|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
75-590 |
4.77e-177 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 511.53 E-value: 4.77e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 75 IESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELP------IPEHMDIYHLSREIEA-SDMSSLE 147
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPdsgevsIPKGLRIGYLPQEPPLdDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 148 AVISCDEERLKLEKE---AESLASQDDGGGEQLDRIYERLEALDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMR 224
Cdd:COG0488 81 TVLDGDAELRALEAEleeLEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 225 IALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKLKIYTGNYDQYVQT 304
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 305 RSELEENQMKMYKWEQDQIASMKEYIARFGhGSAKLARQAQSKEKTLAKMERgglTEKVVRDKVLVFRFVDVGKLPPPVL 384
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRFR-AKARKAKQAQSRIKALEKLER---EEPPRRDKTVEIRFPPPERLGKKVL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 385 QFVEVTFGYtPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIAQFHQHLAEkLDLEL 464
Cdd:COG0488 317 ELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEE-LDPDK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 465 SALQFMIREYPGNEEEKMRGAIGKFGLSGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEA 544
Cdd:COG0488 395 TVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1955823976 545 LNEWDGGLVLVSHDFRLINQVAQEIWVCENQAVTKWEGDIMDFKAH 590
Cdd:COG0488 475 LDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
68-592 |
5.08e-170 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 500.54 E-value: 5.08e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 68 PLSRDIRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELP-IPEHMDIYHLSREIEASDMSSL 146
Cdd:PLN03073 173 PAIKDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIDgIPKNCQILHVEQEVVGDDTTAL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 147 EAVISCDEERLKL-EKEAESLASQ---------------------DDGGGEQLDRIYERLEALDAATAEKRAAEILYGLG 204
Cdd:PLN03073 253 QCVLNTDIERTQLlEEEAQLVAQQrelefetetgkgkgankdgvdKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 205 FNKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNII 284
Cdd:PLN03073 333 FTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDIL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 285 HMQNRKLKIYTGNYDQYVQTRSELEENQMKMYKWEQDQIASMKEYIARFGHgSAKLARQAQSKEKTLakmERGGLTEKVV 364
Cdd:PLN03073 413 HLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRY-NAKRASLVQSRIKAL---DRLGHVDAVV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 365 RDKVLVFRFVDVGKLP-PPVLQFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRR 443
Cdd:PLN03073 489 NDPDYKFEFPTPDDRPgPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 444 HNHLRIAQFHQHLAEKLDLELSALQFMIREYPGNEEEKMRGAIGKFGLSGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHL 523
Cdd:PLN03073 569 SAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHI 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955823976 524 LLLDEPTNHLDIETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWVCENQAVTKWEGDIMDFKAHLK 592
Cdd:PLN03073 649 LLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKTLQ 717
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
95-591 |
2.18e-113 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 352.17 E-value: 2.18e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 95 LNYGRRYGLLGLNGCGKSTLLAAIGCR------ELPIPEHMDIYHLSREIEASDMSSLEAVISCDEERLKLEKEAESLAS 168
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEisadggSYTFPGNWQLAWVNQETPALPQPALEYVIDGDREYRQLEAQLHDANE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 169 QDDGggEQLDRIYERLEALDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:PRK10636 104 RNDG--HAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 249 LEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKLKIYTGNYDQYVQTRSELEENQMKMYKWEQDQIASMKE 328
Cdd:PRK10636 182 LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQAMYESQQERVAHLQS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 329 YIARFGHGSAKlARQAQSKEKTLAKMErggLTEKVVRDKVLVFRFVDVGKLPPPVLQFVEVTFGYTpENLIYKNLDFGVD 408
Cdd:PRK10636 262 YIDRFRAKATK-AKQAQSRIKMLERME---LIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSAGYG-DRIILDSIKLNLV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 409 LDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIAQFHQHLAEKLDLELSALQFMIREYPGNEEEKMRGAIGK 488
Cdd:PRK10636 337 PGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLARLAPQELEQKLRDYLGG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 489 FGLSGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEWDGGLVLVSHDFRLINQVAQE 568
Cdd:PRK10636 417 FGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDD 496
|
490 500
....*....|....*....|...
gi 1955823976 569 IWVCENQAVTKWEGDIMDFKAHL 591
Cdd:PRK10636 497 LYLVHDGKVEPFDGDLEDYQQWL 519
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
98-593 |
2.38e-86 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 278.31 E-value: 2.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 98 GRRYGLLGLNGCGKSTLlaaigcrelpipehMDIyhLSREIEAS-----------------------DMSSLEAVISCDE 154
Cdd:PRK15064 27 GNRYGLIGANGCGKSTF--------------MKI--LGGDLEPSagnvsldpnerlgklrqdqfafeEFTVLDTVIMGHT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 155 ERLKLEKEAESL-----ASQDDGGgeqldRIYErLEA----LDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRI 225
Cdd:PRK15064 91 ELWEVKQERDRIyalpeMSEEDGM-----KVAD-LEVkfaeMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 226 ALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKLKIYTGNYDQYVQTR 305
Cdd:PRK15064 165 LLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 306 SELEENQMKMYKWEQDQIASMKEYIARFGHGSAKlARQAQSKEKTLAKMErggLTEKVVRDKVLVF-RFVDVGKLPPPVL 384
Cdd:PRK15064 245 TQARERLLADNAKKKAQIAELQSFVSRFSANASK-AKQATSRAKQIDKIK---LEEVKPSSRQNPFiRFEQDKKLHRNAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 385 QFVEVTFGYtPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIAQFHQHLAEKLDLEL 464
Cdd:PRK15064 321 EVENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 465 SALQFMiREY--PGNEEEKMRGAIGKFGLSGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLA 542
Cdd:PRK15064 400 TLFDWM-SQWrqEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLN 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 543 EALNEWDGGLVLVSHDFRLINQVAQEIWVCENQAVTKWEGDIMDFKAHLKM 593
Cdd:PRK15064 479 MALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQGI 529
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
73-573 |
6.24e-66 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 227.14 E-value: 6.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGcRELPIPEHMDIYHLS-----------REIEAS 141
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN-GEVLLDDGRIIYEQDlivarlqqdppRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 142 DMSSLEAVISCDEERLKLEKEAESLASQD--DGGGEQLDRIYERLEALDAATAEKRAAEILYGLGFNKQmqaKKTRDFSG 219
Cdd:PRK11147 83 VYDFVAEGIEEQAEYLKRYHDISHLVETDpsEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPD---AALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 220 GWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKLKIYTGNYD 299
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 300 QYVQTRSE---LEENQMKmykwEQDQIASMKEYIARFGhgsAKlARQAQSKEKTLA----KMERGGLTEKVVRDKVLVFR 372
Cdd:PRK11147 240 QYLLEKEEalrVEELQNA----EFDRKLAQEEVWIRQG---IK-ARRTRNEGRVRAlkalRRERSERREVMGTAKMQVEE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 373 FVDVGKLpppVLQFVEVTFGYTPENLIyKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIAQF 452
Cdd:PRK11147 312 ASRSGKI---VFEMENVNYQIDGKQLV-KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 453 HQHLAEkLDLELSAL--------QFMIreypGNEEEKMRGAIGKFGLSGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLL 524
Cdd:PRK11147 388 DQHRAE-LDPEKTVMdnlaegkqEVMV----NGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLL 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1955823976 525 LLDEPTNHLDIETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWVCE 573
Cdd:PRK11147 463 ILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFE 511
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
97-596 |
4.01e-56 |
|
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: 198.62 E-value: 4.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 97 YGRRYGLLGLNGCGKSTLL-----------------AAIGCRELPIPEHMDIYHLSREIEASDMSSLEAVIScdeerlKL 159
Cdd:TIGR03719 30 PGAKIGVLGLNGAGKSTLLrimagvdkdfngearpqPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKDALD------RF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 160 EKEAESLASQD---DGGGEQLDRIYERLEALDAATAEKRAaEIlyglgfnkQMQA-------KKTRDFSGGWRMRIALAR 229
Cdd:TIGR03719 104 NEISAKYAEPDadfDKLAAEQAELQEIIDAADAWDLDSQL-EI--------AMDAlrcppwdADVTKLSGGERRRVALCR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 230 ALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKLKIYTGNYDQYV---QTRS 306
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLeqkQKRL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 307 ELEENQ----MKMYKWEQDQIASmkeyiarfghgSAKlARQAQSKEKtLAKMERGGLTEKVVRDKVLVFrFVDVG-KLPP 381
Cdd:TIGR03719 255 EQEEKEesarQKTLKRELEWVRQ-----------SPK-GRQAKSKAR-LARYEELLSQEFQKRNETAEI-YIPPGpRLGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 382 PVLQFVEVTFGYTpENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIA---QFHQHLAE 458
Cdd:TIGR03719 321 KVIEAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAyvdQSRDALDP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 459 KLDL--ELSALQFMIReyPGNEEEKMRGAIGKFGLSGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIE 536
Cdd:TIGR03719 400 NKTVweEISGGLDIIK--LGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 537 TIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWVCENQAVTKW-EGDIMDFKAHLKMKAG 596
Cdd:TIGR03719 478 TLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWfEGNFSEYEEDKKRRLG 538
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
384-575 |
1.64e-52 |
|
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: 176.49 E-value: 1.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYtPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIAQFHQhlaekldle 463
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 464 lsalqfmireypgneeekmrgaigkfglsgkaqvmpmknLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAE 543
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|..
gi 1955823976 544 ALNEWDGGLVLVSHDFRLINQVAQEIWVCENQ 575
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
97-558 |
1.84e-45 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 169.14 E-value: 1.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 97 YGRRYGLLGLNGCGKSTLL-------------------AAIGCreLPIPEHMDIYHLSREIEASDMSSLEAVIScdeerl 157
Cdd:PRK11819 32 PGAKIGVLGLNGAGKSTLLrimagvdkefegearpapgIKVGY--LPQEPQLDPEKTVRENVEEGVAEVKAALD------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 158 KLEKEAESLASQDDGGGEQLD---RIYERLEALDAATAEkRAAEIlyglgfnkQMQA-------KKTRDFSGGWRMRIAL 227
Cdd:PRK11819 104 RFNEIYAAYAEPDADFDALAAeqgELQEIIDAADAWDLD-SQLEI--------AMDAlrcppwdAKVTKLSGGERRRVAL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 228 ARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKLKIYTGNYDQYV---QT 304
Cdd:PRK11819 175 CRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLeqkAK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 305 RSELEENQ----MKMYKWEQDQIASmkeyiarfghgSAKlARQAQSK------EKTLAKMErggltEKVVRDKVLVfrfv 374
Cdd:PRK11819 255 RLAQEEKQeaarQKALKRELEWVRQ-----------SPK-ARQAKSKarlaryEELLSEEY-----QKRNETNEIF---- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 375 dvgkLPPP------VLQFVEVTFGYtPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLR 448
Cdd:PRK11819 314 ----IPPGprlgdkVIEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 449 IA---QFHQHLAEKLDL--ELSALQFMIReyPGNEEEKMRGAIGKFGLSGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHL 523
Cdd:PRK11819 389 LAyvdQSRDALDPNKTVweEISGGLDIIK--VGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNV 466
|
490 500 510
....*....|....*....|....*....|....*
gi 1955823976 524 LLLDEPTNHLDIETIDSLAEALNEWDGGLVLVSHD 558
Cdd:PRK11819 467 LLLDEPTNDLDVETLRALEEALLEFPGCAVVISHD 501
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
73-290 |
1.13e-44 |
|
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: 155.30 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPI------PEHMDIYHLsreieasdmssl 146
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDegivtwGSTVKIGYF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 147 eaviscdeerlklekeaeslasqddgggEQLdriyerlealdaataekraaeilyglgfnkqmqakktrdfSGGWRMRIA 226
Cdd:cd03221 69 ----------------------------EQL----------------------------------------SGGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 227 LARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRK 290
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
73-303 |
6.11e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 135.58 E-value: 6.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPipehmdiyhLSREIEASdmssleavisc 152
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEP---------DSGTVKLG----------- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 deERLKLekeaeSLASQDdggGEQLD---RIYERLEALDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALAR 229
Cdd:COG0488 376 --ETVKI-----GYFDQH---QEELDpdkTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 230 ALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKLKIYTGNYDQYVQ 303
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
73-571 |
2.71e-28 |
|
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: 118.85 E-value: 2.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIV--DSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPIPEHM---------DIYHLSREIEAS 141
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAvdGVSLTIAPGETVALVGESGSGKSTLALAL-MGLLPHGGRIsgevlldgrDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 142 D--------MSSLEAVISCDEerlklekEAESLasqddgggeqldriyeRLEALDAATAEKRAAEILYGLGFNKQMQAkK 213
Cdd:COG1123 84 RigmvfqdpMTQLNPVTVGDQ-------IAEAL----------------ENLGLSRAEARARVLELLEAVGLERRLDR-Y 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 214 TRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLD----LEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNR 289
Cdd:COG1123 140 PHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 290 KLkIYTGNYDQYVQTRSELEEnqmkmykweqdqiasmkeyIARFGHGSAKLARQAQSKEKTLAkmerggltekvVRDkvL 369
Cdd:COG1123 220 RI-VEDGPPEEILAAPQALAA-------------------VPRLGAARGRAAPAAAAAEPLLE-----------VRN--L 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 370 VFRFVDVGKLPPPVLQfvevtfgytpenliyknldfGVDLD----SRIALVGPNGAGKSTLLKLMTGdLVP-------LD 438
Cdd:COG1123 267 SKRYPVRGKGGVRAVD--------------------DVSLTlrrgETLGLVGESGSGKSTLARLLLG-LLRptsgsilFD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 439 GM-VRRHNHLRIAQFHQH---------------------LAEKLDLelsalqfmIREYPGNE-EEKMRGAIGKFGLSGK- 494
Cdd:COG1123 326 GKdLTKLSRRSLRELRRRvqmvfqdpysslnprmtvgdiIAEPLRL--------HGLLSRAErRERVAELLERVGLPPDl 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 495 AQVMPMkNLSDGQRSRV-IFAWLAwRQPHLLLLDEPTNHLDIET----IDSLAEALNEWDGGLVLVSHDFRLINQVAQEI 569
Cdd:COG1123 398 ADRYPH-ELSGGQRQRVaIARALA-LEPKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDLAVVRYIADRV 475
|
..
gi 1955823976 570 WV 571
Cdd:COG1123 476 AV 477
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
284-373 |
5.18e-28 |
|
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: 107.27 E-value: 5.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 284 IHMQNRKLKIYTGNYDQYVQTRSELEENQMKMYKWEQDQIASMKEYIARFGHGsAKLARQAQSKEKTLAKMERgglTEKV 363
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAK-ASKAKQAQSRIKALEKMER---IEKP 76
|
90
....*....|
gi 1955823976 364 VRDKVlVFRF 373
Cdd:pfam12848 77 ERDKP-KLRF 85
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
382-558 |
3.00e-27 |
|
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: 109.11 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 382 PVLQFVEVTFGYtPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHN---HLRIAQFHQHLA- 457
Cdd:COG4133 1 MMLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepiRDAREDYRRRLAy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 458 ----EKLDLELSA---LQFMIREYPGN-EEEKMRGAIGKFGLSGKAQVmPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEP 529
Cdd:COG4133 80 lghaDGLKPELTVrenLRFWAALYGLRaDREAIDEALEAVGLAGLADL-PVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 1955823976 530 TNHLDIETIDSLAEALNEW--DGGLVLV-SHD 558
Cdd:COG4133 159 FTALDAAGVALLAELIAAHlaRGGAVLLtTHQ 190
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
389-565 |
3.20e-26 |
|
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: 106.46 E-value: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 389 VTFGYTpENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR------RHNHLRIAQFHQHLAEKLDL 462
Cdd:cd03235 5 LTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 463 ELSALQF----------MIREYPGNEEEKMRGAIGKFGLSGKAQvMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNH 532
Cdd:cd03235 84 PISVRDVvlmglyghkgLFRRLSKADKAKVDEALERVGLSELAD-RQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 1955823976 533 LDIETIDSLAEALNEW--DG-GLVLVSHDfrlINQV 565
Cdd:cd03235 163 VDPKTQEDIYELLRELrrEGmTILVVTHD---LGLV 195
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
383-571 |
4.09e-26 |
|
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: 107.44 E-value: 4.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 383 VLQFVEVTFGYtPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV----RRHNHLRIAQFHQHLA- 457
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgRDLASLSRRELARRIAy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 458 ----EKLDLELSALQF----------MIREYPGNEEEKMRGAIGKFGLSGKAQvMPMKNLSDGQRSRVIFAW-LAwRQPH 522
Cdd:COG1120 80 vpqePPAPFGLTVRELvalgryphlgLFGRPSAEDREAVEEALERTGLEHLAD-RPVDELSGGERQRVLIARaLA-QEPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 523 LLLLDEPTNHLDI----ETIDsLAEALNEWDG-GLVLVSHDFRLINQVAQEIWV 571
Cdd:COG1120 158 LLLLDEPTSHLDLahqlEVLE-LLRRLARERGrTVVMVLHDLNLAARYADRLVL 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
380-567 |
5.73e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 106.71 E-value: 5.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 380 PPPVLQFVEVTFGYtPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIAQFH------ 453
Cdd:COG1121 3 MMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRrigyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 454 QHLAEKLDLELSALQF----------MIREYPGNEEEKMRGAIGKFGLSGKAQVmPMKNLSDGQRSRVIFA-WLAwRQPH 522
Cdd:COG1121 82 QRAEVDWDFPITVRDVvlmgrygrrgLFRRPSRADREAVDEALERVGLEDLADR-PIGELSGGQQQRVLLArALA-QDPD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1955823976 523 LLLLDEPTNHLDIETIDSLAEALNEW-DGGL--VLVSHDfrlINQVAQ 567
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELrREGKtiLVVTHD---LGAVRE 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
73-565 |
3.80e-25 |
|
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: 109.51 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAI-GCRELPIPEHMDIYHLSR--EIEASDMSSL--E 147
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrGMDQYEPTSGRIIYHVALceKCGYVERPSKvgE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 148 AVISCDEErlkLEKEAESLASQDD---------------------GGGEQLDRIYERLEAL--DAATAEKRAAEILYGLG 204
Cdd:TIGR03269 81 PCPVCGGT---LEPEEVDFWNLSDklrrrirkriaimlqrtfalyGDDTVLDNVLEALEEIgyEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 205 FNKQMqAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVW----LEENLKKFDRILVVVSHSQDFLNGVC 280
Cdd:TIGR03269 158 LSHRI-THIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 281 TNIIHMQNRKLKiytgnydqyvqtrseleenqmkmykweqdQIASMKEYIARFghgsaklarqaqskektlakMERGGLT 360
Cdd:TIGR03269 237 DKAIWLENGEIK-----------------------------EEGTPDEVVAVF--------------------MEGVSEV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 361 EKvvrdkvlvFRFVDVGKlppPVLQFVEVTFGY-TPENLIYKNLDfGVDLDSR----IALVGPNGAGKSTLLKLMTGDLV 435
Cdd:TIGR03269 268 EK--------ECEVEVGE---PIIKVRNVSKRYiSVDRGVVKAVD-NVSLEVKegeiFGIVGTSGAGKTTLSKIIAGVLE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 436 PLDG------------MVRRHNHLR------IAQFHQ------------HLAEKLDLELSALQFMIR-----EYPGNEEE 480
Cdd:TIGR03269 336 PTSGevnvrvgdewvdMTKPGPDGRgrakryIGILHQeydlyphrtvldNLTEAIGLELPDELARMKavitlKMVGFDEE 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 481 KMRGAIGKfglsgkaqvMPmKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLD----IETIDSLAEALNEWDGGLVLVS 556
Cdd:TIGR03269 416 KAEEILDK---------YP-DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVS 485
|
....*....
gi 1955823976 557 HDFRLINQV 565
Cdd:TIGR03269 486 HDMDFVLDV 494
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
93-245 |
1.24e-24 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 100.03 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 93 LELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIPEHMDIyhLSREIEASDMSSLEAVISC--DEERLKLEKEAEslasqd 170
Cdd:pfam00005 6 LTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILL--DGQDLTDDERKSLRKEIGYvfQDPQLFPRLTVR------ 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 171 dgggEQLdRIYERLEALDAATAEKRAAEILYGLG---FNKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTN 245
Cdd:pfam00005 78 ----ENL-RLGLLLKGLSKREKDARAEEALEKLGlgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
381-557 |
1.60e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 102.86 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 381 PPVLQFVEVTFGYTpENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGM----------------VRRH 444
Cdd:COG1119 1 DPLLELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgerrggedvweLRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 445 nhlrIAQFHQHLAEKLDLELSALQFMI----------REYPGNEEEKMRGAIGKFGLSGKAQvMPMKNLSDGQRSRVIFA 514
Cdd:COG1119 80 ----IGLVSPALQLRFPRDETVLDVVLsgffdsiglyREPTDEQRERARELLELLGLAHLAD-RPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1955823976 515 wlawR----QPHLLLLDEPTNHLD-------IETIDSLAEalnewDGG--LVLVSH 557
Cdd:COG1119 155 ----RalvkDPELLILDEPTAGLDlgarellLALLDKLAA-----EGAptLVLVTH 201
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
73-323 |
2.05e-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: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPiPEHMDIYHLSREIEASDMSSLEAV-IS 151
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRML-AGLLK-PDSGSILIDGEDVRKEPREARRQIgVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 152 CDE----ERLKLEkeaeslasqddgggEQLdRIYERLEALDAATAEKRAAEILYGLGFNKQMqAKKTRDFSGGWRMRIAL 227
Cdd:COG4555 80 PDErglyDRLTVR--------------ENI-RYFAELYGLFDEELKKRIEELIELLGLEEFL-DRRVGELSTGMKKKVAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 228 ARALFMNPTVLLLDEPTNHLDLEACVWLEE---NLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKLkIYTGNYDQYVQ- 303
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREilrALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV-VAQGSLDELREe 222
|
250 260
....*....|....*....|.
gi 1955823976 304 -TRSELEENQMKMYKWEQDQI 323
Cdd:COG4555 223 iGEENLEDAFVALIGSEEGEA 243
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
389-571 |
8.63e-24 |
|
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: 98.66 E-value: 8.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 389 VTFGYtPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVrrhnhlriaqfhqHLAEKLDLELSALQ 468
Cdd:cd03214 5 LSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-------------LLDGKDLASLSPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 469 FmireypgneeEKMRG----AIGKFGLSGKAQvMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDI----ETIDS 540
Cdd:cd03214 71 L----------ARKIAyvpqALELLGLAHLAD-RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIahqiELLEL 139
|
170 180 190
....*....|....*....|....*....|.
gi 1955823976 541 LAEALNEWDGGLVLVSHDFRLINQVAQEIWV 571
Cdd:cd03214 140 LRRLARERGKTVVMVLHDLNLAARYADRVIL 170
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
385-571 |
9.10e-24 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 97.70 E-value: 9.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 385 QFVEVTFGYtPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHlriaqfhqHLAEKLDLEL 464
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK--------DIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 465 SALQFMIreypgneeekmrgaigkFGLSGkaqvmpmknlsdGQRSRVIFAwLAW-RQPHLLLLDEPTNHLDIETIDSLAE 543
Cdd:cd00267 72 RRRIGYV-----------------PQLSG------------GQRQRVALA-RALlLNPDLLLLDEPTSGLDPASRERLLE 121
|
170 180 190
....*....|....*....|....*....|.
gi 1955823976 544 ALNEW-DGG--LVLVSHDFRLINQVAQEIWV 571
Cdd:cd00267 122 LLRELaEEGrtVIIVTHDPELAELAADRVIV 152
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
385-574 |
3.51e-23 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 97.92 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 385 QFVEVTFGY-TPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV----RRHNHLRIAQFHQH---- 455
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgKDLTKLSLKELRRKvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 456 ------------LAEklDLELSALQFMIREYpgNEEEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFAWLAWRQPHL 523
Cdd:cd03225 81 fqnpddqffgptVEE--EVAFGLENLGLPEE--EIEERVEEALELVGLEGLRDRSP-FTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 524 LLLDEPTNHLDIETIDSLAEALNEW-DGG--LVLVSHDFRLINQVAQEIWVCEN 574
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLkAEGktIIIVTHDLDLLLELADRVIVLED 209
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
406-558 |
4.09e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 406 GVDLD----SRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIAQFHQHLAEKLDLELSALQFM----------I 471
Cdd:NF040873 10 GVDLTipagSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRDLVamgrwarrglW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 472 REYPGNEEEKMRGAIGKFGLSGKAqVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEW--D 549
Cdd:NF040873 90 RRLTRDDRAAVDDALERVGLADLA-GRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEhaR 168
|
170
....*....|
gi 1955823976 550 G-GLVLVSHD 558
Cdd:NF040873 169 GaTVVVVTHD 178
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
73-291 |
4.92e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 97.19 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPIPEHmDIYHLSREIEASDMSSLeavisc 152
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRAL-ADLDPPTSG-EIYLDGKPLSAMPPPEW------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 deeRLKLekeaeSLASQ-----DDGGGEQLDRIYE-RLEALDaataEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIA 226
Cdd:COG4619 73 ---RRQV-----AYVPQepalwGGTVRDNLPFPFQlRERKFD----RERALELLERLGLPPDILDKPVERLSGGERQRLA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955823976 227 LARALFMNPTVLLLDEPTNHLDLE--ACV--WLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKL 291
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPEntRRVeeLLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
381-578 |
8.38e-23 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 102.53 E-value: 8.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 381 PPVLQFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR----RHNHLRIAQFHQHL 456
Cdd:COG4988 334 PPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvDLSDLDPASWRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 457 AekldlelsalqFM----------IRE-----YPGNEEEKMRGAIGKFGLSGKAQVMPM----------KNLSDGQRSRV 511
Cdd:COG4988 414 A-----------WVpqnpylfagtIREnlrlgRPDASDEELEAALEAAGLDEFVAALPDgldtplgeggRGLSGGQAQRL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955823976 512 IFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEWDGG--LVLVSHDFRLINQvAQEIWVCENQAVT 578
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALLAQ-ADRILVLDDGRIV 550
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
375-571 |
9.75e-23 |
|
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: 101.98 E-value: 9.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 375 DVGKLPPPVLQFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR-----------R 443
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladadaD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 444 HNHLRIAQFHQH-------LAEKLDLELsalqfmireyPGNEEEKMRGAIGKFGLSGKAQVMPM----------KNLSDG 506
Cdd:TIGR02857 393 SWRDQIAWVPQHpflfagtIAENIRLAR----------PDASDAEIREALERAGLDEFVAALPQgldtpigeggAGLSGG 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955823976 507 QRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEWDGG--LVLVSHDFRLInQVAQEIWV 571
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRLALA-ALADRIVV 528
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
74-290 |
2.45e-22 |
|
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: 93.85 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 74 RIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPIPEhmdiyhlsreieasdmssleaviscd 153
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAI-AGLLKPTS-------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 154 eerlklekeaeslasqddggGEqldriyerLEALDAATAEKRAAEILYGLGFNKQMqakktrdfSGGWRMRIALARALFM 233
Cdd:cd00267 54 --------------------GE--------ILIDGKDIAKLPLEELRRRIGYVPQL--------SGGQRQRVALARALLL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 234 NPTVLLLDEPTNHLDLEACVWLEENLKKF---DRILVVVSHSQDFLNGVCTNIIHMQNRK 290
Cdd:cd00267 98 NPDLLLLDEPTSGLDPASRERLLELLRELaeeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
384-571 |
3.46e-22 |
|
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: 95.48 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVP------LDGM-VRRHNHLRIAQ----- 451
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPtsgevlVDGKdITKKNLRELRRkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 452 --------FHQHLAEklDLELSALQFmireypGNEEEKMR----GAIGKFGLSGKAQVMPMkNLSDGQRSRVIFAW-LAW 518
Cdd:COG1122 81 fqnpddqlFAPTVEE--DVAFGPENL------GLPREEIRerveEALELVGLEHLADRPPH-ELSGGQKQRVAIAGvLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1955823976 519 RqPHLLLLDEPTNHLDIETIDSLAEALNEWDG---GLVLVSHDFRLINQVAQEIWV 571
Cdd:COG1122 152 E-PEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIV 206
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
375-571 |
8.27e-22 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 99.91 E-value: 8.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 375 DVGKLPPPVLQ----FVEVTFGYTP-ENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR------- 442
Cdd:COG2274 461 GRSKLSLPRLKgdieLENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlr 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 443 --RHNHLR--IAQFHQhlaeklDLELsalqFM--IRE-----YPGNEEEKMRGAIGKFGLSGKAQVMPM----------K 501
Cdd:COG2274 541 qiDPASLRrqIGVVLQ------DVFL----FSgtIREnitlgDPDATDEEIIEAARLAGLHDFIEALPMgydtvvgeggS 610
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 502 NLSDGQRSRVIFA--WLawRQPHLLLLDEPTNHLDIETIDSLAEALNEWDGG--LVLVSHDFRLINQvAQEIWV 571
Cdd:COG2274 611 NLSGGQRQRLAIAraLL--RNPRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAHRLSTIRL-ADRIIV 681
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
391-583 |
1.56e-21 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 98.87 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 391 FGYTPenlIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDlVPLD-GMVRRHNHLRIAQFHQ--------------- 454
Cdd:PRK11147 13 FSDAP---LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGE-VLLDdGRIIYEQDLIVARLQQdpprnvegtvydfva 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 455 ----HLAEKL--------DLE----------LSALQFMIREYPGNE-EEKMRGAIGKFGLSGKAqvmPMKNLSDGQRSRV 511
Cdd:PRK11147 89 egieEQAEYLkryhdishLVEtdpseknlneLAKLQEQLDHHNLWQlENRINEVLAQLGLDPDA---ALSSLSGGWLRKA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955823976 512 IFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWVCENQAVTKWEGD 583
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGN 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
380-578 |
1.58e-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: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 380 PPPVLQFVEVTFGYTPEN-LIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR---------RHNHLR- 448
Cdd:COG4987 330 GGPSLELEDVSFRYPGAGrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdlDEDDLRr 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 449 ----IAQ----FHQHLAEKLDLelsAlqfmireYPGNEEEKMRGAIGKFGLSGKAQVMPMK----------NLSDGQRSR 510
Cdd:COG4987 410 riavVPQrphlFDTTLRENLRL---A-------RPDATDEELWAALERVGLGDWLAALPDGldtwlgeggrRLSGGERRR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 511 VIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEWDGG--LVLVSHDFRLINQvAQEIWVCENQAVT 578
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHRLAGLER-MDRILVLEDGRIV 548
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
383-574 |
2.07e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 93.19 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 383 VLQFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV-------RRHNHLRIAQFHQH 455
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvngqdlSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 456 L---------------AEKLDLelsALQfmIREYPGNE-EEKMRGAIGKFGLSGKAQVMPMkNLSDGQRSRVIFAwlawR 519
Cdd:COG2884 81 IgvvfqdfrllpdrtvYENVAL---PLR--VTGKSRKEiRRRVREVLDLVGLSDKAKALPH-ELSGGEQQRVAIA----R 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 520 ----QPHLLLLDEPTNHLDIET---IDSLAEALNEwDGGLVLV-SHDFRLINQVAQEIWVCEN 574
Cdd:COG2884 151 alvnRPELLLADEPTGNLDPETsweIMELLEEINR-RGTTVLIaTHDLELVDRMPKRVLELED 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
400-531 |
5.06e-21 |
|
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: 89.63 E-value: 5.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 400 YKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTG-----------DLVPLDGMVRRHNHLRIAQFHQHLAekLDLELSALQ 468
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGllsptegtillDGQDLTDDERKSLRKEIGYVFQDPQ--LFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955823976 469 FMIR----EYPGNEEEKMR--GAIGKFGLSGKA---QVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTN 531
Cdd:pfam00005 79 NLRLglllKGLSKREKDARaeEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
389-571 |
6.11e-21 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 90.15 E-value: 6.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 389 VTFGYtPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHlriaqfhqhlaekldlelsalq 468
Cdd:cd03230 6 LSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK---------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 469 fmireYPGNEEEKMRGAIG----KFGLSGKAQVMPMKNLSDGQRSRVIFAwLAW-RQPHLLLLDEPTNHLDIETIDSLAE 543
Cdd:cd03230 63 -----DIKKEPEEVKRRIGylpeEPSLYENLTVRENLKLSGGMKQRLALA-QALlHDPELLILDEPTSGLDPESRREFWE 136
|
170 180 190
....*....|....*....|....*....|.
gi 1955823976 544 ALNEW--DGGLVLV-SHDFRLINQVAQEIWV 571
Cdd:cd03230 137 LLRELkkEGKTILLsSHILEEAERLCDRVAI 167
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
384-574 |
1.01e-20 |
|
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: 89.36 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYTP-ENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLriaqfhqhlaekldl 462
Cdd:cd03228 1 IEFKNVSFSYPGrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 463 elsalqfmIREYPgneEEKMRGAIGkfglsgkaqVMP----------MKN-LSDGQRSRVIFAWLAWRQPHLLLLDEPTN 531
Cdd:cd03228 66 --------LRDLD---LESLRKNIA---------YVPqdpflfsgtiRENiLSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1955823976 532 HLDIETIDSLAEALNEWDGG--LVLVSHDFRLINQvAQEIWVCEN 574
Cdd:cd03228 126 ALDPETEALILEALRALAKGktVIVIAHRLSTIRD-ADRIIVLDD 169
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
399-571 |
6.46e-20 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 88.33 E-value: 6.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 399 IYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMtGDLVPLD-GMVRRHN---------HLR-----IAQ----FHQHLAEK 459
Cdd:COG4619 15 ILSPVSLTLEAGECVAITGPSGSGKSTLLRAL-ADLDPPTsGEIYLDGkplsampppEWRrqvayVPQepalWGGTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 460 LdlelsALQFMIREYPGNEEeKMRGAIGKFGLSGKAQVMPMKNLSDGQRSRV--IFAWLawRQPHLLLLDEPTNHLDIET 537
Cdd:COG4619 94 L-----PFPFQLRERKFDRE-RALELLERLGLPPDILDKPVERLSGGERQRLalIRALL--LQPDVLLLDEPTSALDPEN 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 1955823976 538 IDSLAEALNEW----DGGLVLVSHDFRLINQVAQEIWV 571
Cdd:COG4619 166 TRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLT 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
73-356 |
2.88e-19 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 91.77 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFhGHDLIVDS-ELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPipehmdiyhLSREIEASDMSSLEAVIS 151
Cdd:PRK10636 313 LKMEKVSAGY-GDRIILDSiKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP---------VSGEIGLAKGIKLGYFAQ 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 152 CDEERLKlekeaeslasQDDGGGEQLDRIYERlealdaaTAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARAL 231
Cdd:PRK10636 383 HQLEFLR----------ADESPLQHLARLAPQ-------ELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIV 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 232 FMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKLKIYTGNYDQYVQTRSELEEN 311
Cdd:PRK10636 446 WQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQ 525
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1955823976 312 QMKMYKWEQDQIASMKEYIARFGHGSAKLARQAQSKEKTLAKMER 356
Cdd:PRK10636 526 ENQTDEAPKENNANSAQARKDQKRREAELRTQTQPLRKEIARLEK 570
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
73-271 |
3.16e-19 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 87.04 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPipehmdiyhlsreieasdmSSLEAVI-- 150
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRP-------------------TSGEVRVlg 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 151 -SCDEERLKLeKEAESLASQDDG------GGEQLdRIYERLEALDAATAEKRAAEILYGLGFNKQMQaKKTRDFSGGWRM 223
Cdd:COG1131 62 eDVARDPAEV-RRRIGYVPQEPAlypdltVRENL-RFFARLYGLPRKEARERIDELLELFGLTDAAD-RKVGTLSGGMKQ 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 224 RIALARALFMNPTVLLLDEPTNHLDLEACVWLEE---NLKKFDRILVVVSH 271
Cdd:COG1131 139 RLGLALALLHDPELLILDEPTSGLDPEARRELWEllrELAAEGKTVLLSTH 189
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
401-569 |
3.16e-19 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 87.04 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 401 KNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVP------LDGM-VRRHNHL---RIAQFHQHLAekLDLELSALQFM 470
Cdd:COG1131 17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPtsgevrVLGEdVARDPAEvrrRIGYVPQEPA--LYPDLTVRENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 471 -----IREYPGNE-EEKMRGAIGKFGLSGKAQVmPMKNLSDGQRSRVIFAwLA-WRQPHLLLLDEPTNHLDIETIDSLAE 543
Cdd:COG1131 95 rffarLYGLPRKEaRERIDELLELFGLTDAADR-KVGTLSGGMKQRLGLA-LAlLHDPELLILDEPTSGLDPEARRELWE 172
|
170 180
....*....|....*....|....*....
gi 1955823976 544 ALNEW--DGGLVLVS-HDFRLINQVAQEI 569
Cdd:COG1131 173 LLRELaaEGKTVLLStHYLEEAERLCDRV 201
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
384-575 |
4.12e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.09 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGytpENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIAQFHQHLAEKLDLE 463
Cdd:PRK09544 7 LENVSVSFG---QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 464 LSALQFMiREYPGNEEEKMRGAIGKFGlSGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAE 543
Cdd:PRK09544 84 LTVNRFL-RLRPGTKKEDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1955823976 544 ALN----EWDGGLVLVSHDFRLINQVAQEIwVCENQ 575
Cdd:PRK09544 162 LIDqlrrELDCAVLMVSHDLHLVMAKTDEV-LCLNH 196
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
406-561 |
4.68e-19 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 87.18 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 406 GVDLD----SRIALVGPNGAGKSTLLKLMTGDLVP-----------LDGMVRRHNHLRIAQFHQHLAEKLDLELSALQFM 470
Cdd:TIGR03873 19 GVDVTappgSLTGLLGPNGSGKSTLLRLLAGALRPdagtvdlagvdLHGLSRRARARRVALVEQDSDTAVPLTVRDVVAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 471 IR--------EYPGNEEEKMRGAIGKFGLSGKAQvMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLA 542
Cdd:TIGR03873 99 GRiphrslwaGDSPHDAAVVDRALARTELSHLAD-RDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETL 177
|
170 180
....*....|....*....|..
gi 1955823976 543 EALNE--WDGGLVLVS-HDFRL 561
Cdd:TIGR03873 178 ALVRElaATGVTVVAAlHDLNL 199
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
74-290 |
4.91e-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: 85.98 E-value: 4.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 74 RIESLSVTFHGHD--LIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIPEHmdIYHLSREIEASDMSSLEAVIS 151
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGE--VLVDGKDLTKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 152 cdeerlklekeaesLASQD-DGggeQL--DRIYE------RLEALDAATAEKRAAEILYGLGFNKQMQaKKTRDFSGGWR 222
Cdd:cd03225 79 --------------LVFQNpDD---QFfgPTVEEevafglENLGLPEEEIEERVEEALELVGLEGLRD-RSPFTLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 223 MRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDR---ILVVVSHSQDFLNGVCTNIIHMQNRK 290
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
73-291 |
9.05e-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: 83.99 E-value: 9.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCreLPIPEHMDIYHLSREIEASDMSSLEAVISC 152
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILG--LLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 DEErlklekeaeslasqddgggeqlDRIYERLealdaataekRAAEILyglgfnkqmqakktrDFSGGWRMRIALARALF 232
Cdd:cd03230 79 PEE----------------------PSLYENL----------TVRENL---------------KLSGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955823976 233 MNPTVLLLDEPTNHLDLEACVWLEENLKKF---DRILVVVSHSQDFLNGVCTNIIHMQNRKL 291
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
384-563 |
1.18e-18 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 84.77 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRH----NHLR---IAQFHQHL 456
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvSDLRgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 457 A-----EKLDLELS-----ALQFMIREYPGNE-EEKMRGAIGKFGLSGKAQVMPMKnLSDGQRSRVIFAWLAWRQPHLLL 525
Cdd:cd03292 81 GvvfqdFRLLPDRNvyenvAFALEVTGVPPREiRKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1955823976 526 LDEPTNHLDIETIDSLAEALNEWD--GGLVLVS-HDFRLIN 563
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINkaGTTVVVAtHAKELVD 200
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
74-291 |
1.23e-18 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 83.64 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 74 RIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPIPEH------MDIYHLSREIEASDMSSLE 147
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTL-AGLLKPSSGeilldgKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 148 AVIscdeERLKLEKEAeslasqddgggeqlDRIYERLealdaataekraaeilyglgfnkqmqakktrdfSGGWRMRIAL 227
Cdd:cd03214 80 QAL----ELLGLAHLA--------------DRPFNEL---------------------------------SGGERQRVLL 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 228 ARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF----DRILVVVSHSQDFLNGVCTNIIHMQNRKL 291
Cdd:cd03214 109 ARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLarerGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
73-288 |
2.44e-18 |
|
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: 83.01 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIpehmdiyhlSREIEASDmssleAVISC 152
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD---------SGSILIDG-----EDLTD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 DEERLKLEKEAESLASQDDGggeqldrIYERLEALDaataekraaEILYGLgfnkqmqakktrdfSGGWRMRIALARALF 232
Cdd:cd03229 67 LEDELPPLRRRIGMVFQDFA-------LFPHLTVLE---------NIALGL--------------SGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 233 MNPTVLLLDEPTNHLDLEACVWLEENLKK----FDRILVVVSHSQDFLNGVCTNIIHMQN 288
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
387-561 |
2.59e-18 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 84.08 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 387 VEVTFGYTPENL-IYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR-----------------RHNHLR 448
Cdd:cd03255 6 LSKTYGGGGEKVqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdisklsekelaafRRRHIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 449 -IAQFHqHLAEkldlELSALQ-----FMIREYPGNE-EEKMRGAIGKFGLSGKAQVMPMKnLSDGQRSRVIFAwlawR-- 519
Cdd:cd03255 86 fVFQSF-NLLP----DLTALEnvelpLLLAGVPKKErRERAEELLERVGLGDRLNHYPSE-LSGGQQQRVAIA----Ral 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1955823976 520 --QPHLLLLDEPTNHLDIET---IDSLAEALNEWDG-GLVLVSHDFRL 561
Cdd:cd03255 156 anDPKIILADEPTGNLDSETgkeVMELLRELNKEAGtTIVVVTHDPEL 203
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
401-571 |
4.33e-18 |
|
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: 83.64 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 401 KNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVP------LDG------MVRRHNHLRIAQFHQH------------- 455
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPtsgsvlFDGeditglPPHEIARLGIGRTFQIprlfpeltvlenv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 456 -LAEKLDLELSALQFMIREYPGNEEEKMRGAIGKFGLSGKAQVmPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPT---N 531
Cdd:cd03219 97 mVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADR-PAGELSYGQQRRLEIARALATDPKLLLLDEPAaglN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1955823976 532 HLDIETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWV 571
Cdd:cd03219 176 PEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTV 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
383-569 |
5.17e-18 |
|
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: 83.75 E-value: 5.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 383 VLQFVEVTFGYtPENLIYKNLDFGVDlDSRI-ALVGPNGAGKSTLLKLMTGDLVP------LDG--------MVRRHnhl 447
Cdd:COG4555 1 MIEVENLSKKY-GKVPALKDVSFTAK-DGEItGLLGPNGAGKTTLLRMLAGLLKPdsgsilIDGedvrkeprEARRQ--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 448 rIAQFHQhlAEKLDLELSA---LQFMIREYPGNEEEKMRGA---IGKFGLSGKAqVMPMKNLSDGQRSRVIFAWLAWRQP 521
Cdd:COG4555 76 -IGVLPD--ERGLYDRLTVrenIRYFAELYGLFDEELKKRIeelIELLGLEEFL-DRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 522 HLLLLDEPTNHLDIETIDSLAEALNEW--DGGLVLVS-HDFRLINQVAQEI 569
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALkkEGKTVLFSsHIMQEVEALCDRV 202
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
73-310 |
5.66e-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: 5.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDS-ELELNYGRRYGLLGLNGCGKSTLLaaigcrelpipEHMD--IYHLSREIEASDMSsleav 149
Cdd:COG1122 1 IELENLSFSYPGGTPALDDvSLSIEKGEFVAIIGPNGSGKSTLL-----------RLLNglLKPTSGEVLVDGKD----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 150 IScdeerlklEKEAESLASQ--------DDgggeQL--DRIYERLE------ALDAATAEKRAAEILYGLGfnkqMQAKK 213
Cdd:COG1122 65 IT--------KKNLRELRRKvglvfqnpDD----QLfaPTVEEDVAfgpenlGLPREEIRERVEEALELVG----LEHLA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 214 TR---DFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEE---NLKKFDRILVVVSHSQDFLNGVCTNIIHMQ 287
Cdd:COG1122 129 DRpphELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLEllkRLNKEGKTVIIVTHDLDLVAELADRVIVLD 208
|
250 260
....*....|....*....|...
gi 1955823976 288 NRKLkIYTGNYDQYVQTRSELEE 310
Cdd:COG1122 209 DGRI-VADGTPREVFSDYELLEE 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
74-292 |
2.08e-17 |
|
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: 81.15 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 74 RIESLSVTFHGHDLIVDS-ELELNYGRRYGLLGLNGCGKSTLLAAIGcrelpipehmdiyHLSREIEASdmSSLEAVISC 152
Cdd:cd03226 1 RIENISFSYKKGTEILDDlSLDLYAGEIIALTGKNGAGKTTLAKILA-------------GLIKESSGS--ILLNGKPIK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 DEERLKlekeAESLASQDDGggEQL------DRIYERLEALDAATAekRAAEILYGLGFNkQMQAKKTRDFSGGWRMRIA 226
Cdd:cd03226 66 AKERRK----SIGYVMQDVD--YQLftdsvrEELLLGLKELDAGNE--QAETVLKDLDLY-ALKERHPLSLSGGQKQRLA 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 227 LARALFMNPTVLLLDEPTNHLDLEA----CVWLEEnLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKLK 292
Cdd:cd03226 137 IAAALLSGKDLLIFDEPTSGLDYKNmervGELIRE-LAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
396-557 |
2.31e-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: 80.87 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 396 ENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR---RHNHLRIAQFHQHLA-----EKLDLELSA- 466
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRwngTPLAEQRDEPHENILylghlPGLKPELSAl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 467 --LQFMiREYPGNEEEKMRGAIGKFGLSGKAQVmPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEA 544
Cdd:TIGR01189 92 enLHFW-AAIHGGAQRTIEDALAAVGLTGFEDL-PAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGL 169
|
170
....*....|....*.
gi 1955823976 545 LNEW---DGGLVLVSH 557
Cdd:TIGR01189 170 LRAHlarGGIVLLTTH 185
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
396-556 |
2.75e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 396 ENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR-----RHNHLRIAQFHqHLAEK--LDLELSA-- 466
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKldggdIDDPDVAEACH-YLGHRnaMKPALTVae 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 467 -LQFMiREYPGNEEEKMRGAIGKFGLSGKAQVmPMKNLSDGQRSRVIFAWL--AWRqpHLLLLDEPTNHLDIETIDSLAE 543
Cdd:PRK13539 93 nLEFW-AAFLGGEELDIAAALEAVGLAPLAHL-PFGYLSAGQKRRVALARLlvSNR--PIWILDEPTAALDAAAVALFAE 168
|
170
....*....|....*
gi 1955823976 544 ALNEW--DGGLVLVS 556
Cdd:PRK13539 169 LIRAHlaQGGIVIAA 183
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
74-291 |
3.09e-17 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 80.71 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 74 RIESLSVTFH-----GHDLIVDSeLELNYGRRYGLLGLNGCGKSTLLAAI-GcreLPIPEHMDIYHLSREIEASDMSSLE 147
Cdd:cd03245 2 RIEFRNVSFSypnqeIPALDNVS-LTIRAGEKVAIIGRVGSGKSTLLKLLaG---LYKPTSGSVLLDGTDIRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 148 AVISC--DEERLKLEKEAESLASqddGGGEQLDRiyERLEALDAATAEKRAAeiLYGLGFNKQMQaKKTRDFSGGWRMRI 225
Cdd:cd03245 78 RNIGYvpQDVTLFYGTLRDNITL---GAPLADDE--RILRAAELAGVTDFVN--KHPNGLDLQIG-ERGRGLSGGQRQAV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 226 ALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF--DRILVVVSHSQDFLNgVCTNIIHMQNRKL 291
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
382-558 |
5.18e-17 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 84.33 E-value: 5.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 382 PVLQFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV---------RRHNHLR---- 448
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvssLDQDEVRrrvs 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 449 -IAQ----FHQHLAEKL--------DLELSA------LQFMIREYPGNEEEKMrGAIGKFglsgkaqvmpmknLSDGQRS 509
Cdd:TIGR02868 413 vCAQdahlFDTTVRENLrlarpdatDEELWAalervgLADWLRALPDGLDTVL-GEGGAR-------------LSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 510 RVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEWDGGL--VLVSHD 558
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRtvVLITHH 529
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
73-288 |
5.20e-17 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 81.00 E-value: 5.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTF--HGHDLIV--DSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPiPEHMDIYHLSREIEASDMSSLEA 148
Cdd:COG1124 2 LEVRNLSVSYgqGGRRVPVlkDVSLEVAPGESFGLVGESGSGKSTLLRAL-AGLER-PWSGEVTFDGRPVTRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 149 VI---------SCDEeRLKLEKE-AESLASQddGGGEQLDRIYERLEA--LDAATAEKRAAEIlyglgfnkqmqakktrd 216
Cdd:COG1124 80 RVqmvfqdpyaSLHP-RHTVDRIlAEPLRIH--GLPDREERIAELLEQvgLPPSFLDRYPHQL----------------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955823976 217 fSGGWRMRIALARALFMNPTVLLLDEPTNHLDL--EACVW--LEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQN 288
Cdd:COG1124 140 -SGGQRQRVAIARALILEPELLLLDEPTSALDVsvQAEILnlLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
381-561 |
7.70e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 79.70 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 381 PPVLQFVEVTFGYTPENLIYKNLDfGVDLD----SRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR-------------- 442
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALR-GVSLSieagEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdisslserel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 443 ---RHNHLR-IAQFHQHLAekldlELSALQ-----FMIREYPGNE-EEKMRGAIGKFGLSGKAQVMPMKnLSDGQRSRVI 512
Cdd:COG1136 81 arlRRRHIGfVFQFFNLLP-----ELTALEnvalpLLLAGVSRKErRERARELLERVGLGDRLDHRPSQ-LSGGQQQRVA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1955823976 513 FAwlawR----QPHLLLLDEPTNHLDIET----IDSLAEALNEWDGGLVLVSHDFRL 561
Cdd:COG1136 155 IA----RalvnRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPEL 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
393-573 |
7.82e-17 |
|
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: 83.83 E-value: 7.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 393 YTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIAQFHQ--HLAEKLDLE------L 464
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQepQLDPTKTVRenveegV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 465 SALQFMIREY---------PGNE-----------EEKMRgAIGKFGLSGKAQV-----------MPMKNLSDGQRSRVIF 513
Cdd:TIGR03719 94 AEIKDALDRFneisakyaePDADfdklaaeqaelQEIID-AADAWDLDSQLEIamdalrcppwdADVTKLSGGERRRVAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 514 AWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEWDGGLVLVSHDFRLINQVAQeiWVCE 573
Cdd:TIGR03719 173 CRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAG--WILE 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
389-566 |
8.57e-17 |
|
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: 79.22 E-value: 8.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 389 VTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV-----RRHNHLRI------AQ------ 451
Cdd:cd03226 5 ISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkPIKAKERRksigyvMQdvdyql 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 452 FHQHLAEKLDLELSALqfmireypGNEEEKMRGAIGKFGLSGKAQVMPMkNLSDGQRSRVIFAWLAWRQPHLLLLDEPTN 531
Cdd:cd03226 85 FTDSVREELLLGLKEL--------DAGNEQAETVLKDLDLYALKERHPL-SLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1955823976 532 HLDIETIDSLAEALNEW--DGGLVLV-SHDFRLINQVA 566
Cdd:cd03226 156 GLDYKNMERVGELIRELaaQGKAVIViTHDYEFLAKVC 193
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
73-290 |
8.91e-17 |
|
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: 79.06 E-value: 8.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPiPEHMDIYHLSREIEASDMSSLEAV-IS 151
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIL-AGLLP-PSAGEVLWNGEPIRDAREDYRRRLaYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 152 CDEERLKLE---KEAESLASQDDGGGEQLDRIYERLEALDaataekraaeiLYGLgfnkqmQAKKTRDFSGGWRMRIALA 228
Cdd:COG4133 81 GHADGLKPEltvRENLRFWAALYGLRADREAIDEALEAVG-----------LAGL------ADLPVRQLSAGQKRRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955823976 229 RALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF---DRILVVVSHSQDFLNGVctNIIHMQNRK 290
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA--RVLDLGDFK 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
384-574 |
9.79e-17 |
|
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: 78.12 E-value: 9.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYTPEN-LIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVrrhnhlriaQFHQHLAEKLDL 462
Cdd:cd03247 1 LSINNVSFSYPEQEqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVPVSDLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 463 ELSALQFMIREYPGNEEEKMRGAIGkfglsgkaqvmpmKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLA 542
Cdd:cd03247 72 ALSSLISVLNQRPYLFDTTLRNNLG-------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL 138
|
170 180 190
....*....|....*....|....*....|....
gi 1955823976 543 EALNEW--DGGLVLVSHDFRLINQVaQEIWVCEN 574
Cdd:cd03247 139 SLIFEVlkDKTLIWITHHLTGIEHM-DKILFLEN 171
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
396-557 |
9.92e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.08 E-value: 9.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 396 ENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRH----NHLRiAQFHQ------HLAeKLDLELS 465
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQgepiRRQR-DEYHQdllylgHQP-GIKTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 466 A---LQFMIREYPGNEEEKMRGAIGKFGLSGKAQVmPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLA 542
Cdd:PRK13538 91 AlenLRFYQRLHGPGDDEALWEALAQVGLAGFEDV-PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLE 169
|
170
....*....|....*...
gi 1955823976 543 EALNEW--DGGLVLV-SH 557
Cdd:PRK13538 170 ALLAQHaeQGGMVILtTH 187
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
73-248 |
1.21e-16 |
|
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: 79.47 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIV----DSELELNYGRRYGLLGLNGCGKSTLLAAI--------GCRELpipEHMDIYHLSREIEA 140
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaldDVSFSIKKGETLGLVGESGSGKSTLARAIlgllkptsGSIIF---DGKDLLKLSRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 141 S----------D-MSSLEAVISCdeerlklekeaeslasqddggGEQLDRIYERLEALDAATAEKRAA-EILYGLGFNKQ 208
Cdd:cd03257 79 IrrkeiqmvfqDpMSSLNPRMTI---------------------GEQIAEPLRIHGKLSKKEARKEAVlLLLVGVGLPEE 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1955823976 209 MQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:cd03257 138 VLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALD 177
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
384-557 |
1.31e-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: 83.38 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYtPENLIY--KNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVP------LDGM--------VRRHNHL 447
Cdd:TIGR03375 464 IEFRNVSFAY-PGQETPalDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPtegsvlLDGVdirqidpaDLRRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 448 RIAQ----FHQHLAEKLDLELsalqfmireyPGNEEEKMRGAIGKFGLSGKAQVMPM----------KNLSDGQRSRVIF 513
Cdd:TIGR03375 543 YVPQdprlFYGTLRDNIALGA----------PYADDEEILRAAELAGVTEFVRRHPDgldmqigergRSLSGGQRQAVAL 612
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1955823976 514 AWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEWDGG--LVLVSH 557
Cdd:TIGR03375 613 ARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGktLVLVTH 658
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
406-571 |
1.50e-16 |
|
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: 79.70 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 406 GVDLD----SRIALVGPNGAGKSTLLKLMTGDLVP------LD---------------GMVR-------------RHNhL 447
Cdd:COG0411 22 DVSLEvergEIVGLIGPNGAGKTTLFNLITGFYRPtsgrilFDgrditglpphriarlGIARtfqnprlfpeltvLEN-V 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 448 RIAQfHQHLAEKLDLELSALQFMIREYPGNEEEKMRgAIGKFGLSGKAQVMPmKNLSDGQRSRVIFAW-LAwRQPHLLLL 526
Cdd:COG0411 101 LVAA-HARLGRGLLAALLRLPRARREEREARERAEE-LLERVGLADRADEPA-GNLSYGQQRRLEIARaLA-TEPKLLLL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1955823976 527 DEPT---NHLDIETIDSLAEALNEWDG-GLVLVSHDFRLINQVAQEIWV 571
Cdd:COG0411 177 DEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVV 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
387-590 |
1.55e-16 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 79.08 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 387 VEVTFGytpENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRiaqfhQHLAEKLDLEL-- 464
Cdd:cd03261 6 LTKSFG---GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDI-----SGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 465 --------SAL----------QFMIREYPGNEEEKMRG----AIGKFGLSGKAQVMPmKNLSDGQRSRVIFAwlawR--- 519
Cdd:cd03261 78 rmgmlfqsGALfdsltvfenvAFPLREHTRLSEEEIREivleKLEAVGLRGAEDLYP-AELSGGMKKRVALA----Rala 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955823976 520 -QPHLLLLDEPTNHLD-------IETIDSLAEALNewdGGLVLVSHDFRLINQVAQEIWVCENQAVTkWEGDIMDFKAH 590
Cdd:cd03261 153 lDPELLLYDEPTAGLDpiasgviDDLIRSLKKELG---LTSIMVTHDLDTAFAIADRIAVLYDGKIV-AEGTPEELRAS 227
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
406-571 |
2.09e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 79.39 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 406 GVDLDSR----IALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHlRIAQF-HQHLAEK---------LDLELSALQF-- 469
Cdd:COG4559 19 DVSLTLRpgelTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR-PLAAWsPWELARRravlpqhssLAFPFTVEEVva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 470 MIRE----YPGNEEEKMRGAIGKFGLSGKAQvmpmKN---LSDGQRSRVIFAW-LA--WR----QPHLLLLDEPTNHLDI 535
Cdd:COG4559 98 LGRAphgsSAAQDRQIVREALALVGLAHLAG----RSyqtLSGGEQQRVQLARvLAqlWEpvdgGPRWLFLDEPTSALDL 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1955823976 536 ---ETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWV 571
Cdd:COG4559 174 ahqHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILL 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
396-577 |
2.64e-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: 76.87 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 396 ENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRH----NHLRIAQFHQHLAekldlelsalqfmi 471
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDgadiSQWDPNELGDHVG-------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 472 reYPGNEEEKMRGAIGKFGLSGkaqvmpmknlsdGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEA---LNEW 548
Cdd:cd03246 80 --YLPQDDELFSGSIAENILSG------------GQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAiaaLKAA 145
|
170 180
....*....|....*....|....*....
gi 1955823976 549 DGGLVLVSHDFRLINQvAQEIWVCENQAV 577
Cdd:cd03246 146 GATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
384-565 |
3.31e-16 |
|
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: 78.02 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYTP-ENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNH---------LR--IAQ 451
Cdd:cd03245 3 IEFRNVSFSYPNqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadLRrnIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 452 FHQH---LAEKL--DLELSALqfmireyPGNEEEKMRgAIGKFGLSGKAQVMPM----------KNLSDGQRSRVIFAWL 516
Cdd:cd03245 83 VPQDvtlFYGTLrdNITLGAP-------LADDERILR-AAELAGVTDFVNKHPNgldlqigergRGLSGGQRQAVALARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 517 AWRQPHLLLLDEPTNHLDIETIDSLAEALNEWDGG--LVLVSHDFRLINQV 565
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLDLV 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
73-288 |
3.39e-16 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 77.56 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAI-GcreLPIPEHMDIYhlsreIEASDMSSLEAvis 151
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIaG---LERPDSGEIL-----IDGRDVTGVPP--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 152 cdeerlklEKEAESLASQDDGGGEQLdRIYE------RLEALDAATAEKRAAEILYGLGFNKQMQaKKTRDFSGGWRMRI 225
Cdd:cd03259 70 --------ERRNIGMVFQDYALFPHL-TVAEniafglKLRGVPKAEIRARVRELLELVGLEGLLN-RYPHELSGGQQQRV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955823976 226 ALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKK----FDRILVVVSHSQDFLNGVCTNIIHMQN 288
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKElqreLGITTIYVTHDQEEALALADRIAVMNE 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
73-249 |
7.07e-16 |
|
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: 77.78 E-value: 7.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPiPEHMDIYHLSREIeaSDMSSLEAvisc 152
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRAL-AGLLK-PSSGEVLLDGRDL--ASLSRREL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 deerlklekeAESLA--SQDDGGGEQLdRIYE--------RLEALDAATAEKRAA--EILYGLGfnkqMQAKKTRDF--- 217
Cdd:COG1120 74 ----------ARRIAyvPQEPPAPFGL-TVRElvalgrypHLGLFGRPSAEDREAveEALERTG----LEHLADRPVdel 138
|
170 180 190
....*....|....*....|....*....|..
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLDL 249
Cdd:COG1120 139 SGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
401-565 |
7.58e-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: 76.80 E-value: 7.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 401 KNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNhlRIAqfhqhlaekLDLELSAlqFMIREYPGNEEE 480
Cdd:cd03220 39 KDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--RVS---------SLLGLGG--GFNPELTGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 481 KMRGAIgkFGLS-----------------GKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAE 543
Cdd:cd03220 106 YLNGRL--LGLSrkeidekideiiefselGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180
....*....|....*....|....*
gi 1955823976 544 ALNEW---DGGLVLVSHDFRLINQV 565
Cdd:cd03220 184 RLRELlkqGKTVILVSHDPSSIKRL 208
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
68-305 |
7.63e-16 |
|
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: 80.58 E-value: 7.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 68 PLSRDIRIESLSVTFHGHDLIV--DSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPiPEHMDIYHLSREIEASDMSS 145
Cdd:COG4987 329 PGGPSLELEDVSFRYPGAGRPVldGLSLTLPPGERVAIVGPSGSGKSTLLALL-LRFLD-PQSGSITLGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 146 LEAVISCDEER-----------LKLEKEAeslASQddgggEQLdriyerLEALDAATAEKRAAEILYGLgfNKQMQAKKT 214
Cdd:COG4987 407 LRRRIAVVPQRphlfdttlrenLRLARPD---ATD-----EEL------WAALERVGLGDWLAALPDGL--DTWLGEGGR 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 215 RdFSGGWRMRIALARALFMNPTVLLLDEPTNHLD--LEACVW--LEENLKkfDRILVVVSHSQDFLNGVcTNIIHMQNRK 290
Cdd:COG4987 471 R-LSGGERRRLALARALLRDAPILLLDEPTEGLDaaTEQALLadLLEALA--GRTVLLITHRLAGLERM-DRILVLEDGR 546
|
250
....*....|....*
gi 1955823976 291 LkIYTGNYDQYVQTR 305
Cdd:COG4987 547 I-VEQGTHEELLAQN 560
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
73-301 |
9.33e-16 |
|
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: 80.36 E-value: 9.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPipehmDiyhlSREIEASDMSSLEAVisc 152
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQP-----D----SGTIEIGETVKLAYV--- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 DEERLKLekeaeslasqdDGGGEQLDRIYERLEALDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALF 232
Cdd:TIGR03719 391 DQSRDAL-----------DPNKTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLK 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 233 MNPTVLLLDEPTNHLDLEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQ-NRKLKIYTGNYDQY 301
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEY 529
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
67-313 |
2.04e-15 |
|
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: 79.49 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 67 HPLSRDIRIESLSVTFHGHDLIV--DSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPiPEHMDIYHLSREIEASDMS 144
Cdd:COG2274 468 PRLKGDIELENVSFRYPGDSPPVldNISLTIKPGERVAIVGRSGSGKSTLLKLL-LGLYE-PTSGRILIDGIDLRQIDPA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 145 SLEAVISCdeerlklekeaeslASQDD------------GGGEQLDriYERL-EALDAAtaekRAAEILYGL--GFNKQM 209
Cdd:COG2274 546 SLRRQIGV--------------VLQDVflfsgtirenitLGDPDAT--DEEIiEAARLA----GLHDFIEALpmGYDTVV 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 210 QAKKTRdFSGGWRMRIALARALFMNPTVLLLDEPTNHLD--LEACVWleENLKKF--DRILVVVSHSQDFLNgVCTNIIH 285
Cdd:COG2274 606 GEGGSN-LSGGQRQRLAIARALLRNPRILILDEATSALDaeTEAIIL--ENLRRLlkGRTVIIIAHRLSTIR-LADRIIV 681
|
250 260 270
....*....|....*....|....*....|.
gi 1955823976 286 MQNRKLkIYTGNYDQYVQTR---SELEENQM 313
Cdd:COG2274 682 LDKGRI-VEDGTHEELLARKglyAELVQQQL 711
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
406-567 |
2.28e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.35 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 406 GVDLDSR----IALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNH-----------LRIAQFHQHlaekldlelSALQF- 469
Cdd:PRK13548 20 DVSLTLRpgevVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspaelaRRRAVLPQH---------SSLSFp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 470 -MIRE------YPGNEEEKMRG-----AIGKFGLSGKAQvMPMKNLSDGQRSRVIFA------WLAWRQPHLLLLDEPTN 531
Cdd:PRK13548 91 fTVEEvvamgrAPHGLSRAEDDalvaaALAQVDLAHLAG-RDYPQLSGGEQQRVQLArvlaqlWEPDGPPRWLLLDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1955823976 532 HLDI---ETIDSLAEALNEWDGGLVL-VSHDfrlINQVAQ 567
Cdd:PRK13548 170 ALDLahqHHVLRLARQLAHERGLAVIvVLHD---LNLAAR 206
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
399-569 |
2.30e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.62 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 399 IYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDG------------------MVRRHNHLRIAQFHQHLAEKL 460
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGdvifngqpmsklssaakaELRNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 461 DLELSALQFMI-REYPGNEEEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETID 539
Cdd:PRK11629 104 ALENVAMPLLIgKKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190
....*....|....*....|....*....|....
gi 1955823976 540 SLAEALNEWD----GGLVLVSHDFRLINQVAQEI 569
Cdd:PRK11629 183 SIFQLLGELNrlqgTAFLVVTHDLQLAKRMSRQL 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
72-272 |
7.00e-15 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 77.40 E-value: 7.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 72 DIRIESLSVTFHGHDLIVDS-ELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPiPEHMDIYHLSREIEASDMSSLEAVI 150
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPVLDGvSLDLPPGERVAILGPSGSGKSTLLATL-AGLLD-PLQGEVTLDGVPVSSLDQDEVRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 151 S-CDE----------ERLKLEKEaeslasqdDGGGEQLdriyerLEALDAATAEKRAAEILYGLgfNKQMQAKKTRdFSG 219
Cdd:TIGR02868 412 SvCAQdahlfdttvrENLRLARP--------DATDEEL------WAALERVGLADWLRALPDGL--DTVLGEGGAR-LSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1955823976 220 GWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFD--RILVVVSHS 272
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALsgRTVVLITHH 529
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
72-251 |
7.25e-15 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 74.85 E-value: 7.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 72 DIRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIPEHM-----DIYHLSREIEASDMSSL 146
Cdd:TIGR03873 1 GLRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVdlagvDLHGLSRRARARRVALV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 147 EAVISCDEERLKLEKEAeslasqddgggeqLDRI-YERLEALDAATAEKRAAEILYGLGfnkqMQAKKTRDF---SGGWR 222
Cdd:TIGR03873 81 EQDSDTAVPLTVRDVVA-------------LGRIpHRSLWAGDSPHDAAVVDRALARTE----LSHLADRDMstlSGGER 143
|
170 180
....*....|....*....|....*....
gi 1955823976 223 MRIALARALFMNPTVLLLDEPTNHLDLEA 251
Cdd:TIGR03873 144 QRVHVARALAQEPKLLLLDEPTNHLDVRA 172
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
85-292 |
8.60e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.62 E-value: 8.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 85 HDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPipEHMDIYHLSREIEASDMSSLEAVIScDEERLKLEKEAE 164
Cdd:PRK10619 18 HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKP--SEGSIVVNGQTINLVRDKDGQLKVA-DKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 165 SLASQDDGGGEQLDRIYERLEA------LDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALFMNPTVL 238
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEApiqvlgLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1955823976 239 LLDEPTNHLDLE---ACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKLK 292
Cdd:PRK10619 175 LFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
384-590 |
1.05e-14 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 73.77 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYTPENLI-YKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTG--------------DLVPLDGMVRRHNHLR 448
Cdd:cd03258 4 LKNVSKVFGDTGGKVTaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlerptsgsvlvdgtDLTLLSGKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 449 IAQFHQH---LAEKLDLELSALQFMIREYPGNE-EEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFAWLAWRQPHLL 524
Cdd:cd03258 84 IGMIFQHfnlLSSRTVFENVALPLEIAGVPKAEiEERVLELLELVGLEDKADAYP-AQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 525 LLDEPTNHLDIETIDSLAEAL----NEWDGGLVLVSHDFRLINQVAQEIWVCENQAVTKwEGDIMDFKAH 590
Cdd:cd03258 163 LCDEATSALDPETTQSILALLrdinRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVE-EGTVEEVFAN 231
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
73-290 |
1.09e-14 |
|
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: 72.03 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIV--DSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPiPEHMDIYHLSREIEASDMSSLEAVI 150
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlkDVSLTIKPGEKVAIVGPSGSGKSTLLKLL-LRLYD-PTSGEILIDGVDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 151 ScdeerlklekeaesLASQDDgggeQL--DRIYErlealdaataekraaEILyglgfnkqmqakktrdfSGGWRMRIALA 228
Cdd:cd03228 79 A--------------YVPQDP----FLfsGTIRE---------------NIL-----------------SGGQRQRIAIA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955823976 229 RALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF--DRILVVVSHSqdfLNGV--CTNIIHMQNRK 290
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRALakGKTVIVIAHR---LSTIrdADRIIVLDDGR 171
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
410-573 |
1.18e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.08 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 410 DSRIALVGPNGAGKSTLLKLM-------TGDLVPLDG-------------------------------MVRRHNHLRiAQ 451
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMagvdkefEGEARPAPGikvgylpqepqldpektvrenveegvaevkaALDRFNEIY-AA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 452 FHQHLAE--KLDLELSALQFMIREYPG-NEEEKMRGAIGKFGL-SGKAQVmpmKNLSDGQRSRVIFAWLAWRQPHLLLLD 527
Cdd:PRK11819 112 YAEPDADfdALAAEQGELQEIIDAADAwDLDSQLEIAMDALRCpPWDAKV---TKLSGGERRRVALCRLLLEKPDMLLLD 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1955823976 528 EPTNHLDIETIDSLAEALNEWDGGLVLVSHDFRLINQVAQeiWVCE 573
Cdd:PRK11819 189 EPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAG--WILE 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
384-558 |
1.29e-14 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 73.27 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYTPENLIYKNLDfGVDLDSR----IALVGPNGAGKSTLLKLMTGDLVPLDGMVR-------RHNHLRIAQF 452
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALE-DISLSVEegefVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvtGPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 453 HQH--LAEKLDLELSALQFMIREYPGNE-EEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFA-WLAwRQPHLLLLDE 528
Cdd:cd03293 80 QQDalLPWLTVLDNVALGLELQGVPKAEaRERAEELLELVGLSGFENAYP-HQLSGGMRQRVALArALA-VDPDVLLLDE 157
|
170 180 190
....*....|....*....|....*....|....
gi 1955823976 529 PTNHLDIET----IDSLAEALNEWDGGLVLVSHD 558
Cdd:cd03293 158 PFSALDALTreqlQEELLDIWRETGKTVLLVTHD 191
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
380-589 |
1.36e-14 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 73.48 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 380 PPPVLQFVEVTFGYTpENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHlRIAQFHQHLAEK 459
Cdd:COG1127 2 SEPMIEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQ-DITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 460 LDLEL------SAL----------QFMIREYPGNEEEKMR----GAIGKFGLSGKAQVMPmKNLSDGQRSRVIFAwlawR 519
Cdd:COG1127 80 LRRRIgmlfqgGALfdsltvfenvAFPLREHTDLSEAEIRelvlEKLELVGLPGAADKMP-SELSGGMRKRVALA----R 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 520 ----QPHLLLLDEPTNHLDIET---IDSLAEALNEWDGG-LVLVSHDFRLINQVAQEIWVCENQAVTkWEGDIMDFKA 589
Cdd:COG1127 155 alalDPEILLYDEPTAGLDPITsavIDELIRELRDELGLtSVVVTHDLDSAFAIADRVAVLADGKII-AEGTPEELLA 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
70-272 |
1.43e-14 |
|
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: 76.56 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 70 SRDIRIESLSVTFHGHDLIVDS-ELELNYGRRYGLLGLNGCGKSTLLAAigcrelpipehmdiyhLSREIEAsdmsslea 148
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRRPALRPvSFTVPPGERVALVGPSGAGKSTLLNL----------------LLGFVDP-------- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 149 viscDEERLKLEKEAESLASQDDGGGE-----QLDRIYE-------RLEALDAATAEKRAAEILYGL---------GFNK 207
Cdd:TIGR02857 375 ----TEGSIAVNGVPLADADADSWRDQiawvpQHPFLFAgtiaeniRLARPDASDAEIREALERAGLdefvaalpqGLDT 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955823976 208 QMqAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF--DRILVVVSHS 272
Cdd:TIGR02857 451 PI-GEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHR 516
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
384-587 |
1.45e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 73.25 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYTPENLiykNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV----RRHNHLRIAQ-------- 451
Cdd:COG3840 2 LRLDDLTYRYGDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngQDLTALPPAErpvsmlfq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 452 ----FHqHL--AEKLDLELSalqfmireyPG---NEEEK--MRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFA-WLAWR 519
Cdd:COG3840 79 ennlFP-HLtvAQNIGLGLR---------PGlklTAEQRaqVEQALERVGLAGLLDRLP-GQLSGGQRQRVALArCLVRK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 520 QPhLLLLDEPTNHLDI----ETIDSLAEALNEWDGGLVLVSHDFRLINQVAQE-IWVCENQAVtkWEGDIMDF 587
Cdd:COG3840 148 RP-ILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHDPEDAARIADRvLLVADGRIA--ADGPTAAL 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
396-569 |
1.55e-14 |
|
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: 72.53 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 396 ENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR---RHNHLRIAQFHQHL-----AEKLDLELSAL 467
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlngGPLDFQRDSIARGLlylghAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 468 QFMIREYPGNEEEKMRGAIGKFGLSGKAQVmPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNE 547
Cdd:cd03231 92 ENLRFWHADHSDEQVEEALARVGLNGFEDR-PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG 170
|
170 180
....*....|....*....|....*.
gi 1955823976 548 W--DGGLVLVS--HDFRLINQVAQEI 569
Cdd:cd03231 171 HcaRGGMVVLTthQDLGLSEAGAREL 196
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
72-300 |
1.90e-14 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 76.34 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 72 DIRIESLSVTFHGHDLIVDS-ELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPiPEHMDIYHLSREIEASDMSSLEAVI 150
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGlSLTIPPGERVALVGPSGAGKSTLLNLL-LGFLP-PYSGSILINGVDLSDLDPASWRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 151 ScdeerlklekeaesLASQD------------DGGGEQLDRiyerlEALDAATAEKRAAEILYGL--GFNKQMQAKKTRd 216
Cdd:COG4988 414 A--------------WVPQNpylfagtirenlRLGRPDASD-----EELEAALEAAGLDEFVAALpdGLDTPLGEGGRG- 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 217 FSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF--DRILVVVSHSQDFLNgVCTNIIHMQNRKLkIY 294
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLA-QADRILVLDDGRI-VE 551
|
....*.
gi 1955823976 295 TGNYDQ 300
Cdd:COG4988 552 QGTHEE 557
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
384-574 |
2.10e-14 |
|
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: 73.03 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHlRIAQFHQH-LAEKL-- 460
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ-DIREVTLDsLRRAIgv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 461 ---DLEL--SALQFMIReY--PGNEEEKMRGAIGKFGLSGKAQVMPMK----------NLSDGQRSRVIFAWLAWRQPHL 523
Cdd:cd03253 80 vpqDTVLfnDTIGYNIR-YgrPDATDEEVIEAAKAAQIHDKIMRFPDGydtivgerglKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 524 LLLDEPTNHLDIETIDSLAEALNEWDGG--LVLVSHDFRLINQvAQEIWVCEN 574
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAHRLSTIVN-ADKIIVLKD 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
73-296 |
2.32e-14 |
|
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: 72.25 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIgcrelpipehMDIYHLSreieasdmsslEAVISC 152
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKII----------LGLIKPD-----------SGEITF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 D-EERLKLEKEAESLASQDDGGG--------EQLdRIYERLEALDaataEKRAAEILYGLGFnKQMQAKKTRDFSGGWRM 223
Cdd:cd03268 60 DgKSYQKNIEALRRIGALIEAPGfypnltarENL-RLLARLLGIR----KKRIDEVLDVVGL-KDSAKKKVKGFSLGMKQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955823976 224 RIALARALFMNPTVLLLDEPTNHLDLEACVWLEE---NLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKLkIYTG 296
Cdd:cd03268 134 RLGIALALLGNPDLLILDEPTNGLDPDGIKELRElilSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL-IEEG 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
401-571 |
2.67e-14 |
|
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: 72.75 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 401 KNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV---------RRHNHLRiaQFHQHLAEKLDL--ELSALQ- 468
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvaglvpwkRRKKFLR--RIGVVFGQKTQLwwDLPVIDs 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 469 -FMIREYPGNEEEKMRGAIGKfgLSGKAQV-----MPMKNLSDGQRSRV-IFAWLAWRqPHLLLLDEPTNHLDI---ETI 538
Cdd:cd03267 116 fYLLAAIYDLPPARFKKRLDE--LSELLDLeelldTPVRQLSLGQRMRAeIAAALLHE-PEILFLDEPTIGLDVvaqENI 192
|
170 180 190
....*....|....*....|....*....|....
gi 1955823976 539 DSLAEALN-EWDGGLVLVSHDFRLINQVAQEIWV 571
Cdd:cd03267 193 RNFLKEYNrERGTTVLLTSHYMKDIEALARRVLV 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
73-291 |
3.17e-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: 72.14 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIV----DSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPipehmdiyhlSR---EIEASDMSS 145
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalkGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRP----------TSgevRVDGTDISK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 146 LEaviscDEERLKLEKEAESLASQDdgggeqldriY---ERLEALD------------AATAEKRAAEILYGLGFNKQMq 210
Cdd:cd03255 71 LS-----EKELAAFRRRHIGFVFQS----------FnllPDLTALEnvelplllagvpKKERRERAEELLERVGLGDRL- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 211 AKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEAC--VW--LEENLKKFDRILVVVSHSQDfLNGVCTNIIHM 286
Cdd:cd03255 135 NHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGkeVMelLRELNKEAGTTIVVVTHDPE-LAEYADRIIEL 213
|
....*
gi 1955823976 287 QNRKL 291
Cdd:cd03255 214 RDGKI 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
389-582 |
6.83e-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: 70.98 E-value: 6.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 389 VTFGYTPENLiykNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDG--------------------MVRRHN--- 445
Cdd:cd03298 6 IRFSYGEQPM---HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGrvlingvdvtaappadrpvsMLFQENnlf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 446 -HLRIAQfHQHLAEKLDLELSALQfmireypgneEEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFAWLAWRQPHLL 524
Cdd:cd03298 83 aHLTVEQ-NVGLGLSPGLKLTAED----------RQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955823976 525 LLDEPTNHLD----IETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWVCENQAVTkWEG 582
Cdd:cd03298 151 LLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA-AQG 211
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
398-583 |
9.57e-14 |
|
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: 70.66 E-value: 9.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 398 LIYKNLDFGVDLD----SRIALVGPNGAGKSTLLKLMTGDLVPLDG--MVRRHNHLRIAQ--------FHQH-------- 455
Cdd:TIGR01277 8 YEYEHLPMEFDLNvadgEIVAIMGPSGAGKSTLLNLIAGFIEPASGsiKVNDQSHTGLAPyqrpvsmlFQENnlfahltv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 456 -----LAEKLDLELSALQfmireypgneEEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFAWLAWRQPHLLLLDEPT 530
Cdd:TIGR01277 88 rqnigLGLHPGLKLNAEQ----------QEKVVDAAQQVGIADYLDRLP-EQLSGGQRQRVALARCLVRPNPILLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1955823976 531 NHLD----IETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWVCENQAVtKWEGD 583
Cdd:TIGR01277 157 SALDpllrEEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI-KVVSD 212
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
380-558 |
9.72e-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: 71.66 E-value: 9.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 380 PPPVLQFVEVTFGYTPEN---LIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHlRIAQFHQHL 456
Cdd:COG1116 4 AAPALELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-PVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 457 A----EKLDLE-LSALQ-----FMIREYPGNE-EEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFA-WLAwRQPHLL 524
Cdd:COG1116 83 GvvfqEPALLPwLTVLDnvalgLELRGVPKAErRERARELLELVGLAGFEDAYP-HQLSGGMRQRVAIArALA-NDPEVL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1955823976 525 LLDEPTNHLDIETIDSL-AEALNEWDGG---LVLVSHD 558
Cdd:COG1116 161 LMDEPFGALDALTRERLqDELLRLWQETgktVLFVTHD 198
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
401-570 |
1.52e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.50 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 401 KNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNhlRIAQFhqhlaekldLELSAlqFMIREYPGNEEE 480
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--RVSAL---------LELGA--GFHPELTGRENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 481 KMRGAIgkFGLSgKAQV------------------MPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLD-------I 535
Cdd:COG1134 110 YLNGRL--LGLS-RKEIdekfdeivefaelgdfidQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDaafqkkcL 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 1955823976 536 ETIDSLAEAlnewDGGLVLVSHDFRLINQVAQE-IW 570
Cdd:COG1134 187 ARIRELRES----GRTVIFVSHSMGAVRRLCDRaIW 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
73-292 |
1.75e-13 |
|
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: 69.53 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRrYGLLGLNGCGKSTLLAAIgCRELPiPEHMDIYHLSREIeASDMSSLEAVISc 152
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRIL-ATLTP-PSSGTIRIDGQDV-LKQPQKLRRRIG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 deerlklekeaesLASQDDGGGEQLdRIYE------RLEALDAATAEKRAAEILYGLGFNkQMQAKKTRDFSGGWRMRIA 226
Cdd:cd03264 76 -------------YLPQEFGVYPNF-TVREfldyiaWLKGIPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 227 LARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF--DRILVVVSHSQDFLNGVCTNIIHMQNRKLK 292
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELgeDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
380-578 |
1.87e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.57 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 380 PPPVLQFVEVTFGYTPenlIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR-----------RHNHLR 448
Cdd:PRK09536 2 PMIDVSDLSVEFGDTT---VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddvealsaRAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 449 IAQFHQHLAEKLDLELSALQFMIR--------EYPGNEEEKMRGAIGKFGLSGKAQvMPMKNLSDGQRSRVIFA-WLAWR 519
Cdd:PRK09536 79 VASVPQDTSLSFEFDVRQVVEMGRtphrsrfdTWTETDRAAVERAMERTGVAQFAD-RPVTSLSGGERQRVLLArALAQA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 520 QPhLLLLDEPTNHLDI----ETIDSLAEaLNEWDGGLVLVSHDFRLINQVAQEIWVCENQAVT 578
Cdd:PRK09536 158 TP-VLLLDEPTASLDInhqvRTLELVRR-LVDDGKTAVAAIHDLDLAARYCDELVLLADGRVR 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
73-307 |
2.12e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.04 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIPEHMDI----YHLSREIEASDMSSLEa 148
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhFDFSKTPSDKAIRELR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 149 viscdeerlklekeaeslasQDDGGGEQ----------LDRIYE---RLEALDAATAEKRAAEILYGLgfnkQMQAKKTR 215
Cdd:PRK11124 82 --------------------RNVGMVFQqynlwphltvQQNLIEapcRVLGLSKDQALARAEKLLERL----RLKPYADR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 216 ---DFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLE---ACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNR 289
Cdd:PRK11124 138 fplHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEitaQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENG 217
|
250
....*....|....*...
gi 1955823976 290 KLkIYTGNYDQYVQTRSE 307
Cdd:PRK11124 218 HI-VEQGDASCFTQPQTE 234
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
384-558 |
2.68e-13 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 69.09 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGytpENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV----RRHNHL-----RIAQFHQ 454
Cdd:cd03259 3 LKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgRDVTGVpperrNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 455 HLA--------EKLDLELsALQFMIREypgNEEEKMRGAIGKFGLSGKAQVMPMKnLSDGQRSRVIFA-WLAwRQPHLLL 525
Cdd:cd03259 80 DYAlfphltvaENIAFGL-KLRGVPKA---EIRARVRELLELVGLEGLLNRYPHE-LSGGQQQRVALArALA-REPSLLL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1955823976 526 LDEPTNHLDIETIDSL----AEALNEWDGGLVLVSHD 558
Cdd:cd03259 154 LDEPLSALDAKLREELreelKELQRELGITTIYVTHD 190
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
396-557 |
2.90e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.61 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 396 ENLI--YKNL----DFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVP------LDGMVRRH------------------N 445
Cdd:PRK10771 5 TDITwlYHHLpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPasgsltLNGQDHTTtppsrrpvsmlfqennlfS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 446 HLRIAqfhQHLAEKLD--LELSALQfmireypgneEEKMRGAIGKFGLSGKAQVMPMKnLSDGQRSRVIFAWLAWRQPHL 523
Cdd:PRK10771 85 HLTVA---QNIGLGLNpgLKLNAAQ----------REKLHAIARQMGIEDLLARLPGQ-LSGGQRQRVALARCLVREQPI 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 1955823976 524 LLLDEPTNHLD----IETIDSLAEALNEWDGGLVLVSH 557
Cdd:PRK10771 151 LLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
354-571 |
3.04e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 72.83 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 354 MERGGLTEKVvrdkvlvFRFVD-------VGKLPPP----VLQFVEVTFGYT--PENLIYKNLDFGVDLDSRIALVGPNG 420
Cdd:TIGR00958 445 MQAVGASEKV-------FEYLDrkpniplTGTLAPLnlegLIEFQDVSFSYPnrPDVPVLKGLTFTLHPGEVVALVGPSG 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 421 AGKSTLLKLM------TGDLVPLDGM-VRRHNHLRIaqfHQHLA----EKLDLELSALQFMIREYPGNEEEKMRGA---- 485
Cdd:TIGR00958 518 SGKSTVAALLqnlyqpTGGQVLLDGVpLVQYDHHYL---HRQVAlvgqEPVLFSGSVRENIAYGLTDTPDEEIMAAakaa 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 486 -----IGKFGLSGKAQVMPMKN-LSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEWDGGLVLVSHDF 559
Cdd:TIGR00958 595 nahdfIMEFPNGYDTEVGEKGSqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRL 674
|
250
....*....|..
gi 1955823976 560 RLINQvAQEIWV 571
Cdd:TIGR00958 675 STVER-ADQILV 685
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
217-271 |
3.22e-13 |
|
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: 68.01 E-value: 3.22e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 217 FSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEEN---LKKFDRILVVVSH 271
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAiaaLKAAGATRIVIAH 154
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
73-310 |
3.23e-13 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 69.73 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAI-GcrELPiPEHMDIYHLSREIEASD--------- 142
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIlG--LLP-PTSGTVRLFGKPPRRARrrigyvpqr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 143 --------MSSLEAVISCDEERLKLEKEAeslasqddgGGEQLDRIYERLEALDAATAEKRaaeilyglgfnkQMqakkt 214
Cdd:COG1121 84 aevdwdfpITVRDVVLMGRYGRRGLFRRP---------SRADREAVDEALERVGLEDLADR------------PI----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 215 RDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEE---NLKKFDRILVVVSHSQDFLNGVCTNIIHMqNRKL 291
Cdd:COG1121 138 GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYEllrELRREGKTILVVTHDLGAVREYFDRVLLL-NRGL 216
|
250
....*....|....*....
gi 1955823976 292 kIYTGNYDQyVQTRSELEE 310
Cdd:COG1121 217 -VAHGPPEE-VLTPENLSR 233
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
384-561 |
3.34e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 72.50 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVP------LDGM-VRrhnHLRIAQFHQHL 456
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPtsgrilIDGVdIR---DLTLESLRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 457 AekldlelSALQ--FM----IRE---Y--PGNEEEKMRGAIGKFGLSGKAQVMPMK----------NLSDGQRSRVIFAW 515
Cdd:COG1132 417 G-------VVPQdtFLfsgtIREnirYgrPDATDEEVEEAAKAAQAHEFIEALPDGydtvvgergvNLSGGQRQRIAIAR 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1955823976 516 LAWRQPHLLLLDEPTNHLDIETIDSLAEALNEWDGG--LVLVSHdfRL 561
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMKGrtTIVIAH--RL 535
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
73-291 |
3.81e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 68.92 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIV----DSELELNYGRRYGLLGLNGCGKSTLLAAIGCreLPIPEHMDIYHLSREIeaSDMSslea 148
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtalrGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG--LDRPTSGEVLIDGQDI--SSLS---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 149 viscDEERLKLEKEAESLASQDdggGEQLDR--IYE------RLEALDAATAEKRAAEILYGLGFNKQMQaKKTRDFSGG 220
Cdd:COG1136 77 ----ERELARLRRRHIGFVFQF---FNLLPEltALEnvalplLLAGVSRKERRERARELLERVGLGDRLD-HRPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955823976 221 WRMRIALARALFMNPTVLLLDEPTNHLDLEAC--VW--LEENLKKFDRILVVVSHSQDFLNgVCTNIIHMQNRKL 291
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGeeVLelLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
381-538 |
4.23e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.72 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 381 PPVLQFVEVTFGYTPENlIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNH-------LRIAQFH 453
Cdd:PRK13543 9 PPLLAAHALAFSRNEEP-VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrSRFMAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 454 QHL-AEKLDLE-LSALQFM-------IREYPGNeeekmrgAIGKFGLSGKAQVMpMKNLSDGQRSRVIFAWLaWRQPH-L 523
Cdd:PRK13543 88 GHLpGLKADLStLENLHFLcglhgrrAKQMPGS-------ALAIVGLAGYEDTL-VRQLSAGQKKRLALARL-WLSPApL 158
|
170
....*....|....*
gi 1955823976 524 LLLDEPTNHLDIETI 538
Cdd:PRK13543 159 WLLDEPYANLDLEGI 173
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
401-569 |
5.01e-13 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 69.13 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 401 KNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV---------------RRHNHlRIAQFHQH--LAEKLDL- 462
Cdd:cd03256 18 KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinklkgkalRQLRR-QIGMIFQQfnLIERLSVl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 463 ---------ELSALQFMIREYPGNEEEKMRGAIGKFGLSGKAQVMpMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHL 533
Cdd:cd03256 97 envlsgrlgRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQR-ADQLSGGQQQRVAIARALMQQPKLILADEPVASL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1955823976 534 DIET---IDSLAEALNEWDGGLVLVS-HDFRLINQVAQEI 569
Cdd:cd03256 176 DPASsrqVMDLLKRINREEGITVIVSlHQVDLAREYADRI 215
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
387-574 |
5.09e-13 |
|
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: 69.06 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 387 VEVTFGYTPENL-IYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTG-----------DLVPLDGMVRRHNHLRI----- 449
Cdd:COG1124 7 LSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGlerpwsgevtfDGRPVTRRRRKAFRRRVqmvfq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 450 ---AQFH------QHLAEKLdlelsALQFMireypGNEEEKMRGAIGKFGLSGK------AQvmpmknLSDGQRSRVIFA 514
Cdd:COG1124 87 dpyASLHprhtvdRILAEPL-----RIHGL-----PDREERIAELLEQVGLPPSfldrypHQ------LSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 515 wlawR----QPHLLLLDEPTNHLDI----ETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWVCEN 574
Cdd:COG1124 151 ----RalilEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
73-307 |
5.74e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 68.89 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIPEHMDI----YHLSREIEASDMSSLEa 148
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaghqFDFSQKPSEKAIRLLR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 149 viscdeerlklekeaeslasQDDGGGEQ----------LDRIYE---RLEALDAATAEKRAAEILYGLgfnkQMQAKKTR 215
Cdd:COG4161 82 --------------------QKVGMVFQqynlwphltvMENLIEapcKVLGLSKEQAREKAMKLLARL----RLTDKADR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 216 ---DFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLE---ACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNR 289
Cdd:COG4161 138 fplHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEitaQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKG 217
|
250
....*....|....*...
gi 1955823976 290 KLkIYTGNYDQYVQTRSE 307
Cdd:COG4161 218 RI-IEQGDASHFTQPQTE 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
73-286 |
7.41e-13 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 67.94 E-value: 7.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRElpipehmdiyhlsrEIEASDmssleavISC 152
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLE--------------EPDSGT-------III 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 DEERLKLEKEAESLASQDDGGGEQLDRIYERLEALD-------------AATAEKRAAEILYGLGFNKQmQAKKTRDFSG 219
Cdd:cd03262 60 DGLKLTDDKKNINELRQKVGMVFQQFNLFPHLTVLEnitlapikvkgmsKAEAEERALELLEKVGLADK-ADAYPAQLSG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 220 GWRMRIALARALFMNPTVLLLDEPTNHLDLEacvWLEE------NLKKFDRILVVVSHSQDFLNGVCTNIIHM 286
Cdd:cd03262 139 GQQQRVAIARALAMNPKVMLFDEPTSALDPE---LVGEvldvmkDLAEEGMTMVVVTHEMGFAREVADRVIFM 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
384-574 |
8.57e-13 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 66.83 E-value: 8.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYtPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNhlriaQFHQHLAEKLDLE 463
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDG-----EDLTDLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 464 LSALQFMIREYPGNEEEKMRGAIGkFGLSGkaqvmpmknlsdGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIET---IDS 540
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIA-LGLSG------------GQQQRVALARALAMDPDVLLLDEPTSALDPITrreVRA 141
|
170 180 190
....*....|....*....|....*....|....*
gi 1955823976 541 LAEALNEWDG-GLVLVSHDFRLINQVAQEIWVCEN 574
Cdd:cd03229 142 LLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRD 176
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
382-571 |
9.71e-13 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 70.70 E-value: 9.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 382 PVLQFVEVTFGYTP-ENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGdLVPLDGMVRRHNHL------------- 447
Cdd:COG1123 3 PLLEVRDLSVRYPGgDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRISGEVLLdgrdllelsealr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 448 --RIAQFHQHLAEKLD----LELSALQFMIREYPGNE-EEKMRGAIGKFGLSGKAQVMPMKnLSDGQRSRVIFAWLAWRQ 520
Cdd:COG1123 82 grRIGMVFQDPMTQLNpvtvGDQIAEALENLGLSRAEaRARVLELLEAVGLERRLDRYPHQ-LSGGQRQRVAIAMALALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1955823976 521 PHLLLLDEPTNHLD----IETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWV 571
Cdd:COG1123 161 PDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVV 215
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
394-569 |
1.19e-12 |
|
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: 67.53 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 394 TPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDG--MVRRHN---HLRIAQFH-----QHLAekLDLE 463
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtaYINGYSirtDRKAARQSlgycpQFDA--LFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 464 LSA---LQFM--IREYPGNEEEK-MRGAIGKFGLSGKAQVmPMKNLSDGQRSR--VIFAWLAwrQPHLLLLDEPTNHLDI 535
Cdd:cd03263 90 LTVrehLRFYarLKGLPKSEIKEeVELLLRVLGLTDKANK-RARTLSGGMKRKlsLAIALIG--GPSVLLLDEPTSGLDP 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1955823976 536 ETIDSLAEALNEWDGG--LVLVSHDFRLINQVAQEI 569
Cdd:cd03263 167 ASRRAIWDLILEVRKGrsIILTTHSMDEAEALCDRI 202
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
204-314 |
1.20e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 204 GFNKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNI 283
Cdd:PRK11819 433 NFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI 512
|
90 100 110
....*....|....*....|....*....|..
gi 1955823976 284 IHMQ-NRKLKIYTGNYDQYvqtrselEENQMK 314
Cdd:PRK11819 513 LAFEgDSQVEWFEGNFQEY-------EEDKKR 537
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
378-591 |
1.48e-12 |
|
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: 70.07 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 378 KLPPP--VLQFVEVTFGYTPENL-IYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRrhnhLRIAQFHQ 454
Cdd:TIGR01842 309 PLPEPegHLSVENVTIVPPGGKKpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVR----LDGADLKQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 455 HLAEKLDLELSALQFMIREYPGNEEEKmrgaIGKFG-------------LSGKAQV---MPM----------KNLSDGQR 508
Cdd:TIGR01842 385 WDRETFGKHIGYLPQDVELFPGTVAEN----IARFGenadpekiieaakLAGVHELilrLPDgydtvigpggATLSGGQR 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 509 SRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEWD---GGLVLVSHDFRLINQVaQEIWVCENQAVTKWeGDIM 585
Cdd:TIGR01842 461 QRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITHRPSLLGCV-DKILVLQDGRIARF-GERD 538
|
....*.
gi 1955823976 586 DFKAHL 591
Cdd:TIGR01842 539 EVLAKL 544
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
102-292 |
1.56e-12 |
|
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: 67.14 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 102 GLLGLNGCGKSTLLAAIgCRELPiPEHMDIYHLSREIeASDMSSLEAVIScdeerlklekeaesLASQDDG-----GGEQ 176
Cdd:cd03263 32 GLLGHNGAGKTTTLKML-TGELR-PTSGTAYINGYSI-RTDRKAARQSLG--------------YCPQFDAlfdelTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 177 LDRIYERLEALDAATAEKRAAEILYGLGFNKQMQaKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEA--CVW 254
Cdd:cd03263 95 HLRFYARLKGLPKSEIKEEVELLLRVLGLTDKAN-KRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASrrAIW 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1955823976 255 --LEEnLKKfDRILVVVSHSQDFLNGVCTNIIHMQNRKLK 292
Cdd:cd03263 174 dlILE-VRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
384-547 |
1.67e-12 |
|
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: 67.26 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYTP-ENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLM------TGDLVPLDGM---------VRRH--- 444
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvDSGRILIDGHdvrdytlasLRRQigl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 445 -------------NHLRIAQFHQHLAEKLD-LELSALQFMIREYPGNEEEKmrgaIGKFGLsgkaqvmpmkNLSDGQRSR 510
Cdd:cd03251 81 vsqdvflfndtvaENIAYGRPGATREEVEEaARAANAHEFIMELPEGYDTV----IGERGV----------KLSGGQRQR 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 1955823976 511 VIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNE 547
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALER 183
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
383-571 |
1.94e-12 |
|
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: 67.15 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 383 VLQFVEVTFGYTPENLIYKNLDfGVDLD----SRIALVGPNGAGKSTLLKLMTG--------------DLVPLDGMVRRH 444
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALD-DVSFSikkgETLGLVGESGSGKSTLARAILGllkptsgsiifdgkDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 445 NHLRIAQFHQHLAEKLDLELSALQfMIRE-------YPGNEEEKMRGAIGKFGLSGKAQVMPMK--NLSDGQRSRVIFAW 515
Cdd:cd03257 80 RRKEIQMVFQDPMSSLNPRMTIGE-QIAEplrihgkLSKKEARKEAVLLLLVGVGLPEEVLNRYphELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 516 -LAwRQPHLLLLDEPTNHLD----IETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWV 571
Cdd:cd03257 159 aLA-LNPKLLIADEPTSALDvsvqAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAV 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
73-273 |
2.62e-12 |
|
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: 66.88 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFhGHDLIVDS-ELELNYGRRYGLLGLNGCGKSTLLAAIGCRElpIPEHMDIYhlsreIEASDMSSLEAvis 151
Cdd:cd03300 1 IELENVSKFY-GGFVALDGvSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFE--TPTSGEIL-----LDGKDITNLPP--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 152 cdeerlklEKEAESLASQDDGGGEQLDrIYE------RLEALDAATAEKRAAEILyglgfnKQMQ-----AKKTRDFSGG 220
Cdd:cd03300 70 --------HKRPVNTVFQNYALFPHLT-VFEniafglRLKKLPKAEIKERVAEAL------DLVQlegyaNRKPSQLSGG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1955823976 221 WRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRIL----VVVSHSQ 273
Cdd:cd03300 135 QQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgitfVFVTHDQ 191
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
378-563 |
2.96e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.52 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 378 KLPPPVLQFVEvTFGYTPENL---IYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLV--PLDGMVRrhnhLRIAQF 452
Cdd:COG2401 22 DLSERVAIVLE-AFGVELRVVeryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVD----VPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 453 HQH--LAEKLDLELSALQFMireypgneeekmrGAIGKFGLSgKAQVM--PMKNLSDGQRSRVIFAWLAWRQPHLLLLDE 528
Cdd:COG2401 97 GREasLIDAIGRKGDFKDAV-------------ELLNAVGLS-DAVLWlrRFKELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1955823976 529 PTNHLDIETIDSLA----EALNEWDGGLVLVSHDFRLIN 563
Cdd:COG2401 163 FCSHLDRQTAKRVArnlqKLARRAGITLVVATHHYDVID 201
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
73-286 |
3.32e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 66.70 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIpehmdiyhlSREIEASDmssleavISC 152
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPE---------AGTIRVGD-------ITI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 DEER-LKLEKEAESLASQDDGGGEQ----------LDRIYE-----RLEALDAATAekRAAEILYGLGFNKQMQAKKTRd 216
Cdd:PRK11264 68 DTARsLSQQKGLIRQLRQHVGFVFQnfnlfphrtvLENIIEgpvivKGEPKEEATA--RARELLAKVGLAGKETSYPRR- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 217 FSGGWRMRIALARALFMNPTVLLLDEPTNHLDLE---ACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHM 286
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPElvgEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFM 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
383-577 |
3.95e-12 |
|
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: 65.96 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 383 VLQFVEVTFGYT--PENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIAQFHQHLAEKL 460
Cdd:cd03248 11 IVKFQNVTFAYPtrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 461 DL---ELSALQFMIRE-----YPGNEEEKMRGAIGKFGLSGKAQVMPM----------KNLSDGQRSRVIFAWLAWRQPH 522
Cdd:cd03248 91 SLvgqEPVLFARSLQDniaygLQSCSFECVKEAAQKAHAHSFISELASgydtevgekgSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1955823976 523 LLLLDEPTNHLDIETIDSLAEALNEW--DGGLVLVSHDFRLINQvAQEIWVCENQAV 577
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
406-566 |
5.49e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 66.31 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 406 GVDLDSR----IALVGPNGAGKSTLLKLMTGDLVPLDGMVR------------RHNHLRIAQFHQHLA---EKLDL--EL 464
Cdd:PRK11264 21 GIDLEVKpgevVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtarslSQQKGLIRQLRQHVGfvfQNFNLfpHR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 465 SALQFMI-------REYPGNEEEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIE- 536
Cdd:PRK11264 101 TVLENIIegpvivkGEPKEEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPEl 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 1955823976 537 ------TIDSLAEALNEwdggLVLVSHDFRLINQVA 566
Cdd:PRK11264 180 vgevlnTIRQLAQEKRT----MVIVTHEMSFARDVA 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
73-271 |
8.96e-12 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 65.49 E-value: 8.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPIPEHMDIYHLSREIEASDMSSLeavisc 152
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLI-TGDLPPTYGNDVRLFGERRGGEDVWEL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 deeRLKLekeaeSLASQddgggEQLDRIYERLEALDA----------------ATAEKRAAEILYGLGfnkqMQAKKTRD 216
Cdd:COG1119 77 ---RKRI-----GLVSP-----ALQLRFPRDETVLDVvlsgffdsiglyreptDEQRERARELLELLG----LAHLADRP 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955823976 217 F---SGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF----DRILVVVSH 271
Cdd:COG1119 140 FgtlSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaegAPTLVLVTH 201
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
400-573 |
9.08e-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: 64.62 E-value: 9.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 400 YKNLDFGVDLD-----SRIALVGPNGAGKSTLLKLMTGDLVP------LDGMV----RRHNHL-----RIAQFHQHLAek 459
Cdd:cd03297 8 KRLPDFTLKIDfdlneEVTGIFGASGAGKSTLLRCIAGLEKPdggtivLNGTVlfdsRKKINLppqqrKIGLVFQQYA-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 460 LDLELSALQFMIREYPGNEEEKMR----GAIGKFGLSGKAQVMPMKnLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDI 535
Cdd:cd03297 86 LFPHLNVRENLAFGLKRKRNREDRisvdELLDLLGLDHLLNRYPAQ-LSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1955823976 536 ETIDSLAEALNE----WDGGLVLVSHDFRLINQVAQEIWVCE 573
Cdd:cd03297 165 ALRLQLLPELKQikknLNIPVIFVTHDLSEAEYLADRIVVME 206
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
72-274 |
1.10e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 66.66 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 72 DIRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAI-GcreLPIPEHMDIYhlsreIEASDMSSLEAvi 150
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIaG---FETPDSGRIL-----LDGRDVTGLPP-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 151 scdEER------------------------LKLEKeaeslasqddgggeqldriyerleaLDAATAEKRAAEILY--GLG 204
Cdd:COG3842 75 ---EKRnvgmvfqdyalfphltvaenvafgLRMRG-------------------------VPKAEIRARVAELLElvGLE 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955823976 205 fnkQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKkfdRIL-------VVVSHSQD 274
Cdd:COG3842 127 ---GLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELR---RLQrelgitfIYVTHDQE 197
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
73-248 |
1.15e-11 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 66.23 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIV----DSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPIPEHM---------DIYHLS---- 135
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkavdGVSFDVRRGETLGLVGESGSGKSTLARAI-LGLLPPPGITsgeilfdgeDLLKLSekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 136 REIEASD--------MSSLEAVISCdeerlklekeaeslasqddggGEQLDRIYERLEALDAATAEKRAAEIL--YGLGf 205
Cdd:COG0444 81 RKIRGREiqmifqdpMTSLNPVMTV---------------------GDQIAEPLRIHGGLSKAEARERAIELLerVGLP- 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1955823976 206 nkqmQAKKTRD-----FSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:COG0444 139 ----DPERRLDrypheLSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
73-286 |
1.17e-11 |
|
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: 64.70 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTF---HGHDLIVDS-ELELNYGRRYGLLGLNGCGKSTLLAAigcrelpipehmdiyhLSREIEASD----MS 144
Cdd:cd03266 2 ITADALTKRFrdvKKTVQAVDGvSFTVKPGEVTGLLGPNGAGKTTTLRM----------------LAGLLEPDAgfatVD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 145 SLEAVISCDEERLKLEKEAESLASQDDGGGEQLDRIYERLEALDAATAEKRAAEILYGLGFNKQMQaKKTRDFSGGWRMR 224
Cdd:cd03266 66 GFDVVKEPAEARRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLD-RRVGGFSTGMRQK 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955823976 225 IALARALFMNPTVLLLDEPTNHLDLEACVWLEE---NLKKFDRILVVVSHSQDFLNGVCTNIIHM 286
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREfirQLRALGKCILFSTHIMQEVERLCDRVVVL 209
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
405-573 |
1.59e-11 |
|
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: 64.10 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 405 FGVDLDSRIALVGPNGAGKSTLLKLMTGdLVP-------LDGMVRRHNHLRIAQFHQHLAEKLDLELSALQFMIREYPG- 476
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILG-LIPpakgtvkVAGASPGKGWRHIGYVPQRHEFAWDFPISVAHTVMSGRTGh 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 477 ---------NEEEKMRGAIGKFGLSGKAQvMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNE 547
Cdd:TIGR03771 80 igwlrrpcvADFAAVRDALRRVGLTELAD-RPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIE 158
|
170 180
....*....|....*....|....*....
gi 1955823976 548 WDG---GLVLVSHDfrlinqVAQEIWVCE 573
Cdd:TIGR03771 159 LAGagtAILMTTHD------LAQAMATCD 181
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
388-578 |
1.62e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.21 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 388 EVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV-------RRHNHLRIAQFHQHLAEKL 460
Cdd:PRK13652 8 DLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepiTKENIREVRKFVGLVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 461 DLEL--SALQFMIREYPGN---EEE----KMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTN 531
Cdd:PRK13652 88 DDQIfsPTVEQDIAFGPINlglDEEtvahRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 532 HLDIETIDSLAEALN----EWDGGLVLVSHDFRLINQVAQEIWVCENQAVT 578
Cdd:PRK13652 167 GLDPQGVKELIDFLNdlpeTYGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
401-570 |
1.90e-11 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 63.70 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 401 KNLDFGVDLDSRIALVGPNGAGKSTLLKLM-------TGDLVpLDGMVRRHNHLRIAQFHQHLA---EKLDL--ELSALQ 468
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlleepdSGTII-IDGLKLTDDKKNINELRQKVGmvfQQFNLfpHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 469 ------FMIREYPGNE-EEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFA-WLAWRqPHLLLLDEPTNHLDIETID- 539
Cdd:cd03262 96 nitlapIKVKGMSKAEaEERALELLEKVGLADKADAYP-AQLSGGQQQRVAIArALAMN-PKVMLFDEPTSALDPELVGe 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1955823976 540 ------SLAEalnewDG-GLVLVSHDFRLINQVAQEIW 570
Cdd:cd03262 174 vldvmkDLAE-----EGmTMVVVTHEMGFAREVADRVI 206
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
384-557 |
1.92e-11 |
|
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: 62.56 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFgYTPEN-LIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMtGDLVPLD----GMVRRHNHLRIAQfhqhlae 458
Cdd:cd03223 1 IELENLSL-ATPDGrVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPWGsgriGMPEGEDLLFLPQ------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 459 kldlelsalqfmiREY--PGNeeekMRGAIgkfglsgkaqVMP-MKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDI 535
Cdd:cd03223 72 -------------RPYlpLGT----LREQL----------IYPwDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180
....*....|....*....|..
gi 1955823976 536 ETIDSLAEALNEWDGGLVLVSH 557
Cdd:cd03223 125 ESEDRLYQLLKELGITVISVGH 146
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
383-566 |
2.04e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 64.34 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 383 VLQFVEVT--FGYTPenlIYKNLDFGVDLDSRIALVGPNGAGKSTLL----KLMT---GDLVpLDGM-----------VR 442
Cdd:PRK09493 1 MIEFKNVSkhFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTLLrcinKLEEitsGDLI-VDGLkvndpkvderlIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 443 RHNHLRIAQFHqhlaekLDLELSALQ------FMIREYPGNEEEKM-RGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFA- 514
Cdd:PRK09493 77 QEAGMVFQQFY------LFPHLTALEnvmfgpLRVRGASKEEAEKQaRELLAKVGLAERAHHYP-SELSGGQQQRVAIAr 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 515 WLAWRqPHLLLLDEPTNHLDIE-------TIDSLAEalnewDG-GLVLVSHDFRLINQVA 566
Cdd:PRK09493 150 ALAVK-PKLMLFDEPTSALDPElrhevlkVMQDLAE-----EGmTMVIVTHEIGFAEKVA 203
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
413-576 |
2.78e-11 |
|
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: 63.97 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 413 IALVGPNGAGKSTLLKLMTGDLVPLDGmvrrhnhlriaqfhqhlaeKLDLELSAL----QFMIREYPGNEEEKMRGAIGK 488
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEG-------------------DIEIELDTVsykpQYIKADYEGTVRDLLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 489 FGLSG--KAQVM-PMK----------NLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIE-------TIDSLAEalNEW 548
Cdd:cd03237 89 FYTHPyfKTEIAkPLQieqildrevpELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmaskVIRRFAE--NNE 166
|
170 180
....*....|....*....|....*...
gi 1955823976 549 DGGLVlVSHDFRLINQVAQEIWVCENQA 576
Cdd:cd03237 167 KTAFV-VEHDIIMIDYLADRLIVFEGEP 193
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
73-288 |
2.84e-11 |
|
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: 63.74 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTF-HGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAaigcrelpipehmdiyHLSREIEASDMSsleaVIS 151
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLR----------------CLNGLVEPTSGS----VLI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 152 CDEERLKLEKEAESLASQDDGGGEQLDRIYERLEALDAA-------------------TAEK-RAAEILYGLGFnKQMQA 211
Cdd:cd03256 61 DGTDINKLKGKALRQLRRQIGMIFQQFNLIERLSVLENVlsgrlgrrstwrslfglfpKEEKqRALAALERVGL-LDKAY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 212 KKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDR---ILVVVS-HSQDFLNGVCTNIIHMQ 287
Cdd:cd03256 140 QRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReegITVIVSlHQVDLAREYADRIVGLK 219
|
.
gi 1955823976 288 N 288
Cdd:cd03256 220 D 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
383-562 |
2.86e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.36 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 383 VLQFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNH------------LR-- 448
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditrlknrevpfLRrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 449 ---IAQFHQHLAEKLDLELSALQFMIREYPGNE-EEKMRGAIGKFGLSGKAQVMPMKnLSDGQRSRVIFAWLAWRQPHLL 524
Cdd:PRK10908 81 igmIFQDHHLLMDRTVYDNVAIPLIIAGASGDDiRRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1955823976 525 LLDEPTNHLD---IETIDSLAEALNEWDGGLVLVSHDFRLI 562
Cdd:PRK10908 160 LADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
73-308 |
3.03e-11 |
|
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: 63.67 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGcRELPiPEHMDIYHLSREIeaSDMSSleavisc 152
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIV-GLLR-PDSGEVLIDGEDI--SGLSE------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 dEERLKLEKEAeSLASQDdggGEQLD----------RIYERLEaLDAATAEKRAAEILYGLGFnKQMQAKKTRDFSGGWR 222
Cdd:cd03261 70 -AELYRLRRRM-GMLFQS---GALFDsltvfenvafPLREHTR-LSEEEIREIVLEKLEAVGL-RGAEDLYPAELSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 223 MRIALARALFMNPTVLLLDEPTNHLD---LEACVWLEENLKK-FDRILVVVSHSQDFLNGVCTNIIHMQNRKLkIYTGNY 298
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKI-VAEGTP 221
|
250
....*....|
gi 1955823976 299 DQYVQTRSEL 308
Cdd:cd03261 222 EELRASDDPL 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
388-564 |
3.05e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.88 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 388 EVTFGYTPENlIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVrRHNHLRIAQFH-QHLAEKLDL---- 462
Cdd:PRK11231 7 NLTVGYGTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTV-FLGDKPISMLSsRQLARRLALlpqh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 463 ----------ELSA------LQFMIReYPGNEEEKMRGAIGKFGLSGKAQvMPMKNLSDGQRSRVIFAWLAWRQPHLLLL 526
Cdd:PRK11231 85 hltpegitvrELVAygrspwLSLWGR-LSAEDNARVNQAMEQTRINHLAD-RRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1955823976 527 DEPTNHLDI----ETIDSLAEaLNEWDGGLVLVSHDfrlINQ 564
Cdd:PRK11231 163 DEPTTYLDInhqvELMRLMRE-LNTQGKTVVTVLHD---LNQ 200
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
73-287 |
3.09e-11 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 63.56 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDL-------IVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIPEHMDIYHLSREIeasDMSS 145
Cdd:TIGR02324 2 LEVEDLSKTFTLHQQggvrlpvLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEGAWV---DLAQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 146 LEaviscdeerlklEKEAESLASQDDGGGEQLDRIYERLEALDAAT------------AEKRAAEILYGLGFNKQMQAKK 213
Cdd:TIGR02324 79 AS------------PREVLEVRRKTIGYVSQFLRVIPRVSALEVVAepllergvpreaARARARELLARLNIPERLWHLP 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955823976 214 TRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDL---EACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQ 287
Cdd:TIGR02324 147 PATFSGGEQQRVNIARGFIADYPILLLDEPTASLDAanrQVVVELIAEAKARGAALIGIFHDEEVRELVADRVMDVT 223
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
83-291 |
3.51e-11 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 64.06 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 83 HGHDLIVDS-ELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIPEHM-----DIYHLSREIEASDMSSLEAVISCDEER 156
Cdd:TIGR02769 21 KQRAPVLTNvSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsfrgqDLYQLDRKQRRAFRRDVQLVFQDSPSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 157 LKLEKEAESLAsqddggGEQLdriyERLEALDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALFMNPT 236
Cdd:TIGR02769 101 VNPRMTVRQII------GEPL----RHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1955823976 237 VLLLDEPTNHLDL----EACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKL 291
Cdd:TIGR02769 171 LIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
399-561 |
3.86e-11 |
|
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: 63.22 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 399 IYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR-----------------RHNHLRIAQ--FH--QHL- 456
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRlagqdlfaldedararlRARHVGFVFqsFQllPTLt 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 457 AEK---LDLELSALqfmireypGNEEEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHL 533
Cdd:COG4181 107 ALEnvmLPLELAGR--------RDARARARALLERVGLGHRLDHYP-AQLSGGEQQRVALARAFATEPAILFADEPTGNL 177
|
170 180 190
....*....|....*....|....*....|...
gi 1955823976 534 DIET----IDsLAEALNEWDGG-LVLVSHDFRL 561
Cdd:COG4181 178 DAATgeqiID-LLFELNRERGTtLVLVTHDPAL 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
73-274 |
4.10e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 64.78 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAI-GcrelpipehmdiyhlsreIEASDmsslEAVIS 151
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIaG------------------LETPD----SGRIV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 152 CDEERLKLekeaeSLASQDdgggeqldR----------------IYE------RLEALDAATAEKRAAEILyglgfnKQM 209
Cdd:COG1118 61 LNGRDLFT-----NLPPRE--------RrvgfvfqhyalfphmtVAEniafglRVRPPSKAEIRARVEELL------ELV 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955823976 210 QAKKTRD-----FSGGWRMRIALARALFMNPTVLLLDEPTNHLD------LEAcvWLEENLKKFDRILVVVSHSQD 274
Cdd:COG1118 122 QLEGLADrypsqLSGGQRQRVALARALAVEPEVLLLDEPFGALDakvrkeLRR--WLRRLHDELGGTTVFVTHDQE 195
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
73-274 |
4.37e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 64.86 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELP-----IPEHMDIYHL---SREIEAsdMS 144
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPtagqiMLDGVDLSHVppyQRPINM--MF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 145 SLEAVIScdeeRLKLEkeaeslasQDDGGGEQLDRiyerleaLDAATAEKRAAEILyGLGFNKQMQAKKTRDFSGGWRMR 224
Cdd:PRK11607 98 QSYALFP----HMTVE--------QNIAFGLKQDK-------LPKAEIASRVNEML-GLVHMQEFAKRKPHQLSGGQRQR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 225 IALARALFMNPTVLLLDEPTNHLD--LEACVWLE--ENLKKFDRILVVVSHSQD 274
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQE 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
73-272 |
5.77e-11 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 62.58 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIPEH----------MDIYHLSREIEAS- 141
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdegevlldgKDIYDLDVDVLELr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 142 -------------DMSSLEAViscdeerlklekeAESLASQDDGGGEQLDRIYErlEALdaataeKRAAeiLYGLGFNKQ 208
Cdd:cd03260 81 rrvgmvfqkpnpfPGSIYDNV-------------AYGLRLHGIKLKEELDERVE--EAL------RKAA--LWDEVKDRL 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955823976 209 mqakKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF--DRILVVVSHS 272
Cdd:cd03260 138 ----HALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
414-582 |
6.68e-11 |
|
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: 62.23 E-value: 6.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 414 ALVGPNGAGKSTLLKLMTGdLVPLDG---------MVRRHNHL-RIAQ------FHQHLAEKLDLELSALQFMIReypgn 477
Cdd:cd03268 30 GFLGPNGAGKTTTMKIILG-LIKPDSgeitfdgksYQKNIEALrRIGAlieapgFYPNLTARENLRLLARLLGIR----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 478 eEEKMRGAIGKFGLSGKAQVmPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEW--DGGLVLV 555
Cdd:cd03268 104 -KKRIDEVLDVVGLKDSAKK-KVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLrdQGITVLI 181
|
170 180
....*....|....*....|....*...
gi 1955823976 556 -SHDFRLINQVAQEIWVCeNQAVTKWEG 582
Cdd:cd03268 182 sSHLLSEIQKVADRIGII-NKGKLIEEG 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
401-569 |
7.51e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.57 E-value: 7.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 401 KNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV---------RRHNHLR-IA-------QFHQHL--AEKLD 461
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrvlgyvpfkRRKEFARrIGvvfgqrsQLWWDLpaIDSFR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 462 L-----ELSALQFmireypgneEEKMRGAIGKFGLSGKAQVmPMKNLSDGQRSRV-IFAWLAWRqPHLLLLDEPTNHLDI 535
Cdd:COG4586 119 LlkaiyRIPDAEY---------KKRLDELVELLDLGELLDT-PVRQLSLGQRMRCeLAAALLHR-PKILFLDEPTIGLDV 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 1955823976 536 ---ETIDSLAEALNEWDGG-LVLVSHDFRLINQVAQEI 569
Cdd:COG4586 188 vskEAIREFLKEYNRERGTtILLTSHDMDDIEALCDRV 225
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
412-570 |
8.28e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.55 E-value: 8.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 412 RIALVGPNGAGKSTLLKLMTGdLVP------LDGM-VRRHNHLRIAQFHQHLAEKldlelSALQFMIREY--------PG 476
Cdd:COG4138 24 LIHLIGPNGAGKSTLLARMAG-LLPgqgeilLNGRpLSDWSAAELARHRAYLSQQ-----QSPPFAMPVFqylalhqpAG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 477 NEEEKMRGAI----GKFGLSGKAQvMPMKNLSDG--QRSRVIFAWL-AWRQ--PH--LLLLDEPTNHLDIE---TIDSLA 542
Cdd:COG4138 98 ASSEAVEQLLaqlaEALGLEDKLS-RPLTQLSGGewQRVRLAAVLLqVWPTinPEgqLLLLDEPMNSLDVAqqaALDRLL 176
|
170 180
....*....|....*....|....*...
gi 1955823976 543 EALNEWDGGLVLVSHDFRLINQVAQEIW 570
Cdd:COG4138 177 RELCQQGITVVMSSHDLNHTLRHADRVW 204
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
388-564 |
8.73e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.70 E-value: 8.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 388 EVTFGYTpENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV-----------RRHNHLRIAQFHQHL 456
Cdd:PRK10253 12 QLTLGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaSKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 457 AEKLDLELSAL--------QFMIREYPGNEEEKMRGAIGKFGLSGKAQvMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDE 528
Cdd:PRK10253 91 TTPGDITVQELvargryphQPLFTRWRKEDEEAVTKAMQATGITHLAD-QSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1955823976 529 PTNHLDIETIDSLAEALNEWDG----GLVLVSHDfrlINQ 564
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNRekgyTLAAVLHD---LNQ 206
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
396-569 |
9.03e-11 |
|
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: 62.00 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 396 ENLIYKNLDF----GVDLDSR----IALVGPNGAGKSTLLKLMTGDLVPLDGM--------------VRRhnhlRIAQFH 453
Cdd:cd03265 4 ENLVKKYGDFeavrGVSFRVRrgeiFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvvrepreVRR----RIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 454 QHLAekLDLELSALQFM-----IREYPGNE-EEKMRGAIGKFGLsGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLD 527
Cdd:cd03265 80 QDLS--VDDELTGWENLyiharLYGVPGAErRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1955823976 528 EPTNHLDIETIDSL---AEALNEWDGGLV-LVSHDFRLINQVAQEI 569
Cdd:cd03265 157 EPTIGLDPQTRAHVweyIEKLKEEFGMTIlLTTHYMEEAEQLCDRV 202
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
383-573 |
9.08e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.21 E-value: 9.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 383 VLQFVEVTFGYTPENLIYKNLDFGVDLD----SRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIAQFHQ---- 454
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEvkkgSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 455 ----------HLAEKLDLELSALQ---FMIREYPGNEEEKMRGAIGKFGLSGKAQVMPMKN---LSDGQRSRVIFAWLAW 518
Cdd:PRK13643 81 pvrkkvgvvfQFPESQLFEETVLKdvaFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSpfeLSGGQMRRVAIAGILA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1955823976 519 RQPHLLLLDEPTNHLD----IETIdSLAEALNEWDGGLVLVSHDFRLINQVAQEIWVCE 573
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDpkarIEMM-QLFESIHQSGQTVVLVTHLMDDVADYADYVYLLE 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
73-287 |
9.47e-11 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 62.07 E-value: 9.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTF-----HGHDLIV--DSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIPEHMDIYHLSREIeasDMSS 145
Cdd:COG4778 5 LEVENLSKTFtlhlqGGKRLPVldGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWV---DLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 146 LEaviscDEERLKLEKEAESLASQddgggeqLDRIYERLEALD------------AATAEKRAAEILYGLGFNKQMQAKK 213
Cdd:COG4778 82 AS-----PREILALRRRTIGYVSQ-------FLRVIPRVSALDvvaepllergvdREEARARARELLARLNLPERLWDLP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955823976 214 TRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDL---EACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQ 287
Cdd:COG4778 150 PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAanrAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
73-300 |
1.01e-10 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 62.30 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLL-AAIGcreLPIPEH-------MDIYHLS-REIEA--- 140
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLkLIIG---LLRPDSgeilvdgQDITGLSeKELYElrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 141 ------------SDMSSLEAVISCDEERLKL-EKEAEslasqddgggeqlDRIYERLEALD-AATAEKRAAEIlyglgfn 206
Cdd:COG1127 83 rigmlfqggalfDSLTVFENVAFPLREHTDLsEAEIR-------------ELVLEKLELVGlPGAADKMPSEL------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 207 kqmqakktrdfSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACvwleenlKKFDR-IL----------VVVSHSQDF 275
Cdd:COG1127 143 -----------SGGMRKRVALARALALDPEILLYDEPTAGLDPITS-------AVIDElIRelrdelgltsVVVTHDLDS 204
|
250 260
....*....|....*....|....*
gi 1955823976 276 LNGVCTNIIHMQNRKLkIYTGNYDQ 300
Cdd:COG1127 205 AFAIADRVAVLADGKI-IAEGTPEE 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
364-571 |
1.13e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 364 VRDKVLVFRfvdvgKLPPPVLQFVEVTFGYTPenlIYKNL-DFGVDLDSR-------IALVGPNGAGKSTLLKLMTGDLV 435
Cdd:PRK13409 319 IRPEPIEFE-----ERPPRDESERETLVEYPD---LTKKLgDFSLEVEGGeiyegevIGIVGPNGIGKTTFAKLLAGVLK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 436 PLDGMVrrhnhlriaqfhqhlaeKLDLELS-ALQFMIREYPGNEEEKMRGAIGKFGLSG-KAQVM-----------PMKN 502
Cdd:PRK13409 391 PDEGEV-----------------DPELKISyKPQYIKPDYDGTVEDLLRSITDDLGSSYyKSEIIkplqlerlldkNVKD 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955823976 503 LSDGQRSRV-IFAWLAwRQPHLLLLDEPTNHLDIE-------TIDSLAEalnEWDGGLVLVSHDFRLINQVAQEIWV 571
Cdd:PRK13409 454 LSGGELQRVaIAACLS-RDADLYLLDEPSAHLDVEqrlavakAIRRIAE---EREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
73-305 |
1.47e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.95 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLaaigcRELP-------IPE-HMDIyhLSREIE----- 139
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLL-----RHLSglitgdkSAGsHIEL--LGRTVQregrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 140 ASDMSSLEAVISCDEERLKLEKEAESLASQDDG--GGEQLDRIYERLEAldaATAEKRAAEILYGLGFnKQMQAKKTRDF 217
Cdd:PRK09984 78 ARDIRKSRANTGYIFQQFNLVNRLSVLENVLIGalGSTPFWRTCFSWFT---REQKQRALQALTRVGM-VHFAHQRVSTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF---DRILVVVS-HSQDFLNGVCTNIIHMQNRKLkI 293
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqnDGITVVVTlHQVDYALRYCERIVALRQGHV-F 232
|
250
....*....|..
gi 1955823976 294 YTGNYDQYVQTR 305
Cdd:PRK09984 233 YDGSSQQFDNER 244
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
386-547 |
1.54e-10 |
|
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: 61.79 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 386 FVEVTFGYT--PENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLM------TGDLVPLDG-MVRRHN--HLR--IAQF 452
Cdd:cd03249 3 FKNVSFRYPsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydpTSGEILLDGvDIRDLNlrWLRsqIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 453 HQhlaEKLDLELSalqfmIRE------YPGNEEEKMRGA----IGKF--GLSGKAQVMPMKN---LSDGQRSRVIFAWLA 517
Cdd:cd03249 83 SQ---EPVLFDGT-----IAEnirygkPDATDEEVEEAAkkanIHDFimSLPDGYDTLVGERgsqLSGGQKQRIAIARAL 154
|
170 180 190
....*....|....*....|....*....|
gi 1955823976 518 WRQPHLLLLDEPTNHLDIETIDSLAEALNE 547
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDR 184
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
83-260 |
1.67e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.52 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 83 HGHDLIVDS-ELELNYGRRYGLLGLNGCGKSTLLaaigcrelpipehmdiyHLSREIEASDMSSLEAvisCDE---ERLK 158
Cdd:PRK13537 17 YGDKLVVDGlSFHVQRGECFGLLGPNGAGKTTTL-----------------RMLLGLTHPDAGSISL---CGEpvpSRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 159 LEKEAESLASQDDgggeQLD---------RIYERLEALDAATAEKRAAEILYGLGFNKQMQAKkTRDFSGGWRMRIALAR 229
Cdd:PRK13537 77 HARQRVGVVPQFD----NLDpdftvrenlLVFGRYFGLSAAAARALVPPLLEFAKLENKADAK-VGELSGGMKRRLTLAR 151
|
170 180 190
....*....|....*....|....*....|.
gi 1955823976 230 ALFMNPTVLLLDEPTNHLDLEACVWLEENLK 260
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLR 182
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
218-356 |
2.22e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 218 SGGWRMRIALARaLFMNPTVLL-LDEPTNHLDLEACVWLEENLKKFDRILVVVSHSQDFL-NGVCTNIIHMQNRKLKIYT 295
Cdd:PRK11147 442 SGGERNRLLLAR-LFLKPSNLLiLDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKIGRYV 520
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955823976 296 GNYDQYVQTRSELEENQMKMYKWEQDQIASMKEYIARfghGSAKLARQAQSKEKTL-AKMER 356
Cdd:PRK11147 521 GGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKR---SSKKLSYKLQRELEQLpQLLED 579
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
73-271 |
2.27e-10 |
|
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: 60.85 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLaaigcrelpipeHMDIYHLSREIEASDMSSLEAVISC 152
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTI------------KMLTTLLKPTSGRATVAGHDVVREP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 DEERLKLEKEAESLASQDDGGGEQLDRIYERLEALDAATAEKRAAEIL--YGLGFNKQMQAKKtrdFSGGWRMRIALARA 230
Cdd:cd03265 69 REVRRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLdfVGLLEAADRLVKT---YSGGMRRRLEIARS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1955823976 231 LFMNPTVLLLDEPTNHLDLEA--CVW--LEENLKKFDRILVVVSH 271
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTraHVWeyIEKLKEEFGMTILLTTH 190
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
385-545 |
2.30e-10 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 61.09 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 385 QFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV----RRHNHLRIAQFHQHLA--- 457
Cdd:cd03254 4 EFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgIDIRDISRKSLRSMIGvvl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 458 -----------EKLDL---------------ELSALQFMIREYPGNEEEkmrgaIGKFGlsgkaqvmpmKNLSDGQRSRV 511
Cdd:cd03254 84 qdtflfsgtimENIRLgrpnatdeevieaakEAGAHDFIMKLPNGYDTV-----LGENG----------GNLSQGERQLL 148
|
170 180 190
....*....|....*....|....*....|....
gi 1955823976 512 IFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEAL 545
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEAL 182
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
93-248 |
2.40e-10 |
|
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: 63.16 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 93 LELNYGRRYGLLGLNGCGKSTLLAAIgCReLpIPEHMDIYHLSREIEA----------SDM--------SSL------EA 148
Cdd:COG4172 307 LTLRRGETLGLVGESGSGKSTLGLAL-LR-L-IPSEGEIRFDGQDLDGlsrralrplrRRMqvvfqdpfGSLsprmtvGQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 149 VIscdeerlklekeAESLASQDDGggeqldriyerleaLDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALA 228
Cdd:COG4172 384 II------------AEGLRVHGPG--------------LSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIA 437
|
170 180
....*....|....*....|
gi 1955823976 229 RALFMNPTVLLLDEPTNHLD 248
Cdd:COG4172 438 RALILEPKLLVLDEPTSALD 457
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
73-274 |
2.69e-10 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 60.35 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGcrELPIPEHMDIYhlsreIEASDMSSLEAvisc 152
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIA--GLEEPTSGRIY-----IGGRDVTDLPP---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 dEER------------------------LKLEKEAEslasqddgggeqlDRIYERLealdaataeKRAAEILyGLGfnkQ 208
Cdd:cd03301 70 -KDRdiamvfqnyalyphmtvydniafgLKLRKVPK-------------DEIDERV---------REVAELL-QIE---H 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 209 MQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRIL----VVVSHSQD 274
Cdd:cd03301 123 LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLgtttIYVTHDQV 192
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
93-294 |
3.42e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 60.24 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 93 LELNYGRRYGLLGLNGCGKSTLLAAIGcrelpipehmDIYHLSR---EIEASDMSSLEAVISCDEErlklekeaeslASq 169
Cdd:cd03220 43 FEVPRGERIGLIGRNGAGKSTLLRLLA----------GIYPPDSgtvTVRGRVSSLLGLGGGFNPE-----------LT- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 170 ddggGEQLDRIYERLEALDAATAEKRAAEIL--YGLG--FNKQMqakktRDFSGGWRMRIALARALFMNPTVLLLDEPTN 245
Cdd:cd03220 101 ----GRENIYLNGRLLGLSRKEIDEKIDEIIefSELGdfIDLPV-----KTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1955823976 246 HLDL---EACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKLKIY 294
Cdd:cd03220 172 VGDAafqEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
402-573 |
4.17e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.77 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 402 NLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVP------LD---------------GMVRRHNHLR------------ 448
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPtggtilLRgqhieglpghqiarmGVVRTFQHVRlfremtvienll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 449 IAQfHQHLAEKLdleLSALqFMIREYPGNEEEKMRGA---IGKFGLSGKAQvMPMKNLSDGQRSRVIFAWLAWRQPHLLL 525
Cdd:PRK11300 103 VAQ-HQQLKTGL---FSGL-LKTPAFRRAESEALDRAatwLERVGLLEHAN-RQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1955823976 526 LDEPTNHLD-IETID---SLAEALNEWDGGLVLVSHDFRLINQVAQEIWVCE 573
Cdd:PRK11300 177 LDEPAAGLNpKETKEldeLIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVN 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
406-571 |
5.90e-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: 58.21 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 406 GVDLDSR----IALVGPNGAGKSTLLKLMTGDLVP------LDGM------VRRHNHLRIAQFHQhlaekldlelsalqf 469
Cdd:cd03216 18 GVSLSVRrgevHALLGENGAGKSTLMKILSGLYKPdsgeilVDGKevsfasPRDARRAGIAMVYQ--------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 470 mireypgneeekmrgaigkfglsgkaqvmpmknLSDGQRSRV-IFAWLAwRQPHLLLLDEPTNHLD-------IETIDSL 541
Cdd:cd03216 83 ---------------------------------LSVGERQMVeIARALA-RNARLLILDEPTAALTpaeverlFKVIRRL 128
|
170 180 190
....*....|....*....|....*....|.
gi 1955823976 542 AEAlnewdG-GLVLVSHDFRLINQVAQEIWV 571
Cdd:cd03216 129 RAQ-----GvAVIFISHRLDEVFEIADRVTV 154
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
73-274 |
5.98e-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: 60.05 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPipehmdiyhlsreieasdmssleavisc 152
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERP---------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 DEERLKLE-KEAESLASQDDGGGEQLD------------------RIYERLEALDAATAEKRAAEILyglgfnKQMQAKK 213
Cdd:cd03296 55 DSGTILFGgEDATDVPVQERNVGFVFQhyalfrhmtvfdnvafglRVKPRSERPPEAEIRAKVHELL------KLVQLDW 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 214 TRD-----FSGGWRMRIALARALFMNPTVLLLDEPTNHLDL----EACVWLEENLKKFDRILVVVSHSQD 274
Cdd:cd03296 129 LADrypaqLSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQE 198
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
401-587 |
6.36e-10 |
|
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: 59.66 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 401 KNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR------------RHNHLRIAQFHQ---HLAEKLDLELS 465
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditnlppeKRDISYVPQNYAlfpHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 466 alqFMIREYPGNE-EEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEA 544
Cdd:cd03299 96 ---LKKRKVDKKEiERKVLEIAEMLGIDHLLNRKP-ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1955823976 545 LNEW---DGGLVL-VSHDFrlinqvaQEIWVCENQAVTKWEGDIMDF 587
Cdd:cd03299 172 LKKIrkeFGVTVLhVTHDF-------EEAWALADKVAIMLNGKLIQV 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
73-291 |
6.45e-10 |
|
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: 59.52 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIV----DSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIpehmdiyhlsreieasdmsslEA 148
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtalkDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPT---------------------SG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 149 VISCDEERLKLEKEAE-SLASQDDGGGEQ----LDR--IYE------RLEALDAATAEKRAAEILYGLGFNKQMQAKKTr 215
Cdd:cd03258 61 SVLVDGTDLTLLSGKElRKARRRIGMIFQhfnlLSSrtVFEnvalplEIAGVPKAEIEERVLELLELVGLEDKADAYPA- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 216 DFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRIL----VVVSHSQDFLNGVCTNIIHMQNRKL 291
Cdd:cd03258 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELgltiVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
90-248 |
6.78e-10 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 60.35 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 90 DSELELNYGRRYGLLGLNGCGKSTLLAAIGcrELPIPEHMDIYhlsreIEASDMSSLEaviscDEERLKLEKEAESLASQ 169
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCIN--RLIEPTSGKVL-----IDGQDIAAMS-----RKELRELRRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 170 DDGGGEQ---LDRIYERLE--ALDAATAEKRAAEILYGLGFnKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPT 244
Cdd:cd03294 110 SFALLPHrtvLENVAFGLEvqGVPRAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
....
gi 1955823976 245 NHLD 248
Cdd:cd03294 189 SALD 192
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
73-274 |
7.72e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.13 E-value: 7.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHD-----LIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIPEHMDIYHL-----SREIEASD 142
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsstSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 143 M-SSLEAVISCDEERLKLEKEAESLASQDDGGGeqldriyerleaLDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGW 221
Cdd:PRK13643 82 VrKKVGVVFQFPESQLFEETVLKDVAFGPQNFG------------IPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1955823976 222 RMRIALARALFMNPTVLLLDEPTNHLDLEACVwleENLKKFDRI------LVVVSHSQD 274
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKARI---EMMQLFESIhqsgqtVVLVTHLMD 205
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
72-248 |
8.77e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 60.47 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 72 DIRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAI-GcreLPIPEHMDIYhlsreIEASDMSSLEAvi 150
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIaG---LEDPTSGEIL-----IGGRDVTDLPP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 151 scdEER------------------------LKLEKEAEslasqddgggeqlDRIYERLEaldaataekRAAEILyGLGfn 206
Cdd:COG3839 73 ---KDRniamvfqsyalyphmtvyeniafpLKLRKVPK-------------AEIDRRVR---------EAAELL-GLE-- 124
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1955823976 207 kQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:COG3839 125 -DLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
413-536 |
8.83e-10 |
|
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: 58.74 E-value: 8.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 413 IALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNH--LRIAQ-FHQHLA---------------EKLDLeLSALQFMIrey 474
Cdd:cd03264 28 YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvLKQPQkLRRRIGylpqefgvypnftvrEFLDY-IAWLKGIP--- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955823976 475 PGNEEEKMRGAIGKFGLSGKAQvMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIE 536
Cdd:cd03264 104 SKEVKARVDEVLELVNLGDRAK-KKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
74-296 |
9.05e-10 |
|
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: 58.70 E-value: 9.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 74 RIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAI--------GCRELPIPEHMDIYHL------SREIE 139
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIlgllkptsGSIRVFGKPLEKERKRigyvpqRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 140 AS-DMSSLEAVIScdeerlklekeaeslasqddgggeqldRIYERLEALDAATAEKRAAeILYGLGFnKQMQAKKTRDF- 217
Cdd:cd03235 81 RDfPISVRDVVLM---------------------------GLYGHKGLFRRLSKADKAK-VDEALER-VGLSELADRQIg 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 218 --SGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF---DRILVVVSHSQDFLNGVCTNIIHMqNRKLk 292
Cdd:cd03235 132 elSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrreGMTILVVTHDLGLVLEYFDRVLLL-NRTV- 209
|
....
gi 1955823976 293 IYTG 296
Cdd:cd03235 210 VASG 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
413-570 |
9.09e-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: 58.33 E-value: 9.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 413 IALVGPNGAGKSTLLKL---------MTGDL----VPLD--------GMVRRHNHLriaqfHQHLAEKLDLELSAlqfmi 471
Cdd:cd03213 38 TAIMGPSGAGKSTLLNAlagrrtglgVSGEVlingRPLDkrsfrkiiGYVPQDDIL-----HPTLTVRETLMFAA----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 472 reypgneeeKMRGaigkfglsgkaqvmpmknLSDGQRSRVIFAW-LAWRqPHLLLLDEPTNHLD-------IETIDSLAE 543
Cdd:cd03213 108 ---------KLRG------------------LSGGERKRVSIALeLVSN-PSLLFLDEPTSGLDsssalqvMSLLRRLAD 159
|
170 180
....*....|....*....|....*..
gi 1955823976 544 alnewDGGLVLVShdfrlINQVAQEIW 570
Cdd:cd03213 160 -----TGRTIICS-----IHQPSSEIF 176
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
86-248 |
9.22e-10 |
|
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: 59.21 E-value: 9.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 86 DLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRelpipehmdiyhlsreieASDMSSLEAVISCDEERLKLEKEAES 165
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR------------------VEGGGTTSGQILFNGQPRKPDQFQKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 166 LASqddggGEQLDR------IYERL---------EALDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARA 230
Cdd:cd03234 83 VAY-----VRQDDIllpgltVRETLtytailrlpRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQ 157
|
170
....*....|....*...
gi 1955823976 231 LFMNPTVLLLDEPTNHLD 248
Cdd:cd03234 158 LLWDPKVLILDEPTSGLD 175
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
94-249 |
1.01e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.36 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 94 ELNYGRRYGLLGLNGCGKSTLlaaigCRELPIpehmdiyhlsreIEASDMSSL----EAVISCDEERLKLEKEAESLASQ 169
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTL-----ARLLTM------------IETPTGGELyyqgQDLLKADPEAQKLLRQKIQIVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 170 DDGG--------GEQLDriyERLE---ALDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALFMNPTVL 238
Cdd:PRK11308 100 NPYGslnprkkvGQILE---EPLLintSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVV 176
|
170
....*....|.
gi 1955823976 239 LLDEPTNHLDL 249
Cdd:PRK11308 177 VADEPVSALDV 187
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
218-279 |
1.02e-09 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 61.30 E-value: 1.02e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLD------LEACVwleENLKKFDRILVVVSHSQDFLNGV 279
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaaLAAAI---RALKARGATVVVITHRPSLLAAV 533
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
84-271 |
1.13e-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: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 84 GHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIgcRELPIPEHMDIYHLSREIEASDMSSLEAVISC--DEERLKLEK 161
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLI--QRFYVPENGRVLVDGHDLALADPAWLRRQVGVvlQENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 162 EAESLASQDDGggEQLDRIyerLEALDAATAEKRAAEILYGLGfnkQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLD 241
Cdd:cd03252 92 IRDNIALADPG--MSMERV---IEAAKLAGAHDFISELPEGYD---TIVGEQGAGLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190
....*....|....*....|....*....|..
gi 1955823976 242 EPTNHLDLEACVWLEENLKKF--DRILVVVSH 271
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDIcaGRTVIIIAH 195
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
384-571 |
1.14e-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: 58.73 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYTPENLIyKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTG--DLVP---------LDGM-----------V 441
Cdd:cd03260 1 IELRDLNVYYGDKHAL-KDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLIPgapdegevlLDGKdiydldvdvleL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 442 RRhnhlRIA---Q----FHQHLAEKLDLELSalqfmIREYPGNEE--EKMRGAIGKFGLSGK-AQVMPMKNLSDGQRSRV 511
Cdd:cd03260 80 RR----RVGmvfQkpnpFPGSIYDNVAYGLR-----LHGIKLKEEldERVEEALRKAALWDEvKDRLHALGLSGGQQQRL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 512 IFAwLAWR-QPHLLLLDEPTNHLDI---ETIDSLAEALNEwDGGLVLVSHDFRLINQVAQEIWV 571
Cdd:cd03260 151 CLA-RALAnEPEVLLLDEPTSALDPistAKIEELIAELKK-EYTIVIVTHNMQQAARVADRTAF 212
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
73-300 |
1.19e-09 |
|
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: 58.99 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPiPEHMDIYHLSREIEA------------ 140
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLI-SGFLR-PTSGSVLFDGEDITGlppheiarlgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 141 ---------SDMSSLEAVIscdeerlklekeaesLASQDDGGGEQLDRIYERLEAldaaTAEKRAAEIL--YGLGFNKQM 209
Cdd:cd03219 79 rtfqiprlfPELTVLENVM---------------VAAQARTGSGLLLARARREER----EARERAEELLerVGLADLADR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 210 QAkktRDFSGGWRMRIALARALFMNPTVLLLDEPT---NHLDLEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHM 286
Cdd:cd03219 140 PA---GELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVL 216
|
250
....*....|....
gi 1955823976 287 QNRKlKIYTGNYDQ 300
Cdd:cd03219 217 DQGR-VIAEGTPDE 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
414-567 |
1.31e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.42 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 414 ALVGPNGAGKSTLLKLM-------TGDLV----PLDGMVRRHNHLRIAQFHQHL--AEKLDL-ELSAlqfmIREYPgnee 479
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLgrhqppsEGEILldaqPLESWSSKAFARKVAYLPQQLpaAEGMTVrELVA----IGRYP---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 480 ekMRGAIGKFGLSGKAQV---------MPMKN-----LSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDI-ETIDSLA-- 542
Cdd:PRK10575 113 --WHGALGRFGAADREKVeeaislvglKPLAHrlvdsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIaHQVDVLAlv 190
|
170 180
....*....|....*....|....*.
gi 1955823976 543 EALNEWDGGLVL-VSHDfrlINQVAQ 567
Cdd:PRK10575 191 HRLSQERGLTVIaVLHD---INMAAR 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
383-571 |
1.48e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 59.32 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 383 VLQFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV---------RRHNHLRIAQ-- 451
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepikyDKKSLLEVRKtv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 452 ---FH----QHLAEKLDlELSALQFMIREYPGNE-EEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFAWLAWRQPHL 523
Cdd:PRK13639 81 givFQnpddQLFAPTVE-EDVAFGPLNLGLSKEEvEKRVKEALKAVGMEGFENKPP-HHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 524 LLLDEPTNHLD---IETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWV 571
Cdd:PRK13639 159 IVLDEPTSGLDpmgASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYV 209
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
73-249 |
1.50e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 60.24 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAigCRELPIPEHMDIYHLSREIEASDMSSL------ 146
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRA--INGTLTPTAGTVLVAGDDVEALSARAAsrrvas 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 147 ---EAVISCD-EERLKLEKEAESLASQDDGGGEQLDRIYERleALDAATAEKRAAEILYGLgfnkqmqakktrdfSGGWR 222
Cdd:PRK09536 82 vpqDTSLSFEfDVRQVVEMGRTPHRSRFDTWTETDRAAVER--AMERTGVAQFADRPVTSL--------------SGGER 145
|
170 180
....*....|....*....|....*..
gi 1955823976 223 MRIALARALFMNPTVLLLDEPTNHLDL 249
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDI 172
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
414-569 |
1.51e-09 |
|
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: 58.06 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 414 ALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNH----------------------LRIAQFHQHLAEKLDLELSALQFMI 471
Cdd:cd03269 30 GLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrigylpeerglypkMKVIDQLVYLAQLKGLKKEEARRRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 472 REYpgneeekmrgaIGKFGLSGKAQVmPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEW-DG 550
Cdd:cd03269 110 DEW-----------LERLELSEYANK-RVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELaRA 177
|
170 180
....*....|....*....|.
gi 1955823976 551 G--LVLVSHDFRLINQVAQEI 569
Cdd:cd03269 178 GktVILSTHQMELVEELCDRV 198
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
391-598 |
1.58e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 59.25 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 391 FGYTPENLIyKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV-----------RRHNHLR--IAQFHQHLA 457
Cdd:PRK13638 9 FRYQDEPVL-KGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkpldyskRGLLALRqqVATVFQDPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 458 EKL---DLElSALQFMIREYPGNEEEKMRGAIGKFGL--SGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNH 532
Cdd:PRK13638 88 QQIfytDID-SDIAFSLRNLGVPEAEITRRVDEALTLvdAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 533 LD-------IETIDSLAEALNEwdggLVLVSHDFRLINQVAQEIWV-CENQAVTKWEGDIMDFKAHLKMKAGLA 598
Cdd:PRK13638 167 LDpagrtqmIAIIRRIVAQGNH----VIISSHDIDLIYEISDAVYVlRQGQILTHGAPGEVFACTEAMEQAGLT 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
379-562 |
1.58e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.09 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 379 LPPPVLQFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHN-----------HL 447
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrkglmKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 448 R--IAQFHQHLAEKL-------DLELSALQFMIreyPGNE-EEKMRGAIGKFGLSgKAQVMPMKNLSDGQRSRVIFAWLA 517
Cdd:PRK13636 81 ResVGMVFQDPDNQLfsasvyqDVSFGAVNLKL---PEDEvRKRVDNALKRTGIE-HLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1955823976 518 WRQPHLLLLDEPTNHLD----IETIDSLAEALNEWDGGLVLVSHDFRLI 562
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIV 205
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
364-571 |
1.73e-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: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 364 VRDKVLVFRfvdvgKLPPPVLQFVEVTFGYTPenlIYKNLD-FGVDLDS-------RIALVGPNGAGKSTLLKLMTGDLV 435
Cdd:COG1245 320 IRDEPIEFE-----VHAPRREKEEETLVEYPD---LTKSYGgFSLEVEGgeiregeVLGIVGPNGIGKTTFAKILAGVLK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 436 PLDGMVrrhnhlriaqfhqhlaeKLDLELS-ALQFMIREYPGNEEEKMRGAIG-KFGLS-GKAQVM-----------PMK 501
Cdd:COG1245 392 PDEGEV-----------------DEDLKISyKPQYISPDYDGTVEEFLRSANTdDFGSSyYKTEIIkplgleklldkNVK 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 502 NLSDGQRSRV-IFAWLAwRQPHLLLLDEPTNHLDIE-------TIDSLAEalnEWDGGLVLVSHDFRLINQVAQEIWV 571
Cdd:COG1245 455 DLSGGELQRVaIAACLS-RDADLYLLDEPSAHLDVEqrlavakAIRRFAE---NRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
72-303 |
2.00e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.22 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 72 DIRIESLSVTFHGHDLIV--DSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPiPEHMDIYHLSREIEASDMSSLEAV 149
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVlkGLSLQIKAGEKVALLGRTGCGKSTLLQLL-TRAWD-PQQGEILLNGQPIADYSEAALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 150 IScdeerlklekeaesLASQddgggeqldRIY-------ERLE-ALDAATAEKrAAEILYGLGFNKQMQAKKT------- 214
Cdd:PRK11160 416 IS--------------VVSQ---------RVHlfsatlrDNLLlAAPNASDEA-LIEVLQQVGLEKLLEDDKGlnawlge 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 215 --RDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF--DRILVVVSHSqdfLNGVCT--NIIHMQN 288
Cdd:PRK11160 472 ggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHR---LTGLEQfdRICVMDN 548
|
250
....*....|....*
gi 1955823976 289 RKLkIYTGNYDQYVQ 303
Cdd:PRK11160 549 GQI-IEQGTHQELLA 562
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
380-558 |
2.19e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 59.34 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 380 PPPVLQFVEVTFGYTpENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV----RRHNHLRIAQ---- 451
Cdd:COG3842 2 AMPALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIlldgRDVTGLPPEKrnvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 452 --FhQHLAekLDLELSALQ---F--MIREYPGNE-EEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVifAwLAwR---- 519
Cdd:COG3842 81 mvF-QDYA--LFPHLTVAEnvaFglRMRGVPKAEiRARVAELLELVGLEGLADRYP-HQLSGGQQQRV--A-LA-Ralap 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1955823976 520 QPHLLLLDEPTNHLD----IETIDSLAEALNEWDGGLVLVSHD 558
Cdd:COG3842 153 EPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHD 195
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
414-566 |
2.61e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 58.17 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 414 ALVGPNGAGKSTLLKLMtGDLVP-------LDGM----------------VRRHNHLriaqfhqhlaekldlelsALQFM 470
Cdd:COG4604 31 ALIGPNGAGKSTLLSMI-SRLLPpdsgevlVDGLdvattpsrelakrlaiLRQENHI------------------NSRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 471 IRE------YP-------GNEEEKMRGAIGKFGLSgkaqvmPMKN-----LSDGQRSRVIFAW-LAwRQPHLLLLDEPTN 531
Cdd:COG4604 92 VRElvafgrFPyskgrltAEDREIIDEAIAYLDLE------DLADryldeLSGGQRQRAFIAMvLA-QDTDYVLLDEPLN 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 1955823976 532 HLDI----ETIDSLAEALNEWDGGLVLVSHDfrlINQVA 566
Cdd:COG4604 165 NLDMkhsvQMMKLLRRLADELGKTVVIVLHD---INFAS 200
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
64-271 |
2.61e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.54 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 64 LCSHPLSRDIRIESLSVTfHGHDLIVDS-ELELNYGRRYGLLGLNGCGKSTL---LAAigcreLPIPEHMDIYHLSREIE 139
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSGK-HQHQTVLNNvSLSLKSGETVALLGRSGCGKSTLarlLVG-----LESPSQGNVSWRGEPLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 140 ASDMSSLEAViscdeerlkleKEAESLASQDDGG--------GEQLDRIYERLEALDAATAEKRAAEILYGLGFNKQMQA 211
Cdd:PRK10419 78 KLNRAQRKAF-----------RRDIQMVFQDSISavnprktvREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 212 KKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDL----EACVWLEENLKKFDRILVVVSH 271
Cdd:PRK10419 147 KRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITH 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
381-558 |
2.80e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.15 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 381 PPVLQFVEVTFGytpENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNH-LRIAQfhqhlaek 459
Cdd:PRK11247 12 PLLLNAVSKRYG---ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTApLAEAR-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 460 ldlELSALQFM-IREYP-------------GNEEEKMRGAIGKFGLSGKAQVMPMKnLSDGQRSRVIFAWLAWRQPHLLL 525
Cdd:PRK11247 81 ---EDTRLMFQdARLLPwkkvidnvglglkGQWRDAALQALAAVGLADRANEWPAA-LSGGQKQRVALARALIHRPGLLL 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 1955823976 526 LDEPTNHLD----IEtIDSLAEALNEWDGGLV-LVSHD 558
Cdd:PRK11247 157 LDEPLGALDaltrIE-MQDLIESLWQQHGFTVlLVTHD 193
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
73-273 |
3.58e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 58.81 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRElpIPEHMDIYhlsreIEASDMSSLEAvisc 152
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFE--TPDSGRIM-----LDGQDITHVPA---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 dEER------------------------LKLEKEAEslasqddgggeqlDRIYER-LEALDAATAEKRAAeilyglgfnk 207
Cdd:PRK09452 84 -ENRhvntvfqsyalfphmtvfenvafgLRMQKTPA-------------AEITPRvMEALRMVQLEEFAQ---------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 208 qmqaKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRIL----VVVSHSQ 273
Cdd:PRK09452 140 ----RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQ 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
66-571 |
3.64e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.33 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 66 SHPLsrdIRIESLSVTF----HGHDLIVDSELELNYGRRYGLLGLNGCGKS-TLLAAIgcRELPIPEhmdIYHLSREIEA 140
Cdd:PRK15134 2 TQPL---LAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSPP---VVYPSGDIRF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 141 SDMSSLEAviscDEERLKLEKeaeslasqddggGEQLDRIY-ERLEALDAA-TAEKRAAEILyglGFNKQMQ-------- 210
Cdd:PRK15134 74 HGESLLHA----SEQTLRGVR------------GNKIAMIFqEPMVSLNPLhTLEKQLYEVL---SLHRGMRreaargei 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 211 ------------AKKTRDF----SGGWRMRIALARALFMNPTVLLLDEPTNHLDL----EACVWLEENLKKFDRILVVVS 270
Cdd:PRK15134 135 lncldrvgirqaAKRLTDYphqlSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaQILQLLRELQQELNMGLLFIT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 271 HSQDFLNGVCTNIIHMQNRKLkiytgnydqyvqtrseLEENQmkmykweqdqiasmkeyiarfghGSAKLARQAQSKEKT 350
Cdd:PRK15134 215 HNLSIVRKLADRVAVMQNGRC----------------VEQNR-----------------------AATLFSAPTHPYTQK 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 351 LAKMERGGLTEKVVRDKVLVFRFVDVGKLPPPVLQFVEVTFGYtpeNLIYKNLDFGVDLDSRIALVGPNGAGKST----L 426
Cdd:PRK15134 256 LLNSEPSGDPVPLPEPASPLLDVEQLQVAFPIRKGILKRTVDH---NVVVKNISFTLRPGETLGLVGESGSGKSTtglaL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 427 LKLMTG------DLVPLDGMVRRHN---HLRIAQFHQHLAEKLDLELSALQfMIRE-----YP----GNEEEKMRGAIGK 488
Cdd:PRK15134 333 LRLINSqgeiwfDGQPLHNLNRRQLlpvRHRIQVVFQDPNSSLNPRLNVLQ-IIEEglrvhQPtlsaAQREQQVIAVMEE 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 489 FGLSGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIET---IDSLAEALNEWDG-GLVLVSHDFRLINQ 564
Cdd:PRK15134 412 VGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVqaqILALLKSLQQKHQlAYLFISHDLHVVRA 491
|
....*..
gi 1955823976 565 VAQEIWV 571
Cdd:PRK15134 492 LCHQVIV 498
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
72-249 |
4.88e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 57.33 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 72 DIRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELpIPEHMDIYHLSREIEASDMSSLEAVIS 151
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCF-ARLL-TPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 152 CDEERLkLEKEAESLASQDDGGGEQLDRIYERLEALDAATAEkRAAEILYGLgfnkQMQAKKTRDFSGGWRMRIALARAL 231
Cdd:PRK11231 80 LLPQHH-LTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVN-QAMEQTRIN----HLADRRLTDLSGGQRQRAFLAMVL 153
|
170
....*....|....*...
gi 1955823976 232 FMNPTVLLLDEPTNHLDL 249
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDI 171
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
74-248 |
4.90e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 56.72 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 74 RIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIgcrelpipehmdIYHLSREIEAS--------DMSS 145
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAI------------AGTLSPAFSASgevllngrRLTA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 146 LEAviscdeerlklEKEAESLASQDD--------------------GGGEQLDRIYERLEALDAAT-AEKRAAEIlyglg 204
Cdd:COG4136 71 LPA-----------EQRRIGILFQDDllfphlsvgenlafalpptiGRAQRRARVEQALEEAGLAGfADRDPATL----- 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1955823976 205 fnkqmqakktrdfSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:COG4136 135 -------------SGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
217-271 |
5.08e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 59.02 E-value: 5.08e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1955823976 217 FSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF--DRILVVVSH 271
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLmkGRTTIVIAH 533
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
77-248 |
5.25e-09 |
|
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: 57.06 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 77 SLSVTFHGHDL-IVDS-ELELNYGRRYGLLGLNGCGKSTLLAAI-GcreLPIPEHMDIYHLSREIEASD----------- 142
Cdd:COG4181 15 TKTVGTGAGELtILKGiSLEVEAGESVAIVGASGSGKSTLLGLLaG---LDRPTSGTVRLAGQDLFALDedararlrarh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 143 -------------MSSLEAVIscdeerLKLEkeaesLASQDDgggeqldriyerlealdaatAEKRAAEIL--YGLG--- 204
Cdd:COG4181 92 vgfvfqsfqllptLTALENVM------LPLE-----LAGRRD--------------------ARARARALLerVGLGhrl 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1955823976 205 --FNKQMqakktrdfSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:COG4181 141 dhYPAQL--------SGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
415-570 |
6.03e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.86 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 415 LVGPNGAGKSTLLKLMTGDL-----VPLDGM-VRRHNHLRIAQFHQHLAEK------------LDLELSAlqfmireypG 476
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLLpgsgsIQFAGQpLEAWSAAELARHRAYLSQQqtppfampvfqyLTLHQPD---------K 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 477 NEEEKMRGAI----GKFGLSGKAQvMPMKNLSDG--QRSRVIFAWL-AWRQ--PH--LLLLDEPTNHLDI---ETIDSLA 542
Cdd:PRK03695 98 TRTEAVASALnevaEALGLDDKLG-RSVNQLSGGewQRVRLAAVVLqVWPDinPAgqLLLLDEPMNSLDVaqqAALDRLL 176
|
170 180
....*....|....*....|....*...
gi 1955823976 543 EALNEWDGGLVLVSHDFRLINQVAQEIW 570
Cdd:PRK03695 177 SELCQQGIAVVMSSHDLNHTLRHADRVW 204
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
405-566 |
6.06e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.45 E-value: 6.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 405 FGVDLD----SRIALVGPNGAGKSTLLKLMTGDLVPLDGMV-------------------RRHNHLrIAQF--HQHLAEK 459
Cdd:PRK13649 24 FDVNLTiedgSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtlitstsknkdikqiRKKVGL-VFQFpeSQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 460 LdleLSALQFMIREYPGNEEEKMRGAIGKFGLSGKAQVMPMKN---LSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDI- 535
Cdd:PRK13649 103 V---LKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPk 179
|
170 180 190
....*....|....*....|....*....|...
gi 1955823976 536 --ETIDSLAEALNEWDGGLVLVSHdfrLINQVA 566
Cdd:PRK13649 180 grKELMTLFKKLHQSGMTIVLVTH---LMDDVA 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
73-274 |
6.28e-09 |
|
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: 56.96 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSeLELNYGRRYGLLGLNGCGKSTLLAAI-GCRElpiPEHMDIYhlsreIEASDMSSLeavis 151
Cdd:cd03299 1 LKVENLSKDWKEFKLKNVS-LEVERGDYFVILGPTGSGKSVLLETIaGFIK---PDSGKIL-----LNGKDITNL----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 152 cdeerlKLEKEAESLASQDDGGGEQLDrIYE------RLEALDAATAEKRAAEILYGLGFNKQMQAKKTRdFSGGWRMRI 225
Cdd:cd03299 67 ------PPEKRDISYVPQNYALFPHMT-VYKniayglKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-LSGGEQQRV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 226 ALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRILVV----VSHSQD 274
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVtvlhVTHDFE 191
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
73-248 |
6.37e-09 |
|
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: 55.78 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIV--DSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPiPEHMDIYhlsreIEASDMSSLEAVI 150
Cdd:cd03247 1 LSINNVSFSYPEQEQQVlkNLSLELKQGEKIALLGRSGSGKSTLLQLL-TGDLK-PQQGEIT-----LDGVPVSDLEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 151 ScdeerlklekEAESLASQddgggeqldRIYerleaLDAATaekraaeILYGLGfnkqmqakktRDFSGGWRMRIALARA 230
Cdd:cd03247 74 S----------SLISVLNQ---------RPY-----LFDTT-------LRNNLG----------RRFSGGERQRLALARI 112
|
170
....*....|....*...
gi 1955823976 231 LFMNPTVLLLDEPTNHLD 248
Cdd:cd03247 113 LLQDAPIVLLDEPTVGLD 130
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
386-579 |
6.85e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 57.34 E-value: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 386 FVEVTFGY---TP-ENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNH-------------LR 448
Cdd:PRK13634 5 FQKVEHRYqykTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitagkknkklkpLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 449 -----IAQF--HQHLAEKL--DLELSALQFMIREypGNEEEKMRGAIGKFGLSGKAQVMPMKNLSDGQRSRVIFAWLAWR 519
Cdd:PRK13634 85 kkvgiVFQFpeHQLFEETVekDICFGPMNFGVSE--EDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 520 QPHLLLLDEPTNHLD----IETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWVCENQAVTK 579
Cdd:PRK13634 163 EPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
73-248 |
7.05e-09 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 57.02 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFH--GHDLIV--DSELELNYGRRYGLLGLNGCGKSTLLAAI-GcreLPIPEHMDIYHLSREIEASD----- 142
Cdd:COG1116 8 LELRGVSKRFPtgGGGVTAldDVSLTVAAGEFVALVGPSGCGKSTLLRLIaG---LEKPTSGEVLVDGKPVTGPGpdrgv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 143 ----------MSSLEAViscdeeRLKLEkeaeslasqddgggeqldriyerLEALDAATAEKRAAEIL--YGL-GFnkqm 209
Cdd:COG1116 85 vfqepallpwLTVLDNV------ALGLE-----------------------LRGVPKAERRERARELLelVGLaGF---- 131
|
170 180 190
....*....|....*....|....*....|....*....
gi 1955823976 210 QAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:COG1116 132 EDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALD 170
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
378-430 |
7.84e-09 |
|
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: 58.29 E-value: 7.84e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 378 KLPPPVLQFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLM 430
Cdd:COG5265 352 VVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLL 404
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
383-583 |
9.55e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 56.67 E-value: 9.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 383 VLQFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIAQFHQHLAEK--- 459
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKvgl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 460 ----------------------LDLELSALQFMIReypgnEEEKMRgAIGKFGLSGKaqvmPMKNLSDGQRSRVIFAWLA 517
Cdd:PRK13647 84 vfqdpddqvfsstvwddvafgpVNMGLDKDEVERR-----VEEALK-AVRMWDFRDK----PPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955823976 518 WRQPHLLLLDEPTNHLDIETIDSLAEALNEW--DGGLVLVS-HDFRLINQVAQEIWVCeNQAVTKWEGD 583
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLhnQGKTVIVAtHDVDLAAEWADQVIVL-KEGRVLAEGD 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
73-249 |
9.90e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 56.66 E-value: 9.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPiPEHMDIYHLSREIEA---SDMSSLEAV 149
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLL-TGELT-PSSGEVRLNGRPLAAwspWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 150 IScdeerlklekEAESLA--------------SQDDGGGEQLDRIYERLEALDAATAEKRaaeiLYglgfnkqmqakktR 215
Cdd:COG4559 80 LP----------QHSSLAfpftveevvalgraPHGSSAAQDRQIVREALALVGLAHLAGR----SY-------------Q 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1955823976 216 DFSGGWRMRIALARAL-------FMNPTVLLLDEPTNHLDL 249
Cdd:COG4559 133 TLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDL 173
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
375-534 |
9.93e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.12 E-value: 9.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 375 DVGKLPPPVLQFVEVTFGytpENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR----------RH 444
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsraRH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 445 NHLRIAQFHQHlaEKLDLElsalqFMIRE-------YPGNEEEKMRGAIGKF----GLSGKAQVmPMKNLSDGQRSRVIF 513
Cdd:PRK13537 78 ARQRVGVVPQF--DNLDPD-----FTVREnllvfgrYFGLSAAAARALVPPLlefaKLENKADA-KVGELSGGMKRRLTL 149
|
170 180
....*....|....*....|.
gi 1955823976 514 AWLAWRQPHLLLLDEPTNHLD 534
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLD 170
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
81-248 |
1.20e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.04 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 81 TFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIPEHM-----DIYHlsREIEASD------------- 142
Cdd:PRK11432 15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgeDVTH--RSIQQRDicmvfqsyalfph 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 143 MSSLEAViscdeerlklekeAESLASQDDGGGEQLDRIYERLEALDAATAEKRaaeilyglgFNKQMqakktrdfSGGWR 222
Cdd:PRK11432 93 MSLGENV-------------GYGLKMLGVPKEERKQRVKEALELVDLAGFEDR---------YVDQI--------SGGQQ 142
|
170 180
....*....|....*....|....*.
gi 1955823976 223 MRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:PRK11432 143 QRVALARALILKPKVLLFDEPLSNLD 168
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
192-291 |
1.22e-08 |
|
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: 57.89 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 192 AEKRAAEILYGLGFN----KQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENL----KKFD 263
Cdd:TIGR03269 399 ARMKAVITLKMVGFDeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEME 478
|
90 100
....*....|....*....|....*...
gi 1955823976 264 RILVVVSHSQDFLNGVCTNIIHMQNRKL 291
Cdd:TIGR03269 479 QTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
397-569 |
1.47e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 397 NLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDL--------------VPLDGM-VRRHNHLRIAQFHQHLAEKLD 461
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgarvtgdVTLNGEpLAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 462 lelSALQFMIRE------YP-----GNEEEKMRGAIGK-FGLSGKAQVM--PMKNLSDGQRSRVIFA------W---LAW 518
Cdd:PRK13547 94 ---PAFAFSAREivllgrYPharraGALTHRDGEIAWQaLALAGATALVgrDVTTLSGGELARVQFArvlaqlWpphDAA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 519 RQPHLLLLDEPTNHLD-------IETIDSLAEalnEWDGGLVLVSHDFRLINQVAQEI 569
Cdd:PRK13547 171 QPPRYLLLDEPTAALDlahqhrlLDTVRRLAR---DWNLGVLAIVHDPNLAARHADRI 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
73-248 |
1.61e-08 |
|
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: 55.17 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIV----DSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPipehmdiyhlsreieasdmSSLEa 148
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaleDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERP-------------------TSGE- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 149 vISCDEERLKLEKEAESLASQDDGggeqL-------DRIYERLEA--LDAATAEKRAAEIL--YGL-GFNKqmqaKKTRD 216
Cdd:cd03293 61 -VLVDGEPVTGPGPDRGYVFQQDA----LlpwltvlDNVALGLELqgVPKAEARERAEELLelVGLsGFEN----AYPHQ 131
|
170 180 190
....*....|....*....|....*....|..
gi 1955823976 217 FSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:cd03293 132 LSGGMRQRVALARALAVDPDVLLLDEPFSALD 163
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
98-274 |
1.70e-08 |
|
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: 54.74 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 98 GRRYGLLGLNGCGKSTLLAAIGcrELPIPEHMDIYHLSREIEASDMSSLEA------VISCDEERLKLEKEAESLASQDD 171
Cdd:TIGR01166 18 GEVLALLGANGAGKSTLLLHLN--GLLRPQSGAVLIDGEPLDYSRKGLLERrqrvglVFQDPDDQLFAADVDQDVAFGPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 172 GGGEQLDRIYER----LEALDAATAEKRAaeilyglgfnkqmqakkTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHL 247
Cdd:TIGR01166 96 NLGLSEAEVERRvreaLTAVGASGLRERP-----------------THCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|...
gi 1955823976 248 DLEAcvwLEENLKKFDRI------LVVVSHSQD 274
Cdd:TIGR01166 159 DPAG---REQMLAILRRLraegmtVVISTHDVD 188
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
72-271 |
1.72e-08 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 55.31 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 72 DIRIESLSVTF-HGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIgCReLPIPEHMDIYHLSREIEASDMSSLEAVI 150
Cdd:cd03254 2 EIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLL-MR-FYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 151 ScdeerlklekeaesLASQDDG--GGEQLDRI-YERLEALD----AATAEKRAAEILYGL--GFNKQMqAKKTRDFSGGW 221
Cdd:cd03254 80 G--------------VVLQDTFlfSGTIMENIrLGRPNATDeeviEAAKEAGAHDFIMKLpnGYDTVL-GENGGNLSQGE 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1955823976 222 RMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF--DRILVVVSH 271
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAH 196
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
218-271 |
1.96e-08 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 55.24 E-value: 1.96e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF--DRILVVVSH 271
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAH 196
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
93-248 |
2.13e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 56.28 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 93 LELNYGRRYGLLGLNGCGKSTLLAAIGCRELP-----IPEHMDIYHLSREieasdmssleaviscdeERLKLEKEAE--- 164
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLGRLLLRLEEPtsgeiLFDGQDITGLSGR-----------------ELRPLRRRMQmvf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 165 --SLASqddgggeqLD---RIYERLEA-------LDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALF 232
Cdd:COG4608 102 qdPYAS--------LNprmTVGDIIAEplrihglASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALA 173
|
170
....*....|....*.
gi 1955823976 233 MNPTVLLLDEPTNHLD 248
Cdd:COG4608 174 LNPKLIVCDEPVSALD 189
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
403-569 |
2.18e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.95 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 403 LDfGVDLDSR----IALVGPNGAGKSTLLKLMTGDLVP------LDG-MVRRHN-----HLRIAQFHQHLAekLDLELSA 466
Cdd:COG1129 20 LD-GVSLELRpgevHALLGENGAGKSTLMKILSGVYQPdsgeilLDGePVRFRSprdaqAAGIAIIHQELN--LVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 467 LQ--FMIREYPGN-------EEEKMRGAIGKFGLSGKAQvMPMKNLSDGQR-----SRVIFawlawRQPHLLLLDEPT-- 530
Cdd:COG1129 97 AEniFLGREPRRGglidwraMRRRARELLARLGLDIDPD-TPVGDLSVAQQqlveiARALS-----RDARVLILDEPTas 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1955823976 531 ------NHLdIETIDSLAEalnewDG-GLVLVSHdfRL--INQVAQEI 569
Cdd:COG1129 171 lterevERL-FRIIRRLKA-----QGvAIIYISH--RLdeVFEIADRV 210
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
73-288 |
2.29e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.10 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRElpipehmdiyhlsrEIEASDMSsleavisC 152
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLE--------------EITSGDLI-------V 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 DEERLKLEKEAESLASQDDGGGEQLDRIYERLEALD-------------AATAEKRAAEILYGLGFNKQMQAKKTrDFSG 219
Cdd:PRK09493 61 DGLKVNDPKVDERLIRQEAGMVFQQFYLFPHLTALEnvmfgplrvrgasKEEAEKQARELLAKVGLAERAHHYPS-ELSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955823976 220 GWRMRIALARALFMNPTVLLLDEPTNHLDLEacvwLEENLKKFDRIL-------VVVSHSQDFLNGVCTNIIHMQN 288
Cdd:PRK09493 140 GQQQRVAIARALAVKPKLMLFDEPTSALDPE----LRHEVLKVMQDLaeegmtmVIVTHEIGFAEKVASRLIFIDK 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
382-567 |
2.33e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 55.79 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 382 PVLQFVEVTFGYtPENLIY--KNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRrhnhlriaQFHQHLAEK 459
Cdd:PRK13635 4 EIIRVEHISFRY-PDAATYalKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT--------VGGMVLSEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 460 LDLELSALQFMIREYPGN----------------------EE--EKMRGAIGKFGLSGKAQVMPMKnLSDGQRSRVIFAW 515
Cdd:PRK13635 75 TVWDVRRQVGMVFQNPDNqfvgatvqddvafglenigvprEEmvERVDQALRQVGMEDFLNREPHR-LSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 516 LAWRQPHLLLLDEPTNHLD-------IETIDSLAEalnewDGGLVLVS--HDfrlINQVAQ 567
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDprgrrevLETVRQLKE-----QKGITVLSitHD---LDEAAQ 206
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
376-534 |
2.41e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 55.99 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 376 VGKLPPPVLQFVEVTFGYTpENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR----------RHN 445
Cdd:PRK13536 34 PGSMSTVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 446 HLRIAQFHQHlaEKLDLElsalqFMIRE-------YPGNEEEKMRGAIG---KFG-LSGKAQVmPMKNLSDGQRSRVIFA 514
Cdd:PRK13536 113 RARIGVVPQF--DNLDLE-----FTVREnllvfgrYFGMSTREIEAVIPsllEFArLESKADA-RVSDLSGGMKRRLTLA 184
|
170 180
....*....|....*....|
gi 1955823976 515 WLAWRQPHLLLLDEPTNHLD 534
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLD 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
190-249 |
2.43e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.82 E-value: 2.43e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 190 ATAEKRAAEILYGLGFNKQMQAKKTrDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDL 249
Cdd:PRK11629 120 AEINSRALEMLAAVGLEHRANHRPS-ELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
188-291 |
2.75e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 54.67 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 188 DAATAEKRAAEIL--YGLGfnkqmqaKKTRDF----SGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACvwlEENLKK 261
Cdd:COG2884 110 SRKEIRRRVREVLdlVGLS-------DKAKALphelSGGEQQRVAIARALVNRPELLLADEPTGNLDPETS---WEIMEL 179
|
90 100 110
....*....|....*....|....*....|....*.
gi 1955823976 262 FDRI------LVVVSHSQDFLNGVCTNIIHMQNRKL 291
Cdd:COG2884 180 LEEInrrgttVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
78-286 |
2.93e-08 |
|
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: 54.61 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 78 LSVTFH----GHDLIVDSELElnyGRRYGLLGLNGCGKSTLLAAIGcrELPIPEHMDIYhlsreieasdmssLEAVISCD 153
Cdd:cd03297 2 LCVDIEkrlpDFTLKIDFDLN---EEVTGIFGASGAGKSTLLRCIA--GLEKPDGGTIV-------------LNGTVLFD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 154 EER---LKLEKEAESLASQDDGGGEQLDrIYERLE--ALDAATAEKR--AAEILYGLGFNkQMQAKKTRDFSGGWRMRIA 226
Cdd:cd03297 64 SRKkinLPPQQRKIGLVFQQYALFPHLN-VRENLAfgLKRKRNREDRisVDELLDLLGLD-HLLNRYPAQLSGGEKQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 227 LARALFMNPTVLLLDEPTNHLD----LEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHM 286
Cdd:cd03297 142 LARALAAQPELLLLDEPFSALDralrLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
401-534 |
3.14e-08 |
|
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: 54.18 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 401 KNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV----RRHNHLR-----IAQFHQHLAekLDLELSALQFM- 470
Cdd:cd03301 17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggRDVTDLPpkdrdIAMVFQNYA--LYPHMTVYDNIa 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955823976 471 ----IREYPGNE-EEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLD 534
Cdd:cd03301 95 fglkLRKVPKDEiDERVREVAELLQIEHLLDRKP-KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
73-249 |
3.82e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.78 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPiPEHMDIYHLSREIE---ASDMSSLEAV 149
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL-SGELS-PDSGEVRLNGRPLAdwsPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 150 ------ISCD---EERLKLEKEAESLASQDDGggeqldriyerlEALDAATAEKRAAEIlyglgfnkqmqakKTRDF--- 217
Cdd:PRK13548 81 lpqhssLSFPftvEEVVAMGRAPHGLSRAEDD------------ALVAAALAQVDLAHL-------------AGRDYpql 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 1955823976 218 SGGWRMRIALARAL------FMNPTVLLLDEPTNHLDL 249
Cdd:PRK13548 136 SGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDL 173
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
382-547 |
4.20e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 54.76 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 382 PVLQFVEVTFGY-TPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHlRIAQfhQHLAEkl 460
Cdd:PRK13648 6 SIIVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ-AITD--DNFEK-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 461 dlelsalqfmIREYPG----NEEEKMRGAIGK----FGLSGkaQVMPMKN------------------------LSDGQR 508
Cdd:PRK13648 81 ----------LRKHIGivfqNPDNQFVGSIVKydvaFGLEN--HAVPYDEmhrrvsealkqvdmleradyepnaLSGGQK 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 1955823976 509 SRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNE 547
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRK 187
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
75-305 |
4.22e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.12 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 75 IESLSVTFHGHDLIV----DSELELNYGRRYGLLGLNGCGKST-------LLAAIG---------CRE-LPIPEHmdiyH 133
Cdd:PRK09473 15 VKDLRVTFSTPDGDVtavnDLNFSLRAGETLGIVGESGSGKSQtafalmgLLAANGriggsatfnGREiLNLPEK----E 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 134 LSReIEASD--------MSSLEAVISCDE---ERLKLEKEAeslasqddGGGEQLDRIYERLEALDAATAEKRAAeiLYg 202
Cdd:PRK09473 91 LNK-LRAEQismifqdpMTSLNPYMRVGEqlmEVLMLHKGM--------SKAEAFEESVRMLDAVKMPEARKRMK--MY- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 203 lgfnkqmqakkTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDL----EACVWLEENLKKFDRILVVVSHSQDFLNG 278
Cdd:PRK09473 159 -----------PHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIMITHDLGVVAG 227
|
250 260
....*....|....*....|....*..
gi 1955823976 279 VCTNIIHMqnrklkiYTGNYDQYVQTR 305
Cdd:PRK09473 228 ICDKVLVM-------YAGRTMEYGNAR 247
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
401-574 |
4.78e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 56.01 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 401 KNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLvPLDGMVRRH----NHLRIAQFHQHLA------------------- 457
Cdd:PRK11174 367 GPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINgielRELDPESWRKHLSwvgqnpqlphgtlrdnvll 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 458 -------EKLD--LELS-ALQFMIREYPGNEEEKMRGAIGkfglsgkaqvmpmknLSDGQRSRVIFAWLAWRQPHLLLLD 527
Cdd:PRK11174 446 gnpdasdEQLQqaLENAwVSEFLPLLPQGLDTPIGDQAAG---------------LSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 528 EPTNHLDIETIDSLAEALNEWDGG--LVLVSHdfrLINQVAQ--EIWVCEN 574
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAASRRqtTLMVTH---QLEDLAQwdQIWVMQD 558
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
385-547 |
5.24e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 55.74 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 385 QFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLM------TGDLVPLDGM-VR-------RHNHLRIA 450
Cdd:PRK13657 336 EFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpQSGRILIDGTdIRtvtraslRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 451 Q----FHQHLAEKL--------DLEL-------SALQFMIReypgnEEEKMRGAIGKFGLSgkaqvmpmknLSDGQRSRV 511
Cdd:PRK13657 416 QdaglFNRSIEDNIrvgrpdatDEEMraaaeraQAHDFIER-----KPDGYDTVVGERGRQ----------LSGGERQRL 480
|
170 180 190
....*....|....*....|....*....|....*.
gi 1955823976 512 IFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNE 547
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDE 516
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
384-574 |
5.65e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.80 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGY-TPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMT-------GDLVpLDG---------------- 439
Cdd:PRK11176 342 IEFRNVTFTYpGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTrfydideGEIL-LDGhdlrdytlaslrnqva 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 440 MVRRHNHL-------RIAQFHQHLAEKLDLELSALQFMIREYPGNEEEKMRGAIGKFGLSgkaqvmpmknLSDGQRSRVI 512
Cdd:PRK11176 421 LVSQNVHLfndtianNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVL----------LSGGQRQRIA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 513 FAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEW--DGGLVLVSHDFRLINQvAQEIWVCEN 574
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTESERAIQAALDELqkNRTSLVIAHRLSTIEK-ADEILVVED 553
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
192-313 |
5.82e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 54.64 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 192 AEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLD----LEACVWLEENLKKFDRILV 267
Cdd:PRK13634 121 AKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTV 200
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1955823976 268 VVSHSQDFLNGVCTNIIHMQNRKLKIyTGNYDQYVQTRSELEENQM 313
Cdd:PRK13634 201 LVTHSMEDAARYADQIVVMHKGTVFL-QGTPREIFADPDELEAIGL 245
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
218-271 |
5.99e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.88 E-value: 5.99e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRILVVVSH 271
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
102-244 |
6.68e-08 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 53.59 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 102 GLLGLNGCGKSTLLAAI-------------GCRELP--------------IPEHMDIYHlsreieasDMSsleaViscdE 154
Cdd:cd03224 30 ALLGRNGAGKTTLLKTImgllpprsgsirfDGRDITglppheraragigyVPEGRRIFP--------ELT----V----E 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 155 ERLKLEkeaeSLASQDDGGGEQLDRIYERLEALdaataekraaeilyglgfnKQMQAKKTRDFSGGWRMRIALARALFMN 234
Cdd:cd03224 94 ENLLLG----AYARRRAKRKARLERVYELFPRL-------------------KERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170
....*....|
gi 1955823976 235 PTVLLLDEPT 244
Cdd:cd03224 151 PKLLLLDEPS 160
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
378-564 |
6.69e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 55.60 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 378 KLPPPVLQFVEVTFGYTPENL-IYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRhNHLRIAQFHQhl 456
Cdd:PRK11160 333 AADQVSLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL-NGQPIADYSE-- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 457 aekldlelSALQFMI--------------RE-----YPGNEEEKMRGAIGKFGLSGKAQVMPMKN---------LSDGQR 508
Cdd:PRK11160 410 --------AALRQAIsvvsqrvhlfsatlRDnlllaAPNASDEALIEVLQQVGLEKLLEDDKGLNawlgeggrqLSGGEQ 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 509 SRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEWDGG--LVLVSHDFRLINQ 564
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNktVLMITHRLTGLEQ 539
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
77-274 |
7.01e-08 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 54.73 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 77 SLSVTFHGHDLIVDSELELNygRRYGLLGLNGCGKSTLLAAIGCRELPIPEHMdiyHLSREIEASDMSSLEaviscdeer 156
Cdd:TIGR02142 4 RFSKRLGDFSLDADFTLPGQ--GVTAIFGRSGSGKTTLIRLIAGLTRPDEGEI---VLNGRTLFDSRKGIF--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 157 LKLEKEAESLASQDD------GGGEQLDRIYERLEALDAATAEKRAAEILyGLGfnkQMQAKKTRDFSGGWRMRIALARA 230
Cdd:TIGR02142 70 LPPEKRRIGYVFQEArlfphlSVRGNLRYGMKRARPSERRISFERVIELL-GIG---HLLGRLPGRLSGGEKQRVAIGRA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1955823976 231 LFMNPTVLLLDEPTNHLDL----EACVWLEENLKKFDRILVVVSHSQD 274
Cdd:TIGR02142 146 LLSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQ 193
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
401-557 |
7.53e-08 |
|
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: 53.14 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 401 KNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVP------LDGMVRRHNHLRIAQ---FHQHlAEKLDLELSA---LQ 468
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPdagfatVDGFDVVKEPAEARRrlgFVSD-STGLYDRLTArenLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 469 FMIREYpGNEEEKMRGAIGKFglsgkAQVMPMKNL--------SDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDS 540
Cdd:cd03266 101 YFAGLY-GLKGDELTARLEEL-----ADRLGMEELldrrvggfSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRA 174
|
170 180
....*....|....*....|
gi 1955823976 541 LAEALNEW-DGG--LVLVSH 557
Cdd:cd03266 175 LREFIRQLrALGkcILFSTH 194
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
103-291 |
8.39e-08 |
|
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: 53.18 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 103 LLGLNGCGKSTLLAAIGCRELPIpehmdiyhlSREIEASDmsslEAVISCDEERLKLEKEAESLASQDDgggeQL--DR- 179
Cdd:cd03292 32 LVGPSGAGKSTLLKLIYKEELPT---------SGTIRVNG----QDVSDLRGRAIPYLRRKIGVVFQDF----RLlpDRn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 180 IYER----LEALDAATAE--KRAAEILYGLGFnkqmqAKKTRDF----SGGWRMRIALARALFMNPTVLLLDEPTNHLDL 249
Cdd:cd03292 95 VYENvafaLEVTGVPPREirKRVPAALELVGL-----SHKHRALpaelSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1955823976 250 EACVWLEENLKKFDR---ILVVVSHSQDFLNGVCTNIIHMQNRKL 291
Cdd:cd03292 170 DTTWEIMNLLKKINKagtTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
73-272 |
8.67e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.69 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGcRELPIPEhmdiyhlSREIEASDMSSLEAVISC 152
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFN-RLLELNE-------EARVEGEVRLFGRNIYSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 DEERLKLEKEA----------ESLASQDDGG-GEQLDRIYERLEALDAAT--AEKRAA---EIlyglgfnKQMQAKKTRD 216
Cdd:PRK14267 77 DVDPIEVRREVgmvfqypnpfPHLTIYDNVAiGVKLNGLVKSKKELDERVewALKKAAlwdEV-------KDRLNDYPSN 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1955823976 217 FSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEE---NLKKfDRILVVVSHS 272
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEEllfELKK-EYTIVLVTHS 207
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
174-290 |
9.28e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.90 E-value: 9.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 174 GEQLDRIYERLealdaataeKRAAEILyGLGFNKqMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEAcv 253
Cdd:PRK13637 113 GLSEEEIENRV---------KRAMNIV-GLDYED-YKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG-- 179
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1955823976 254 wLEENL-------KKFDRILVVVSHSQDFLNGVCTNIIHMQNRK 290
Cdd:PRK13637 180 -RDEILnkikelhKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
378-534 |
9.52e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 53.84 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 378 KLPPPVLQFVEVTFGYTP-ENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVrrhnhlriaqfhqhl 456
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI--------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 457 aeKLD-LELSALQF-MIREYPG----NEEEKMRGAIGK----FGLSGK--------------AQVMPMK--------NLS 504
Cdd:PRK13632 67 --KIDgITISKENLkEIRKKIGiifqNPDNQFIGATVEddiaFGLENKkvppkkmkdiiddlAKKVGMEdyldkepqNLS 144
|
170 180 190
....*....|....*....|....*....|
gi 1955823976 505 DGQRSRVIFAWLAWRQPHLLLLDEPTNHLD 534
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
384-537 |
9.98e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 55.30 E-value: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYTPenlIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIA-QFHQHLAEKL-D 461
Cdd:TIGR01271 429 LFFSNFSLYVTP---VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSpQTSWIMPGTIkD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 462 LELSALQFmireypgnEEEKMRGAIGKFGLSGKAQVMPMKN----------LSDGQRSRVIFAWLAWRQPHLLLLDEPTN 531
Cdd:TIGR01271 506 NIIFGLSY--------DEYRYTSVIKACQLEEDIALFPEKDktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
....*.
gi 1955823976 532 HLDIET 537
Cdd:TIGR01271 578 HLDVVT 583
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
399-565 |
1.01e-07 |
|
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: 52.53 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 399 IYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTG--DLVPLDGmvrrhnhlRIAQFHQHLAEkLDLELSALQ--FMIREY 474
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEG--------EILFKGEDITD-LPPEERARLgiFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 475 PgneeEKMRG-AIGKF------GLSGkaqvmpmknlsdGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNE 547
Cdd:cd03217 86 P----PEIPGvKNADFlryvneGFSG------------GEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINK 149
|
170 180
....*....|....*....|.
gi 1955823976 548 W---DGGLVLVSHDFRLINQV 565
Cdd:cd03217 150 LreeGKSVLIITHYQRLLDYI 170
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
73-271 |
1.15e-07 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 53.00 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIV--DSELELNYGRRYGLLGLNGCGKSTLLAAIgcrelpiPEHMDIY--------HLSREIEASD 142
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlrDISLDIPAGETVALVGPSGSGKSTLVNLI-------PRFYDVDsgrilidgHDVRDYTLAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 143 MSSLEAVISCDEeRLKLEKEAESLAsqddgggeqldriYERLEALDAATaeKRAAEILYGLGFNKQM-QAKKTR------ 215
Cdd:cd03251 74 LRRQIGLVSQDV-FLFNDTVAENIA-------------YGRPGATREEV--EEAARAANAHEFIMELpEGYDTVigergv 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 216 DFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF--DRILVVVSH 271
Cdd:cd03251 138 KLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAH 195
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
384-537 |
1.15e-07 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 52.87 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYTP-ENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNH---------LRiAQFH 453
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaladpawLR-RQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 454 QHLAEKLDLELSALQFMIREYPGNEEEKMRGAIGKFGLSGKAQVMPM----------KNLSDGQRSRVIFAWLAWRQPHL 523
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgAGLSGGQRQRIAIARALIHNPRI 159
|
170
....*....|....
gi 1955823976 524 LLLDEPTNHLDIET 537
Cdd:cd03252 160 LIFDEATSALDYES 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
73-274 |
1.23e-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: 53.07 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDS-ELELNYGRRYGLLGLNGCGKSTLLAAIGcrELPIPEHMDIYhlsreIEASDMSSLEAVis 151
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNlNLEIAKGEFLVLIGPSGSGKTTTMKMIN--RLIEPTSGEIF-----IDGEDIREQDPV-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 152 cdEERLKLekeaeSLASQDDG-----GGEQLDRIYERLEALDAATAEKRAAEILYGLGFN-KQMQAKKTRDFSGGWRMRI 225
Cdd:cd03295 72 --ELRRKI-----GYVIQQIGlfphmTVEENIALVPKLLKWPKEKIRERADELLALVGLDpAEFADRYPHELSGGQQQRV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 226 ALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRIL----VVVSHSQD 274
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgktiVFVTHDID 197
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
406-558 |
1.47e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 53.54 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 406 GVDLD----SRIALVGPNGAGKSTLLKLMTGDLVPLDGMV----RRHNHL-----RIAQFHQ------HL--AEKLdleL 464
Cdd:COG3839 21 DIDLDiedgEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIliggRDVTDLppkdrNIAMVFQsyalypHMtvYENI---A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 465 SALQfmIREYPGNE-EEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVifAwLAW---RQPHLLLLDEPTNHLD----IE 536
Cdd:COG3839 98 FPLK--LRKVPKAEiDRRVREAAELLGLEDLLDRKP-KQLSGGQRQRV--A-LGRalvREPKVFLLDEPLSNLDaklrVE 171
|
170 180
....*....|....*....|..
gi 1955823976 537 TIDSLAEALNEWDGGLVLVSHD 558
Cdd:COG3839 172 MRAEIKRLHRRLGTTTIYVTHD 193
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
413-571 |
1.85e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.90 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 413 IALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIAQFHQHLAEKLD-LELSALQFMIREYPGNEEEKMRGAIGKFGL 491
Cdd:PRK13546 53 IGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTgIENIEFKMLCMGFKRKEIKAMTPKIIEFSE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 492 SGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDI----ETIDSLAEaLNEWDGGLVLVSHDFRLINQVAQ 567
Cdd:PRK13546 133 LGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQtfaqKCLDKIYE-FKEQNKTIFFVSHNLGQVRQFCT 211
|
....*
gi 1955823976 568 EI-WV 571
Cdd:PRK13546 212 KIaWI 216
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
72-251 |
1.90e-07 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 53.95 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 72 DIRIESLSVTFHGHDL-IVDS-ELELNYGRRYGLLGLNGCGKSTLLAAIgcRELPIPEHMDIYHLSREIEASDMSSLEAV 149
Cdd:TIGR02203 330 DVEFRNVTFRYPGRDRpALDSiSLVIEPGETVALVGRSGSGKSTLVNLI--PRFYEPDSGQILLDGHDLADYTLASLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 150 ISCDEERLKL--EKEAESLASqddGGGEQLDRIyERLEALDAATAEkraaEILYGL--GFNKQMQAKKTRdFSGGWRMRI 225
Cdd:TIGR02203 408 VALVSQDVVLfnDTIANNIAY---GRTEQADRA-EIERALAAAYAQ----DFVDKLplGLDTPIGENGVL-LSGGQRQRL 478
|
170 180
....*....|....*....|....*.
gi 1955823976 226 ALARALFMNPTVLLLDEPTNHLDLEA 251
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNES 504
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
90-248 |
2.56e-07 |
|
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: 52.08 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 90 DSELELNYGRRYGLLGLNGCGKSTLLAAIGcrELPIPEHMDIYHLSREIEASDMSSLeaVISCDEERLKLEKEAESLASQ 169
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLIS--GLAQPTSGGVILEGKQITEPGPDRM--VVFQNYSLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955823976 170 DDGGGEQLDRiYERLEALDAATAekraaeiLYGLGfnkQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:TIGR01184 79 VDRVLPDLSK-SERRAIVEEHIA-------LVGLT---EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
74-271 |
2.83e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 74 RIESLSVTFHgHDLIVDSEL--ELNY----GRRYGLLGLNGCGKSTLLAAIgcRELPIPEHMDIY----HLSREIEASDM 143
Cdd:PTZ00265 382 KIQFKNVRFH-YDTRKDVEIykDLNFtlteGKTYAFVGESGCGKSTILKLI--ERLYDPTEGDIIindsHNLKDINLKWW 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 144 SSLEAVISCDE---------------------ERLKLEKEAESLASQDDGGGE------------------------QLD 178
Cdd:PTZ00265 459 RSKIGVVSQDPllfsnsiknnikyslyslkdlEALSNYYNEDGNDSQENKNKRnscrakcagdlndmsnttdsneliEMR 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 179 RIYERLEALDAATAEKRAA------------EILYGLGFNKqmqakktrdFSGGWRMRIALARALFMNPTVLLLDEPTNH 246
Cdd:PTZ00265 539 KNYQTIKDSEVVDVSKKVLihdfvsalpdkyETLVGSNASK---------LSGGQKQRISIARAIIRNPKILILDEATSS 609
|
250 260
....*....|....*....|....*....
gi 1955823976 247 LDLEACVWLEE---NLK-KFDRILVVVSH 271
Cdd:PTZ00265 610 LDNKSEYLVQKtinNLKgNENRITIIIAH 638
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
192-314 |
3.21e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.40 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 192 AEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACV-WLE--ENLKKFDRILVV 268
Cdd:PRK13651 141 AKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKeILEifDNLNKQGKTIIL 220
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1955823976 269 VSHSQDflngvctNIIHMQNRKLK------IYTGNYDQYVQTRSELEENQMK 314
Cdd:PRK13651 221 VTHDLD-------NVLEWTKRTIFfkdgkiIKDGDTYDILSDNKFLIENNME 265
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
383-534 |
3.22e-07 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 51.50 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 383 VLQFVEVTFGYTPEN---LIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGdLVPLDGMVR-----RHNHLRIAQFHQ 454
Cdd:cd03234 3 VLPWWDVGLKAKNWNkyaRILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGTTSgqilfNGQPRKPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 455 HLA--EKLDLELSAL----------QFMIREYPGNEEEKMRGAIGKFGLSGKAQV--MPMKNLSDGQRSRV-IFAWLAWr 519
Cdd:cd03234 82 CVAyvRQDDILLPGLtvretltytaILRLPRKSSDAIRKKRVEDVLLRDLALTRIggNLVKGISGGERRRVsIAVQLLW- 160
|
170
....*....|....*
gi 1955823976 520 QPHLLLLDEPTNHLD 534
Cdd:cd03234 161 DPKVLILDEPTSGLD 175
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
73-248 |
3.29e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 52.01 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGcrELPIPEHMDIYHLSREIEASdmSSLEAVISC 152
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIA--GFVPYQHGSITLDGKPVEGP--GAERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 DEERLK----LEKEAESLASQDDGGGEQLDRIYERLEALDAATAEKRaaeilyglgFNKQMqakktrdfSGGWRMRIALA 228
Cdd:PRK11248 78 NEGLLPwrnvQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKR---------YIWQL--------SGGQRQRVGIA 140
|
170 180
....*....|....*....|
gi 1955823976 229 RALFMNPTVLLLDEPTNHLD 248
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALD 160
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
384-567 |
3.64e-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: 50.93 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGYTPE----NLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNhlRIA--------- 450
Cdd:cd03250 1 ISVEDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAyvsqepwiq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 451 --------QFHQHL-AEKLD--LELSALQFMIREYP-GNEEEkmrgaIGKFGLsgkaqvmpmkNLSDGQRSRVIFAWLAW 518
Cdd:cd03250 79 ngtireniLFGKPFdEERYEkvIKACALEPDLEILPdGDLTE-----IGEKGI----------NLSGGQKQRISLARAVY 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 519 RQPHLLLLDEPTNHLDIETIDSLAEA--LNEWDGG--LVLVSHDFRLINQVAQ 567
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNktRILVTHQLQLLPHADQ 196
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
75-248 |
3.76e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.60 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 75 IESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIpehmdiyhlSREIEASDMSSLEAViscDE 154
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPS---------AGELLAGTAPLAEAR---ED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 155 ERLKLEkEAESLASQ---DDGG-GEQLDRIYERLEALDAATAEKRAAEILYGLgfnkqmqakktrdfSGGWRMRIALARA 230
Cdd:PRK11247 83 TRLMFQ-DARLLPWKkviDNVGlGLKGQWRDAALQALAAVGLADRANEWPAAL--------------SGGQKQRVALARA 147
|
170
....*....|....*...
gi 1955823976 231 LFMNPTVLLLDEPTNHLD 248
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALD 165
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
195-271 |
3.85e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 53.10 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 195 RAAEILYGLGFNKQMqaKKTRD---------FSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEA----CVWLEEnLKK 261
Cdd:PRK11176 452 EAARMAYAMDFINKM--DNGLDtvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESeraiQAALDE-LQK 528
|
90
....*....|
gi 1955823976 262 fDRILVVVSH 271
Cdd:PRK11176 529 -NRTSLVIAH 537
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
73-293 |
4.06e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 51.91 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTF-HGHDLIVDSELELNYGRRYGLLGLNGCGKSTLlaAIGCRELPIPEHMDIyhLSREIEASDMSSLEA--- 148
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTL--ALHLNGLLRPQKGKV--LVSGIDTGDFSKLQGirk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 149 ----VISCDEERLKLEKEAESLASqddgGGEQLdriyerleALDAATAEKRAAEILYGLGFNKqMQAKKTRDFSGGWRMR 224
Cdd:PRK13644 78 lvgiVFQNPETQFVGRTVEEDLAF----GPENL--------CLPPIEIRKRVDRALAEIGLEK-YRHRSPKTLSGGQGQC 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955823976 225 IALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDR---ILVVVSHSQDFLNgVCTNIIHMQNRKLKI 293
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkgkTIVYITHNLEELH-DADRIIVMDRGKIVL 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
414-557 |
4.17e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 414 ALVGPNGAGKSTLLKLMTGDLVP------LDGMVRRHNHLR------IAQFHQHL--------AEKLDL-ELSALQFMIR 472
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPdagsilIDGQEMRFASTTaalaagVAIIYQELhlvpemtvAENLYLgQLPHKGGIVN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 473 EYPGNEEekMRGAIGKFGLSGKAQvMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEW--DG 550
Cdd:PRK11288 114 RRLLNYE--AREQLEHLGVDIDPD-TPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELraEG 190
|
....*...
gi 1955823976 551 GLVL-VSH 557
Cdd:PRK11288 191 RVILyVSH 198
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
73-248 |
4.48e-07 |
|
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: 49.73 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLlaaigcrelpipehmdiyhlsreieasdMSSLEAVISC 152
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTL----------------------------MKILSGLYKP 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 DEERLKLEKEAESLASqddgggeqldriyeRLEALDAataekraaeilyGLGFNKQMqakktrdfSGGWRMRIALARALF 232
Cdd:cd03216 53 DSGEILVDGKEVSFAS--------------PRDARRA------------GIAMVYQL--------SVGERQMVEIARALA 98
|
170
....*....|....*.
gi 1955823976 233 MNPTVLLLDEPTNHLD 248
Cdd:cd03216 99 RNARLLILDEPTAALT 114
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
73-272 |
4.53e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 51.58 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGcrelPIPEHMDIYHLSREIEASDMSSLEAVISC 152
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN----RMNELESEVRVEGRVEFFNQNIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 DEERLKL-----EKEAESLASQDD-GGGEQLDRIYERLEALDAATAEKRAAEILYGLgfnKQMQAKKTRDFSGGWRMRIA 226
Cdd:PRK14258 84 NRLRRQVsmvhpKPNLFPMSVYDNvAYGVKIVGWRPKLEIDDIVESALKDADLWDEI---KHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1955823976 227 LARALFMNPTVLLLDEPTNHLDLEACVWLE---ENLK-KFDRILVVVSHS 272
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVEsliQSLRlRSELTMVIVSHN 210
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
105-271 |
4.54e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 50.78 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 105 GLNGCGKSTLLAAI-----GCRELPIPEHMDIYHlsreiEASDMSSLEAVISCDEERLKLEK---EAESLASQDDG---- 172
Cdd:COG0419 30 GPNGAGKSTILEAIryalyGKARSRSKLRSDLIN-----VGSEEASVELEFEHGGKRYRIERrqgEFAEFLEAKPSerke 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 173 ------GGEQLDRIYERL----EALDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALfmnptVLLLDe 242
Cdd:COG0419 105 alkrllGLEIYEELKERLkeleEALESALEELAELQKLKQEILAQLSGLDPIETLSGGERLRLALADLL-----SLILD- 178
|
170 180
....*....|....*....|....*....
gi 1955823976 243 pTNHLDLEACVWLEENLKKfdriLVVVSH 271
Cdd:COG0419 179 -FGSLDEERLERLLDALEE----LAIITH 202
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
217-271 |
4.58e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 51.45 E-value: 4.58e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 217 FSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEE---NLKKfDRILVVVSH 271
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESlflELKK-DMTIVLVTH 203
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
413-534 |
4.75e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 52.74 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 413 IALVGPNGAGKSTLL-----KLMTGDL----VPLDGMVRRHNHLR-IAQFHQ-------HLAEKLDLELSALQFMIREYP 475
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMnalafRSPKGVKgsgsVLLNGMPIDAKEMRaISAYVQqddlfipTLTVREHLMFQAHLRMPRRVT 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955823976 476 GNEE-EKMRGAIGKFGLSGKAQVM-----PMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLD 534
Cdd:TIGR00955 134 KKEKrERVDEVLQALGLRKCANTRigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
93-244 |
4.76e-07 |
|
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: 51.14 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 93 LELNYGRRYGLLGLNGCGKSTLLAAIgCRELPI----------------------------PEHMDIYhlsreieaSDMS 144
Cdd:COG0410 24 LEVEEGEIVALLGRNGAGKTTLLKAI-SGLLPPrsgsirfdgeditglpphriarlgigyvPEGRRIF--------PSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 145 sleaViscdEERLKLekeAESLASQDDGGGEQLDRIYERLEALdaataekraaeilyglgfnKQMQAKKTRDFSGGWRMR 224
Cdd:COG0410 95 ----V----EENLLL---GAYARRDRAEVRADLERVYELFPRL-------------------KERRRQRAGTLSGGEQQM 144
|
170 180
....*....|....*....|
gi 1955823976 225 IALARALFMNPTVLLLDEPT 244
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPS 164
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
73-272 |
5.32e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 51.31 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIPE-----------------HMDIYHLS 135
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEvtitgsivynghniyspRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 136 REI-------EASDMSSLEAVIScdEERLKLEKEAEslasqddgggeQLDRIYERleALDAATAEKRAAEILY--GLGFn 206
Cdd:PRK14239 86 KEIgmvfqqpNPFPMSIYENVVY--GLRLKGIKDKQ-----------VLDEAVEK--SLKGASIWDEVKDRLHdsALGL- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 207 kqmqakktrdfSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLK--KFDRILVVVSHS 272
Cdd:PRK14239 150 -----------SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLglKDDYTMLLVTRS 206
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
218-271 |
5.47e-07 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 50.93 E-value: 5.47e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF--DRILVVVSH 271
Cdd:cd03248 152 SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH 207
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
101-310 |
5.57e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.20 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 101 YGLLGLNGCGKSTLLAAIGcrelpipEHMDIYHLSREIEASDMSSLEAVISCDEerLKLEKEAESLASQDDGGGEQ--LD 178
Cdd:PRK14246 39 FGIMGPSGSGKSTLLKVLN-------RLIEIYDSKIKVDGKVLYFGKDIFQIDA--IKLRKEVGMVFQQPNPFPHLsiYD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 179 RIYERLEA---LDAATAEKRAAEILYGLGFNKQMQAK---KTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEAC 252
Cdd:PRK14246 110 NIAYPLKShgiKEKREIKKIVEECLRKVGLWKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 253 VWLEENLKKFDR--ILVVVSHSQDFLNGVCTNIIHMQNRKLKIYTGNYDQYVQTRSELEE 310
Cdd:PRK14246 190 QAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
85-287 |
5.62e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 51.32 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 85 HDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIPEHMDIYHLSREIEASDM------SSLEAVISCDEERL- 157
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpvrKRIGMVFQFPESQLf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 158 --KLEKEAESlasqddgGGEQLDriyerleaLDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALFMNP 235
Cdd:PRK13646 100 edTVEREIIF-------GPKNFK--------MNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1955823976 236 TVLLLDEPTNHLDLEACVWLEENLKKF----DRILVVVSHSQDFLNGVCTNIIHMQ 287
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLqtdeNKTIILVSHDMNEVARYADEVIVMK 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
383-569 |
6.35e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.34 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 383 VLQFVEVTFGYT-PENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDgmvrrHNHLRIAQFHQHLAEKLD 461
Cdd:PRK13640 5 IVEFKHVSFTYPdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD-----NPNSKITVDGITLTAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 462 LElsalqfmIREYPG----NEEEKMRGA-IGK---FGLSGKAQVMP-MK---------------------NLSDGQRSRV 511
Cdd:PRK13640 80 WD-------IREKVGivfqNPDNQFVGAtVGDdvaFGLENRAVPRPeMIkivrdvladvgmldyidsepaNLSGGQKQRV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 512 IFAWLAWRQPHLLLLDEPTNHLDI---ETIDSLAEALNEwDGGLVLVS--HDFRLINQVAQEI 569
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPagkEQILKLIRKLKK-KNNLTVISitHDIDEANMADQVL 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
187-248 |
6.84e-07 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 50.76 E-value: 6.84e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955823976 187 LDAATAEKRAAEILYGLGfnkqMQAKKT---RDFSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:COG1126 108 MSKAEAEERAMELLERVG----LADKADaypAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
405-540 |
7.09e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 51.62 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 405 FGVdldsrialVGPNGAGKSTLLKLMTG--------------DLVPLDG----MVRRhnhlRIAQFHQH---LAEK---- 459
Cdd:COG1135 34 FGI--------IGYSGAGKSTLIRCINLlerptsgsvlvdgvDLTALSErelrAARR----KIGMIFQHfnlLSSRtvae 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 460 ---LDLELSalqfmirEYPGNE-EEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFAwlawR----QPHLLLLDEPTN 531
Cdd:COG1135 102 nvaLPLEIA-------GVPKAEiRKRVAELLELVGLSDKADAYP-SQLSGGQKQRVGIA----RalanNPKVLLCDEATS 169
|
....*....
gi 1955823976 532 HLDIETIDS 540
Cdd:COG1135 170 ALDPETTRS 178
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
389-545 |
7.91e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.03 E-value: 7.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 389 VTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR---------RHNHLR--IAQFHQhla 457
Cdd:PRK10790 346 VSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRldgrplsslSHSVLRqgVAMVQQ--- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 458 eklDLELSALQFMIREYPGNE--EEKMRGAIGKFGLSGKAQVMPM----------KNLSDGQRSRVIFAWLAWRQPHLLL 525
Cdd:PRK10790 423 ---DPVVLADTFLANVTLGRDisEEQVWQALETVQLAELARSLPDglytplgeqgNNLSVGQKQLLALARVLVQTPQILI 499
|
170 180
....*....|....*....|
gi 1955823976 526 LDEPTNHLDIETIDSLAEAL 545
Cdd:PRK10790 500 LDEATANIDSGTEQAIQQAL 519
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
380-571 |
8.36e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.98 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 380 PPPVLQFVEVTFGYTPENLIyKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV----RRHNHLRIAQFHQ- 454
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVL-KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeiggNPCARLTPAKAHQl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 455 --HLAEKLDL---ELSALQFMIREYPGNE--EEKMRGAIGKFG----LSGKAQVMpmkNLSDGQRSRVIFAWLawRQPHL 523
Cdd:PRK15439 87 giYLVPQEPLlfpNLSVKENILFGLPKRQasMQKMKQLLAALGcqldLDSSAGSL---EVADRQIVEILRGLM--RDSRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 524 LLLDEPTNHL---DIETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWV 571
Cdd:PRK15439 162 LILDEPTASLtpaETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISV 212
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
406-565 |
8.43e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 50.45 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 406 GVDLDSR----IALVGPNGAGKSTLLKLMTG----------------DLVPLD-------GM------------VRRHNH 446
Cdd:COG0396 18 GVNLTIKpgevHAIMGPNGSGKSTLAKVLMGhpkyevtsgsilldgeDILELSpderaraGIflafqypveipgVSVSNF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 447 LRIAqfhqhLAEKLDLELSALQFMireypgneeEKMRGAIGKFGLSgkaQVMPMKNL----SDGQRSRVIFAWLAWRQPH 522
Cdd:COG0396 98 LRTA-----LNARRGEELSAREFL---------KLLKEKMKELGLD---EDFLDRYVnegfSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1955823976 523 LLLLDEPTNHLDIETIDSLAEALNEW---DGGLVLVSHDFRLINQV 565
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKLrspDRGILIITHYQRILDYI 206
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
413-562 |
9.51e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.91 E-value: 9.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 413 IALVGPNGAGKSTLLKLMTGDLVPLDGMVRRhnhlriaqfhqhlaekLDLElsalqfMIREYPGNEEEKMRGAIGKFGLS 492
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGVIY----------------IDGE------DILEEVLDQLLLIIVGGKKASGS 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 493 GkaqvmpmknlsdGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEWDGGLVLVSHDFRLI 562
Cdd:smart00382 63 G------------ELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
393-580 |
9.71e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.43 E-value: 9.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 393 YTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNhlRIAQFHQHLAEKLDLELSALQFMIR 472
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 473 EYP-------------------GNEEEK-----MRGAIGKFGLSGKAQ---VMPMKNLSDGQRSRVIFAWLAWRQPHLLL 525
Cdd:PRK14246 97 QQPnpfphlsiydniayplkshGIKEKReikkiVEECLRKVGLWKEVYdrlNSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1955823976 526 LDEPTNHLDIETIDSLAEALNEWDG--GLVLVSHDFRLINQVAQEIWVCENQAVTKW 580
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEW 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
209-248 |
1.13e-06 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 49.47 E-value: 1.13e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1955823976 209 MQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:cd03213 104 MFAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
383-557 |
1.16e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 383 VLQFVEVTFGYTpENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGmvrrhnhlRIAQFHQHLAEKLDL 462
Cdd:PRK13540 1 MLDVIELDFDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKG--------EILFERQSIKKDLCT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 463 ELSALQFMIREYPGNEEEKMRG--------AIGKFGLSGKAQVMPMKN--------LSDGQRSRVIFAWLAWRQPHLLLL 526
Cdd:PRK13540 72 YQKQLCFVGHRSGINPYLTLREnclydihfSPGAVGITELCRLFSLEHlidypcglLSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180 190
....*....|....*....|....*....|....
gi 1955823976 527 DEPTNHLD---IETIDSLAEALNEWDGGLVLVSH 557
Cdd:PRK13540 152 DEPLVALDelsLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
414-578 |
1.45e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 414 ALVGPNGAGKSTLLKLMTGDLVPLDGmvRRHNHL-RIAQFH----QHLAEKL--------------DLELSALQfMIREY 474
Cdd:PRK10938 33 AFVGANGSGKSALARALAGELPLLSG--ERQSQFsHITRLSfeqlQKLVSDEwqrnntdmlspgedDTGRTTAE-IIQDE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 475 PGNEEEKMRGAiGKFGLSGKAQvMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEWDGG--- 551
Cdd:PRK10938 110 VKDPARCEQLA-QQFGITALLD-RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSgit 187
|
170 180
....*....|....*....|....*..
gi 1955823976 552 LVLVSHDFRLINQVAQEIWVCENQAVT 578
Cdd:PRK10938 188 LVLVLNRFDEIPDFVQFAGVLADCTLA 214
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
399-563 |
1.65e-06 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 49.57 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 399 IYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGdlvpldgmvrrHNHLRIAQFHQHLAEK--LDLE------------- 463
Cdd:TIGR01978 15 ILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG-----------HPSYEVTSGTILFKGQdlLELEpderaraglflaf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 464 --------LSALQFM------IREYPGNEEEKMRGAIGKfgLSGKAQVMPM------KNL----SDGQRSRVIFAWLAWR 519
Cdd:TIGR01978 84 qypeeipgVSNLEFLrsalnaRRSARGEEPLDLLDFEKL--LKEKLALLDMdeeflnRSVnegfSGGEKKRNEILQMALL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1955823976 520 QPHLLLLDEPTNHLDIETIDSLAEALNEW---DGGLVLVSHDFRLIN 563
Cdd:TIGR01978 162 EPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLN 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
88-288 |
1.90e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 50.42 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 88 IVDSELELNYGRRYGLLGLNGCGKSTLLAAIGcrELPIPEHMDIYhlsreIEASDMSSLEAVISCDEERLKLEKEAESLA 167
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLN--RLIEPTRGQVL-----IDGVDIAKISDAELREVRRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 168 SQDDGGGEQLDRIYERLEALDAATAEKRAAEILYGLGFNKQMQAKKTrDFSGGWRMRIALARALFMNPTVLLLDEPTNHL 247
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPD-ELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1955823976 248 DLEACVWLEENLKKF----DRILVVVSHSQDFLNGVCTNIIHMQN 288
Cdd:PRK10070 196 DPLIRTEMQDELVKLqakhQRTIVFISHDLDEAMRIGDRIAIMQN 240
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
403-571 |
1.94e-06 |
|
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: 49.19 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 403 LDF-GVDLDSRIALVGPNGAGKSTLLKLMTgdlVPLDGMVRRHNHLRIAQFHQHLAEK-----LDLELSALQFMIREYPG 476
Cdd:cd03279 20 IDFtGLDNNGLFLICGPTGAGKSTILDAIT---YALYGKTPRYGRQENLRSVFAPGEDtaevsFTFQLGGKKYRVERSRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 477 NEEEKMRGAI----GKFglsgkAQVM--PMKNLSDGQRSRVIFAW-------LAWR---QPHLLLLDEPTNHLDIETIDS 540
Cdd:cd03279 97 LDYDQFTRIVllpqGEF-----DRFLarPVSTLSGGETFLASLSLalalsevLQNRggaRLEALFIDEGFGTLDPEALEA 171
|
170 180 190
....*....|....*....|....*....|....
gi 1955823976 541 LAEALNEW--DGGLVLV-SHDFRLINQVAQEIWV 571
Cdd:cd03279 172 VATALELIrtENRMVGViSHVEELKERIPQRLEV 205
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
73-294 |
2.01e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 49.31 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSE----------------------LELNYGRRYGLLGLNGCGKSTLLAAIGcrelpipehmD 130
Cdd:COG1134 5 IEVENVSKSYRLYHEPSRSLkelllrrrrtrreefwalkdvsFEVERGESVGIIGRNGAGKSTLLKLIA----------G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 131 IYHLSR-EIEAS-DMSSLEAViscdeerlklekeaeslasqddGGGEQLD-------RIYERLEALDAATAEKRAAEILY 201
Cdd:COG1134 75 ILEPTSgRVEVNgRVSALLEL----------------------GAGFHPEltgreniYLNGRLLGLSRKEIDEKFDEIVE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 202 --GLG--FNKQMqakKTrdFSGGWRMRIALARALFMNPTVLLLDEptnhldleacvWLE--------------ENLKKFD 263
Cdd:COG1134 133 faELGdfIDQPV---KT--YSSGMRARLAFAVATAVDPDILLVDE-----------VLAvgdaafqkkclariRELRESG 196
|
250 260 270
....*....|....*....|....*....|.
gi 1955823976 264 RILVVVSHSQDFLNGVCTNIIHMQNRKLKIY 294
Cdd:COG1134 197 RTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
76-248 |
2.03e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.51 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 76 ESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTllaaigcrelpipehmdIYHLSREIEASDMSSleavISCDEE 155
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT-----------------TFYMVVGIVPRDAGN----IIIDDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 156 RLKLEKEAESlASQDDGGGEQLDRIYERLEALDAATA-------------EKRAAEILyglgfnKQMQAKKTRD-----F 217
Cdd:PRK10895 66 DISLLPLHAR-ARRGIGYLPQEASIFRRLSVYDNLMAvlqirddlsaeqrEDRANELM------EEFHIEHLRDsmgqsL 138
|
170 180 190
....*....|....*....|....*....|.
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:PRK10895 139 SGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
415-558 |
2.20e-06 |
|
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: 49.29 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 415 LVGPNGAGKSTLLKLMTGDLVP----------LDGMVRrhnHLRIAQFHQHLAEKLDLELSALQ------FMIREYPGNE 478
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPnlgkfddppdWDEILD---EFRGSELQNYFTKLLEGDVKVIVkpqyvdLIPKAVKGKV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 479 EEKMRGAIGKFGLSGKAQVMPMKN--------LSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIE---TIDSLAEALNE 547
Cdd:cd03236 108 GELLKKKDERGKLDELVDQLELRHvldrnidqLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAE 187
|
170
....*....|.
gi 1955823976 548 WDGGLVLVSHD 558
Cdd:cd03236 188 DDNYVLVVEHD 198
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
90-273 |
2.45e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.03 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 90 DSELELNYGRRYGLLGLNGCGKSTLLAAIGCRElpipehmdiyhlsreieasDMSSLEAVIscDEERLKlekeaeSLASQ 169
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLE-------------------DITSGDLFI--GEKRMN------DVPPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 170 DDGGGE--QLDRIYERLE-------ALDAATAEKR--------AAEILyglgfnkQMQA---KKTRDFSGGWRMRIALAR 229
Cdd:PRK11000 74 ERGVGMvfQSYALYPHLSvaenmsfGLKLAGAKKEeinqrvnqVAEVL-------QLAHlldRKPKALSGGQRQRVAIGR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1955823976 230 ALFMNPTVLLLDEPTNHLDLEACVWLEENL----KKFDRILVVVSHSQ 273
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDAALRVQMRIEIsrlhKRLGRTMIYVTHDQ 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
82-271 |
2.56e-06 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 48.38 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 82 FHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPipehmdiyhLSREIEASDMSSLEAVI--SCDEERLKL 159
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRP---------TSGTVRRAGGARVAYVPqrSEVPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 160 E-KEAESLAS-QDDGGGEQLDR-----IYERLEALDAATAEKRAaeilyglgfnkqmqakkTRDFSGGWRMRIALARALF 232
Cdd:NF040873 73 TvRDLVAMGRwARRGLWRRLTRddraaVDDALERVGLADLAGRQ-----------------LGELSGGQRQRALLAQGLA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1955823976 233 MNPTVLLLDEPTNHLDLEACVWLEENLKKF---DRILVVVSH 271
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEEharGATVVVVTH 177
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
73-286 |
2.74e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 49.21 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGcrELPIPEHMDIYHLSREIE--ASDMSSLEAVI 150
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLS--RLMTPAHGHVWLDGEHIQhyASKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 151 SCDEERLKLEKEAESLASQDDGGGEQLDRIYeRLEALDAATAEKRAAEIlyglgfnKQMQAKKTRDFSGGWRMRIALARA 230
Cdd:PRK10253 86 LAQNATTPGDITVQELVARGRYPHQPLFTRW-RKEDEEAVTKAMQATGI-------THLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 231 LFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDR----ILVVVSHSqdfLNGVCTNIIHM 286
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNRekgyTLAAVLHD---LNQACRYASHL 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
81-568 |
2.76e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.21 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 81 TFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAaIGCRELPIPEHM-DIYHLSREIEASDMSSLEAV-ISCDEERLK 158
Cdd:TIGR02633 10 TFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMK-ILSGVYPHGTWDgEIYWSGSPLKASNIRDTERAgIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 159 LEKEAeSLASQDDGGGEqldrIYERLEALDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALFMNPTVL 238
Cdd:TIGR02633 89 LVPEL-SVAENIFLGNE----ITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 239 LLDEPTNHL---DLEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNrklkiytgnyDQYVQTRSeleenqmkM 315
Cdd:TIGR02633 164 ILDEPSSSLtekETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRD----------GQHVATKD--------M 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 316 YKWEQDQIASM---KEYIARFGHGSAKL------ARQAQSKEKTLAKMER-GGLTEKVVRDKVL-VFRFVDVGKlpppvL 384
Cdd:TIGR02633 226 STMSEDDIITMmvgREITSLYPHEPHEIgdvileARNLTCWDVINPHRKRvDDVSFSLRRGEILgVAGLVGAGR-----T 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 385 QFVEVTFGYTP---ENLIYKNldfGVDLDSRialvGPNGAGKSTLLklmtgdLVPLDgmvrRHNHLRIAQfhqhLAEKLD 461
Cdd:TIGR02633 301 ELVQALFGAYPgkfEGNVFIN---GKPVDIR----NPAQAIRAGIA------MVPED----RKRHGIVPI----LGVGKN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 462 LELSALQ---FMIREYPGNEEEKMRGAIGKFGLSGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETI 538
Cdd:TIGR02633 360 ITLSVLKsfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAK 439
|
490 500 510
....*....|....*....|....*....|
gi 1955823976 539 DSLaealnewdgglvlvshdFRLINQVAQE 568
Cdd:TIGR02633 440 YEI-----------------YKLINQLAQE 452
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
187-249 |
2.81e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.24 E-value: 2.81e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 187 LDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDL 249
Cdd:PRK10261 434 LPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
218-300 |
2.82e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 49.70 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLD----LEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNrklki 293
Cdd:PRK10851 138 SGGQKQRVALARALAVEPQILLLDEPFGALDaqvrKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQ----- 212
|
....*..
gi 1955823976 294 ytGNYDQ 300
Cdd:PRK10851 213 --GNIEQ 217
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
413-575 |
3.30e-06 |
|
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: 47.57 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 413 IALVGPNGAGKSTLLKLMTGDLVPLDGMVrrhnhlriaqfhqhlaekldlelsalqfmirEYPGNEeekmrgaigkfgLS 492
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDND-------------------------------EWDGIT------------PV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 493 GKAQVMpmkNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALN----EWDGGLVLVSHDFRLINQVAQE 568
Cdd:cd03222 65 YKPQYI---DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRrlseEGKKTALVVEHDLAVLDYLSDR 141
|
....*..
gi 1955823976 569 IWVCENQ 575
Cdd:cd03222 142 IHVFEGE 148
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
393-557 |
3.45e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.68 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 393 YTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTgDLVPLDGMVRRHNHLRIAQFHQHLAEKLDLELSALQFMIR 472
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFN-RLLELNEEARVEGEVRLFGRNIYSPDVDPIEVRREVGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 473 EYP-------------------------GNEEEKMRGAIGKFGL----SGKAQVMPmKNLSDGQRSRVIFAWLAWRQPHL 523
Cdd:PRK14267 92 QYPnpfphltiydnvaigvklnglvkskKELDERVEWALKKAALwdevKDRLNDYP-SNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1955823976 524 LLLDEPTNHLDIETIDSLAEALNEW--DGGLVLVSH 557
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTH 206
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
209-315 |
4.10e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 48.69 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 209 MQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLD----LEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNII 284
Cdd:PRK13636 134 LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVF 213
|
90 100 110
....*....|....*....|....*....|.
gi 1955823976 285 HMQNRKLkIYTGNYDQYVQTRSELEENQMKM 315
Cdd:PRK13636 214 VMKEGRV-ILQGNPKEVFAEKEMLRKVNLRL 243
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
413-583 |
4.20e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.43 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 413 IALVGPNGAGKSTLLKLMTGDLVPLDG----------MVR-RHNHLRIAQFHQHLAEKLDLELSALQFMIREYPGNEEEK 481
Cdd:PRK10619 34 ISIIGSSGSGKSTFLRCINFLEKPSEGsivvngqtinLVRdKDGQLKVADKNQLRLLRTRLTMVFQHFNLWSHMTVLENV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 482 MRGAI------------------GKFGLSGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDS--- 540
Cdd:PRK10619 114 MEAPIqvlglskqeareravkylAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEvlr 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1955823976 541 LAEALNEWDGGLVLVSHDFRLINQVAQEIwVCENQAVTKWEGD 583
Cdd:PRK10619 194 IMQQLAEEGKTMVVVTHEMGFARHVSSHV-IFLHQGKIEEEGA 235
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
192-313 |
4.21e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.59 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 192 AEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDR---ILVV 268
Cdd:PRK13649 121 AEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsgmTIVL 200
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1955823976 269 VSHSQDFLNGVCTNIIHMQNRKLkIYTGNYDQYVQTRSELEENQM 313
Cdd:PRK13649 201 VTHLMDDVANYADFVYVLEKGKL-VLSGKPKDIFQDVDFLEEKQL 244
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
355-563 |
4.39e-06 |
|
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: 48.93 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 355 ERGGLTEKVVRDKVLVFRFVDVG--KLPPPVLQFVEVTFGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTG 432
Cdd:pfam13304 85 EKLSSKPTLLEKRLLLREDSEERepKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 433 DLVPLDGMVRRHNHLRIAQFHQHLAEKLDLELSALQFM--IREYPGNEEEKMRGAIGKFGLSGKAQVMPMKNLSDGQRSR 510
Cdd:pfam13304 165 DWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLgeGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRL 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1955823976 511 VIFAWLAWRQPH---LLLLDEPTNHLDIETIDSLAEALN---EWDGGLVLVSHDFRLIN 563
Cdd:pfam13304 245 LALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKelsRNGAQLILTTHSPLLLD 303
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
73-248 |
4.46e-06 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 48.32 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIV----DSELELNYGRRYGLLGLNGCGKSTLLAAIgcrelpipehmdiyhlsreieASDMSSLEA 148
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQpalqDVSLTIESGEFVVALGASGCGKTTLLNLI---------------------AGFLAPSSG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 149 VISCDEERLKLEKEAESLASQDDGGGEQLDrIYE------RLEALDAATAEKRAAEILYGLGFNKQMQAKkTRDFSGGWR 222
Cdd:COG4525 63 EITLDGVPVTGPGADRGVVFQKDALLPWLN-VLDnvafglRLRGVPKAERRARAEELLALVGLADFARRR-IWQLSGGMR 140
|
170 180
....*....|....*....|....*.
gi 1955823976 223 MRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALD 166
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
215-317 |
5.12e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 215 RDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENL----KKFDRILVVVSHSqdflngvctniIHMQNRK 290
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKADKTIITIAHR-----------IASIKRS 1425
|
90 100 110
....*....|....*....|....*....|....
gi 1955823976 291 LKIY-------TGNYDQYVQTRSELEENQMKMYK 317
Cdd:PTZ00265 1426 DKIVvfnnpdrTGSFVQAHGTHEELLSVQDGVYK 1459
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
73-243 |
5.24e-06 |
|
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: 47.92 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLL-----------AAIGCRELPIpEHMDIYHLSR----- 136
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFymivglvkpdsGKILLDGQDI-TKLPMHKRARlgigy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 137 -EIEASDMSSL--EAVISCDEERLKLEKEaeslasqddgggEQLDRIYERLEALDAATAEKRAAEILyglgfnkqmqakk 213
Cdd:cd03218 80 lPQEASIFRKLtvEENILAVLEIRGLSKK------------EREEKLEELLEEFHITHLRKSKASSL------------- 134
|
170 180 190
....*....|....*....|....*....|
gi 1955823976 214 trdfSGGWRMRIALARALFMNPTVLLLDEP 243
Cdd:cd03218 135 ----SGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
203-276 |
5.29e-06 |
|
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: 47.71 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 203 LGFNKQMQ-AKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWL-EENLKKF----DRILVVVSHSQDFL 276
Cdd:cd03290 126 LPFGDQTEiGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmQEGILKFlqddKRTLVLVTHKLQYL 205
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
217-277 |
5.38e-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: 46.76 E-value: 5.38e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 217 FSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRILVVVSHSQDFLN 277
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWK 152
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
387-557 |
6.01e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.99 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 387 VEVTFGYTPenlIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTG--DLVP---------LDG---------MVRRH-- 444
Cdd:PRK14247 9 LKVSFGQVE---VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPearvsgevyLDGqdifkmdviELRRRvq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 445 ------NHLRIAQFHQHLAekLDLELSALQFMIREYpgneEEKMRGAIGKFGLSGKAQV---MPMKNLSDGQRSRVIFAW 515
Cdd:PRK14247 86 mvfqipNPIPNLSIFENVA--LGLKLNRLVKSKKEL----QERVRWALEKAQLWDEVKDrldAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1955823976 516 LAWRQPHLLLLDEPTNHLDIET---IDSLAEALNEwDGGLVLVSH 557
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENtakIESLFLELKK-DMTIVLVTH 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
402-574 |
6.41e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 402 NLDFGVDLDSRIALVGPNGAGKS----TLLKLM-TGDLVPLDGMVRRHN------------HLR---IAQFHQ------- 454
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGesllhaseqtlrGVRgnkIAMIFQepmvsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 455 --HLAEKLDLELSALQFMIREYPGNEEekMRGAIGKFGLSGKAQVM---PMKnLSDGQRSRVIFAWLAWRQPHLLLLDEP 529
Cdd:PRK15134 107 plHTLEKQLYEVLSLHRGMRREAARGE--ILNCLDRVGIRQAAKRLtdyPHQ-LSGGERQRVMIAMALLTRPELLIADEP 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1955823976 530 TNHLDI----ETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWVCEN 574
Cdd:PRK15134 184 TTALDVsvqaQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQN 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
72-251 |
6.57e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 48.67 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 72 DIRIESLSVTFHGHDLIVDSELELNY--GRRYGLLGLNGCGKSTLLAAIgcRELPIPEHMDIYHLSREIEAsdmssleav 149
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVasGECFGLLGPNGAGKSTIARMI--LGMTSPDAGKITVLGVPVPA--------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 150 iscdeeRLKLEKEAESLASQDDgggeQLDR---------IYERLEALDAATAEkraAEILYGLGFNKQMQAKKTR--DFS 218
Cdd:PRK13536 108 ------RARLARARIGVVPQFD----NLDLeftvrenllVFGRYFGMSTREIE---AVIPSLLEFARLESKADARvsDLS 174
|
170 180 190
....*....|....*....|....*....|...
gi 1955823976 219 GGWRMRIALARALFMNPTVLLLDEPTNHLDLEA 251
Cdd:PRK13536 175 GGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
218-274 |
6.82e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.33 E-value: 6.82e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLDL----EACVWLEENLKKFDRILVVVSHSQD 274
Cdd:PRK11144 130 SGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHSLD 190
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
182-250 |
7.27e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 48.80 E-value: 7.27e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 182 ERLEALDAATA----EKRAaeilygLGFNKqMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLE 250
Cdd:PRK13657 440 EMRAAAERAQAhdfiERKP------DGYDT-VVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
80-272 |
8.71e-06 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 47.44 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 80 VTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAI-GCRElpiPEHMDIY-----HLSREIEASDMSSLeaviscd 153
Cdd:COG3840 7 LTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIaGFLP---PDSGRILwngqdLTALPPAERPVSML------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 154 eerlklekeaeslaSQDDGGGEQLDrIYE----------RLEALDAATAEKRAAEI-LYGLGfnkqmqAKKTRDFSGGWR 222
Cdd:COG3840 77 --------------FQENNLFPHLT-VAQniglglrpglKLTAEQRAQVEQALERVgLAGLL------DRLPGQLSGGQR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 223 MRIALARALFMNPTVLLLDEPTNHLD----LEACVWLEENLKKFDRILVVVSHS 272
Cdd:COG3840 136 QRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
177-267 |
8.74e-06 |
|
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: 47.33 E-value: 8.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 177 LDRIYErleaLDAATAEKRAAEILYGLGFNKQMQaKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEAcvwlE 256
Cdd:cd03267 119 LAAIYD----LPPARFKKRLDELSELLDLEELLD-TPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA----Q 189
|
90
....*....|.
gi 1955823976 257 ENLKKFDRILV 267
Cdd:cd03267 190 ENIRNFLKEYN 200
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
73-285 |
8.90e-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: 46.75 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIPEHMDIYhlsreIEASDMSSLEAvisc 152
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEIL-----FKGEDITDLPP---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 dEERLKLekeAESLASQDDgggeqldriyERLEALdaataekRAAEILYGLGFNkqmqakktrdFSGGWRMRIALARALF 232
Cdd:cd03217 72 -EERARL---GIFLAFQYP----------PEIPGV-------KNADFLRYVNEG----------FSGGEKKRNEILQLLL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1955823976 233 MNPTVLLLDEPTNHLDLEACVWLEENLKKF---DRILVVVSHSQDFLNGVCTNIIH 285
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKLreeGKSVLIITHYQRLLDYIKPDRVH 176
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
74-284 |
9.55e-06 |
|
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: 47.34 E-value: 9.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 74 RIESLSVTFHGHdLIVDS-ELELNYGRRYGLLGLNGCGKSTLLAAIgCRELPiPEHMDIYHLSREIEA------------ 140
Cdd:COG0411 6 EVRGLTKRFGGL-VAVDDvSLEVERGEIVGLIGPNGAGKTTLFNLI-TGFYR-PTSGRILFDGRDITGlpphriarlgia 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 141 ---------SDMSSLEAViscdeerlklekeaesLASQDDGGGEQLDRIYERLEALDAATAE--KRAAEILYGLGFNKQM 209
Cdd:COG0411 83 rtfqnprlfPELTVLENV----------------LVAAHARLGRGLLAALLRLPRARREEREarERAEELLERVGLADRA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 210 QAKkTRDFSGGWRMRIALARALFMNPTVLLLDEPT---NHLDLEAcvwLEENLKK----FDRILVVVSHSQDFLNGVCTN 282
Cdd:COG0411 147 DEP-AGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEE---LAELIRRlrdeRGITILLIEHDMDLVMGLADR 222
|
..
gi 1955823976 283 II 284
Cdd:COG0411 223 IV 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
404-558 |
9.94e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.39 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 404 DFGVDLDSRIALV--GPNGAGKSTLLKLMTG-----------DLVPLDG------MVRRHNHLRIAQFHQHLAEkLDLEL 464
Cdd:PRK11248 19 DINLTLESGELLVvlGPSGCGKTTLLNLIAGfvpyqhgsitlDGKPVEGpgaergVVFQNEGLLPWRNVQDNVA-FGLQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 465 SALQFMIREypgneeEKMRGAIGKFGLSGkAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEA 544
Cdd:PRK11248 98 AGVEKMQRL------EIAHQMLKKVGLEG-AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTL 170
|
170
....*....|....*...
gi 1955823976 545 L----NEWDGGLVLVSHD 558
Cdd:PRK11248 171 LlklwQETGKQVLLITHD 188
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
218-248 |
1.04e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 47.77 E-value: 1.04e-05
10 20 30
....*....|....*....|....*....|.
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
218-271 |
1.07e-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: 47.22 E-value: 1.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF--DRILVVVSH 271
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAH 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
80-296 |
1.16e-05 |
|
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: 46.72 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 80 VTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPipehmdiyhlsreieASDMSSLEAViscDEERLKL 159
Cdd:cd03298 6 IRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETP---------------QSGRVLINGV---DVTAAPP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 160 EKEAESLASQDDGGGEQLDrIYE----------RLEALDAATAEKRAAEIlyGLGfnkQMQAKKTRDFSGGWRMRIALAR 229
Cdd:cd03298 68 ADRPVSMLFQENNLFAHLT-VEQnvglglspglKLTAEDRQAIEVALARV--GLA---GLEKRLPGELSGGERQRVALAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 230 ALFMNPTVLLLDEPTNHLD----LEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKLkIYTG 296
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI-AAQG 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
105-299 |
1.22e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 46.63 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 105 GLNGCGKSTLLAAIGcrELPIPEHMDIYhlsreIEASDMSSLeaviSCDEERLKLEKEAESLASQDDGGGEQLDRIYE-R 183
Cdd:PRK10247 40 GPSGCGKSTLLKIVA--SLISPTSGTLL-----FEGEDISTL----KPEIYRQQVSYCAQTPTLFGDTVYDNLIFPWQiR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 184 LEALDaataEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDleacvwlEENLKKFD 263
Cdd:PRK10247 109 NQQPD----PAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD-------ESNKHNVN 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1955823976 264 RIL-----------VVVSHSQDFLNGvCTNIIHMQNRKLKIYTGNYD 299
Cdd:PRK10247 178 EIIhryvreqniavLWVTHDKDEINH-ADKVITLQPHAGEMQEARYE 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
218-288 |
1.30e-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: 46.31 E-value: 1.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENL----KKFDRILVVVSHSQDFLNgVCTNIIHMQN 288
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCilglLLNNKTRILVTHQLQLLP-HADQIVVLDN 202
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
73-271 |
1.30e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.03 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIgcRELPIPEhmdiyhlSREIEASDMSSLEAVisc 152
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV--LGLVAPD-------EGVIKRNGKLRIGYV--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 153 dEERLKLEKeaeslasqddgggeQLDRIYERLEALDAATaekRAAEILYGLgfnKQMQAKKTRDF-----SGGWRMRIAL 227
Cdd:PRK09544 73 -PQKLYLDT--------------TLPLTVNRFLRLRPGT---KKEDILPAL---KRVQAGHLIDApmqklSGGETQRVLL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1955823976 228 ARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRIL----VVVSH 271
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcavLMVSH 179
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
413-560 |
1.30e-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: 46.77 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 413 IALVGPNGAGKSTLLKLMTGDLVPLDGMVRRhNHLRIAQFHQH---------LAE------KLDLE---LSALQfmIREY 474
Cdd:cd03218 29 VGLLGPNGAGKTTTFYMIVGLVKPDSGKILL-DGQDITKLPMHkrarlgigyLPQeasifrKLTVEeniLAVLE--IRGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 475 PGNE-EEKMRGAIGKFGLSGKAQVMPMKnLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLD---IETIDSLAEALNEWDG 550
Cdd:cd03218 106 SKKErEEKLEELLEEFHITHLRKSKASS-LSGGERRRVEIARALATNPKFLLLDEPFAGVDpiaVQDIQKIIKILKDRGI 184
|
170
....*....|
gi 1955823976 551 GLVLVSHDFR 560
Cdd:cd03218 185 GVLITDHNVR 194
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
187-248 |
1.34e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 47.11 E-value: 1.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955823976 187 LDAATAEKRAAEILYGLGFnKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:PRK13652 109 LDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
413-578 |
1.41e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 46.99 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 413 IALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHlRIAQFH--QHLAEKLDLEL------SAL--QFMIREY-------- 474
Cdd:PRK10419 41 VALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE-PLAKLNraQRKAFRRDIQMvfqdsiSAVnpRKTVREIireplrhl 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 475 ----PGNEEEKMRGAIGKFGLS-GKAQVMPmKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDI----ETIDSLAEAL 545
Cdd:PRK10419 120 lsldKAERLARASEMLRAVDLDdSVLDKRP-PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQ 198
|
170 180 190
....*....|....*....|....*....|....*....
gi 1955823976 546 NEWDGGLVLVSHDFRLINQVAQEIWV------CENQAVT 578
Cdd:PRK10419 199 QQFGTACLFITHDLRLVERFCQRVMVmdngqiVETQPVG 237
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
185-303 |
1.48e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 47.92 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 185 EALDAATAEKRAAEILYGL--GFNKQMQAKKTRdFSGGWRMRIALARALFMNPTVLLLDEPTNHLD-------LEAcvwL 255
Cdd:PRK11174 453 EQLQQALENAWVSEFLPLLpqGLDTPIGDQAAG-LSVGQAQRLALARALLQPCQLLLLDEPTASLDahseqlvMQA---L 528
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1955823976 256 EENLKkfDRILVVVSHSQDFLNGvCTNIIHMQNRKLkIYTGNYDQYVQ 303
Cdd:PRK11174 529 NAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQI-VQQGDYAELSQ 572
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
413-558 |
1.51e-05 |
|
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: 47.86 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 413 IALVGPNGAGKSTLLKLMTGDLVPLDGMVRRH-------NHLRIAQFHQHLAEKLDLELSA---LQF--MIREY-PGN-- 477
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEEpswdevlKRFRGTELQDYFKKLANGEIKVahkPQYvdLIPKVfKGTvr 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 478 -------EEEKMRGAIGKFGLSgkaQVM--PMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDI-------ETIDSL 541
Cdd:COG1245 182 ellekvdERGKLDELAEKLGLE---NILdrDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIyqrlnvaRLIREL 258
|
170
....*....|....*..
gi 1955823976 542 AEAlnewDGGLVLVSHD 558
Cdd:COG1245 259 AEE----GKYVLVVEHD 271
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
501-583 |
1.63e-05 |
|
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: 47.87 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 501 KNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETI----DSLAEALNEWDGGLVLVSHDFRLINQVAQE-IWVcENQ 575
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSDKaIWL-ENG 245
|
....*...
gi 1955823976 576 AVTKwEGD 583
Cdd:TIGR03269 246 EIKE-EGT 252
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
503-571 |
1.81e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.04 E-value: 1.81e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 503 LSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDI----ETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWV 571
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITHDLALVAEAAHKIIV 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
414-569 |
1.84e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.33 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 414 ALVGPNGAGKSTLLKLMTGDLVP------LDGMVRRHNH------LRIAQFHQH--LAEKLD--------LELSALQFM- 470
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPdsgeilIDGKPVRIRSprdaiaLGIGMVHQHfmLVPNLTvaenivlgLEPTKGGRLd 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 471 IREypgnEEEKMRGAIGKFGLsgkaQVMPMK---NLSDGQRSRV-IFAWLaWRQPHLLLLDEPTNHLD-------IETID 539
Cdd:COG3845 115 RKA----ARARIRELSERYGL----DVDPDAkveDLSVGEQQRVeILKAL-YRGARILILDEPTAVLTpqeadelFEILR 185
|
170 180 190
....*....|....*....|....*....|..
gi 1955823976 540 SLAEAlnewdgGL--VLVSHDFRLINQVAQEI 569
Cdd:COG3845 186 RLAAE------GKsiIFITHKLREVMAIADRV 211
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
402-590 |
1.88e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 402 NLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIAQFHQHLAEKL----DLELSALQFmireypGN 477
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLtgieNIELKGLMM------GL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 478 EEEKMRGAIGK---FGLSGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEW-DGG-- 551
Cdd:PRK13545 116 TKEKIKEIIPEiieFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFkEQGkt 195
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1955823976 552 LVLVSHDfrlINQV----AQEIWVCENQavTKWEGDIMDFKAH 590
Cdd:PRK13545 196 IFFISHS---LSQVksfcTKALWLHYGQ--VKEYGDIKEVVDH 233
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
93-297 |
1.90e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 47.01 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 93 LELNYGRRYGLLGLNGCGKSTLL-AAIGcreLPIPEHMDIYHLSREIeaSDMSsleaviscDEERLKLEKE-----AESL 166
Cdd:PRK15079 42 LRLYEGETLGVVGESGCGKSTFArAIIG---LVKATDGEVAWLGKDL--LGMK--------DDEWRAVRSDiqmifQDPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 167 ASQD------DGGGEQLdRIYErlEALDAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLL 240
Cdd:PRK15079 109 ASLNprmtigEIIAEPL-RTYH--PKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 241 DEPTNHLD--LEACV--WLEENLKKFDRILVVVSHSQDFLNgvctniiHMQNRKLKIYTGN 297
Cdd:PRK15079 186 DEPVSALDvsIQAQVvnLLQQLQREMGLSLIFIAHDLAVVK-------HISDRVLVMYLGH 239
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
414-571 |
2.18e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 414 ALVGPNGAGKSTLLKLM---------TGDLVpLDGMVRRHNHLR------IAQFHQHLAekLDLELSalqfmIRE--YPG 476
Cdd:NF040905 31 ALCGENGAGKSTLMKVLsgvyphgsyEGEIL-FDGEVCRFKDIRdsealgIVIIHQELA--LIPYLS-----IAEniFLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 477 NEEEKmRGAI-------------GKFGLSgKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDSLAE 543
Cdd:NF040905 103 NERAK-RGVIdwnetnrrarellAKVGLD-ESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLD 180
|
170 180 190
....*....|....*....|....*....|.
gi 1955823976 544 ALNEWDG-GL--VLVSHDFRLINQVAQEIWV 571
Cdd:NF040905 181 LLLELKAqGItsIIISHKLNEIRRVADSITV 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
405-442 |
2.21e-05 |
|
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: 46.13 E-value: 2.21e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1955823976 405 FGVDLD----SRIALVGPNGAGKSTLLKLMTGDLVPLDGMVR 442
Cdd:COG0410 20 HGVSLEveegEIVALLGRNGAGKTTLLKAISGLLPPRSGSIR 61
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
81-534 |
2.29e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 81 TFHGHD---LIVDSeLELNYGRRYGLLGLNGCGKSTLLAAIgCRELPIPEHMDIYHLSREIEASdMSSLEAVIScdEERL 157
Cdd:PRK10938 10 TFRLSDtktLQLPS-LTLNAGDSWAFVGANGSGKSALARAL-AGELPLLSGERQSQFSHITRLS-FEQLQKLVS--DEWQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 158 KLEKEAESlASQDDGGGEQLDRIYErlEALDAATAEKRAAEIlyglgfnkQMQAKKTRDF---SGGWRMRIALARALFMN 234
Cdd:PRK10938 85 RNNTDMLS-PGEDDTGRTTAEIIQD--EVKDPARCEQLAQQF--------GITALLDRRFkylSTGETRKTLLCQALMSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 235 PTVLLLDEPTNHLDLEACVWLEENLKKFDR---ILVVVSHSQDFLNGVCTNIIHMQNRKLkIYTGnydqyvqTRSELEen 311
Cdd:PRK10938 154 PDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLVLNRFDEIPDFVQFAGVLADCTL-AETG-------EREEIL-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 312 qmkmykweQDQIAsmkeyiarfghgsAKLARQAQSKEKTLAKMERGGLTEKVVRDKvlvfrfvdvgklPPPVLQFVEVTF 391
Cdd:PRK10938 224 --------QQALV-------------AQLAHSEQLEGVQLPEPDEPSARHALPANE------------PRIVLNNGVVSY 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 392 GYTPenlIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDL-------VPLDGMvRRHNHLRIAQFHQHL---AEKLD 461
Cdd:PRK10938 271 NDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpqgysndLTLFGR-RRGSGETIWDIKKHIgyvSSSLH 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 462 LE----LSALQFMIREY----------PGNEEEKMRGAIGKFGLSGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLD 527
Cdd:PRK10938 347 LDyrvsTSVRNVILSGFfdsigiyqavSDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILD 426
|
....*..
gi 1955823976 528 EPTNHLD 534
Cdd:PRK10938 427 EPLQGLD 433
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
383-556 |
2.89e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 383 VLQFVEVTFGYTPENLIYKNLDFgvdLDSRIALV-GPNGAGKSTLLKLMTGDLVPLDGMVRRHNhLRIAQFHQ------- 454
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFDLSITF---LPSAITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYKN-CNINNIAKpyctyig 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 455 -HLAEKLDLE-LSALQFMIREYpgNEEEKMRGAIGKFGLSgkaQVMPMK--NLSDGQRSRVIFAWLAWRQPHLLLLDEPT 530
Cdd:PRK13541 77 hNLGLKLEMTvFENLKFWSEIY--NSAETLYAAIHYFKLH---DLLDEKcySLSSGMQKIVAIARLIACQSDLWLLDEVE 151
|
170 180
....*....|....*....|....*...
gi 1955823976 531 NHLDIETIDSLAE--ALNEWDGGLVLVS 556
Cdd:PRK13541 152 TNLSKENRDLLNNliVMKANSGGIVLLS 179
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
389-571 |
3.07e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 46.19 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 389 VTFGYTP----ENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV-----------RRHNHLR----- 448
Cdd:PRK13637 8 LTHIYMEgtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditdkkVKLSDIRkkvgl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 449 IAQF--HQHLAEKLDLELSalqFMIREYPGNEEE---KMRGAIGKFGLS--GKAQVMPMKnLSDGQRSRVIFAWLAWRQP 521
Cdd:PRK13637 88 VFQYpeYQLFEETIEKDIA---FGPINLGLSEEEienRVKRAMNIVGLDyeDYKDKSPFE-LSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 522 HLLLLDEPTNHLDIETIDSLAEAL----NEWDGGLVLVSHDFRLINQVAQEIWV 571
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIkelhKEYNMTIILVSHSMEDVAKLADRIIV 217
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
218-277 |
3.21e-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: 45.29 E-value: 3.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 218 SGGWRM------RIALARALFMNPTVLLLDEPTNHLDLEACVW-----LEENLKKFDRILVVVSHSQDFLN 277
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVD 187
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
218-272 |
3.24e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 45.80 E-value: 3.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEE---NLKKfDRILVVVSHS 272
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEElilELKK-DYTIVIVTHN 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
70-289 |
3.31e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 46.72 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 70 SRDIRIESLSVTF-HGHDLIVDSELELNYGRRygLL--GLNGCGKSTLLAAI------GCRELPIPEHMDIYHLSRE--- 137
Cdd:COG4178 360 DGALALEDLTLRTpDGRPLLEDLSLSLKPGER--LLitGPSGSGKSTLLRAIaglwpyGSGRIARPAGARVLFLPQRpyl 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 138 IEASDMSSL---EAVISCDEERLK--LEKEaeslasqddgggeQLDRIYERLEAldaataEKRAAEILyglgfnkqmqak 212
Cdd:COG4178 438 PLGTLREALlypATAEAFSDAELReaLEAV-------------GLGHLAERLDE------EADWDQVL------------ 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 213 ktrdfSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEAcvwlEENL------KKFDRILVVVSHsQDFLNGVCTNIIHM 286
Cdd:COG4178 487 -----SLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN----EAALyqllreELPGTTVISVGH-RSTLAAFHDRVLEL 556
|
...
gi 1955823976 287 QNR 289
Cdd:COG4178 557 TGD 559
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
75-285 |
3.69e-05 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 45.33 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 75 IESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRElpipeHMDIYHLSREIEASDMSSLEAviscdE 154
Cdd:TIGR01978 3 IKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHP-----SYEVTSGTILFKGQDLLELEP-----D 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 155 ERLKLekeAESLASQ---DDGGGEQLD---------RIYERLEALDAATAEKRAAEILYGLGFNKQMqakKTRD----FS 218
Cdd:TIGR01978 73 ERARA---GLFLAFQypeEIPGVSNLEflrsalnarRSARGEEPLDLLDFEKLLKEKLALLDMDEEF---LNRSvnegFS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 219 GGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF---DRILVVVSHSQDFLNGVCTNIIH 285
Cdd:TIGR01978 147 GGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLNYIKPDYVH 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
98-275 |
4.05e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 45.50 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 98 GRRYGLLGLNGCGKSTLLAAIGcrELPIPEHMDIYHLSREIEASdmssleaviSCDEERLKLekeaeSLASQDDGggeql 177
Cdd:PRK13647 31 GSKTALLGPNGAGKSTLLLHLN--GIYLPQRGRVKVMGREVNAE---------NEKWVRSKV-----GLVFQDPD----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 178 DRIYE-----------RLEALDAATAEKRAAEILYGLGFnKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNH 246
Cdd:PRK13647 90 DQVFSstvwddvafgpVNMGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180 190
....*....|....*....|....*....|..
gi 1955823976 247 LDLEACVWLEENLKKFDR---ILVVVSHSQDF 275
Cdd:PRK13647 169 LDPRGQETLMEILDRLHNqgkTVIVATHDVDL 200
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
73-248 |
4.07e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 45.95 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIV----DSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPipehmdiyhlsreieasdmSSLEa 148
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhalnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERP-------------------TSGR- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 149 VISCDEERLKLEKEAESLASQDDGggeqldRIYE------------------RLEALDAATAEKRAAEIL--YGLgfnkq 208
Cdd:PRK11153 62 VLVDGQDLTALSEKELRKARRQIG------MIFQhfnllssrtvfdnvalplELAGTPKAEIKARVTELLelVGL----- 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1955823976 209 mQAKKTR---DFSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:PRK11153 131 -SDKADRypaQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
384-534 |
4.51e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 45.46 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 384 LQFVEVTFGY-TP-ENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVP------LDGM--------------- 440
Cdd:COG1101 4 LKNLSKTFNPgTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPdsgsilIDGKdvtklpeykrakyig 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 441 --------------------------------VRRHNHLRIAQFHQHLAEkLDLELsalqfmireypgneEEKMRgaigk 488
Cdd:COG1101 84 rvfqdpmmgtapsmtieenlalayrrgkrrglRRGLTKKRRELFRELLAT-LGLGL--------------ENRLD----- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1955823976 489 fglsgkaqvMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLD 534
Cdd:COG1101 144 ---------TKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
217-272 |
4.52e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.47 E-value: 4.52e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 217 FSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF-DRI-LVVVSHS 272
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLaDRLtVIIVTHN 221
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
391-562 |
5.02e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 45.01 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 391 FGYTPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHLRIAQFHQ-----------HLAEK 459
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEatrsrnrysvaYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 460 -LDLELSALQFMIREYPGNEEeKMRGAIGKFGLSGKAQVMPMK----------NLSDGQRSRVIFAWLAWRQPHLLLLDE 528
Cdd:cd03290 88 pWLLNATVEENITFGSPFNKQ-RYKAVTDACSLQPDIDLLPFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 1955823976 529 PTNHLDIETIDSLAEA-----LNEWDGGLVLVSHDFRLI 562
Cdd:cd03290 167 PFSALDIHLSDHLMQEgilkfLQDDKRTLVLVTHKLQYL 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
405-589 |
5.08e-05 |
|
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: 44.73 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 405 FGVDLDSR----IALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHN--------HLR----IAQ-------FHQHLAEKlD 461
Cdd:cd03224 17 FGVSLTVPegeiVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditglppHERaragIGYvpegrriFPELTVEE-N 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 462 LELSALQFMIREYPGNEEE---------KMRGAigkfglsgKAQvmpmkNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNH 532
Cdd:cd03224 96 LLLGAYARRRAKRKARLERvyelfprlkERRKQ--------LAG-----TLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 533 LD---IETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWVCENQAVtKWEGDIMDFKA 589
Cdd:cd03224 163 LApkiVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRV-VLEGTAAELLA 221
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
396-565 |
5.78e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.02 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 396 ENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTG----------------DLVPLDGMVRRH--------------- 444
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykilegdilfkgeSILDLEPEERAHlgiflafqypieipg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 445 ----NHLRIAQFHQHLAEKLDlELSALQF--MIREypgneeekmrgaigKFGLSGKAQVMPMKNL----SDGQRSRVIFA 514
Cdd:CHL00131 99 vsnaDFLRLAYNSKRKFQGLP-ELDPLEFleIINE--------------KLKLVGMDPSFLSRNVnegfSGGEKKRNEIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 515 WLAWRQPHLLLLDEPTNHLDIETIDSLAEALNEW---DGGLVLVSHDFRLINQV 565
Cdd:CHL00131 164 QMALLDSELAILDETDSGLDIDALKIIAEGINKLmtsENSIILITHYQRLLDYI 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
103-248 |
6.74e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.81 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 103 LLGLNGCGKSTLLAAIGCRELP-IPEHMDIYHLSREIEASDMSSLEAVISCDEERLKlekeaeSLASQddgggEQLdrIY 181
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFRSPKgVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIP------TLTVR-----EHL--MF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 182 E---RLEAlDAATAEKRAA--EILYGLGFNKqmqAKKTR--------DFSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:TIGR00955 123 QahlRMPR-RVTKKEKRERvdEVLQALGLRK---CANTRigvpgrvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
218-300 |
6.82e-05 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 45.89 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF-DRILVVVSHSQDFLNGVcTNIIHMQNRKLkIYTG 296
Cdd:TIGR01193 613 SGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLqDKTIIFVAHRLSVAKQS-DKIIVLDHGKI-IEQG 690
|
....
gi 1955823976 297 NYDQ 300
Cdd:TIGR01193 691 SHDE 694
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
400-533 |
6.84e-05 |
|
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: 45.38 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 400 YKNL-DFGVDLDSRI-ALVGPNGAGKSTLLK----LMTGDLVP-------------------------------LDGMVR 442
Cdd:COG3593 11 FRSIkDLSIELSDDLtVLVGENNSGKSSILEalrlLLGPSSSRkfdeedfylgddpdlpeieieltfgsllsrlLRLLLK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 443 RHNHLRIAQFHQHLAEKLDLELSALQFMIREY--------------PGNEEEKMRGAIgKFGLSGKAQVmPMKNLSDGQR 508
Cdd:COG3593 91 EEDKEELEEALEELNEELKEALKALNELLSEYlkelldgldlelelSLDELEDLLKSL-SLRIEDGKEL-PLDRLGSGFQ 168
|
170 180 190
....*....|....*....|....*....|..
gi 1955823976 509 SRVIFAWLAW-------RQPHLLLLDEPTNHL 533
Cdd:COG3593 169 RLILLALLSAlaelkraPANPILLIEEPEAHL 200
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
414-558 |
6.93e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 45.60 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 414 ALVGPNGAGKSTLLKLMTGDLVPLDGmvrrhnhlriaqfhQHLAEKLDLELSA-----LQFMIREYP------------- 475
Cdd:PRK11607 49 ALLGASGCGKSTLLRMLAGFEQPTAG--------------QIMLDGVDLSHVPpyqrpINMMFQSYAlfphmtveqniaf 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 476 GNEEEKM-RGAIgkfglsgKAQVMPM--------------KNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIETIDS 540
Cdd:PRK11607 115 GLKQDKLpKAEI-------ASRVNEMlglvhmqefakrkpHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
|
170 180
....*....|....*....|..
gi 1955823976 541 L----AEALNEWDGGLVLVSHD 558
Cdd:PRK11607 188 MqlevVDILERVGVTCVMVTHD 209
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
194-273 |
7.25e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.22 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 194 KRAAEILyGLGfnkQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLD--LEACVWLEenLKKFDRIL----V 267
Cdd:PRK11650 116 AEAARIL-ELE---PLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDakLRVQMRLE--IQRLHRRLkttsL 189
|
....*.
gi 1955823976 268 VVSHSQ 273
Cdd:PRK11650 190 YVTHDQ 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
98-286 |
7.69e-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: 46.16 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 98 GRRYGLLGLNGCGKSTLLAAIGCrelpipehmDIYHLSREIEASDMSSLEAvISCDEERLKLEKEAESLasqDD--GGGE 175
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTG---------DTTVTSGDATVAGKSILTN-ISDVHQNMGYCPQFDAI---DDllTGRE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 176 QLdRIYERLEALDAATAEKRAAEILYGLGFNKQMQaKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEA--CV 253
Cdd:TIGR01257 2032 HL-YLYARLRGVPAEEIEKVANWSIQSLGLSLYAD-RLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQArrML 2109
|
170 180 190
....*....|....*....|....*....|....
gi 1955823976 254 W-LEENLKKFDRILVVVSHSQDFLNGVCTNIIHM 286
Cdd:TIGR01257 2110 WnTIVSIIREGRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
94-276 |
7.85e-05 |
|
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: 44.71 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 94 ELNYGRRYGLLGLNGCGKSTLLAAIGCRELP-----IPEHMDIYHLSREIEASDMSSLEAViscdeerlklekeaesLAS 168
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPdegdiEIELDTVSYKPQYIKADYEGTVRDL----------------LSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 169 QDDGGGE------------QLDRIYERLealdaataekraaeilyglgfnkqmqakkTRDFSGGWRMRIALARALFMNPT 236
Cdd:cd03237 85 ITKDFYThpyfkteiakplQIEQILDRE-----------------------------VPELSGGELQRVAIAACLSKDAD 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1955823976 237 VLLLDEPTNHLDLEACVWLEENLKKF----DRILVVVSHsqDFL 276
Cdd:cd03237 136 IYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEH--DII 177
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
401-533 |
7.89e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.69 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 401 KNLDfGVDLDSR----IALVGPNGAGKSTLLKLMTGdLVP---------LDGMVRRHNHLR------IAQFHQHLAekLD 461
Cdd:PRK13549 19 KALD-NVSLKVRageiVSLCGENGAGKSTLMKVLSG-VYPhgtyegeiiFEGEELQASNIRdteragIAIIHQELA--LV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 462 LELSALQFMireYPGNEeekmrgaIGKFGLSG------KAQVM------------PMKNLSDGQRSRVIFAWLAWRQPHL 523
Cdd:PRK13549 95 KELSVLENI---FLGNE-------ITPGGIMDydamylRAQKLlaqlkldinpatPVGNLGLGQQQLVEIAKALNKQARL 164
|
170
....*....|
gi 1955823976 524 LLLDEPTNHL 533
Cdd:PRK13549 165 LILDEPTASL 174
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
413-558 |
8.09e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 413 IALVGPNGAGKSTLLKLMTGDLVP----------LDGMVRrhnHLRIAQFHQHLAEKLDLELSAL---QF--MIREY--- 474
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPnlgdyeeepsWDEVLK---RFRGTELQNYFKKLYNGEIKVVhkpQYvdLIPKVfkg 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 475 -------PGNEEEKMRGAIGKFGLSgkaQVM--PMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDI-------ETI 538
Cdd:PRK13409 179 kvrellkKVDERGKLDEVVERLGLE---NILdrDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIrqrlnvaRLI 255
|
170 180
....*....|....*....|
gi 1955823976 539 DSLAEalnewDGGLVLVSHD 558
Cdd:PRK13409 256 RELAE-----GKYVLVVEHD 270
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
192-291 |
8.36e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.84 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 192 AEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEA---CVWLEENLKKFDRILVV 268
Cdd:PRK13631 152 AKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGeheMMQLILDAKANNKTVFV 231
|
90 100
....*....|....*....|...
gi 1955823976 269 VSHSQDFLNGVCTNIIHMQNRKL 291
Cdd:PRK13631 232 ITHTMEHVLEVADEVIVMDKGKI 254
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
215-252 |
8.77e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 44.09 E-value: 8.77e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1955823976 215 RDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEAC 252
Cdd:PRK13539 126 GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
194-248 |
9.10e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.00 E-value: 9.10e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1955823976 194 KRAAEILYGLGFNKQMQAKKTRdFSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:PRK10584 125 NGAKALLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
73-271 |
9.19e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.39 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIP----EHMDIYHlSREIEASDMSSLEA 148
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrvEGKVTFH-GKNLYAPDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 149 ------VISCDEERLKLEKEAESLASQDDGGGEQLDRIYERlealdaatAEKRAAeiLYGLGFNKQMQAKKTrdFSGGWR 222
Cdd:PRK14243 90 rrrigmVFQKPNPFPKSIYDNIAYGARINGYKGDMDELVER--------SLRQAA--LWDEVKDKLKQSGLS--LSGGQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 223 MRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDR--ILVVVSH 271
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTH 208
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
183-277 |
1.01e-04 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 44.29 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 183 RLEALDAATAEKRAAEILYGLGFNKQMqakKTRD----FSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEAcvwLE-- 256
Cdd:COG0396 106 RGEELSAREFLKLLKEKMKELGLDEDF---LDRYvnegFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDA---LRiv 179
|
90 100
....*....|....*....|....*
gi 1955823976 257 ----ENLKKFDRILVVVSHSQDFLN 277
Cdd:COG0396 180 aegvNKLRSPDRGILIITHYQRILD 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
414-534 |
1.04e-04 |
|
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: 45.77 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 414 ALVGPNGAGKSTLLKLMTGD--LVPLDGMVRRHNHL-RIAQFHQHLA-----EKLDLELSALQFM-----IREYPGNEEE 480
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDttVTSGDATVAGKSILtNISDVHQNMGycpqfDAIDDLLTGREHLylyarLRGVPAEEIE 2048
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1955823976 481 KMRG-AIGKFGLSGKAQVMPmKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLD 534
Cdd:TIGR01257 2049 KVANwSIQSLGLSLYADRLA-GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
405-574 |
1.08e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 44.79 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 405 FGVdldsrialVGPNGAGKSTLLKLMTG--------------DLVPLDGMVRRHNHLRIAQFHQH---LAEK-------L 460
Cdd:PRK11153 34 FGV--------IGASGAGKSTLIRCINLlerptsgrvlvdgqDLTALSEKELRKARRQIGMIFQHfnlLSSRtvfdnvaL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 461 DLELSAlqfmireypgneeeKMRGAIGK--------FGLSGKAQVMPmKNLSDGQRSRVIFA-WLAWRqPHLLLLDEPTN 531
Cdd:PRK11153 106 PLELAG--------------TPKAEIKArvtellelVGLSDKADRYP-AQLSGGQKQRVAIArALASN-PKVLLCDEATS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1955823976 532 HLDIETIDSLAEAL---NEwDGGL--VLVSHDFRLINQVAQEIWVCEN 574
Cdd:PRK11153 170 ALDPATTRSILELLkdiNR-ELGLtiVLITHEMDVVKRICDRVAVIDA 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
217-280 |
1.11e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 45.29 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 217 FSGGWRMRIALARALFMNPTVLLLDEPTNHLDL-------EACVW-------------LEENLKKFDRILVVvsHsqdfl 276
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDVvtekeifESCLCklmsnktrilvtsKLEHLKKADKILLL--H----- 621
|
....
gi 1955823976 277 NGVC 280
Cdd:TIGR01271 622 EGVC 625
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
86-248 |
1.24e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.10 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 86 DLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIPehmDIYhlsrEIEASDMSSLEaviscDEERLKLEKEaes 165
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTS---GTY----RVAGQDVATLD-----ADALAQLRRE--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 166 lasqddgggeQLDRIYERLEALDAATAE------------------KRAAEILYGLGFNKQMQAKKTRdFSGGWRMRIAL 227
Cdd:PRK10535 87 ----------HFGFIFQRYHLLSHLTAAqnvevpavyaglerkqrlLRAQELLQRLGLEDRVEYQPSQ-LSGGQQQRVSI 155
|
170 180
....*....|....*....|.
gi 1955823976 228 ARALFMNPTVLLLDEPTNHLD 248
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALD 176
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
73-244 |
1.29e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 44.62 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLSVTFHG----HDliVDseLELNYGRRYGLLGLNGCGKSTLLAAI-GcreLPIPEHMDIYHLSREIE-ASDMSSL 146
Cdd:COG1129 5 LEMRGISKSFGGvkalDG--VS--LELRPGEVHALLGENGAGKSTLMKILsG---VYQPDSGEILLDGEPVRfRSPRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 147 EAVISCDEERLKLEKE---AESLAsqddgggeqLDRIYERLEALDAATAEKRAAEILYGLGFNKQMQAKkTRDFSGGWRM 223
Cdd:COG1129 78 AAGIAIIHQELNLVPNlsvAENIF---------LGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTP-VGDLSVAQQQ 147
|
170 180
....*....|....*....|.
gi 1955823976 224 RIALARALFMNPTVLLLDEPT 244
Cdd:COG1129 148 LVEIARALSRDARVLILDEPT 168
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
188-291 |
1.33e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 44.23 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 188 DAATAEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLD---LEACVWLEENL-KKFD 263
Cdd:PRK13645 122 NKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDpkgEEDFINLFERLnKEYK 201
|
90 100
....*....|....*....|....*...
gi 1955823976 264 RILVVVSHSQDFLNGVCTNIIHMQNRKL 291
Cdd:PRK13645 202 KRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
66-248 |
1.39e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 44.68 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 66 SHPLsrdIRIESLSVTFHGHD---LIVDS-ELELNYGRRYGLLGLNGCGKS-TLLAAIgcRELPIPEHM----------D 130
Cdd:COG4172 3 SMPL---LSVEDLSVAFGQGGgtvEAVKGvSFDIAAGETLALVGESGSGKSvTALSIL--RLLPDPAAHpsgsilfdgqD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 131 IYHLS----REIEASD--------MSSLEAVISCdeerlklekeaeslasqddggGEQldrIYERLE---ALDAATAEKR 195
Cdd:COG4172 78 LLGLSerelRRIRGNRiamifqepMTSLNPLHTI---------------------GKQ---IAEVLRlhrGLSGAAARAR 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 196 AAEILyglgfnKQMQ----AKKTRDF----SGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:COG4172 134 ALELL------ERVGipdpERRLDAYphqlSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
213-269 |
1.58e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 43.32 E-value: 1.58e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 213 KTRDF----SGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRILVVV 269
Cdd:PRK10908 130 KAKNFpiqlSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTV 190
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
215-259 |
1.68e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.49 E-value: 1.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1955823976 215 RDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENL 259
Cdd:PLN03211 205 RGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
218-243 |
1.71e-04 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 43.94 E-value: 1.71e-04
10 20
....*....|....*....|....*.
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEP 243
Cdd:COG4148 135 SGGERQRVAIGRALLSSPRLLLMDEP 160
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
192-291 |
2.06e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 43.66 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 192 AEKRAAEILYGLGFNKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDR---ILVV 268
Cdd:PRK13641 121 AKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVIL 200
|
90 100
....*....|....*....|...
gi 1955823976 269 VSHSQDFLNGVCTNIIHMQNRKL 291
Cdd:PRK13641 201 VTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
413-543 |
2.41e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.10 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 413 IALVGPNGAGKSTLLKLM---------TGDLVPLDGMVRRHNHLRIAQFHQ------HLAEKLDLELSALQFMIREYpgN 477
Cdd:PLN03211 97 LAVLGPSGSGKSTLLNALagriqgnnfTGTILANNRKPTKQILKRTGFVTQddilypHLTVRETLVFCSLLRLPKSL--T 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 478 EEEKMRGA---IGKFGLSGKAQVMP----MKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLD-------IETIDSLAE 543
Cdd:PLN03211 175 KQEKILVAesvISELGLTKCENTIIgnsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDataayrlVLTLGSLAQ 254
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
193-248 |
2.45e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 43.14 E-value: 2.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1955823976 193 EKRAAEILYGLGFnKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:PRK13639 115 EKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
198-250 |
2.52e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 2.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 198 EILYGLGFNKQMQaKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLE 250
Cdd:PRK13409 436 EIIKPLQLERLLD-KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
371-579 |
2.81e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.48 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 371 FRFVDVGKLPPPVLQFVEVTFGYtpenliyKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMV--------- 441
Cdd:PRK10070 22 FKYIEQGLSKEQILEKTGLSLGV-------KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiak 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 442 ------RRHNHLRIAQFHQHLA---EKLDLELSALQFMIREYPGNE-EEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRV 511
Cdd:PRK10070 95 isdaelREVRRKKIAMVFQSFAlmpHMTVLDNTAFGMELAGINAEErREKALDALRQVGLENYAHSYP-DELSGGMRQRV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955823976 512 IFAWLAWRQPHLLLLDEPTNHLD----IETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWVCENQAVTK 579
Cdd:PRK10070 174 GLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
401-571 |
2.83e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.69 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 401 KNLDFGVDLDSRIALVGPNGAGKS-TLLKLM-----TGDLVPLDGM-VRRHNHLRIAQFHQHLAEKLDLELSALQFMIRE 473
Cdd:PRK10261 33 RNLSFSLQRGETLAIVGESGSGKSvTALALMrlleqAGGLVQCDKMlLRRRSRQVIELSEQSAAQMRHVRGADMAMIFQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 474 --------YPGNEE--EKMRGAIGKFGLSGKAQVMPM-----------------KNLSDGQRSRVIFAWLAWRQPHLLLL 526
Cdd:PRK10261 113 pmtslnpvFTVGEQiaESIRLHQGASREEAMVEAKRMldqvripeaqtilsrypHQLSGGMRQRVMIAMALSCRPAVLIA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1955823976 527 DEPTNHLDIeTIDS----LAEALN-EWDGGLVLVSHDFRLINQVAQEIWV 571
Cdd:PRK10261 193 DEPTTALDV-TIQAqilqLIKVLQkEMSMGVIFITHDMGVVAEIADRVLV 241
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
407-570 |
2.91e-04 |
|
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: 42.21 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 407 VDLDSRIAL-VGPNGAGKSTLLKLM----TGDLVP-------LDGMVRRHNhlRIAQFHQHLAEKLDLELSAlqfmIREY 474
Cdd:cd03240 18 IEFFSPLTLiVGQNGAGKTTIIEALkyalTGELPPnskggahDPKLIREGE--VRAQVKLAFENANGKKYTI----TRSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 475 pgneeEKMRGAIgkF---GLSGKAQVMPMKNLSDGQRsrvIFAWLAWR---------QPHLLLLDEPTNHLDIETID-SL 541
Cdd:cd03240 92 -----AILENVI--FchqGESNWPLLDMRGRCSGGEK---VLASLIIRlalaetfgsNCGILALDEPTTNLDEENIEeSL 161
|
170 180 190
....*....|....*....|....*....|...
gi 1955823976 542 AEALNEWDGG----LVLVSHDFRLInQVAQEIW 570
Cdd:cd03240 162 AEIIEERKSQknfqLIVITHDEELV-DAADHIY 193
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
218-274 |
3.16e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 42.65 E-value: 3.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLD----LEACVWLEENLKKFDRILVVVSHSQD 274
Cdd:PRK10771 131 SGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHSLE 191
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
415-571 |
3.38e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.25 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 415 LVGPNGAGKSTLLKLMTG------------------DLVPLDGMVRR----HNHLRIAQFHQHLaekLDLELSALQFMIR 472
Cdd:PRK15093 38 LVGESGSGKSLIAKAICGvtkdnwrvtadrmrfddiDLLRLSPRERRklvgHNVSMIFQEPQSC---LDPSERVGRQLMQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 473 EYPGNEEE---------KMRGAI---GKFGLSGKAQVM---PMKnLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDIET 537
Cdd:PRK15093 115 NIPGWTYKgrwwqrfgwRKRRAIellHRVGIKDHKDAMrsfPYE-LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTT 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 1955823976 538 ---IDSLAEALNEWDG-GLVLVSHDFRLINQVAQEIWV 571
Cdd:PRK15093 194 qaqIFRLLTRLNQNNNtTILLISHDLQMLSQWADKINV 231
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
218-243 |
3.85e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 42.32 E-value: 3.85e-04
10 20
....*....|....*....|....*.
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEP 243
Cdd:COG1137 138 SGGERRRVEIARALATNPKFILLDEP 163
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
212-345 |
3.91e-04 |
|
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: 43.78 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 212 KKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLD-------LEACVWLEENLKKFDRILvvVSHSQDFLNGVcTNII 284
Cdd:TIGR00957 756 EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhiFEHVIGPEGVLKNKTRIL--VTHGISYLPQV-DVII 832
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 285 HMQNRKLKiYTGNYDQYVQtRSELEENQMKMYKWEQDQIASMKEYIARFGhGSAKLARQAQ 345
Cdd:TIGR00957 833 VMSGGKIS-EMGSYQELLQ-RDGAFAEFLRTYAPDEQQGHLEDSWTALVS-GEGKEAKLIE 890
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
98-276 |
4.41e-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: 40.82 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 98 GRRYGLLGLNGCGKSTLLAAIgCRELPIPEHMDIYhlsreieasdmssleavISCDEERlklekeaeslasqddgggeql 177
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARAL-ARELGPPGGGVIY-----------------IDGEDIL--------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 178 driyerlealdaATAEKRAAEILYGLGFNKQMQAKktrdfsggwRMRIALARALFMNPTVLLLDEPTNHLD--------- 248
Cdd:smart00382 43 ------------EEVLDQLLLIIVGGKKASGSGEL---------RLRLALALARKLKPDVLILDEITSLLDaeqeallll 101
|
170 180
....*....|....*....|....*...
gi 1955823976 249 LEACVWLEENLKKFDRILVVVSHSQDFL 276
Cdd:smart00382 102 LEELRLLLLLKSEKNLTVILTTNDEKDL 129
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
73-271 |
4.90e-04 |
|
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: 43.20 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 73 IRIESLS-VTFHGHDLIVDSELELNYGRRYGLLGLNGCGKSTLLAAIG------CRELPIPEHMDIYHLSREIEASDMSS 145
Cdd:TIGR00954 452 IKFENIPlVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyGGRLTKPAKGKLFYVPQRPYMTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 146 LEAVI---SCDEERLKLEKEAESLASQDDgggEQLDRIYERLEALDAATAEKraaEILyglgfnkqmqakktrdfSGGWR 222
Cdd:TIGR00954 532 RDQIIypdSSEDMKRRGLSDKDLEQILDN---VQLTHILEREGGWSAVQDWM---DVL-----------------SGGEK 588
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1955823976 223 MRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKFDRILVVVSH 271
Cdd:TIGR00954 589 QRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
218-268 |
4.90e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 42.54 E-value: 4.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLDL-------EACVW-------------LEENLKKFDRILVV 268
Cdd:cd03291 161 SGGQRARISLARAVYKDADLYLLDSPFGYLDVftekeifESCVCklmanktrilvtsKMEHLKKADKILIL 231
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
218-248 |
6.56e-04 |
|
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: 42.50 E-value: 6.56e-04
10 20 30
....*....|....*....|....*....|.
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
93-251 |
6.64e-04 |
|
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: 41.19 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 93 LELNYGRRYGLLGLNGCGKSTLL-----------AAIGCRELPIPEHMDIYHlsREIE-ASDMSSLEAVISCdeerlkle 160
Cdd:TIGR01189 21 FTLNAGEALQVTGPNGIGKTTLLrilagllrpdsGEVRWNGTPLAEQRDEPH--ENILyLGHLPGLKPELSA-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 161 keAESLA-SQDDGGGEQLDrIYERLEALDAATAEKRAAEILyglgfnkqmqakktrdfSGGWRMRIALARALFMNPTVLL 239
Cdd:TIGR01189 91 --LENLHfWAAIHGGAQRT-IEDALAAVGLTGFEDLPAAQL-----------------SAGQQRRLALARLWLSRRPLWI 150
|
170
....*....|..
gi 1955823976 240 LDEPTNHLDLEA 251
Cdd:TIGR01189 151 LDEPTTALDKAG 162
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
407-559 |
8.08e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.15 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 407 VDLDSRIAL-VGPNGAGKSTLL--------------KLMTGDLVPL-----------------------DGMVRRHNHLR 448
Cdd:COG0419 19 IDFDDGLNLiVGPNGAGKSTILeairyalygkarsrSKLRSDLINVgseeasvelefehggkryrierrQGEFAEFLEAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 449 IAQFHQHLAEKLDLE-LSALQFMIREYPGNEEEKMRGAIGKFGLSGK-AQVM----PMKNLSDGQRSRVIFAWLAwrqph 522
Cdd:COG0419 99 PSERKEALKRLLGLEiYEELKERLKELEEALESALEELAELQKLKQEiLAQLsgldPIETLSGGERLRLALADLL----- 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1955823976 523 LLLLDepTNHLDIETIDSLAEALNEwdggLVLVSHDF 559
Cdd:COG0419 174 SLILD--FGSLDEERLERLLDALEE----LAIITHVI 204
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
90-248 |
8.76e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.45 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 90 DSELELNYGRRYGLLGLNGCGKSTLLAAIGCReLPiPEHMDIYHLSREIEASDMSSL-EAviscdEERLKLEKE------ 162
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSAR-LA-PDAGEVHYRMRDGQLRDLYALsEA-----ERRRLLRTEwgfvhq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 163 --AESLASQDDGGGEqldrIYERLEAL---------DAATAEKRAAEIlyglgfnkqmQAKKTRD----FSGGWRMRIAL 227
Cdd:PRK11701 97 hpRDGLRMQVSAGGN----IGERLMAVgarhygdirATAGDWLERVEI----------DAARIDDlpttFSGGMQQRLQI 162
|
170 180
....*....|....*....|.
gi 1955823976 228 ARALFMNPTVLLLDEPTNHLD 248
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
413-569 |
9.13e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 42.40 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 413 IALVGPNGAGKSTLLKLM-------TG-------DLVPLDG----MVRRHNHLRIAQ-FH--QHLAEKLDLELSALqfmi 471
Cdd:PRK10535 37 VAIVGASGSGKSTLMNILgcldkptSGtyrvagqDVATLDAdalaQLRREHFGFIFQrYHllSHLTAAQNVEVPAV---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 472 reYPGNE----EEKMRGAIGKFGLSGKAQVMPmKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLDI---ETIDSLAEA 544
Cdd:PRK10535 113 --YAGLErkqrLLRAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVILADEPTGALDShsgEEVMAILHQ 189
|
170 180
....*....|....*....|....*
gi 1955823976 545 LNEWDGGLVLVSHDFRLINQvAQEI 569
Cdd:PRK10535 190 LRDRGHTVIIVTHDPQVAAQ-AERV 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
389-557 |
9.15e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 41.61 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 389 VTFGY-----TPENLIYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVrrhnhlriaqfhqhLAEKLDLE 463
Cdd:PRK13633 10 VSYKYesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV--------------YVDGLDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 464 LSALQFMIR-------EYPGN-------EE-----------------EKMRGAIGKFGLSGKAQVMPMKnLSDGQRSRVI 512
Cdd:PRK13633 76 DEENLWDIRnkagmvfQNPDNqivativEEdvafgpenlgippeeirERVDESLKKVGMYEYRRHAPHL-LSGGQKQRVA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1955823976 513 FAWLAWRQPHLLLLDEPTNHLD----IETIDSLAEaLNEWDG-GLVLVSH 557
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKE-LNKKYGiTIILITH 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
197-250 |
9.92e-04 |
|
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: 42.08 E-value: 9.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 197 AEILYGLGFNKQMQaKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLE 250
Cdd:COG1245 437 TEIIKPLGLEKLLD-KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
184-277 |
1.14e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 40.71 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 184 LEALDAATAEKRAAEILYGLGFNK-QMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF 262
Cdd:COG2401 103 IDAIGRKGDFKDAVELLNAVGLSDaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKL 182
|
90
....*....|....*....
gi 1955823976 263 DR----ILVVVSHSQDFLN 277
Cdd:COG2401 183 ARragiTLVVATHHYDVID 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
414-571 |
1.14e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.91 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 414 ALVGPNGAGKSTLLKLMTGdLVPLD-------GMVRRHNHLRIAQ------FHQHLAEKLDLELSALQFMIREYPGN--- 477
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTG-IYTRDagsilylGKEVTFNGPKSSQeagigiIHQELNLIPQLTIAENIFLGREFVNRfgr 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 478 -EEEKMRGA----IGKFGLSGKAQVMpMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHL-DIETiDSLAEALNEWDG- 550
Cdd:PRK10762 113 iDWKKMYAEadklLARLNLRFSSDKL-VGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTET-ESLFRVIRELKSq 190
|
170 180
....*....|....*....|...
gi 1955823976 551 --GLVLVSHDFRLINQVAQEIWV 571
Cdd:PRK10762 191 grGIVYISHRLKEIFEICDDVTV 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
209-250 |
1.20e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 41.26 E-value: 1.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1955823976 209 MQAKKTRD---FSGGWRMRIALARALFMNPTVLLLDEPTNHLDLE 250
Cdd:PRK13650 130 MQDFKEREparLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
406-559 |
1.24e-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: 40.11 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 406 GVDLDSR----IALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNH-LRIAQFHQHLAEKLdlelsalqFMIreyPgnEEE 480
Cdd:cd03215 18 DVSFEVRageiVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpVTRRSPRDAIRAGI--------AYV---P--EDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 481 KMRGAIGKFGLsgkAQVMPMKN-LSDGQRSRVIFA-WLAwRQPHLLLLDEPTNHLDIETIDSLAEALNEW-DGGL--VLV 555
Cdd:cd03215 85 KREGLVLDLSV---AENIALSSlLSGGNQQKVVLArWLA-RDPRVLILDEPTRGVDVGAKAEIYRLIRELaDAGKavLLI 160
|
....
gi 1955823976 556 SHDF 559
Cdd:cd03215 161 SSEL 164
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
217-318 |
1.29e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.78 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 217 FSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF---DRILVVVSHSQDFLNGVCTNIIH-MQNRKLk 292
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLmtsENSIILITHYQRLLDYIKPDYVHvMQNGKI- 230
|
90 100
....*....|....*....|....*.
gi 1955823976 293 IYTGNydqyVQTRSELEEnqmKMYKW 318
Cdd:CHL00131 231 IKTGD----AELAKELEK---KGYDW 249
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
173-248 |
1.36e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.26 E-value: 1.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955823976 173 GGEQLDRIYERLEaLDAATAEKRAAEILYGLGFNkQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLD 248
Cdd:NF000106 103 GRENLYMIGR*LD-LSRKDARARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
400-427 |
1.36e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.45 E-value: 1.36e-03
10 20
....*....|....*....|....*....
gi 1955823976 400 YKNL-DFGVDLDSRIALVGPNGAGKSTLL 427
Cdd:COG4637 10 FKSLrDLELPLGPLTVLIGANGSGKSNLL 38
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
94-356 |
1.42e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.41 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 94 ELNYGRRYGLLGLNGCGKSTLLAAIGCRELPIPEHMDIyhlsreieasdmssleaviscdeerlkleKEAESLASQDDGG 173
Cdd:PRK13545 46 EVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-----------------------------KGSAALIAISSGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 174 GEQLDRIYE-RLEALDAATAEKRAAEILYGL----GFNKQM-QAKKTrdFSGGWRMRIALARALFMNPTVLLLDEPTNHL 247
Cdd:PRK13545 97 NGQLTGIENiELKGLMMGLTKEKIKEIIPEIiefaDIGKFIyQPVKT--YSSGMKSRLGFAISVHINPDILVIDEALSVG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 248 D---LEACVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKLKIY------TGNYDQYVQtrselEENQMKMYKW 318
Cdd:PRK13545 175 DqtfTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYgdikevVDHYDEFLK-----KYNQMSVEER 249
|
250 260 270
....*....|....*....|....*....|....*...
gi 1955823976 319 EQDQiasmKEYIARFGHGSAKLARQAQSKEKTLAKMER 356
Cdd:PRK13545 250 KDFR----EEQISQFQHGLLQEDQTGRERKRKKGKKTS 283
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
401-571 |
1.45e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 41.35 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 401 KNLDfGVDLDSR----IALVGPNGAGKSTLLKLMTGdLVP---------LDGMVRRHNHLR------IAQFHQHLAekLD 461
Cdd:TIGR02633 15 KALD-GIDLEVRpgecVGLCGENGAGKSTLMKILSG-VYPhgtwdgeiyWSGSPLKASNIRdteragIVIIHQELT--LV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 462 LELSALQ--FMIRE--YPG---NEEEKMRGA---IGKFGLSGKAQVMPMKNLSDGQRSRVIFAWLAWRQPHLLLLDEPTN 531
Cdd:TIGR02633 91 PELSVAEniFLGNEitLPGgrmAYNAMYLRAknlLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1955823976 532 HL---DIETIDSLAEALNEWDGGLVLVSHDFRLINQVAQEIWV 571
Cdd:TIGR02633 171 SLtekETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICV 213
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
413-558 |
1.52e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 40.84 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 413 IALVGPNGAGKSTLLKLMTGDLVPLDGMV----RRHNHLRIAQFHQHLAEKLDLELSALQ---------------FMIRE 473
Cdd:PRK13651 36 IAIIGQTGSGKTTFIEHLNALLLPDTGTIewifKDEKNKKKTKEKEKVLEKLVIQKTRFKkikkikeirrrvgvvFQFAE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 474 YPGNEE--EK--MRGAIgKFGLSGK-AQVMPMK-----------------NLSDGQRSRVIFAWLAWRQPHLLLLDEPTN 531
Cdd:PRK13651 116 YQLFEQtiEKdiIFGPV-SMGVSKEeAKKRAAKyielvgldesylqrspfELSGGQKRRVALAGILAMEPDFLVFDEPTA 194
|
170 180 190
....*....|....*....|....*....|
gi 1955823976 532 HLD---IETIDSLAEALNEWDGGLVLVSHD 558
Cdd:PRK13651 195 GLDpqgVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
85-248 |
1.55e-03 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 40.59 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 85 HDLIVDSEL-----ELNYGRRYGLLGLNGCGKSTLLAAIgcrelpipehmdiyhlsreieaSDMSSLEAVISCDEERLKl 159
Cdd:COG4138 4 NDVAVAGRLgpisaQVNAGELIHLIGPNGAGKSTLLARM----------------------AGLLPGQGEILLNGRPLS- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 160 EKEAESLA------SQDDGGGEQLdRIYERL-----EALDAATAEKRAAEILYGLGFNKqmqaKKTRDF---SGG-W-RM 223
Cdd:COG4138 61 DWSAAELArhraylSQQQSPPFAM-PVFQYLalhqpAGASSEAVEQLLAQLAEALGLED----KLSRPLtqlSGGeWqRV 135
|
170 180 190
....*....|....*....|....*....|...
gi 1955823976 224 RIAlarALFM------NPT--VLLLDEPTNHLD 248
Cdd:COG4138 136 RLA---AVLLqvwptiNPEgqLLLLDEPMNSLD 165
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
403-472 |
1.66e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 403 LDfGVDLD----SRIALVGPNGAGKSTLL-------KLMTGDLVPLDGMVRRHNHL-----RIAQFHQHLAEKLDLELSA 466
Cdd:NF033858 17 LD-DVSLDipagCMVGLIGPDGVGKSSLLsliagarKIQQGRVEVLGGDMADARHRravcpRIAYMPQGLGKNLYPTLSV 95
|
....*....
gi 1955823976 467 ---LQFMIR 472
Cdd:NF033858 96 fenLDFFGR 104
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
402-534 |
2.14e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 402 NLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDG---MVR-----------------RHNHLRIAQFHQHLAEKLd 461
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDasvVIRgtvayvpqvswifnatvRDNILFGSPFDPERYERA- 713
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 462 LELSALQFMIREYPGNEEEKmrgaIGKFGLsgkaqvmpmkNLSDGQRSRVIFAWLAWRQPHLLLLDEPTNHLD 534
Cdd:PLN03130 714 IDVTALQHDLDLLPGGDLTE----IGERGV----------NISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
503-571 |
2.22e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 40.82 E-value: 2.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955823976 503 LSDGQRSRVIFAW-LAWRqPHLLLLDEPTNHLDIeTI-----DSLAEALNEWDGGLVLVSHDFRLINQVAQEIWV 571
Cdd:COG4172 157 LSGGQRQRVMIAMaLANE-PDLLIADEPTTALDV-TVqaqilDLLKDLQRELGMALLLITHDLGVVRRFADRVAV 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
406-569 |
2.26e-03 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 40.42 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 406 GVDLD----SRIALVGPNGAGKSTLLKLMTG-----------------DLVPLD------------GMV----------- 441
Cdd:COG0444 23 GVSFDvrrgETLGLVGESGSGKSTLARAILGllpppgitsgeilfdgeDLLKLSekelrkirgreiQMIfqdpmtslnpv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 442 -----------RRHNHLRIAQFHQHLAEKLDL-ELSALQFMIREYPgneeekmrgaigkFGLSGkaqvmpmknlsdGQRS 509
Cdd:COG0444 103 mtvgdqiaeplRIHGGLSKAEARERAIELLERvGLPDPERRLDRYP-------------HELSG------------GMRQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955823976 510 RVIFAW-LAWRqPHLLLLDEPTNHLD-------IETIDSLAEALNewdGGLVLVSHDFRLINQVAQEI 569
Cdd:COG0444 158 RVMIARaLALE-PKLLIADEPTTALDvtiqaqiLNLLKDLQRELG---LAILFITHDLGVVAEIADRV 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
401-571 |
2.26e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.92 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 401 KNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNH------------LRIAQFHQHLAekLDLELSALQ 468
Cdd:PRK09700 22 KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqLGIGIIYQELS--VIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 469 FM------IREYPG---NEEEKMRgaigkfglsGKAQVMPMK------------NLSDGQRSRVIFAWLAWRQPHLLLLD 527
Cdd:PRK09700 100 NLyigrhlTKKVCGvniIDWREMR---------VRAAMMLLRvglkvdldekvaNLSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1955823976 528 EPTNHLDIETIDSLAEALNEWDG---GLVLVSHDFRLINQVAQEIWV 571
Cdd:PRK09700 171 EPTSSLTNKEVDYLFLIMNQLRKegtAIVYISHKLAEIRRICDRYTV 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
218-251 |
2.97e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 39.73 E-value: 2.97e-03
10 20 30
....*....|....*....|....*....|....
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLDLEA 251
Cdd:PRK13648 144 SGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
188-251 |
2.99e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.42 E-value: 2.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955823976 188 DAATAEKRAAEIlyGLGFNKQMQAKKTrdFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEA 251
Cdd:PRK15439 379 ENAVLERYRRAL--NIKFNHAEQAART--LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
213-244 |
3.92e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.00 E-value: 3.92e-03
10 20 30
....*....|....*....|....*....|..
gi 1955823976 213 KTRDFSGGWRMRIALARALFMNPTVLLLDEPT 244
Cdd:COG1129 391 PVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
179-251 |
3.97e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 39.69 E-value: 3.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955823976 179 RIYErleaLDAATAEKRAAEILYGLGFNKQMQaKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEA 251
Cdd:COG4586 122 AIYR----IPDAEYKKRLDELVELLDLGELLD-TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
218-251 |
4.27e-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: 38.57 E-value: 4.27e-03
10 20 30
....*....|....*....|....*....|....
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLDLEA 251
Cdd:cd03215 106 SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
218-251 |
4.93e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.60 E-value: 4.93e-03
10 20 30
....*....|....*....|....*....|....
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLDLEA 251
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGA 430
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
216-276 |
5.25e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 38.32 E-value: 5.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955823976 216 DFSGGWRMRIALARALFMNPTVLLLDEPTNHLDLEACVWLEENLKKF----DRILVVVSHsqDFL 276
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEH--DLA 133
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
362-439 |
5.33e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 362 KVVRDKVLVFRFVDVGKLPP-PVLQFVEVTFGY-TPENL-IYKNLDFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVPLD 438
Cdd:PTZ00265 360 EIINRKPLVENNDDGKKLKDiKKIQFKNVRFHYdTRKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE 439
|
.
gi 1955823976 439 G 439
Cdd:PTZ00265 440 G 440
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
413-566 |
5.60e-03 |
|
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: 38.57 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 413 IALVGPNGAGKSTLLKLMTGDLVPLDGMVR-RHNHLRIaqfhqHLAEKLDLELSAL---------QFMiREYP------- 475
Cdd:COG4778 40 VALTGPSGAGKSTLLKCIYGNYLPDSGSILvRHDGGWV-----DLAQASPREILALrrrtigyvsQFL-RVIPrvsaldv 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 476 --------GNEEEKMRgaigkfglsGKAQVM-------------PMKNLSDGQRSRV-I---FAwlawRQPHLLLLDEPT 530
Cdd:COG4778 114 vaepllerGVDREEAR---------ARARELlarlnlperlwdlPPATFSGGEQQRVnIargFI----ADPPLLLLDEPT 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1955823976 531 NHLDIET----IDSLAEALnewDGG--LVLVSHDFRLINQVA 566
Cdd:COG4778 181 ASLDAANravvVELIEEAK---ARGtaIIGIFHDEEVREAVA 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
218-291 |
6.56e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.33 E-value: 6.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955823976 218 SGGWRMRIALARALFMNPTVLLLDEPTNHLDLEA---CVWLEENLKKFDRILVVVSHSQDFLNGVCTNIIHMQNRKL 291
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAkfeIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
404-436 |
7.71e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 7.71e-03
10 20 30
....*....|....*....|....*....|...
gi 1955823976 404 DFGVDLDSRIALVGPNGAGKSTLLKLMTGDLVP 436
Cdd:pfam13555 16 TIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVP 48
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
414-547 |
8.58e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 38.55 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955823976 414 ALVGPNGAGKSTLLKLMTGDLVPLDGMVRRHNHlRIAQFHQH----LAE------KLDLE-----LSALqfmiREYPGNE 478
Cdd:COG4152 31 GLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE-PLDPEDRRrigyLPEerglypKMKVGeqlvyLARL----KGLSKAE 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955823976 479 -EEKMRGAIGKFGLSGKAQvMPMKNLSDGQRSRV-IFAWLAwRQPHLLLLDEPTNHLDIETIDSLAEALNE 547
Cdd:COG4152 106 aKRRADEWLERLGLGDRAN-KKVEELSKGNQQKVqLIAALL-HDPELLILDEPFSGLDPVNVELLKDVIRE 174
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
174-249 |
8.97e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.07 E-value: 8.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955823976 174 GEQLD---RIYERLEALDAATAEKRAAEILYgLGFNKQMQAKKTRDFSGGWRMRIALARALFMNPTVLLLDEPTNHLDL 249
Cdd:PRK10261 124 GEQIAesiRLHQGASREEAMVEAKRMLDQVR-IPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDV 201
|
|
| |
