPNVLLLDEPTNGLDIP 549
Cdd:COG4637 218 LEALRDAFPGF-EDIEVEPDEDGRVLLEfrekGLDRPFPARELSDGTL--RFLALLAAllspRPPPLLCIEEPENGLHPD 294
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 285811661 550 TIDSLADAINEF--NGGVVVVSHDFRLLDKIA-QDIFVVE 586
Cdd:COG4637 295 LLPALAELLREAseRTQVIVTTHSPALLDALEpEEVLVLE 334
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
425-571 |
3.50e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 46.37 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 425 ALVGPNGVGKSTLLKIMTGELTPQSGRVSRhthvklgvysqhsqDQLDLT-----KSALEFVRDKYS-----NISQDFQF 494
Cdd:PRK11607 49 ALLGASGCGKSTLLRMLAGFEQPTAGQIML--------------DGVDLShvppyQRPINMMFQSYAlfphmTVEQNIAF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 495 WRGQ--LGRYGLTGEGQT----VQMA--------TLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSL----AD 556
Cdd:PRK11607 115 GLKQdkLPKAEIASRVNEmlglVHMQefakrkphQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqlevVD 194
|
170
....*....|....*
gi 285811661 557 AINEFNGGVVVVSHD 571
Cdd:PRK11607 195 ILERVGVTCVMVTHD 209
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
459-576 |
3.95e-05 |
|
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: 45.84 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 459 KLGVYSQHSQDQLDLTKSALEFVRDKYSNISQDFQFWRGQLGRYGLTGEGQTVQMATLSEGQRS--RVVFALLALEQPN- 535
Cdd:pfam13304 180 DLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRllALLAALLSALPKGg 259
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 285811661 536 VLLLDEPTNGLDIPTIDSLADAINEF---NGGVVVVSHDFRLLD 576
Cdd:pfam13304 260 LLLIDEPESGLHPKLLRRLLELLKELsrnGAQLILTTHSPLLLD 303
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
93-258 |
4.14e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.83 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 93 GKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALatreypipehidIYLLDEPAEPSeLSALDYVVTEAQHELKRIEDL 172
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL------------LRLLSTEGEIQ-IDGVSWNSVTLQTWRKAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 173 VEKTILEDGPESELLEPlYERMDslDPDTFESRAAIILiglgfnkKTILKKTKD------------MSGGWKMRVALAKA 240
Cdd:TIGR01271 1298 PQKVFIFSGTFRKNLDP-YEQWS--DEEIWKVAEEVGL-------KSVIEQFPDkldfvlvdggyvLSNGHKQLMCLARS 1367
|
170
....*....|....*...
gi 285811661 241 LFVKPTLLLLDDPTAHLD 258
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLD 1385
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
390-573 |
4.15e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.56 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 390 PPVLAFDDISFHYESNpsenlyE-HlnfgvdmdsriALVGPNGVGKSTLLKIMTGELTPQSGRV----------SRHTHV 458
Cdd:COG3845 16 GGVVANDDVSLTVRPG------EiH-----------ALLGENGAGKSTLMKILYGLYQPDSGEIlidgkpvrirSPRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 459 KLG---VYsQH---------------SQDQLDLTKSALEFVRDKYSNISQdfqfwrgqlgRYGLtgegqTVQM----ATL 516
Cdd:COG3845 79 ALGigmVH-QHfmlvpnltvaenivlGLEPTKGGRLDRKAARARIRELSE----------RYGL-----DVDPdakvEDL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 517 SEGQRSRV--VFALLAleQPNVLLLDEPTNGLDIPTIDSLADAINEF--NG-GVVVVSHDFR 573
Cdd:COG3845 143 SVGEQQRVeiLKALYR--GARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITHKLR 202
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
97-281 |
4.36e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 46.36 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 97 IQDSGLELNYGRRYGLLGENGCGKSTFLkALATREYPiPEHIDIYLLDEP-AEPSE--LSALDYVVTEaqhelkRIeDLV 173
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLL-QLLTRAWD-PQQGEILLNGQPiADYSEaaLRQAISVVSQ------RV-HLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 174 EKTI-------LEDGPESEL--------LEPLYERMDSLDpdtfesraaiILIGLGfnkktilkkTKDMSGGWKMRVALA 238
Cdd:PRK11160 427 SATLrdnlllaAPNASDEALievlqqvgLEKLLEDDKGLN----------AWLGEG---------GRQLSGGEQRRLGIA 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 285811661 239 KALFVKPTLLLLDDPTAHLD-------LEAcvwLEEYLKrfDRTLVLVSH 281
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDaeterqiLEL---LAEHAQ--NKTVLMITH 532
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
389-570 |
4.60e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 45.41 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 389 PPPVLAFDDISFHYESNpsenlyeHLNFGVDMD---SRI-ALVGPNGVGKSTLLKI---MTgELTPQ---SGRV------ 452
Cdd:COG1117 8 LEPKIEVRNLNVYYGDK-------QALKDINLDipeNKVtALIGPSGCGKSTLLRClnrMN-DLIPGarvEGEIlldged 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 453 --SRHTHV-----KLGVYSQ----------------------HSQDQLD------LTKSAL-EFVRDKysnisqdfqfwr 496
Cdd:COG1117 80 iyDPDVDVvelrrRVGMVFQkpnpfpksiydnvayglrlhgiKSKSELDeiveesLRKAALwDEVKDR------------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 497 gqLGRYGLTgegqtvqmatLSEGQRSRVVFA-LLALEqPNVLLLDEPTNGLD-IPT------IDSLADainEFngGVVVV 568
Cdd:COG1117 148 --LKKSALG----------LSGGQQQRLCIArALAVE-PEVLLMDEPTSALDpISTakieelILELKK---DY--TIVIV 209
|
..
gi 285811661 569 SH 570
Cdd:COG1117 210 TH 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
107-286 |
4.64e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.86 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 107 GRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYlldepaepselSALDYVVTEAQHElkriEDLVEKTILEDGPeseL 186
Cdd:TIGR00957 664 GALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMK-----------GSVAYVPQQAWIQ----NDSLRENILFGKA---L 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 187 LEPLYERmdsldpdTFESRAAI--ILIGLGFNKKTILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLD------ 258
Cdd:TIGR00957 726 NEKYYQQ-------VLEACALLpdLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkh 798
|
170 180
....*....|....*....|....*....
gi 285811661 259 -LEACVWLEEYLKrfDRTLVLVSHSQDFL 286
Cdd:TIGR00957 799 iFEHVIGPEGVLK--NKTRILVTHGISYL 825
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
107-296 |
4.94e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 46.55 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 107 GRRYGLLGENGCGKSTFLKALATreypipehiDIYLLDEPAEPSELSALDYVVTEAQH-----ELKRIEDLVEktiledG 181
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTG---------DTTVTSGDATVAGKSILTNISDVHQNmgycpQFDAIDDLLT------G 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 182 PESELLeplYERMDSLDPDTFESRA--AIILIGLGFNKKTIlkkTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDL 259
Cdd:TIGR01257 2030 REHLYL---YARLRGVPAEEIEKVAnwSIQSLGLSLYADRL---AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 285811661 260 EACVWLEEYLK---RFDRTLVLVSHSQDFLNGVCTNMIDM 296
Cdd:TIGR01257 2104 QARRMLWNTIVsiiREGRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
80-282 |
4.94e-05 |
|
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: 44.46 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 80 RDIKLSSVSLLF-HGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREypIPEHI--DIYLLDEPAEPSELSAL- 155
Cdd:cd03213 7 RNLTVTVKSSPSkSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRR--TGLGVsgEVLINGRPLDKRSFRKIi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 156 DYVVTEAQHelkrIEDLvekTILEdgpeselleplyermdsldpdTFESRAAIiliglgfnkktilkktKDMSGGWKMRV 235
Cdd:cd03213 85 GYVPQDDIL----HPTL---TVRE---------------------TLMFAAKL----------------RGLSGGERKRV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 285811661 236 ALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF---DRTLVLVSHS 282
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLadtGRTIICSIHQ 170
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
93-259 |
5.52e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.20 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 93 GKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATrEYPIPEHI-------DIYLLDEP---AEPSELSALDYVVTEA 162
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGGAPrgarvtgDVTLNGEPlaaIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 163 QHEL--KRIEDLVektILEDGPESELLEPLYERMDSLDPDTFESRAAIILIGlgfnkktilKKTKDMSGGWKMRVALAKA 240
Cdd:PRK13547 92 AQPAfaFSAREIV---LLGRYPHARRAGALTHRDGEIAWQALALAGATALVG---------RDVTTLSGGELARVQFARV 159
|
170 180
....*....|....*....|....*...
gi 285811661 241 L---------FVKPTLLLLDDPTAHLDL 259
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
424-547 |
5.69e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.03 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIM---------TGELTPQSGRVSRHTHVKLGVYSQHSQDQLDLT-KSALEFV---RDKYSNISQ 490
Cdd:PLN03211 97 LAVLGPSGSGKSTLLNALagriqgnnfTGTILANNRKPTKQILKRTGFVTQDDILYPHLTvRETLVFCsllRLPKSLTKQ 176
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 491 D-FQFWRGQLGRYGLTGEGQTVQMAT----LSEGQRSRVVFALLALEQPNVLLLDEPTNGLD 547
Cdd:PLN03211 177 EkILVAESVISELGLTKCENTIIGNSfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
227-287 |
6.59e-05 |
|
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: 44.14 E-value: 6.59e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 227 MSGGWKM------RVALAKALFVKPTLLLLDDPTAHLDLEACVW-----LEEYLKRFDRTLVLVSHSQDFLN 287
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVD 187
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
82-281 |
6.60e-05 |
|
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: 44.53 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFH-GKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKaLATREYPIPE---HIDIYLLDEPAEPSELSALDY 157
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILR-LLFRFYDVSSgsiLIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 158 VVteaqhelkriEDLV--EKTILEDgpesellePLYERMDSLDPDTFES-RAAII---LIGLGFNKKTIL--KKTKdMSG 229
Cdd:cd03253 80 VP----------QDTVlfNDTIGYN--------IRYGRPDATDEEVIEAaKAAQIhdkIMRFPDGYDTIVgeRGLK-LSG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 285811661 230 GWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF--DRTLVLVSH 281
Cdd:cd03253 141 GEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAH 194
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
82-282 |
6.62e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 44.75 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDsgLELNYGRRYGLLGENGCGKSTFLKALATreYPIPEHIDIYLLDE---PAEPSE------- 151
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFD--LTIAAGERVAILGPSGAGKSTLLNLIAG--FLPPDSGRILWNGQdltALPPAErpvsmlf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 152 --------LSALDYV---------VTEAQHelKRIEDLVEKTILEDgpeselleplyermdsldpdtFESRaaiiliglg 214
Cdd:COG3840 78 qennlfphLTVAQNIglglrpglkLTAEQR--AQVEQALERVGLAG---------------------LLDR--------- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 215 fnkktilkKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLD----LEACVWLEEYLKRFDRTLVLVSHS 282
Cdd:COG3840 126 --------LPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
199-259 |
6.99e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 44.81 E-value: 6.99e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 199 PDTFESRAAIILIGLGFNKKTiLKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDL 259
Cdd:PRK11629 119 PAEINSRALEMLAAVGLEHRA-NHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
517-571 |
7.47e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.10 E-value: 7.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 517 SEGQRSRVVFALLALEQPNVLLLDEPTNGLDIpTIDS-----LADAINEFNGGVVVVSHD 571
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAqimtlLNELKREFNTAIIMITHD 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
98-351 |
7.52e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 98 QDSGLELNYGRRYGLLGENGCGKSTFLKaLATREYPiPEHIDIYLLDE------------------PAEPSELSalDYVV 159
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILK-LIERLYD-PTEGDIIINDShnlkdinlkwwrskigvvSQDPLLFS--NSIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 160 TEAQHELKRIEDL--VEKTILEDGPESE------------LLEPLYERMDSLDPDTF-ESRAAIILIG----LGFNKKTI 220
Cdd:PTZ00265 478 NNIKYSLYSLKDLeaLSNYYNEDGNDSQenknkrnscrakCAGDLNDMSNTTDSNELiEMRKNYQTIKdsevVDVSKKVL 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 221 L----------------KKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF----DRTLVLVS 280
Cdd:PTZ00265 558 IhdfvsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgneNRITIIIA 637
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 285811661 281 HSQDFLNGVCTNMIDMRAQKLTAYGGNYDSYHKTRSELETNQ-------MKQYNKQQEEIQHIKKFIASAGTYANLVK 351
Cdd:PTZ00265 638 HRLSTIRYANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNNknnkddnNNNNNNNNNKINNAGSYIIEQGTHDALMK 715
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
94-258 |
8.21e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 94 KVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATReypIPEHIDIYLLDEPAepselsaldyvvteaqHELKRIEDL- 172
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL---INSQGEIWFDGQPL----------------HNLNRRQLLp 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 173 VEKTI---LEDgPESEL----------LEPLYERMDSLDPDTFESRAAIILIGLGFNKKTILKKTKDMSGGWKMRVALAK 239
Cdd:PRK15134 360 VRHRIqvvFQD-PNSSLnprlnvlqiiEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIAR 438
|
170
....*....|....*....
gi 285811661 240 ALFVKPTLLLLDDPTAHLD 258
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLD 457
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
389-610 |
9.03e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.43 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 389 PPPVLAFDDISFHYESNPsenLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHV---------- 458
Cdd:PRK15439 8 APPLLCARSISKQYSGVE---VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPcarltpakah 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 459 KLGVYSQHSQDQLDLTKSALEfvrdkysNISqdFQFWRGQLGRYGLTGEGQT--------VQMATLSEGQRSRVVFALLA 530
Cdd:PRK15439 85 QLGIYLVPQEPLLFPNLSVKE-------NIL--FGLPKRQASMQKMKQLLAAlgcqldldSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 531 LEQPNVLLLDEPTNGLDIPTIDSLADAINEFNG---GVVVVSHDFRLLDKIAQDIFVVEN-------KTATRWDGSILQY 600
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLAqgvGIVFISHKLPEIRQLADRISVMRDgtialsgKTADLSTDDIIQA 235
|
250
....*....|
gi 285811661 601 KNKLAKNVVL 610
Cdd:PRK15439 236 ITPAAREKSL 245
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
517-584 |
1.02e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.57 E-value: 1.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 517 SEGQRSRVVFALLALEQPNVLLLDEPTNGLDIP----TIDSLADAINEFNGGVVVVSHDFRLLDKIAQDIFV 584
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSvqaqVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMV 227
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
516-585 |
1.25e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.41 E-value: 1.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 285811661 516 LSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPT---IDSLADAINEFNG-GVVVVSHDFRLLDKIAQDIFVV 585
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqIFRLLTRLNQNNNtTILLISHDLQMLSQWADKINVL 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
227-281 |
1.35e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.00 E-value: 1.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR--TLVLVSH 281
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTH 208
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
227-282 |
1.37e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 43.93 E-value: 1.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF-DR-TLVLVSHS 282
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLaDRlTVIIVTHN 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
425-587 |
1.43e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.48 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 425 ALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVklgVYSQHSQDQLDLTKSALEFVrdkysnisqdFQFWR-------- 496
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRV---LFDAEKGICLPPEKRRIGYV----------FQDARlfphykvr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 497 GQLgRYGLTGE-----GQTVQM-----------ATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPT-------IDS 553
Cdd:PRK11144 95 GNL-RYGMAKSmvaqfDKIVALlgieplldrypGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRkrellpyLER 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 285811661 554 LAdaiNEFNGGVVVVSHDfrlLDKI---AQDIFVVEN 587
Cdd:PRK11144 174 LA---REINIPILYVSHS---LDEIlrlADRVVVLEQ 204
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
90-259 |
1.50e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.19 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 90 LFHGKVLIQ---DSGLELNYGRRYGLLGENGCGKSTFLKALAtreypipehidiyLLDEPAEpSELS--ALDYVV--TEA 162
Cdd:PRK11308 21 LFKPERLVKaldGVSFTLERGKTLAVVGESGCGKSTLARLLT-------------MIETPTG-GELYyqGQDLLKadPEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 163 QHELKRIEDLV----------EKTIledgpESELLEPLyERMDSLDPDTFESRAAIIL--IGLgfnKKTILKKTKDM-SG 229
Cdd:PRK11308 87 QKLLRQKIQIVfqnpygslnpRKKV-----GQILEEPL-LINTSLSAAERREKALAMMakVGL---RPEHYDRYPHMfSG 157
|
170 180 190
....*....|....*....|....*....|
gi 285811661 230 GWKMRVALAKALFVKPTLLLLDDPTAHLDL 259
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
228-286 |
1.75e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 44.45 E-value: 1.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLD-------LEAcvwLEEYLKRfdRTLVLVSHSQDFL 286
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDahseqlvMQA---LNAASRR--QTTLMVTHQLEDL 547
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
184-286 |
2.10e-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: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 184 SELLEPLYERMDSLDPDTFESRAAII------LIGLGFNKKTILKKTKDMSGGWKMRVALAKALFV--KPTLLLLDDPTA 255
Cdd:cd03238 39 NEGLYASGKARLISFLPKFSRNKLIFidqlqfLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSepPGTLFILDEPST 118
|
90 100 110
....*....|....*....|....*....|....
gi 285811661 256 HLDLEACVWLEEYLKRF---DRTLVLVSHSQDFL 286
Cdd:cd03238 119 GLHQQDINQLLEVIKGLidlGNTVILIEHNLDVL 152
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
114-281 |
2.11e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.69 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 114 GENGCGKSTFLKALAT----REYPIPEHIDIYLLDEPAEPS-----ELSALDYVVTEAQHELKR--------IEDLVEKt 176
Cdd:COG0419 30 GPNGAGKSTILEAIRYalygKARSRSKLRSDLINVGSEEASvelefEHGGKRYRIERRQGEFAEfleakpseRKEALKR- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 177 ILEDGPESELLEPLYERMDSLDPDTFESRAAIILIGLGFNKKTILKKTKDMSGGWKMRVALAKALfvkptLLLLDdpTAH 256
Cdd:COG0419 109 LLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSGLDPIETLSGGERLRLALADLL-----SLILD--FGS 181
|
170 180
....*....|....*....|....*
gi 285811661 257 LDLEACVWLEEYLkrfdRTLVLVSH 281
Cdd:COG0419 182 LDEERLERLLDAL----EELAIITH 202
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
227-281 |
2.26e-04 |
|
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: 42.99 E-value: 2.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF--DRTLVLVSH 281
Cdd:cd03251 139 LSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAH 195
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
514-610 |
2.27e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 43.11 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 514 ATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNG--GVVVVSHDFRLLDKIAQDIFVVENKTAT 591
Cdd:PRK14246 152 SQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
90 100
....*....|....*....|..
gi 285811661 592 RWDGS---ILQYKNKLAKNVVL 610
Cdd:PRK14246 232 EWGSSneiFTSPKNELTEKYVI 253
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
425-584 |
2.42e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.84 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 425 ALVGPNGVGKSTLLKIMTGELTPQSGRVS---RHTHVKLGVYSQ-------HSQ----DQLDLTKSAL---EFVRdKYSN 487
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILylgKEVTFNGPKSSQeagigiiHQElnliPQLTIAENIFlgrEFVN-RFGR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 488 ISqdfqfWR-------GQLGRYGLTGEGQTVqMATLSEGQRSRVVFA-LLALEQpNVLLLDEPTNGL-DIPTiDSLADAI 558
Cdd:PRK10762 113 ID-----WKkmyaeadKLLARLNLRFSSDKL-VGELSIGEQQMVEIAkVLSFES-KVIIMDEPTDALtDTET-ESLFRVI 184
|
170 180
....*....|....*....|....*....
gi 285811661 559 NEF---NGGVVVVSHDFRLLDKIAQDIFV 584
Cdd:PRK10762 185 RELksqGRGIVYISHRLKEIFEICDDVTV 213
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
107-261 |
2.56e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.10 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 107 GRRYGLLGENGCGKSTFLKALATReypIPEH-IDIYLLDEPAEPselsaldyvvteAQHELKRIEDLVEKTILEdgP--- 182
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGR---IQGNnFTGTILANNRKP------------TKQILKRTGFVTQDDILY--Phlt 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 183 --ESELLEPLYERMDSLDPDTFESRAAIILIGLGFNK--KTILKKT--KDMSGGWKMRVALAKALFVKPTLLLLDDPTAH 256
Cdd:PLN03211 157 vrETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKceNTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
....*
gi 285811661 257 LDLEA 261
Cdd:PLN03211 237 LDATA 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
397-585 |
2.76e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.08 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 397 DISFHYESNPSENLyEHLNFGVDMDSRIALVGPNGVGKS-TLLKIMtgELTPQSGRVSRHTHVKLGVYSQHSQDQLDLTK 475
Cdd:PRK10261 19 NIAFMQEQQKIAAV-RNLSFSLQRGETLAIVGESGSGKSvTALALM--RLLEQAGGLVQCDKMLLRRRSRQVIELSEQSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 476 SALEFVRDkySNISQDFQFWRGQLGRYGLTGE------------GQTVQMA-----------------------TLSEGQ 520
Cdd:PRK10261 96 AQMRHVRG--ADMAMIFQEPMTSLNPVFTVGEqiaesirlhqgaSREEAMVeakrmldqvripeaqtilsryphQLSGGM 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 521 RSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAIN----EFNGGVVVVSHDFRLLDKIAQDIFVV 585
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEIADRVLVM 242
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
227-284 |
2.84e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 42.65 E-value: 2.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLD----LEACVWLEEYLKRFDRTLVLVSHSQD 284
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHSLE 191
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
516-584 |
2.89e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 43.36 E-value: 2.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 516 LSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPT---IDSLADAINEFNG-GVVVVSHDFRLLDKIAQDIFV 584
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTqaqIFRLLARLNQLQGtSILLISHDLESISQWADTITV 231
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
414-584 |
3.19e-04 |
|
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: 42.26 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 414 LNF-GVDMDSRIALVGPNGVGKSTLLKIMTGELTpqsGRVSRHTHVKLGVYSQHSQDqlDLTKSALEFVR-------DKY 485
Cdd:cd03279 20 IDFtGLDNNGLFLICGPTGAGKSTILDAITYALY---GKTPRYGRQENLRSVFAPGE--DTAEVSFTFQLggkkyrvERS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 486 SNISQDfQFWRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFAL-LALE---------QPNVLLLDEPTNGLDIPTIDSLA 555
Cdd:cd03279 95 RGLDYD-QFTRIVLLPQGEFDRFLARPVSTLSGGETFLASLSLaLALSevlqnrggaRLEALFIDEGFGTLDPEALEAVA 173
|
170 180 190
....*....|....*....|....*....|..
gi 285811661 556 DAINEFNGG---VVVVSHDFRLLDKIAQDIFV 584
Cdd:cd03279 174 TALELIRTEnrmVGVISHVEELKERIPQRLEV 205
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
228-281 |
3.54e-04 |
|
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: 42.80 E-value: 3.54e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLD-------LEACVWLEeylKRFDRTLVLVSH 281
Cdd:TIGR04520 138 SGGQKQRVAIAGVLAMRPDIIILDEATSMLDpkgrkevLETIRKLN---KEEGITVISITH 195
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
424-547 |
4.09e-04 |
|
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: 42.22 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYSQHSQDQLDLTKSALEFVRDKYSNISqdfqfwrgqlgrYG 503
Cdd:cd03300 29 FTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQNYALFPHLTVFENIA------------FG 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285811661 504 LTGEG--------------QTVQM--------ATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLD 547
Cdd:cd03300 97 LRLKKlpkaeikervaealDLVQLegyanrkpSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
392-452 |
4.15e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 4.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811661 392 VLAFDDISFHYESNpsenlyehlnfgvdmdSRIALVGPNGVGKSTLLKIMTGELTPQSGRV 452
Cdd:NF033858 14 TVALDDVSLDIPAG----------------CMVGLIGPDGVGKSSLLSLIAGARKIQQGRV 58
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
107-286 |
4.30e-04 |
|
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: 41.20 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 107 GRRYGLLGENGCGKSTFLKALAtREYPIPEHIDIYlldepaepselsaldyvvteaqhelkriedlvektiledgpesel 186
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALA-RELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 187 leplyermdsLDPDTFESRAAIILIGLGFNkktilKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLD-------- 258
Cdd:smart00382 36 ----------IDGEDILEEVLDQLLLIIVG-----GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDaeqealll 100
|
170 180
....*....|....*....|....*....
gi 285811661 259 -LEACVWLEEYLKRFDRTLVLVSHSQDFL 286
Cdd:smart00382 101 lLEELRLLLLLKSEKNLTVILTTNDEKDL 129
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
102-258 |
4.60e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 42.37 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 102 LELNYGRRYGLLGENGCGKST-FLKALATREypiPEHIDIYLLDEPAEPSELSALDyvvteaqhelkriedlVEKT--IL 178
Cdd:PRK13639 23 FKAEKGEMVALLGPNGAGKSTlFLHFNGILK---PTSGEVLIKGEPIKYDKKSLLE----------------VRKTvgIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 179 EDGPESELLEPlyermdsldpdTFESRAAIILIGLGFNKKTILKKTKD-----------------MSGGWKMRVALAKAL 241
Cdd:PRK13639 84 FQNPDDQLFAP-----------TVEEDVAFGPLNLGLSKEEVEKRVKEalkavgmegfenkpphhLSGGQKKRVAIAGIL 152
|
170
....*....|....*..
gi 285811661 242 FVKPTLLLLDDPTAHLD 258
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLD 169
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
112-289 |
4.86e-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: 42.68 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 112 LLGENGCGKSTFLKALA-----TREYPIPEHiDIYLLDEPAEPS-----ELSALDYVVTEAQHELKRIEDLVEKtiLEDG 181
Cdd:COG3593 28 LVGENNSGKSSILEALRlllgpSSSRKFDEE-DFYLGDDPDLPEieielTFGSLLSRLLRLLLKEEDKEELEEA--LEEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 182 PE--SELLEPLYERMDSLDPDTFESRAAIILIGLGfNKKTILKKTK-DMSGGWKMRV-------------ALAKALF--- 242
Cdd:COG3593 105 NEelKEALKALNELLSEYLKELLDGLDLELELSLD-ELEDLLKSLSlRIEDGKELPLdrlgsgfqrlillALLSALAelk 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 285811661 243 --VKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRT---LVLVSHSQDFLNGV 289
Cdd:COG3593 184 raPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKpnqVIITTHSPHLLSEV 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
508-587 |
5.68e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 508 GQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEF---NGGVVVVSHDFRLLDKIAQDIFV 584
Cdd:PRK10982 384 GHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELakkDKGIIIISSEMPELLGITDRILV 463
|
...
gi 285811661 585 VEN 587
Cdd:PRK10982 464 MSN 466
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
83-281 |
5.74e-04 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 41.70 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 83 KLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATReypIPEHI----DIYLLDEPaepselsaldyv 158
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGT---LSPAFsasgEVLLNGRR------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 159 VTEAQHELKRIedlvekTILedgPESELLEPLYERMDSLD---PDTF--ESRAAIIL-----IGL-GFNKKTIlkktKDM 227
Cdd:COG4136 68 LTALPAEQRRI------GIL---FQDDLLFPHLSVGENLAfalPPTIgrAQRRARVEqaleeAGLaGFADRDP----ATL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLD--LEACV--WLEEYLKRFDRTLVLVSH 281
Cdd:COG4136 135 SGGQRARVALLRALLAEPRALLLDEPFSKLDaaLRAQFreFVFEQIRQRGIPALLVTH 192
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
391-547 |
5.77e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.19 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 391 PVLAFDDISFHYESNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQS-------GRVSRHTHVKLgVY 463
Cdd:PLN03130 613 PAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdasvvirGTVAYVPQVSW-IF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 464 SQHSQDQLDLtksALEFVRDKY------SNISQDFQFWRG----QLGRYGLtgegqtvqmaTLSEGQRSRVVFALLALEQ 533
Cdd:PLN03130 692 NATVRDNILF---GSPFDPERYeraidvTALQHDLDLLPGgdltEIGERGV----------NISGGQKQRVSMARAVYSN 758
|
170
....*....|....
gi 285811661 534 PNVLLLDEPTNGLD 547
Cdd:PLN03130 759 SDVYIFDDPLSALD 772
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
228-258 |
5.95e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 42.37 E-value: 5.95e-04
10 20 30
....*....|....*....|....*....|.
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLD 258
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
513-576 |
5.99e-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: 41.15 E-value: 5.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 513 MATLSEGQRSRVVFA-LLALEQPNVL-LLDEPTNGLDIPTIDSLADAINEF---NGGVVVVSHDFRLLD 576
Cdd:cd03238 85 LSTLSGGELQRVKLAsELFSEPPGTLfILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEHNLDVLS 153
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
425-589 |
8.79e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.08 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 425 ALVGPNGVGKSTLLKIMTGELTPQSGRV-------SRHTH---VKLG---VYSQHSQ-DQLdltkSALE--FV----RDK 484
Cdd:PRK09700 35 ALLGENGAGKSTLMKVLSGIHEPTKGTItinninyNKLDHklaAQLGigiIYQELSViDEL----TVLEnlYIgrhlTKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 485 YSNIS-QDFQFWRGQ----LGRYGLTGEGQTvQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAIN 559
Cdd:PRK09700 111 VCGVNiIDWREMRVRaammLLRVGLKVDLDE-KVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMN 189
|
170 180 190
....*....|....*....|....*....|...
gi 285811661 560 EFNG---GVVVVSHDFRLLDKIAQDIFVVENKT 589
Cdd:PRK09700 190 QLRKegtAIVYISHKLAEIRRICDRYTVMKDGS 222
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
228-258 |
8.98e-04 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 41.13 E-value: 8.98e-04
10 20 30
....*....|....*....|....*....|.
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLD 258
Cdd:COG1126 138 SGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
226-306 |
9.64e-04 |
|
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: 40.63 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 226 DMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF----DRTLVLVSHsqDFLngvctnMIDMRAQKL 301
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEH--DLA------VLDYLSDRI 142
|
....*
gi 285811661 302 TAYGG 306
Cdd:cd03222 143 HVFEG 147
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
427-547 |
1.13e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 41.55 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 427 VGPNGVGKSTLLK-------IMTGEL---------TPQSGR------VSRHTHVKLGVYSQHSQDqLDLTKSALEFVRDK 484
Cdd:PRK11000 35 VGPSGCGKSTLLRmiagledITSGDLfigekrmndVPPAERgvgmvfQSYALYPHLSVAENMSFG-LKLAGAKKEEINQR 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 485 YSNISQDFQFWRgQLGRygltgegqtvQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLD 547
Cdd:PRK11000 114 VNQVAEVLQLAH-LLDR----------KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
499-605 |
1.13e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.64 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 499 LGRYGLTgEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEF--NGGVVVVSHDF-RLL 575
Cdd:NF000106 129 LERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvrDGATVLLTTQYmEEA 207
|
90 100 110
....*....|....*....|....*....|
gi 285811661 576 DKIAQDIFVVENKTATRwDGSILQYKNKLA 605
Cdd:NF000106 208 EQLAHELTVIDRGRVIA-DGKVDELKTKVG 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
228-290 |
1.23e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 41.32 E-value: 1.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDR----TLVLVSHSQDFLNGVC 290
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelglTIVLITHEMDVVKRIC 208
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
516-587 |
1.31e-03 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 41.71 E-value: 1.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285811661 516 LSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTI----DSLADAINEFNGGVVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLEN 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
84-257 |
1.58e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.44 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 84 LSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATrEYpIPEHIDIYLLDEPAE-PSELSALDYVVTEA 162
Cdd:PRK11288 7 FDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSG-NY-QPDAGSILIDGQEMRfASTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 163 QHELKriedLV-EKTILEDgpesELLEPLYERMDSLDPDTFESRAAIILIGLG--FNKKTilkKTKDMS-GGWKMrVALA 238
Cdd:PRK11288 85 YQELH----LVpEMTVAEN----LYLGQLPHKGGIVNRRLLNYEAREQLEHLGvdIDPDT---PLKYLSiGQRQM-VEIA 152
|
170
....*....|....*....
gi 285811661 239 KALFVKPTLLLLDDPTAHL 257
Cdd:PRK11288 153 KALARNARVIAFDEPTSSL 171
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
226-282 |
1.78e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 40.41 E-value: 1.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 226 DMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLK--RFDRTLVLVSHS 282
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILelKKDYTIVIVTHN 212
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
516-584 |
1.95e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.88 E-value: 1.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 516 LSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIP----TIDSLADAINEFNGGVVVVSHDFRLLDKIAQDIFV 584
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTiqaqIIELLLELQQKENMALVLITHDLALVAEAAHKIIV 226
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
421-460 |
2.10e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.45 E-value: 2.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 285811661 421 DSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS------RHT--HVKL 460
Cdd:pfam03193 106 GKTTVLAGQSGVGKSTLLNALLPELDLRTGEISeklgrgRHTttHVEL 153
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
414-547 |
2.13e-03 |
|
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: 39.93 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 414 LNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVS----RHTHVK------------LGVYSQHSQDQ-----LD 472
Cdd:cd03301 19 LNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrDVTDLPpkdrdiamvfqnYALYPHMTVYDniafgLK 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285811661 473 LTKSALEFVRDKYSNISQDFQFwRGQLGRYgltgegqtvqMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLD 547
Cdd:cd03301 99 LRKVPKDEIDERVREVAELLQI-EHLLDRK----------PKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
94-258 |
2.14e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 94 KVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATrEYPIpEHIDIYlldepAEPSelsaLDYVVTEAQhelkRIEDLV 173
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS-QFEI-SEGRVW-----AERS----IAYVPQQAW----IMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 174 EKTILEDGPESElleplyERM-DSLDPDTFESRAAIILIGLgfnKKTILKKTKDMSGGWKMRVALAKALFVKPTLLLLDD 252
Cdd:PTZ00243 738 RGNILFFDEEDA------ARLaDAVRVSQLEADLAQLGGGL---ETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
|
....*.
gi 285811661 253 PTAHLD 258
Cdd:PTZ00243 809 PLSALD 814
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
424-460 |
2.52e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.69 E-value: 2.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 285811661 424 IALVGPNGVGKSTLLKIMTGELTPQSGRVS------RHT--HVKL 460
Cdd:cd01854 88 SVLVGQSGVGKSTLLNALLPELVLATGEISeklgrgRHTttHREL 132
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
227-290 |
3.06e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 40.66 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDL-------EACVW-------------LEEYLKRFDRTLVLvsHsqdfl 286
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDVvtekeifESCLCklmsnktrilvtsKLEHLKKADKILLL--H----- 621
|
....
gi 285811661 287 NGVC 290
Cdd:TIGR01271 622 EGVC 625
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
392-452 |
3.40e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 39.59 E-value: 3.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 392 VLAFDDISFHY-ESNPSenlYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRV 452
Cdd:PRK13644 1 MIRLENVSYSYpDGTPA---LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV 59
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
395-585 |
3.42e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 39.99 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 395 FDDISFHY-ESNPSE-NLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHvKLGVYSQHSQDQLD 472
Cdd:PRK13645 9 LDNVSYTYaKKTPFEfKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDY-AIPANLKKIKEVKR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 473 LTKS-ALEFVRDKYS----NISQDFQFWRGQLGR-----YGLTGEG-QTVQMA---------TLSEGQRSRVVFALLALE 532
Cdd:PRK13645 88 LRKEiGLVFQFPEYQlfqeTIEKDIAFGPVNLGEnkqeaYKKVPELlKLVQLPedyvkrspfELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 533 QPNVLLLDEPTNGLDiPTIDSlaDAIN-------EFNGGVVVVSHDFRLLDKIAQDIFVV 585
Cdd:PRK13645 168 DGNTLVLDEPTGGLD-PKGEE--DFINlferlnkEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
227-279 |
3.48e-03 |
|
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: 39.34 E-value: 3.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLdleACVWLEE------YLKRFDRTLVLV 279
Cdd:cd03224 133 LSGGEQQMLAIARALMSRPKLLLLDEPSEGL---APKIVEEifeairELRDEGVTILLV 188
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
520-587 |
4.68e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 39.30 E-value: 4.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 520 QRSRVVFALLAlEQPnVLLLDEPTNGLDIPT----IDSLADAINEFNGGVVVVSHDFRLLDKIAQDIFVVEN 587
Cdd:PRK10418 147 QRMMIALALLC-EAP-FIIADEPTTDLDVVAqariLDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSH 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
82-289 |
4.89e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 39.20 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 82 IKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALaTREYPiPEHIDIYLLDEPAE--PSELSALDYVV 159
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCL-TGFYK-PTGGTILLRGQHIEglPGHQIARMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 160 TEAQH-----ELKRIEDLV--EKTILEDGPESELLE-PLYER--MDSLDpdtfesRAAIIL--IGLgfnKKTILKKTKDM 227
Cdd:PRK11300 84 RTFQHvrlfrEMTVIENLLvaQHQQLKTGLFSGLLKtPAFRRaeSEALD------RAATWLerVGL---LEHANRQAGNL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHL------DLEAcvwLEEYLKR-FDRTLVLVSHSQDFLNGV 289
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLnpketkELDE---LIAELRNeHNVTVLLIEHDMKLVMGI 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
226-284 |
5.03e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 39.63 E-value: 5.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285811661 226 DMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRF----DRTLVLVSHSQD 284
Cdd:PRK10070 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqakhQRTIVFISHDLD 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
91-258 |
5.61e-03 |
|
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: 38.68 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 91 FHGKVLIQDSGLELNYGRRYGLLGENGCGKST----------------FLKALATREYPIPE--HIDI-YLldePAEPS- 150
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTtfymivglvkpdsgkiLLDGQDITKLPMHKraRLGIgYL---PQEASi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 151 --ELSALD--YVVTEAQHELKRIEdlveKTILEdgpesELLEPlyermdsldpdtfesraaiiliglgFNKKTILKKTKD 226
Cdd:cd03218 87 frKLTVEEniLAVLEIRGLSKKER----EEKLE-----ELLEE-------------------------FHITHLRKSKAS 132
|
170 180 190
....*....|....*....|....*....|...
gi 285811661 227 -MSGGWKMRVALAKALFVKPTLLLLDDPTAHLD 258
Cdd:cd03218 133 sLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
228-261 |
5.76e-03 |
|
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: 38.18 E-value: 5.76e-03
10 20 30
....*....|....*....|....*....|....
gi 285811661 228 SGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEA 261
Cdd:cd03215 106 SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
514-548 |
5.82e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.53 E-value: 5.82e-03
10 20 30
....*....|....*....|....*....|....*
gi 285811661 514 ATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDI 548
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
227-278 |
5.82e-03 |
|
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: 39.07 E-value: 5.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDL-------EACVW-------------LEEYLKRFDRTLVL 278
Cdd:cd03291 160 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVftekeifESCVCklmanktrilvtsKMEHLKKADKILIL 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
227-284 |
7.05e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 38.94 E-value: 7.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLD----LEACVWLEEYLKRFDRTLVLVSHSQD 284
Cdd:PRK13650 141 LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLD 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
227-547 |
8.35e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 38.92 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLDL----EACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLt 302
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 303 ayggnydsyhktrseLETNQMKQYnkqqeeiqhikkFIASAGTYAnlvkqaksrQKILDKmEADGLVQPVVPDKV----- 377
Cdd:PRK15134 236 ---------------VEQNRAATL------------FSAPTHPYT---------QKLLNS-EPSGDPVPLPEPASplldv 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 378 ------FSFRFPQVERLPPPVLAFDDISFhyESNPSENLyehlnfgvdmdsriALVGPNGVGKST----LLKIMTGE--- 444
Cdd:PRK15134 279 eqlqvaFPIRKGILKRTVDHNVVVKNISF--TLRPGETL--------------GLVGESGSGKSTtglaLLRLINSQgei 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 445 ---------LTPQSGRVSRHthvKLGVYSQHSQDQLDLTKSALEF------VRDKYSNISQDFQFWRGQLGRYGLTGEGQ 509
Cdd:PRK15134 343 wfdgqplhnLNRRQLLPVRH---RIQVVFQDPNSSLNPRLNVLQIieeglrVHQPTLSAAQREQQVIAVMEEVGLDPETR 419
|
330 340 350
....*....|....*....|....*....|....*...
gi 285811661 510 TVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLD 547
Cdd:PRK15134 420 HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
227-258 |
8.56e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 38.63 E-value: 8.56e-03
10 20 30
....*....|....*....|....*....|..
gi 285811661 227 MSGGWKMRVALAKALFVKPTLLLLDDPTAHLD 258
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
504-584 |
9.23e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 38.88 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811661 504 LTGEGQTVQmaTLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPT---IDSLADAINEFNGGVVVVSHDFRLLDKIAQ 580
Cdd:PRK15439 394 FNHAEQAAR--TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSArndIYQLIRSIAAQNVAVLFISSDLEEIEQMAD 471
|
....
gi 285811661 581 DIFV 584
Cdd:PRK15439 472 RVLV 475
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
514-571 |
9.83e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 38.52 E-value: 9.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 285811661 514 ATLSEGQRSRVVFA-LLALEqPNVLLLDEPTNGLDIPTIDS----LADaIN-EFNGGVVVVSHD 571
Cdd:COG1135 139 SQLSGGQKQRVGIArALANN-PKVLLCDEATSALDPETTRSildlLKD-INrELGLTIVLITHE 200
|
|
| |
