|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-482 |
1.04e-150 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 442.20 E-value: 1.04e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 7 LTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-LRKDIKLALVEQET---------- 75
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVsIPKGLRIGYLPQEPpldddltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 76 --------------------AAYSFADQTPAE--------------------KKLLEKWHVPLRDFHQ----LSGGEKLK 111
Cdd:COG0488 81 tvldgdaelraleaeleeleAKLAEPDEDLERlaelqeefealggweaearaEEILSGLGFPEEDLDRpvseLSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 112 ARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKGNYSGYMKF 191
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 192 REKKRLTQQREYEKQQKMVERIEAQMNglaswsekahaqstkkegfkeyhRVKAK-RTDAQIKSKQKRLEKeLEkaKAEP 270
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIR-----------------------RFRAKaRKAKQAQSRIKALEK-LE--REEP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 271 VTPEYTVRFSIDTTHKTGKRFLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV 349
Cdd:COG0488 295 PRRDKTVEIRFPPPERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPdSGTVKL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 350 SPSANIGYLTQEVFDLPLEQTP-EELFENETFKARGHVQNLMRHLGFTAAQWTEPIKHMSMGERVKIKLMAYILEEKDVL 428
Cdd:COG0488 375 GETVKIGYFDQHQEELDPDKTVlDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2828494 429 ILDEPTNHLDLPSREQLEETLSQYSGTLLAVSHDRYFLEKTTNSKLVISNNGIE 482
Cdd:COG0488 455 LLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-468 |
3.80e-69 |
|
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: 232.13 E-value: 3.80e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEV-KDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQ-ILRKDIKLALVEQE------- 74
Cdd:TIGR03719 4 IYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEaRPQPGIKVGYLPQEpqldptk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 75 -----------------------TAAYS---------FADQTPAEKKL-----------LEKWHVPLR------DFHQLS 105
Cdd:TIGR03719 84 tvrenveegvaeikdaldrfneiSAKYAepdadfdklAAEQAELQEIIdaadawdldsqLEIAMDALRcppwdaDVTKLS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 106 GGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKGNY 185
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 186 SGYMKFREkKRLTQQreyEKQqkmverieaqmnglaswsEKAHAQSTKKEgfKEYHRVKAKRTDAQIKSKQKRLEKELEK 265
Cdd:TIGR03719 244 SSWLEQKQ-KRLEQE---EKE------------------ESARQKTLKRE--LEWVRQSPKGRQAKSKARLARYEELLSQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 266 AKAEPVTpeyTVRFSIDTTHKTGKRFLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAE- 344
Cdd:TIGR03719 300 EFQKRNE---TAEIYIPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDs 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 345 GSVWVSPSANIGYLTQEVFDLPLEQTP-EELFE--------NETFKARGHVQNlmrhLGFTAAQWTEPIKHMSMGERVKI 415
Cdd:TIGR03719 377 GTIEIGETVKLAYVDQSRDALDPNKTVwEEISGgldiiklgKREIPSRAYVGR----FNFKGSDQQKKVGQLSGGERNRV 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2828494 416 KLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYSGTLLAVSHDRYFLEK 468
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDR 505
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
20-481 |
9.46e-67 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 225.16 E-value: 9.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 20 FKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI----------LRKD-----------------IKLALVE 72
Cdd:PRK15064 17 FENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVsldpnerlgkLRQDqfafeeftvldtvimghTELWEVK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 73 QE-TAAYSFADQT--------------------PAEKK---LLEKWHVPLrDFH-----QLSGGEKLKARLAKGLSEDAD 123
Cdd:PRK15064 97 QErDRIYALPEMSeedgmkvadlevkfaemdgyTAEARageLLLGVGIPE-EQHyglmsEVAPGWKLRVLLAQALFSNPD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 124 LLLLDEPTNHLDEKSLQFLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKGNYSGYMkfrekKRLTQQRey 203
Cdd:PRK15064 176 ILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYM-----TAATQAR-- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 204 EKQQKMVERIEAQMNGLASWSEKAHAQSTkkegfkeyhrvKAKrtdaQIKSKQKRLEK-ELEKAKAEP-VTPeyTVRFsi 281
Cdd:PRK15064 249 ERLLADNAKKKAQIAELQSFVSRFSANAS-----------KAK----QATSRAKQIDKiKLEEVKPSSrQNP--FIRF-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 282 DTTHKTGKRFLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWVSPSANIGYLTQ 360
Cdd:PRK15064 310 EQDKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPdSGTVKWSENANIGYYAQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 361 EvfdlpleqtPEELFENET--------FKARGHVQNLMRH-LG---FTAAQWTEPIKHMSMGERVKI---KLMayiLEEK 425
Cdd:PRK15064 390 D---------HAYDFENDLtlfdwmsqWRQEGDDEQAVRGtLGrllFSQDDIKKSVKVLSGGEKGRMlfgKLM---MQKP 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2828494 426 DVLILDEPTNHLDLPSREQLEETLSQYSGTLLAVSHDRYFLEKTTNSKLVISNNGI 481
Cdd:PRK15064 458 NVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-466 |
2.23e-63 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 216.91 E-value: 2.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIV-TLTNVSYEV-KDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQ-ILRKDIKLALVEQE--- 74
Cdd:PRK11819 2 MAQYIyTMNRVSKVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIKVGYLPQEpql 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 75 ---------------------------TAAYSFA----DQTPAEK-KLLEK------WHV---------PLR------DF 101
Cdd:PRK11819 82 dpektvrenveegvaevkaaldrfneiYAAYAEPdadfDALAAEQgELQEIidaadaWDLdsqleiamdALRcppwdaKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 102 HQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIEF 181
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 182 KGNYSGYMKFREkKRLTQQreyEKQqkmverieaqmnglaswsEKAHAQSTKKEgfKEYHRVKAKRTDAQIKSKQKRLEK 261
Cdd:PRK11819 242 EGNYSSWLEQKA-KRLAQE---EKQ------------------EAARQKALKRE--LEWVRQSPKARQAKSKARLARYEE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 262 ELEKA------KAE---PVTPeytvrfsidtthKTGKRFLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTT 332
Cdd:PRK11819 298 LLSEEyqkrneTNEifiPPGP------------RLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKST 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 333 LLNIILGQETA-EGSVWVSPSANIGYLTQEVFDLPLEQTpeeLFE------------NETFKARGHVQNlmrhLGFTAAQ 399
Cdd:PRK11819 366 LFKMITGQEQPdSGTIKIGETVKLAYVDQSRDALDPNKT---VWEeisggldiikvgNREIPSRAYVGR----FNFKGGD 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 400 WTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYSGTLLAVSHDRYFL 466
Cdd:PRK11819 439 QQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFL 505
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-541 |
8.06e-63 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 217.13 E-value: 8.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-LRKDIKLALVEQ------ETA 76
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiYEQDLIVARLQQdpprnvEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 77 AYSFADQTPAEK-KLLEKWHVPLRDF--------------------HQ--------------------------LSGGEK 109
Cdd:PRK11147 83 VYDFVAEGIEEQaEYLKRYHDISHLVetdpseknlnelaklqeqldHHnlwqlenrinevlaqlgldpdaalssLSGGWL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 110 LKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKGNYSGYM 189
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 190 KfrekkrltqqreyEKQQKMveRIEAQMNglASWSEK-AHAQSTKKEGfkeyhrVKAKRTDAQiksKQKRLEKELEKAKA 268
Cdd:PRK11147 243 L-------------EKEEAL--RVEELQN--AEFDRKlAQEEVWIRQG------IKARRTRNE---GRVRALKALRRERS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 269 EPVTPEYTVRFSIDTTHKTGKRFLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAE-GSV 347
Cdd:PRK11147 297 ERREVMGTAKMQVEEASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADsGRI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 348 WVSPSANIGYLTQEVFDLPLEQTPEE-LFENetfKARGHVQNLMRH-LG------FTAAQWTEPIKHMSMGERVKIKLMA 419
Cdd:PRK11147 377 HCGTKLEVAYFDQHRAELDPEKTVMDnLAEG---KQEVMVNGRPRHvLGylqdflFHPKRAMTPVKALSGGERNRLLLAR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 420 YILEEKDVLILDEPTNHLDLPSREQLEETLSQYSGTLLAVSHDRYFLEKTTNSKLVISNNGI------------EKQLND 487
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKigryvggyhdarQQQAQY 533
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 488 VPSE---RNEREELRLKLETERQEVLGKLSFmtpndKGYKELDQafneLTKRIKELD 541
Cdd:PRK11147 534 LALKqpaVKKKEEAAAPKAETVKRSSKKLSY-----KLQRELEQ----LPQLLEDLE 581
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-471 |
6.92e-60 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 209.26 E-value: 6.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 24 NASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-LRKDIKLALVEQETAAYSfadqTPA--------------EK 88
Cdd:PRK10636 21 TATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtFPGNWQLAWVNQETPALP----QPAleyvidgdreyrqlEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 89 KL---------------------LEKWHV--------------------PLRDFhqlSGGEKLKARLAKGLSEDADLLLL 127
Cdd:PRK10636 97 QLhdanerndghaiatihgkldaIDAWTIrsraasllhglgfsneqlerPVSDF---SGGWRMRLNLAQALICRSDLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 128 DEPTNHLDEKSLQFLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKGNYSGYMKFREKKRLTQQREYEKQQ 207
Cdd:PRK10636 174 DEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQAMYESQQ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 208 KMVerieaqmnglaswsekAHAQSTkkegfkeYHRVKAKRTDA-QIKSKQKRLEKELEKAKAEPVTPeytVRFSIDTTHK 286
Cdd:PRK10636 254 ERV----------------AHLQSY-------IDRFRAKATKAkQAQSRIKMLERMELIAPAHVDNP---FHFSFRAPES 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 287 TGKRFLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ-ETAEGSVWVSPSANIGYLTQEVFD- 364
Cdd:PRK10636 308 LPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGElAPVSGEIGLAKGIKLGYFAQHQLEf 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 365 LPLEQTPEE----LFENETfkarghVQNLMRHL---GFTAAQWTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHL 437
Cdd:PRK10636 388 LRADESPLQhlarLAPQEL------EQKLRDYLggfGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
490 500 510
....*....|....*....|....*....|....
gi 2828494 438 DLPSREQLEETLSQYSGTLLAVSHDRYFLEKTTN 471
Cdd:PRK10636 462 DLDMRQALTEALIDFEGALVVVSHDRHLLRSTTD 495
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
294-513 |
2.92e-57 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 199.52 E-value: 2.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 294 VQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWVSPSANIGYLTQEVFDLP------ 366
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPdSGEVSIPKGLRIGYLPQEPPLDDdltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 367 -----------LEQTPEEL-----FENETFKARGHVQNLMRH----------------LGFTAAQWTEPIKHMSMGERVK 414
Cdd:COG0488 81 tvldgdaelraLEAELEELeaklaEPDEDLERLAELQEEFEAlggweaearaeeilsgLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 415 IKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYSGTLLAVSHDRYFLEKTTNSKLVISNNGI----------EKQ 484
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLtlypgnysayLEQ 240
|
250 260
....*....|....*....|....*....
gi 2828494 485 lndvpseRNEREELRLKLETERQEVLGKL 513
Cdd:COG0488 241 -------RAERLEQEAAAYAKQQKKIAKE 262
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
292-480 |
9.46e-56 |
|
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: 183.80 E-value: 9.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWVSPSANIGYLTQevfdlpleqt 370
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPdEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 371 peelfenetfkarghvqnlmrhlgftaaqwtepikhMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLS 450
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180 190
....*....|....*....|....*....|
gi 2828494 451 QYSGTLLAVSHDRYFLEKTTNSKLVISNNG 480
Cdd:cd03221 115 EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-177 |
1.22e-55 |
|
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: 183.42 E-value: 1.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDiklalveQETAAYsfadqt 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-------TVKIGY------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 85 paekkllekwhvplrdFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLKHYNGTVILVSHDRYFLD 164
Cdd:cd03221 68 ----------------FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLD 131
|
170
....*....|...
gi 2828494 165 EAATKIWSLEDQT 177
Cdd:cd03221 132 QVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-190 |
3.73e-50 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 180.26 E-value: 3.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 2 KEIVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR-KDIKLALVEQETAAYSf 80
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKIGYFDQHQEELD- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 81 ADQTPAE--KKLLEKWH-VPLRDF---------------HQLSGGEklKAR--LAKGLSEDADLLLLDEPTNHLDEKSLQ 140
Cdd:COG0488 392 PDKTVLDelRDGAPGGTeQEVRGYlgrflfsgddafkpvGVLSGGE--KARlaLAKLLLSPPNVLLLDEPTNHLDIETLE 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2828494 141 FLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKGNYSGYMK 190
Cdd:COG0488 470 ALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
98-477 |
6.02e-43 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 163.11 E-value: 6.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 98 LRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQT 177
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 178 LIEFKGNYSGYMKFREKKRLTQQREYEKQQKmverieaqmnglaswsEKAHAQStkkegFKEYHRVKAKRTdAQIKSKQK 257
Cdd:PLN03073 419 LVTYKGDYDTFERTREEQLKNQQKAFESNER----------------SRSHMQA-----FIDKFRYNAKRA-SLVQSRIK 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 258 RLEKeLEKAKAEPVTPEYTVRFSIdTTHKTGKRFLEVQNVTKAF-GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNI 336
Cdd:PLN03073 477 ALDR-LGHVDAVVNDPDYKFEFPT-PDDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKL 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 337 ILGQ-ETAEGSVWVSPSANIGYLTQEVFD-LPLEQTPeELFENETF------KARGHVQNlmrhLGFTAAQWTEPIKHMS 408
Cdd:PLN03073 555 ISGElQPSSGTVFRSAKVRMAVFSQHHVDgLDLSSNP-LLYMMRCFpgvpeqKLRAHLGS----FGVTGNLALQPMYTLS 629
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2828494 409 MGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYSGTLLAVSHDRYFLEKTTNSKLVIS 477
Cdd:PLN03073 630 GGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVS 698
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-179 |
1.87e-35 |
|
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: 131.02 E-value: 1.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 6 TLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL----------RKDI--KLALVEQ 73
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILldgkdlaslsPKELarKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 ---ETAAYSFADqtpaekkllekwhvplRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKS----LQfLIQQL 146
Cdd:cd03214 81 aleLLGLAHLAD----------------RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHqielLE-LLRRL 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 2828494 147 KHYNG-TVILVSHDryfLDEA---ATKIWSLEDQTLI 179
Cdd:cd03214 144 ARERGkTVVMVLHD---LNLAaryADRVILLKDGRIV 177
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-167 |
7.19e-35 |
|
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: 131.70 E-value: 7.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL----------RKDI--KLALV 71
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlaslsRRELarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 72 EQETAA-----------------------YSFADQTPAEK--KLLEKWHVPLRDFHQLSGGEKLKARLAKGLSEDADLLL 126
Cdd:COG1120 81 PQEPPApfgltvrelvalgryphlglfgrPSAEDREAVEEalERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2828494 127 LDEPTNHLDEKSlQF----LIQQLKHYNG-TVILVSHDryfLDEAA 167
Cdd:COG1120 161 LDEPTSHLDLAH-QLevleLLRRLARERGrTVVMVLHD---LNLAA 202
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
292-467 |
7.50e-35 |
|
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: 130.29 E-value: 7.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV----------SPSANIGYLTQ 360
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPsAGEVLWngepirdareDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 361 EVfDLPLEQTPEelfENETFKARGH--------VQNLMRHLGFTAAQWTePIKHMSMGERVKIKLMAYILEEKDVLILDE 432
Cdd:COG4133 83 AD-GLKPELTVR---ENLRFWAALYglradreaIDEALEAVGLAGLADL-PVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 2828494 433 PTNHLDLPSREQLEETLSQYS---GTLLAVSHDRYFLE 467
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELA 195
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-462 |
7.72e-33 |
|
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: 131.56 E-value: 7.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVKDQTVF--KHVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDLAPAQGQI----------------- 61
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVPavDGVSLTIAPGETVALVGESGSGKSTLALAL-MGLLPHGGRIsgevlldgrdllelsea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 62 -LRKDIklALVEQETAA----YSFADQ----------TPAE-----KKLLEKWHVPL---RDFHQLSGGEKLKARLAKGL 118
Cdd:COG1123 80 lRGRRI--GMVFQDPMTqlnpVTVGDQiaealenlglSRAEararvLELLEAVGLERrldRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 119 SEDADLLLLDEPTNHLD---EKSLQFLIQQL-KHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIEfkgnysgymkfrek 194
Cdd:COG1123 158 ALDPDLLIADEPTTALDvttQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVE-------------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 195 krltqqreyekqQKMVERIEAQMNGLAswsekahaqstkkegfkeyhrvkakrtdAQIKSKQKRLEKELEKAKAEPVtpe 274
Cdd:COG1123 224 ------------DGPPEEILAAPQALA----------------------------AVPRLGAARGRAAPAAAAAEPL--- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 275 ytvrfsidtthktgkrfLEVQNVTKAF-----GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVW 348
Cdd:COG1123 261 -----------------LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGlLRPTSGSIL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 349 V--------SPSA------NIGYLTQE----------VFDL---PLEQ----TPEElfenetfkARGHVQNLMRHLGFTA 397
Cdd:COG1123 324 FdgkdltklSRRSlrelrrRVQMVFQDpysslnprmtVGDIiaePLRLhgllSRAE--------RRERVAELLERVGLPP 395
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 398 AQWTEPIKHMSMGERVKIKL-MAYILeEKDVLILDEPTNHLDLPSREQLEETL----SQYSGTLLAVSHD 462
Cdd:COG1123 396 DLADRYPHELSGGQRQRVAIaRALAL-EPKLLILDEPTSALDVSVQAQILNLLrdlqRELGLTYLFISHD 464
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-175 |
1.84e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 120.69 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 6 TLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDL-APAQGQI--------------LRKDIklAL 70
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRAL-ADLdPPTSGEIyldgkplsampppeWRRQV--AY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 71 VEQETA------------AYSFADQTPAE---KKLLEKWHVPL----RDFHQLSGGEKLKARLAKGLSEDADLLLLDEPT 131
Cdd:COG4619 79 VPQEPAlwggtvrdnlpfPFQLRERKFDReraLELLERLGLPPdildKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2828494 132 NHLDEKS----LQFLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLED 175
Cdd:COG4619 159 SALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-175 |
2.60e-31 |
|
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: 118.89 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 6 TLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLAlveqetaaysfadqtp 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 86 aeKKLLEKWHVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLKHYNG---TVILVSHDRYF 162
Cdd:cd00267 65 --KLPLEELRRRIGYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPEL 142
|
170
....*....|...
gi 2828494 163 LDEAATKIWSLED 175
Cdd:cd00267 143 AELAADRVIVLKD 155
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
292-480 |
4.40e-31 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 118.65 E-value: 4.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV----------SPSANIGYLTQ 360
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPdSGEIKVlgkdikkepeEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 361 EVFdlpleqtpeeLFENETFKarghvQNLmrhlgftaaqwtepikHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLP 440
Cdd:cd03230 81 EPS----------LYENLTVR-----ENL----------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2828494 441 SREQLEETLSQYS---GTLLAVSHDRYFLEKTTNsKLVISNNG 480
Cdd:cd03230 130 SRREFWELLRELKkegKTILLSSHILEEAERLCD-RVAILNNG 171
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
292-462 |
4.80e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 120.55 E-value: 4.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV----------SPSANIGYLTQ 360
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPtSGEVRVlgedvardpaEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 361 EvFDLPLEQTPEE-------LFENETFKARGHVQNLMRHLGFTAAQwTEPIKHMSMGERVKIKLMAYILEEKDVLILDEP 433
Cdd:COG1131 81 E-PALYPDLTVREnlrffarLYGLPRKEARERIDELLELFGLTDAA-DRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 2828494 434 TNHLDLPSREQLEETLSQYSG---TLLAVSHD 462
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAegkTVLLSTHY 190
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-159 |
1.54e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.42 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------RKDIKLALVEQ 73
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkpprRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 -ETAAYSF------------------------ADQTPAEK-----KLLEKWHvplRDFHQLSGGEKLKARLAKGLSEDAD 123
Cdd:COG1121 83 rAEVDWDFpitvrdvvlmgrygrrglfrrpsrADREAVDEalervGLEDLAD---RPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 2828494 124 LLLLDEPTNHLDEKSLQF---LIQQLKHYNGTVILVSHD 159
Cdd:COG1121 160 LLLLDEPFAGVDAATEEAlyeLLRELRREGKTILVVTHD 198
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
307-435 |
3.22e-30 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 115.44 E-value: 3.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 307 FKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSVWV-----------SPSANIGYLTQEVFDLPLEQTPEEL 374
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLdgqdltdderkSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 375 FENETFKARGH------VQNLMRHLGFTAAQ---WTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTN 435
Cdd:pfam00005 81 RLGLLLKGLSKrekdarAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
292-481 |
4.24e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 117.22 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWV--------SPSA---NIGYLT 359
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADlDPPTSGEIYLdgkplsamPPPEwrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 360 QEVFdlPLEQTPEELFEnETFKARG------HVQNLMRHLGFTAAQWTEPIKHMSMGERVKIKLMAYILEEKDVLILDEP 433
Cdd:COG4619 81 QEPA--LWGGTVRDNLP-FPFQLRErkfdreRALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2828494 434 TNHLDLPSREQLEETLSQYS----GTLLAVSHDRYFLEKTTNSKLVISNNGI 481
Cdd:COG4619 158 TSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
295-508 |
1.08e-29 |
|
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: 122.74 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 295 QNVTKAF-GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWVSPSANIGYLTQE--------VFD 364
Cdd:TIGR03719 8 NRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDfNGEARPQPGIKVGYLPQEpqldptktVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 365 LPLEQTPE---------ELFE---------NETFKARGHVQNLMRHLGF--------TAAQ------WTEPIKHMSMGER 412
Cdd:TIGR03719 88 NVEEGVAEikdaldrfnEISAkyaepdadfDKLAAEQAELQEIIDAADAwdldsqleIAMDalrcppWDADVTKLSGGER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 413 VKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYSGTLLAVSHDRYFLEKTTNSKLVIS-NNGIekqlndvPSE 491
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDrGRGI-------PWE 240
|
250 260
....*....|....*....|..
gi 2828494 492 RN-----EREELRLKLEtERQE 508
Cdd:TIGR03719 241 GNysswlEQKQKRLEQE-EKEE 261
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-197 |
1.97e-29 |
|
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: 121.97 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-LRKDIKLALVEQETAAYSfADQTPAE 87
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIeIGETVKLAYVDQSRDALD-PNKTVWE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 88 K-------KLLEKWHVPLRDF---------------HQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQ 145
Cdd:TIGR03719 406 EisggldiIKLGKREIPSRAYvgrfnfkgsdqqkkvGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEA 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2828494 146 LKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIE-FKGNYSGYMKFReKKRL 197
Cdd:TIGR03719 486 LLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEwFEGNFSEYEEDK-KRRL 537
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-275 |
4.12e-29 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 121.60 E-value: 4.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 7 LTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIlRKDIKLALveqetaAYsFaDQTPA 86
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTKLEV------AY-F-DQHRA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 87 ----EKKLLE--------------KWHVP--LRDF-----------HQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD 135
Cdd:PRK11147 393 eldpEKTVMDnlaegkqevmvngrPRHVLgyLQDFlfhpkramtpvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 136 EKSLQFLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLI-EFKGnysGYMKFRekkrltQQRE--YEKQQKMVER 212
Cdd:PRK11147 473 VETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIgRYVG---GYHDAR------QQQAqyLALKQPAVKK 543
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 213 IEAQmnglASWSEKAHAQSTKKEGFKEyhrvkaKRTDAQIKSKQKRLEKELEKAKAEPVTPEY 275
Cdd:PRK11147 544 KEEA----AAPKAETVKRSSKKLSYKL------QRELEQLPQLLEDLEAEIEALQAQVADADF 596
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-190 |
6.29e-29 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 120.38 E-value: 6.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-LRKDIKLALVEQETAAYsFADq 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYYAQDHAYD-FEN- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 84 tpaEKKLLE---KWHVPLRD------------FHQ---------LSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSL 139
Cdd:PRK15064 398 ---DLTLFDwmsQWRQEGDDeqavrgtlgrllFSQddikksvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESI 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2828494 140 QFLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKGNYSGYMK 190
Cdd:PRK15064 475 ESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLR 525
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-166 |
8.07e-29 |
|
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: 112.49 E-value: 8.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL---------RKDIK--LALVEQ 73
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkdikkePEEVKrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 ETAAYsfadqtpaekkllekWHVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLKHYN--- 150
Cdd:cd03230 81 EPSLY---------------ENLTVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKkeg 145
|
170
....*....|....*.
gi 2828494 151 GTVILVSHDryfLDEA 166
Cdd:cd03230 146 KTILLSSHI---LEEA 158
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
292-462 |
1.86e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 113.65 E-value: 1.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSVWV------SPSANIGYLTQ-EVF 363
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPpTSGTVRLfgkpprRARRRIGYVPQrAEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 364 D--LPLeqTPEE-----------LFENETFKARGHVQNLMRHLGfTAAQWTEPIKHMSMGE--RVkikLMAYIL-EEKDV 427
Cdd:COG1121 87 DwdFPI--TVRDvvlmgrygrrgLFRRPSRADREAVDEALERVG-LEDLADRPIGELSGGQqqRV---LLARALaQDPDL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 2828494 428 LILDEPTNHLDLPSREQLEETLSQYSG---TLLAVSHD 462
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHD 198
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-175 |
1.14e-27 |
|
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: 110.25 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 7 LTNVS--YEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDIKLALVEQ--ETAAYSF 80
Cdd:cd03225 2 LKNLSfsYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdGKDLTKLSLKElrRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 81 ---ADQ----TPAE--------------------KKLLEK---WHVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEP 130
Cdd:cd03225 82 qnpDDQffgpTVEEevafglenlglpeeeieervEEALELvglEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2828494 131 TNHLDEKSLQFL---IQQLKHYNGTVILVSHDRYFLDEAATKIWSLED 175
Cdd:cd03225 162 TAGLDPAGRRELlelLKKLKAEGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-159 |
2.46e-27 |
|
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: 109.55 E-value: 2.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 7 LTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKL-------ALVEQ-ETAAY 78
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLekerkriGYVPQrRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 79 SF-----------------------------ADQTPAEKKLLEKWHVPLRdfhQLSGGEKLKARLAKGLSEDADLLLLDE 129
Cdd:cd03235 82 DFpisvrdvvlmglyghkglfrrlskadkakVDEALERVGLSELADRQIG---ELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190
....*....|....*....|....*....|...
gi 2828494 130 PTNHLD---EKSLQFLIQQLKHYNGTVILVSHD 159
Cdd:cd03235 159 PFAGVDpktQEDIYELLRELRREGMTILVVTHD 191
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
292-499 |
3.19e-27 |
|
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: 109.95 E-value: 3.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV----------SPSANIGYLTQ 360
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPdSGSILIdgedvrkeprEARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 361 EvFDLPLEQTPEE-------LFENETFKARGHVQNLMRHLGFTAAQwTEPIKHMSMGERVKIKLMAYILEEKDVLILDEP 433
Cdd:COG4555 82 E-RGLYDRLTVREniryfaeLYGLFDEELKKRIEELIELLGLEEFL-DRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2828494 434 TNHLDLPSREQLEETLSQYSG---TLLAVSHDRYFLEKTTNsKLVISNNG--IEKQLNDVPSERNEREELR 499
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCD-RVVILHKGkvVAQGSLDELREEIGEENLE 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
293-478 |
3.25e-27 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 107.33 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 293 EVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSVWVSPsanigyltQEVFDLPLEQtp 371
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEILIDG--------KDIAKLPLEE-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 372 eelfenetfkarghvqnLMRHLGFtaaqwtepIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQ 451
Cdd:cd00267 71 -----------------LRRRIGY--------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRE 125
|
170 180 190
....*....|....*....|....*....|
gi 2828494 452 YSG---TLLAVSHDRYFLEKTTNSKLVISN 478
Cdd:cd00267 126 LAEegrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-175 |
4.76e-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: 108.34 E-value: 4.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVE---QETAAYS-- 79
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARedyRRRLAYLgh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 ----FADQTPAE------------------KKLLEKWH-VPLRD--FHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHL 134
Cdd:COG4133 83 adglKPELTVREnlrfwaalyglradreaiDEALEAVGlAGLADlpVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2828494 135 DEKSLQFLIQQLKHYN---GTVILVSHDRyfLDEAATKIWSLED 175
Cdd:COG4133 163 DAAGVALLAELIAAHLargGAVLLTTHQP--LELAAARVLDLGD 204
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
291-461 |
8.53e-27 |
|
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: 109.02 E-value: 8.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 291 FLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNII--------------LGQETAEGSVW-VSPsaNI 355
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItgdlpptygndvrlFGERRGGEDVWeLRK--RI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 356 GYLTQEVF-DLPLEQTPEE-----------LFENETFKARGHVQNLMRHLGFTA-AQwtEPIKHMSMGERVKI----KLM 418
Cdd:COG1119 81 GLVSPALQlRFPRDETVLDvvlsgffdsigLYREPTDEQRERARELLELLGLAHlAD--RPFGTLSQGEQRRVliarALV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 419 AyileEKDVLILDEPTNHLDLPSREQLEETLSQYSG----TLLAVSH 461
Cdd:COG1119 159 K----DPELLILDEPTAGLDLGARELLLALLDKLAAegapTLVLVTH 201
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
293-462 |
1.94e-26 |
|
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: 105.98 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 293 EVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWvspsanigyltqeVFDLPLEQTP 371
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGlLKPSSGEIL-------------LDGKDLASLS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 372 EElfenETFKARGHVQNLMRHLGFTA-AQwtEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLS 450
Cdd:cd03214 68 PK----ELARKIAYVPQALELLGLAHlAD--RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLR 141
|
170
....*....|....*.
gi 2828494 451 QYSG----TLLAVSHD 462
Cdd:cd03214 142 RLARergkTVVMVLHD 157
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-197 |
2.90e-26 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 112.52 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKD-IKLALVEQetaaysFADQTPAE 87
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGEtVKLAYVDQ------SRDALDPN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 88 KKLLE------------KWHVPLR------DFH---------QLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQ 140
Cdd:PRK11819 403 KTVWEeisggldiikvgNREIPSRayvgrfNFKggdqqkkvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLR 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2828494 141 FLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIE-FKGNYSGYMKFReKKRL 197
Cdd:PRK11819 483 ALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDSQVEwFEGNFQEYEEDK-KRRL 539
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
292-462 |
4.66e-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: 107.05 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWV--------SPSA---NIGYLT 359
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGlLKPSSGEVLLdgrdlaslSRRElarRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 360 QE---VFDLpleqTPEEL-----------FENETFKARGHVQNLMRHLGfTAAQWTEPIKHMSMGERVKIKL-MAyILEE 424
Cdd:COG1120 82 QEppaPFGL----TVRELvalgryphlglFGRPSAEDREAVEEALERTG-LEHLADRPVDELSGGERQRVLIaRA-LAQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2828494 425 KDVLILDEPTNHLDLPSREQLEETLSQYSG----TLLAVSHD 462
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARergrTVVMVLHD 197
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
10-274 |
1.11e-25 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 111.42 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 10 VSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-LRKDIKLALVEQETAAYSFADQTP--- 85
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLRADESPlqh 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 86 ----AEKKLLEKwhvpLRDF---------------HQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQL 146
Cdd:PRK10636 398 larlAPQELEQK----LRDYlggfgfqgdkvteetRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 147 KHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKGNYSGYMKFrekkrLTQQREYEKQQKmverieaqmnglaswSEK 226
Cdd:PRK10636 474 IDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQW-----LSDVQKQENQTD---------------EAP 533
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2828494 227 AHAQSTKKEGFKEYHRVKAK-RTDAQIKSKQ-KRLEKELEKAKAEPVTPE 274
Cdd:PRK10636 534 KENNANSAQARKDQKRREAElRTQTQPLRKEiARLEKEMEKLNAQLAQAE 583
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-167 |
1.87e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.77 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 16 DQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRK-DIKLALVEQETAA----------------- 77
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAgGARVAYVPQRSEVpdslpltvrdlvamgrw 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 78 --------YSFADQTPAEKKL-------LEKwhvplRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFL 142
Cdd:NF040873 84 arrglwrrLTRDDRAAVDDALervgladLAG-----RQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180
....*....|....*....|....*...
gi 2828494 143 IQQLKHYNG---TVILVSHDryfLDEAA 167
Cdd:NF040873 159 IALLAEEHArgaTVVVVTHD---LELVR 183
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-180 |
1.89e-24 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 107.16 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVS--YEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRKdiKL 68
Cdd:COG4987 334 LELEDVSfrYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdlrdldeddLRR--RI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 ALVEQETAAYS--------FADQTPAEKKL---LEKwhVPLRDF----------------HQLSGGEKlkARL--AKGLS 119
Cdd:COG4987 412 AVVPQRPHLFDttlrenlrLARPDATDEELwaaLER--VGLGDWlaalpdgldtwlgeggRRLSGGER--RRLalARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 120 EDADLLLLDEPTNHLDEKSLQFLIQQLKHY--NGTVILVSHDRYFLdEAATKIWSLEDQTLIE 180
Cdd:COG4987 488 RDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAGL-ERMDRILVLEDGRIVE 549
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-175 |
3.79e-24 |
|
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: 98.99 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVS--YEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRKDIkl 68
Cdd:cd03228 1 IEFKNVSfsYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgvdlrdldlesLRKNI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 ALVEQETaaYSFADqtpaekkllekwhvPLRDfHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD---EKSLQFLIQQ 145
Cdd:cd03228 79 AYVPQDP--FLFSG--------------TIRE-NILSGGQRQRIAIARALLRDPPILILDEATSALDpetEALILEALRA 141
|
170 180 190
....*....|....*....|....*....|
gi 2828494 146 LKHyNGTVILVSHdRYFLDEAATKIWSLED 175
Cdd:cd03228 142 LAK-GKTVIVIAH-RLSTIRDADRIIVLDD 169
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-179 |
4.05e-24 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 100.87 E-value: 4.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQT-VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRKDIKL- 68
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlvdgkditkknlreLRRKVGLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 ----------ALVEQETAaysFA----DQTPAE-----KKLLEKwhVPLRDF-----HQLSGGEKLKARLAKGLSEDADL 124
Cdd:COG1122 81 fqnpddqlfaPTVEEDVA---FGpenlGLPREEirervEEALEL--VGLEHLadrppHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2828494 125 LLLDEPTNHLDEKSLQFLIQQLKHYNG---TVILVSHDRYFLDEAATKIWSLEDQTLI 179
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
293-462 |
4.74e-24 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 100.30 E-value: 4.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 293 EVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSVWVSP------SANIGYLTQ--EV- 362
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKpTSGSIRVFGkplekeRKRIGYVPQrrSId 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 363 FDLPLeqTPEEL-----------FENETFKARGHVQNLMRHLGFTAAqWTEPIKHMSMGERVKIkLMAYIL-EEKDVLIL 430
Cdd:cd03235 81 RDFPI--SVRDVvlmglyghkglFRRLSKADKAKVDEALERVGLSEL-ADRQIGELSGGQQQRV-LLARALvQDPDLLLL 156
|
170 180 190
....*....|....*....|....*....|....*
gi 2828494 431 DEPTNHLDLPSREQLEETLSQYSG---TLLAVSHD 462
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRRegmTILVVTHD 191
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-166 |
1.54e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 99.37 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL---------RKDIK--LALVEQ 73
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvardPAEVRrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 ETAAYSF---------------ADQTPAEKK---LLEK---WHVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTN 132
Cdd:COG1131 81 EPALYPDltvrenlrffarlygLPRKEARERideLLELfglTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 2828494 133 HLD-EKSLQF--LIQQLKHYNGTVILVSHDryfLDEA 166
Cdd:COG1131 161 GLDpEARRELweLLRELAAEGKTVLLSTHY---LEEA 194
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-180 |
1.62e-23 |
|
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: 99.55 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 6 TLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDI-----------KLALVEQE 74
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdvrkeprearrQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 75 TAAYSF----------------ADQTPAEK--KLLEKwhVPLRDF-----HQLSGGEKLKARLAKGLSEDADLLLLDEPT 131
Cdd:COG4555 83 RGLYDRltvreniryfaelyglFDEELKKRieELIEL--LGLEEFldrrvGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2828494 132 NHLDEKSLQFL---IQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:COG4555 161 NGLDVMARRLLreiLRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVA 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-466 |
1.62e-23 |
|
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: 104.11 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIH--NDLAPAQGQIL-------------------- 62
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmDQYEPTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 63 -----------------------RKDIK----------LALVEQET-----------AAYSFADQTPAEKKLLEKWHVPL 98
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsdklRRRIRkriaimlqrtFALYGDDTvldnvlealeeIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 99 RDFH---QLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQF----LIQQLKHYNGTVILVSHDRYFLDEAATKiw 171
Cdd:TIGR03269 161 RITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDLSDK-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 172 sledqtliefkgnysgymkfrekkrltqqreyekqqkmverieaqmnglASWSEKAhaqSTKKEGfkeyhrvkakrTDAQ 251
Cdd:TIGR03269 239 -------------------------------------------------AIWLENG---EIKEEG-----------TPDE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 252 IKSKQKRLEKELEKAKAEPVtpeytvrfsidtthktGKRFLEVQNVTKAFG--ERTLFK---NANFTIQHGEKVAIIGPN 326
Cdd:TIGR03269 256 VVAVFMEGVSEVEKECEVEV----------------GEPIIKVRNVSKRYIsvDRGVVKavdNVSLEVKEGEIFGIVGTS 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 327 GSGKTTLLNIILG-QETAEGSVWV------------------SPSANIGYLTQEVFDLPLEQTPEELFEN------ETFK 381
Cdd:TIGR03269 320 GAGKTTLSKIIAGvLEPTSGEVNVrvgdewvdmtkpgpdgrgRAKRYIGILHQEYDLYPHRTVLDNLTEAiglelpDELA 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 382 ARGHVQNLmRHLGFTAAQWTEPIK----HMSMGERVKIKLMAYILEEKDVLILDEPTNHLD-----------LPSREQLE 446
Cdd:TIGR03269 400 RMKAVITL-KMVGFDEEKAEEILDkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkvdvthsiLKAREEME 478
|
570 580
....*....|....*....|
gi 2828494 447 EtlsqysgTLLAVSHDRYFL 466
Cdd:TIGR03269 479 Q-------TFIIVSHDMDFV 491
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-179 |
3.15e-23 |
|
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: 97.98 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL------------RKDIklALVE 72
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILidgrdvtgvppeRRNI--GMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 73 Q-----------ETAAYSFADQTPAEKKLLEKWH-----VPLRDF-----HQLSGGEKLKARLAKGLSEDADLLLLDEPT 131
Cdd:cd03259 79 QdyalfphltvaENIAFGLKLRGVPKAEIRARVRellelVGLEGLlnrypHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2828494 132 NHLDEKSLQFLIQQLKHY---NG-TVILVSHDryfLDEAatkiWSLEDQTLI 179
Cdd:cd03259 159 SALDAKLREELREELKELqreLGiTTIYVTHD---QEEA----LALADRIAV 203
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-168 |
3.41e-23 |
|
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: 96.49 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVEQETAAY----SF 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrriGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 81 ADQTPAekkLLEkwHVPLRD--FHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEK---SLQFLIQQLKHYNG-TVI 154
Cdd:cd03229 81 VFQDFA---LFP--HLTVLEniALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPItrrEVRALLKSLQAQLGiTVV 155
|
170
....*....|....
gi 2828494 155 LVSHDryfLDEAAT 168
Cdd:cd03229 156 LVTHD---LDEAAR 166
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-166 |
6.21e-23 |
|
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: 97.16 E-value: 6.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVS--YEVKDQ--TVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------RKDIKLALVEQ 73
Cdd:cd03293 1 LEVRNVSktYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 ETA-------------AYSFADQTPAEKK-----LLEKwhVPLRDF-----HQLSGGEKLKARLAKGLSEDADLLLLDEP 130
Cdd:cd03293 81 QDAllpwltvldnvalGLELQGVPKAEAReraeeLLEL--VGLSGFenaypHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2828494 131 TNHLDE---KSLQFLIQQLKHYNG-TVILVSHDryfLDEA 166
Cdd:cd03293 159 FSALDAltrEQLQEELLDIWRETGkTVLLVTHD---IDEA 195
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
9-158 |
1.12e-22 |
|
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: 95.07 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVEQETAAY-SFADQTPae 87
Cdd:cd03247 7 SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLiSVLNQRP-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 88 kkllekwHV---PLRDF--HQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKS----LQFLIQQLKhyNGTVILVSH 158
Cdd:cd03247 85 -------YLfdtTLRNNlgRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITerqlLSLIFEVLK--DKTLIWITH 155
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
292-478 |
2.58e-22 |
|
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: 94.18 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSVWVSpsaNIGYLTQEVFDLPLEQT 370
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpDSGSILID---GEDLTDLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 371 PEELFENetfkarghvQNLMRHLgfTAAQ-WTEPikhMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETL 449
Cdd:cd03229 78 IGMVFQD---------FALFPHL--TVLEnIALG---LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALL 143
|
170 180 190
....*....|....*....|....*....|...
gi 2828494 450 SQY---SG-TLLAVSHDRYFLEKTTNSKLVISN 478
Cdd:cd03229 144 KSLqaqLGiTVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
293-478 |
2.81e-22 |
|
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: 94.84 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 293 EVQNVTKAF--GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWVSP-----------SANIGYL 358
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPtSGEVLVDGkdltklslkelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQ-------------EV-FDLPLEQTPEElfenetfKARGHVQNLMRHLGFtAAQWTEPIKHMSMGERVKIKLMAYILEE 424
Cdd:cd03225 81 FQnpddqffgptveeEVaFGLENLGLPEE-------EIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 425 KDVLILDEPTNHLDLPSREQLEETLSQYSG---TLLAVSHDRYFLEKTTNSKLVISN 478
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-159 |
2.83e-22 |
|
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: 95.65 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYEVKDQTVF--KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR--KDI-------------KLALV 71
Cdd:cd03257 8 SVSFPTGGGSVKalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdgKDLlklsrrlrkirrkEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 72 EQ-----------------ETAAYSFADQTPAEKK---LLEKWHVPL-RDF-----HQLSGGEKLKARLAKGLSEDADLL 125
Cdd:cd03257 88 FQdpmsslnprmtigeqiaEPLRIHGKLSKKEARKeavLLLLVGVGLpEEVlnrypHELSGGQRQRVAIARALALNPKLL 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 2828494 126 LLDEPTNHLDeKSLQFLIQQL-----KHYNGTVILVSHD 159
Cdd:cd03257 168 IADEPTSALD-VSVQAQILDLlkklqEELGLTLLFITHD 205
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-180 |
6.61e-22 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 99.45 E-value: 6.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVS--YEvKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKL------------AL 70
Cdd:COG4988 337 IELEDVSfsYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLsdldpaswrrqiAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 71 VEQETaaYSFA------------DQTPAE-KKLLEKwhVPLRDF----------------HQLSGGEklkAR---LAKGL 118
Cdd:COG4988 416 VPQNP--YLFAgtirenlrlgrpDASDEElEAALEA--AGLDEFvaalpdgldtplgeggRGLSGGQ---AQrlaLARAL 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2828494 119 SEDADLLLLDEPTNHLDEKSLQFLIQQLKHY--NGTVILVSHDRYFLdEAATKIWSLEDQTLIE 180
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALL-AQADRILVLDDGRIVE 551
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-166 |
6.93e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 95.16 E-value: 6.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVS--YEVK--DQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------RKDIKLALVE 72
Cdd:COG1116 7 ALELRGVSkrFPTGggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvtGPGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 73 QETA-------------AYSFADQTPAEKK-----LLEKwhVPLRDF-----HQLSGGEKLKARLAKGLSEDADLLLLDE 129
Cdd:COG1116 87 QEPAllpwltvldnvalGLELRGVPKAERRerareLLEL--VGLAGFedaypHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2828494 130 PTNHLDE---KSLQFLIQQL-KHYNGTVILVSHDryfLDEA 166
Cdd:COG1116 165 PFGALDAltrERLQDELLRLwQETGKTVLFVTHD---VDEA 202
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
292-478 |
9.19e-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: 93.94 E-value: 9.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAF-GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV--------SPSA---NIGYL 358
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPtSGEVLVdgkditkkNLRElrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQE---------VFD------LPLEQTPEELfenetfKARghVQNLMRHLGFtAAQWTEPIKHMSMGE--RVKIklmAYI 421
Cdd:COG1122 81 FQNpddqlfaptVEEdvafgpENLGLPREEI------RER--VEEALELVGL-EHLADRPPHELSGGQkqRVAI---AGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2828494 422 LE-EKDVLILDEPTNHLDLPSREQLEETLSQYSG---TLLAVSHDRYFLEKTTNSKLVISN 478
Cdd:COG1122 149 LAmEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
292-461 |
1.05e-21 |
|
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: 92.06 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERT--LFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ-ETAEGSVWV--------SPSA---NIGY 357
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLyDPTSGEILIdgvdlrdlDLESlrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 358 LTQEVFdlpleqtpeeLFeNETFKarghvQNLmrhlgftaaqwtepikhMSMGERVKIKLMAYILEEKDVLILDEPTNHL 437
Cdd:cd03228 81 VPQDPF----------LF-SGTIR-----ENI-----------------LSGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180
....*....|....*....|....*.
gi 2828494 438 DLPSREQLEETLSQYSG--TLLAVSH 461
Cdd:cd03228 128 DPETEALILEALRALAKgkTVIVIAH 153
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-159 |
1.28e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.45 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 8 TNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDIK----------LALVEQET 75
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlnGRPLAdwspaelarrRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 76 A--------------AYSFADQTPAEKKLLEK-------WHVPLRDFHQLSGGEKLKARLAKGL------SEDADLLLLD 128
Cdd:PRK13548 86 SlsfpftveevvamgRAPHGLSRAEDDALVAAalaqvdlAHLAGRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWLLLD 165
|
170 180 190
....*....|....*....|....*....|....*
gi 2828494 129 EPTNHLD----EKSLQFLIQQLKHYNGTVILVSHD 159
Cdd:PRK13548 166 EPTSALDlahqHHVLRLARQLAHERGLAVIVVLHD 200
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
302-476 |
1.98e-21 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 98.32 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 302 GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEGSVWVSPSA-NIGYLTQEVFDLP-------------- 366
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPALPqpaleyvidgdrey 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 367 --LEQTPEELFENETFKARGHVQ----------------NLMRHLGFTAAQWTEPIKHMSMGERVKIKLMAYILEEKDVL 428
Cdd:PRK10636 92 rqLEAQLHDANERNDGHAIATIHgkldaidawtirsraaSLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2828494 429 ILDEPTNHLDLPSREQLEETLSQYSGTLLAVSHDRYFLEKTTNSKLVI 476
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHI 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
292-461 |
3.09e-21 |
|
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: 92.27 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAF--GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV--------SPS---ANIGY 357
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPtSGSVLLdgtdirqlDPAdlrRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 358 LTQEVF--------DLPL---EQTPEELFENETFK-----ARGHVQNLMRHLGftaaqwtEPIKHMSMGERVKIKLMAYI 421
Cdd:cd03245 83 VPQDVTlfygtlrdNITLgapLADDERILRAAELAgvtdfVNKHPNGLDLQIG-------ERGRGLSGGQRQAVALARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2828494 422 LEEKDVLILDEPTNHLDLPSREQLEETLSQYSG--TLLAVSH 461
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH 197
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-175 |
3.62e-21 |
|
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: 92.17 E-value: 3.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVS--YEVKDQTVF--KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLA-LVEQETAAY- 78
Cdd:cd03255 1 IELKNLSktYGGGGEKVQalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISkLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 79 ---------------------------SFADQTPAEKK-----LLEKwhVPLRDFH-----QLSGGEKLKARLAKGLSED 121
Cdd:cd03255 81 rrhigfvfqsfnllpdltalenvelplLLAGVPKKERReraeeLLER--VGLGDRLnhypsELSGGQQQRVAIARALAND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2828494 122 ADLLLLDEPTNHLDEKS----LQFLIQQLKHYNGTVILVSHDRyFLDEAATKIWSLED 175
Cdd:cd03255 159 PKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRD 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-180 |
4.35e-21 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 97.21 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVS--YEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRKDIkl 68
Cdd:COG2274 474 IELENVSfrYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqidpasLRRQI-- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 ALVEQETAAYS--------FADQTPAEKKLLE----------------KWHVPLRDF-HQLSGGEKLKARLAKGLSEDAD 123
Cdd:COG2274 552 GVVLQDVFLFSgtirenitLGDPDATDEEIIEaarlaglhdfiealpmGYDTVVGEGgSNLSGGQRQRLAIARALLRNPR 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2828494 124 LLLLDEPTNHLDEKSLQFLIQQLKHYNG--TVILVSHDRYFLdEAATKIWSLEDQTLIE 180
Cdd:COG2274 632 ILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTI-RLADRIIVLDKGRIVE 689
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
5-159 |
7.94e-21 |
|
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: 92.18 E-value: 7.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL------------RKDIKLALVE 72
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhglsrrARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 73 QETAA------------------YSFADQTPAEKKLLEKW-------HVPLRDFHQLSGGEKLKARLAKGLSEDADLLLL 127
Cdd:TIGR03873 82 QDSDTavpltvrdvvalgriphrSLWAGDSPHDAAVVDRAlartelsHLADRDMSTLSGGERQRVHVARALAQEPKLLLL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 2828494 128 DEPTNHLDeKSLQF----LIQQLKHYNGTVILVSHD 159
Cdd:TIGR03873 162 DEPTNHLD-VRAQLetlaLVRELAATGVTVVAALHD 196
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
292-462 |
9.57e-21 |
|
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: 90.99 E-value: 9.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFG----ERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWVS------PSANIGYLTQ 360
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPtSGEVLVDgepvtgPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 361 E--------VFD---LPLEQT---PEElfenetfkARGHVQNLMRHLGFTAAQWTEPiKHMS--MGERVKIkLMAYILeE 424
Cdd:cd03293 81 QdallpwltVLDnvaLGLELQgvpKAE--------ARERAEELLELVGLSGFENAYP-HQLSggMRQRVAL-ARALAV-D 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2828494 425 KDVLILDEPTNHLDLPSREQLEETL----SQYSGTLLAVSHD 462
Cdd:cd03293 150 PDVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
292-480 |
1.72e-20 |
|
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: 89.97 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV---------SPSANIGYL--T 359
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPdSGEITFdgksyqkniEALRRIGALieA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 360 QEVFDlplEQTPEELFENetfKARGH------VQNLMRHLGFTAAQwTEPIKHMSMGERVKIKLMAYILEEKDVLILDEP 433
Cdd:cd03268 81 PGFYP---NLTARENLRL---LARLLgirkkrIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2828494 434 TNHLDLPSREQLEET---LSQYSGTLLAVSHDRYFLEKTTnSKLVISNNG 480
Cdd:cd03268 154 TNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVA-DRIGIINKG 202
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
287-462 |
2.16e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 90.92 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 287 TGKRFLEVQNVTKAF----GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV------SPSANI 355
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPtSGEVLVdgkpvtGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 356 GYLTQE--------VFD---LPLEQ---TPEElfenetfkARGHVQNLMRHLGFTAAQWTEPiKHMSMGE--RVKIkLMA 419
Cdd:COG1116 83 GVVFQEpallpwltVLDnvaLGLELrgvPKAE--------RRERARELLELVGLAGFEDAYP-HQLSGGMrqRVAI-ARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 420 YILeEKDVLILDEPTNHLDLPSREQLEETL----SQYSGTLLAVSHD 462
Cdd:COG1116 153 LAN-DPEVLLMDEPFGALDALTRERLQDELlrlwQETGKTVLFVTHD 198
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
292-462 |
2.28e-20 |
|
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: 94.90 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERT--LFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV--------SPSA---NIGY 357
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPtSGRILIdgidlrqiDPASlrrQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 358 LTQEVFdlpleqtpeeLF-----ENETFkARGHV--QNLMRhlgftAAQWT---EPIKHMSMG------ER-------VK 414
Cdd:COG2274 554 VLQDVF----------LFsgtirENITL-GDPDAtdEEIIE-----AARLAglhDFIEALPMGydtvvgEGgsnlsggQR 617
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2828494 415 IKLM---AyILEEKDVLILDEPTNHLDLPSREQLEETLSQYSG--TLLAVSHD 462
Cdd:COG2274 618 QRLAiarA-LLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHR 669
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
9-173 |
2.33e-20 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 94.28 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYEVKDQtVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKL------------ALVEQ--- 73
Cdd:TIGR02857 328 SVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLadadadswrdqiAWVPQhpf 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 -------ETAAYSFADQTPAE--------------KKLLEKWHVPL-RDFHQLSGGEKLKARLAKGLSEDADLLLLDEPT 131
Cdd:TIGR02857 407 lfagtiaENIRLARPDASDAEirealeragldefvAALPQGLDTPIgEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2828494 132 NHLDEKSLQFLIQQLKHY--NGTVILVSHDRYFLdEAATKIWSL 173
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALaqGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-180 |
2.62e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 89.73 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVK-DQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-----------------LRKD 65
Cdd:COG2884 1 MIRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvngqdlsrlkrreipyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 66 I-------------------KLALVEQETAAYSFADQTPAekkLLEKwhVPLRDF-----HQLSGGEKLKARLAKGLSED 121
Cdd:COG2884 81 IgvvfqdfrllpdrtvyenvALPLRVTGKSRKEIRRRVRE---VLDL--VGLSDKakalpHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2828494 122 ADLLLLDEPTNHLDEKSLQFLIQQLKHYN--G-TVILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINrrGtTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-180 |
3.25e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 89.33 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVS--YEVKDQ--TVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--------RKDIKL 68
Cdd:COG1136 1 MSPLLELRNLTksYGTGEGevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdissLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 A---------------LVEQETA------AYSFADQTPAE-----KKLLEKwhVPLRDF-----HQLSGGEKLKARLAKG 117
Cdd:COG1136 81 ArlrrrhigfvfqffnLLPELTAlenvalPLLLAGVSRKErreraRELLER--VGLGDRldhrpSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 118 LSEDADLLLLDEPTNHLDEKS----LQFLIQQLKHYNGTVILVSHDRyFLDEAATKIWSLEDQTLIE 180
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
292-470 |
4.01e-20 |
|
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: 89.09 E-value: 4.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFG----ERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV--------SPSA----- 353
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVRVdgtdisklSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 354 --NIGYLTQE--------VFD---LPLEQTPEELFENETfKARghvqNLMRHLGFTAAQwTEPIKHMSMGE--RVKI--K 416
Cdd:cd03255 81 rrHIGFVFQSfnllpdltALEnveLPLLLAGVPKKERRE-RAE----ELLERVGLGDRL-NHYPSELSGGQqqRVAIarA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2828494 417 LMAyileEKDVLILDEPTNHLDLPSREQLEETL----SQYSGTLLAVSHDRYFLEKTT 470
Cdd:cd03255 155 LAN----DPKIILADEPTGNLDSETGKEVMELLrelnKEAGTTIVVVTHDPELAEYAD 208
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
292-463 |
6.04e-20 |
|
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: 88.35 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSVWVSpsanigylTQEVFDLPLEQT 370
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERpDSGEILID--------GRDVTGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 371 PEEL-------------FENETF----------KARGHVQNLMRHLGFTAaQWTEPIKHMSMGERVKIKLMAYILEEKDV 427
Cdd:cd03259 73 NIGMvfqdyalfphltvAENIAFglklrgvpkaEIRARVRELLELVGLEG-LLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2828494 428 LILDEPTNHLDLPSREQLEETLSQYSG----TLLAVSHDR 463
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQ 191
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-181 |
7.43e-20 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 88.71 E-value: 7.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL---------------RKDIKLA 69
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedisglseaelyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 70 LVEQETAAysFADQTPAE------------------KKLLEKWH-VPLRDFH-----QLSGGEKLKARLAKGLSEDADLL 125
Cdd:cd03261 81 MLFQSGAL--FDSLTVFEnvafplrehtrlseeeirEIVLEKLEaVGLRGAEdlypaELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 126 LLDEPTNHLDEKS---LQFLIQQLK-HYNGTVILVSHDRYFLDEAATKIWSLEDQTLIEF 181
Cdd:cd03261 159 LYDEPTAGLDPIAsgvIDDLIRSLKkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-132 |
8.11e-20 |
|
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: 86.16 E-value: 8.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 20 FKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDI------------KLALVEQET------------ 75
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkEIGYVFQDPqlfprltvrenl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 76 --AAYSFADQTPAEKKLLEKW--HVPLRDF---------HQLSGGEKLKARLAKGLSEDADLLLLDEPTN 132
Cdd:pfam00005 81 rlGLLLKGLSKREKDARAEEAleKLGLGDLadrpvgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-158 |
8.24e-20 |
|
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: 88.99 E-value: 8.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 3 EIVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR-----------KDIK--LA 69
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerrggedvWELRkrIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 70 LVEQE----------------TAAYS----FADQTPAEKKLLEKW-------HVPLRDFHQLSGGEKLKARLAKGLSEDA 122
Cdd:COG1119 82 LVSPAlqlrfprdetvldvvlSGFFDsiglYREPTDEQRERARELlellglaHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2828494 123 DLLLLDEPTNHLDEKSLQFLIQQLKHYNG----TVILVSH 158
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAegapTLVLVTH 201
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-179 |
8.30e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 88.74 E-value: 8.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 23 VNASVQQGDIIGIIGKNGAGKSTLLHLIhNDLAPAQGQILRKDIKLA-------------LVEQETA----------AYS 79
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARM-AGLLPGQGEILLNGRPLSdwsaaelarhrayLSQQQSPpfampvfqylALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 FADQTPAEK------------KLLEKWHvplRDFHQLSGGEKLKARLAK-------GLSEDADLLLLDEPTNHLD---EK 137
Cdd:COG4138 94 QPAGASSEAveqllaqlaealGLEDKLS---RPLTQLSGGEWQRVRLAAvllqvwpTINPEGQLLLLDEPMNSLDvaqQA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 138 SLQFLIQQLKHYNGTVILVSHD-----RYfldeaATKIWSLEDQTLI 179
Cdd:COG4138 171 ALDRLLRELCQQGITVVMSSHDlnhtlRH-----ADRVWLLKQGKLV 212
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-166 |
1.29e-19 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 85.94 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 21 KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILrkdiklalVEQEtaAYSFADqtPAEKKLLekwhvPLRD 100
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL--------VDGK--EVSFAS--PRDARRA-----GIAM 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2828494 101 FHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFL---IQQLKHYNGTVILVSHdryFLDEA 166
Cdd:cd03216 80 VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLfkvIRRLRAQGVAVIFISH---RLDEV 145
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-159 |
2.37e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.45 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDI----------KLALVE 72
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLvdGLDVattpsrelakRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 73 QETA----------------AYSFADQTPAEKKL---------LEkwhvPLRD--FHQLSGGEKLKARLAKGLSEDADLL 125
Cdd:COG4604 82 QENHinsrltvrelvafgrfPYSKGRLTAEDREIideaiayldLE----DLADryLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 2828494 126 LLDEPTNHLDEK-SLQfLIQQLKH----YNGTVILVSHD 159
Cdd:COG4604 158 LLDEPLNNLDMKhSVQ-MMKLLRRladeLGKTVVIVLHD 195
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
292-461 |
3.17e-19 |
|
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: 86.18 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG--QETaEGSVWV-------SPSANIGYLtqev 362
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiiLPD-SGEVLFdgkpldiAARNRIGYL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 363 fdlpleqtPEE--LFENETFK----------------ARGHVQNLMRHLGFTaAQWTEPIKHMSMGERVKIKLMAYILEE 424
Cdd:cd03269 76 --------PEErgLYPKMKVIdqlvylaqlkglkkeeARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHD 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2828494 425 KDVLILDEPTNHLDLPSREQLEETLSQYSG---TLLAVSH 461
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTH 186
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-164 |
4.42e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 86.17 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDL--APAQGQILRKDI----KLALVEQETAAYSFAD 82
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNqfgrEASLIDAIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 83 QtpaeKKLLEK--------WhvpLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFL---IQQL-KHYN 150
Cdd:COG2401 115 A----VELLNAvglsdavlW---LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVarnLQKLaRRAG 187
|
170
....*....|....
gi 2828494 151 GTVILVSHDRYFLD 164
Cdd:COG2401 188 ITLVVATHHYDVID 201
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-178 |
5.46e-19 |
|
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: 84.58 E-value: 5.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 7 LTNVS--YEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDIKLALVEQ--ETAAYsf 80
Cdd:cd03246 3 VENVSfrYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRldGADISQWDPNElgDHVGY-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 81 adqTPAEKKLLEKwhvPLRDfHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD---EKSLQFLIQQLKHYNGTVILVS 157
Cdd:cd03246 81 ---LPQDDELFSG---SIAE-NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDvegERALNQAIAALKAAGATRIVIA 153
|
170 180
....*....|....*....|.
gi 2828494 158 HdRYFLDEAATKIWSLEDQTL 178
Cdd:cd03246 154 H-RPETLASADRILVLEDGRV 173
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
300-462 |
5.55e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.98 E-value: 5.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 300 AFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSVWVSPSANIGYLTQ--EVFD-LPLeqTPEELF 375
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRpTSGTVRRAGGARVAYVPQrsEVPDsLPL--TVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 376 ENETFKARGHVQNLMRHLGFTAAQWTE----------PIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQL 445
Cdd:NF040873 79 AMGRWARRGLWRRLTRDDRAAVDDALErvgladlagrQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180
....*....|....*....|
gi 2828494 446 EETLSQYSG---TLLAVSHD 462
Cdd:NF040873 159 IALLAEEHArgaTVVVVTHD 178
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
18-190 |
6.50e-19 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 90.30 E-value: 6.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 18 TVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRK-DIKLALVEQETAAYSFADQTP----------- 85
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSaKVRMAVFSQHHVDGLDLSSNPllymmrcfpgv 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 86 AEKKLLEKW-------HVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLKHYNGTVILVSH 158
Cdd:PLN03073 603 PEQKLRAHLgsfgvtgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSH 682
|
170 180 190
....*....|....*....|....*....|..
gi 2828494 159 DRYFLDEAATKIWSLEDQTLIEFKGNYSGYMK 190
Cdd:PLN03073 683 DEHLISGSVDELWVVSEGKVTPFHGTFHDYKK 714
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-167 |
6.52e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 6.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDI------------KLALVE 72
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 73 QETA-AYSF----------------------ADQTPAEKKlLEKWHVPL---RDFHQLSGGEKLKARLAKGLSEDADLLL 126
Cdd:PRK09536 84 QDTSlSFEFdvrqvvemgrtphrsrfdtwteTDRAAVERA-MERTGVAQfadRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2828494 127 LDEPTNHLD----EKSLQfLIQQLKHYNGTVILVSHDryfLDEAA 167
Cdd:PRK09536 163 LDEPTASLDinhqVRTLE-LVRRLVDDGKTAVAAIHD---LDLAA 203
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-159 |
7.44e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 86.32 E-value: 7.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 8 TNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDI----------KLALVEQET 75
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlnGRPLaawspwelarRRAVLPQHS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 76 A-AYSF-------------ADQTPAEKKLLEK-------WHVPLRDFHQLSGGEKLKARLAKGL-------SEDADLLLL 127
Cdd:COG4559 85 SlAFPFtveevvalgraphGSSAAQDRQIVREalalvglAHLAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFL 164
|
170 180 190
....*....|....*....|....*....|....*
gi 2828494 128 DEPTNHLDEKSLQFLIQQLKHY---NGTVILVSHD 159
Cdd:COG4559 165 DEPTSALDLAHQHAVLRLARQLarrGGGVVAVLHD 199
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
292-468 |
8.34e-19 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 89.83 E-value: 8.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAF--GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV-----------SPSANIGY 357
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPqSGSITLggvdlrdldedDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 358 LTQE--VFDLPLEQ---------TPEELFEN------ETFkARGHVQNLMRHLGFTAAQwtepikhMSMGERVKIKLMAY 420
Cdd:COG4987 414 VPQRphLFDTTLREnlrlarpdaTDEELWAAlervglGDW-LAALPDGLDTWLGEGGRR-------LSGGERRRLALARA 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2828494 421 ILEEKDVLILDEPTNHLDLPSREQLEETLSQYSG--TLLAVSHDRYFLEK 468
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRLAGLER 535
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-175 |
8.89e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 84.62 E-value: 8.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 6 TLTNVSYEVKDQT-VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDIKLA-------LVEQET 75
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlnGKPIKAKerrksigYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 76 AAYSF-----------ADQTPAEK----KLLEKWHV-PLRDFH--QLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEK 137
Cdd:cd03226 81 DYQLFtdsvreelllgLKELDAGNeqaeTVLKDLDLyALKERHplSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2828494 138 SLQF---LIQQLKHYNGTVILVSHDRYFLDEAATKIWSLED 175
Cdd:cd03226 161 NMERvgeLIRELAAQGKAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
293-481 |
1.55e-18 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 84.23 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 293 EVQNVTKAFGERT-LFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSV-----WVSPSA---NIGYLTQEV 362
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGlIKESSGSIllngkPIKAKErrkSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 363 -FDLPLEQTPEELFEN--ETFKARGHVQNLMRHLGFTAAQWTEPIKhMSMGERVKIKLMAYILEEKDVLILDEPTNHLDL 439
Cdd:cd03226 81 dYQLFTDSVREELLLGlkELDAGNEQAETVLKDLDLYALKERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2828494 440 PSREQLEE---TLSQYSGTLLAVSHDRYFLEKTTNSKLVISNNGI 481
Cdd:cd03226 160 KNMERVGElirELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
292-463 |
2.10e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 86.74 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSV---------WVSPSA-NIGYLTQ 360
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPdSGRIvlngrdlftNLPPRErRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 361 E--------VFD-----LPLEQTPEElfenetfKARGHVQNLMR--HLGFTA----AQwtepikhMSMGERVKIKLmAYI 421
Cdd:COG1118 83 HyalfphmtVAEniafgLRVRPPSKA-------EIRARVEELLElvQLEGLAdrypSQ-------LSGGQRQRVAL-ARA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 422 LE-EKDVLILDEPTNHLDLPSREQLE----ETLSQYSGTLLAVSHDR 463
Cdd:COG1118 148 LAvEPEVLLLDEPFGALDAKVRKELRrwlrRLHDELGGTTVFVTHDQ 194
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
308-477 |
2.17e-18 |
|
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: 84.31 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 308 KNANFTIQHGEKVAIIGPNGSGKTTLLNIILG--QETaEGSVWVS---PS-------ANIGYL----TQEVFDLPLEQTP 371
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGllQPT-SGEVRVAglvPWkrrkkflRRIGVVfgqkTQLWWDLPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 372 E---ELFENETFKARGHVQNLMRHLGFTAAQWTePIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEET 448
Cdd:cd03267 117 YllaAIYDLPPARFKKRLDELSELLDLEELLDT-PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNF 195
|
170 180 190
....*....|....*....|....*....|...
gi 2828494 449 LSQYS----GTLLAVSHDRYFLEKTTNSKLVIS 477
Cdd:cd03267 196 LKEYNrergTTVLLTSHYMKDIEALARRVLVID 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
292-462 |
4.79e-18 |
|
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: 82.94 E-value: 4.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLF--KNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWVS----------PSANIGYL 358
Cdd:cd03263 1 LQIRNLTKTYKKGTKPavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPtSGTAYINgysirtdrkaARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQevFD-LPLEQTPEELFEnetFKAR--GH--------VQNLMRHLGFTaAQWTEPIKHMSMGERVKIKLMAYILEEKDV 427
Cdd:cd03263 81 PQ--FDaLFDELTVREHLR---FYARlkGLpkseikeeVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 2828494 428 LILDEPTNHLDLPSREQLEETLSQYSG--TLLAVSHD 462
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-180 |
5.77e-18 |
|
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: 83.01 E-value: 5.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQ----TVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDL-APAQGQIL---------------- 62
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-NGLeRPTSGSVLvdgtdltllsgkelrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 63 -RKDIKLA-----LVEQETAAYSFA--------DQTPAEKKLLEKWH-VPLRDFH-----QLSGGEKLKARLAKGLSEDA 122
Cdd:cd03258 80 aRRRIGMIfqhfnLLSSRTVFENVAlpleiagvPKAEIEERVLELLElVGLEDKAdaypaQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2828494 123 DLLLLDEPTNHLDEKSLQFLIQQLKHYNG----TVILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRelglTIVLITHEMEVVKRICDRVAVMEKGEVVE 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-181 |
5.96e-18 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 83.11 E-value: 5.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------------RKDI- 66
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvdgqditglsekeLYELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 67 -KLALVEQETAAYS--------------FADQTPAEKK-----LLEkwHVPLRDFH-----QLSGGEKLKARLAKGLSED 121
Cdd:COG1127 82 rRIGMLFQGGALFDsltvfenvafplreHTDLSEAEIRelvleKLE--LVGLPGAAdkmpsELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 122 ADLLLLDEPTNHLDEKS---LQFLIQQLKH-YNGTVILVSHDryfLDEA---ATKIWSLEDQTLIEF 181
Cdd:COG1127 160 PEILLYDEPTAGLDPITsavIDELIRELRDeLGLTSVVVTHD---LDSAfaiADRVAVLADGKIIAE 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
292-463 |
6.09e-18 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 86.96 E-value: 6.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAF-GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ-ETAEGSVWV--------SPSA---NIGYL 358
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFvDPTEGSIAVngvpladaDADSwrdQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQEVFDLP-----------LEQTPEELFE-------NETFKARGhvQNLMRHLGFTAAQwtepikhMSMGERVKIKLMAY 420
Cdd:TIGR02857 402 PQHPFLFAgtiaenirlarPDASDAEIREaleraglDEFVAALP--QGLDTPIGEGGAG-------LSGGQAQRLALARA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2828494 421 ILEEKDVLILDEPTNHLDLPSREQLEETLSQYSG--TLLAVSHDR 463
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL 517
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-466 |
1.04e-17 |
|
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: 86.38 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 28 QQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQ---------ILR----------------KDIKLALVEQetaaysFAD 82
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDydeepswdeVLKrfrgtelqdyfkklanGEIKVAHKPQ------YVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 83 QTPAE-----KKLLEKW----------------HVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEK---S 138
Cdd:COG1245 171 LIPKVfkgtvRELLEKVdergkldelaeklgleNILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYqrlN 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 139 LQFLIQQLKHYNGTVILVSHDRYFLDeaatkiwSLEDQTLIeFKGNYSGYmkfrekkrltqqreyekqqkmverieaqmn 218
Cdd:COG1245 251 VARLIRELAEEGKYVLVVEHDLAILD-------YLADYVHI-LYGEPGVY------------------------------ 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 219 GLASwsekaHAQSTKK------EGFKEYHRVKakrtdaqIKSKQKRLE-KELEKAKAEPVTPEYTvrfsidtthktgkrf 291
Cdd:COG1245 293 GVVS-----KPKSVRVginqylDGYLPEENVR-------IRDEPIEFEvHAPRREKEEETLVEYP--------------- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 levqNVTKAFGERTLFKNANfTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSvwVSPSANIGYLTQEV---FDLP- 366
Cdd:COG1245 346 ----DLTKSYGGFSLEVEGG-EIREGEVLGIVGPNGIGKTTFAKILAGVLKPdEGE--VDEDLKISYKPQYIspdYDGTv 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 367 ---LEQTPEELFENETFKARghvqnLMRHLGFtaaqwtEPI-----KHMSMGERVKIKLMAYILEEKDVLILDEPTNHLD 438
Cdd:COG1245 419 eefLRSANTDDFGSSYYKTE-----IIKPLGL------EKLldknvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
490 500 510
....*....|....*....|....*....|..
gi 2828494 439 LPSREQLEETLSQY----SGTLLAVSHDRYFL 466
Cdd:COG1245 488 VEQRLAVAKAIRRFaenrGKTAMVVDHDIYLI 519
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
292-462 |
1.21e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 82.01 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFG----ERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV--------SPSA----- 353
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVLIdgqdisslSERElarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 354 --NIGY----------LTqeVFD---LPLeqtpeELFENETFKARGHVQNLMRHLGFtAAQWTEPIKHMSMGE--RVKI- 415
Cdd:COG1136 85 rrHIGFvfqffnllpeLT--ALEnvaLPL-----LLAGVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQqqRVAIa 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2828494 416 -KLMAyileEKDVLILDEPTNHLDLPSREQLEETL----SQYSGTLLAVSHD 462
Cdd:COG1136 157 rALVN----RPKLILADEPTGNLDSKTGEEVLELLrelnRELGTTIVMVTHD 204
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-177 |
1.28e-17 |
|
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: 82.10 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 19 VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI---------------------LRKDIkLALVEQ---- 73
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggwvdlaqaspreilaLRRRT-IGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 -------ETAAYS-FADQTPAE------KKLLEK-------WHVPLRDFhqlSGGEKLKARLAKGLSEDADLLLLDEPTN 132
Cdd:COG4778 105 iprvsalDVVAEPlLERGVDREeararaRELLARlnlperlWDLPPATF---SGGEQQRVNIARGFIADPPLLLLDEPTA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2828494 133 HLDEKSLQF---LIQQLKHyNGTVIL-VSHDRYFLDEAATKIWSLEDQT 177
Cdd:COG4778 182 SLDAANRAVvveLIEEAKA-RGTAIIgIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-159 |
1.66e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.53 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 6 TLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVEQETAAYSFA---D 82
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAylpQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 83 QTPAEKKLLEK---------WH--------------------VPLRDFHQ-----LSGGEKLKARLAKGLSEDADLLLLD 128
Cdd:PRK10575 93 QLPAAEGMTVRelvaigrypWHgalgrfgaadrekveeaislVGLKPLAHrlvdsLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190
....*....|....*....|....*....|....*
gi 2828494 129 EPTNHLD---EKSLQFLIQQLKHYNG-TVILVSHD 159
Cdd:PRK10575 173 EPTSALDiahQVDVLALVHRLSQERGlTVIAVLHD 207
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-181 |
1.97e-17 |
|
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: 81.46 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 7 LTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIH--NDL---APAQGQIL--RKDI------------K 67
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlNDLipgAPDEGEVLldGKDIydldvdvlelrrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 68 LALVEQETA----------AYSFADQTPAEKKLLEKW-HVPLR------------DFHQLSGGEKLKARLAKGLSEDADL 124
Cdd:cd03260 83 VGMVFQKPNpfpgsiydnvAYGLRLHGIKLKEELDERvEEALRkaalwdevkdrlHALGLSGGQQQRLCLARALANEPEV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 125 LLLDEPTNHLDEKS---LQFLIQQLKHyNGTVILVSHDryfLDEA---ATKIWSLEDQTLIEF 181
Cdd:cd03260 163 LLLDEPTSALDPIStakIEELIAELKK-EYTIVIVTHN---MQQAarvADRTAFLLNGRLVEF 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
292-462 |
2.69e-17 |
|
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: 84.81 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAF-GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ-ETAEGSVWV-----------SPSANIGYL 358
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFlPPYSGSILIngvdlsdldpaSWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQEVFdlpleqtpeeLF-----ENETFKARG----HVQNLMRHLG---FTAAQ---WTEPI----KHMSMGERVKIKLMA 419
Cdd:COG4988 417 PQNPY----------LFagtirENLRLGRPDasdeELEAALEAAGldeFVAALpdgLDTPLgeggRGLSGGQAQRLALAR 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2828494 420 YILEEKDVLILDEPTNHLDLPSREQLEETLSQYSG--TLLAVSHD 462
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHR 531
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-166 |
2.69e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 80.80 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 30 GDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL---------RKDI-------KLALVEQETA-----------AYSFAD 82
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsRKKInlppqqrKIGLVFQQYAlfphlnvrenlAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 83 QTPAEKK--------LLEKWHVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKS----LQFLIQQLKHYN 150
Cdd:cd03297 103 KRNREDRisvdelldLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKKNLN 182
|
170
....*....|....*.
gi 2828494 151 GTVILVSHDryfLDEA 166
Cdd:cd03297 183 IPVIFVTHD---LSEA 195
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-194 |
3.31e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.88 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVS--YEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLA------------L 70
Cdd:PRK11160 339 LTLNNVSftYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdyseaalrqaisV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 71 VEQETAAYS--------FADQTPAEKKL---LEKwhVPLRDF---------------HQLSGGEKLKARLAKGLSEDADL 124
Cdd:PRK11160 419 VSQRVHLFSatlrdnllLAAPNASDEALievLQQ--VGLEKLleddkglnawlgeggRQLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2828494 125 LLLDEPTNHLDEKSLQFLIQQLKHY--NGTVILVSHDRYFLdEAATKIWSLEDQTLIEfKGNYS-------GYMKFREK 194
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHRLTGL-EQFDRICVMDNGQIIE-QGTHQellaqqgRYYQLKQR 573
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-467 |
3.35e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 84.86 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 27 VQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQ---------ILR----------------KDIKLALVEQ--ETAAYS 79
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDyeeepswdeVLKrfrgtelqnyfkklynGEIKVVHKPQyvDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 F----------ADQTPAEKKLLEKW---HVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEK---SLQFLI 143
Cdd:PRK13409 176 FkgkvrellkkVDERGKLDEVVERLgleNILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRqrlNVARLI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 144 QQLKHyNGTVILVSHDRYFLDeaatkiwSLEDQTLIEFkGNYSGYmkfrekkrltqqreyekqqkmverieaqmnGLASw 223
Cdd:PRK13409 256 RELAE-GKYVLVVEHDLAVLD-------YLADNVHIAY-GEPGAY------------------------------GVVS- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 224 sekaHAQSTKkEGFKEYhrvkakrTDAQIKSKQKRLEKElekakaePVtpEYTVRFSIDTTHktGKRFLEVQNVTKAFGE 303
Cdd:PRK13409 296 ----KPKGVR-VGINEY-------LKGYLPEENMRIRPE-------PI--EFEERPPRDESE--RETLVEYPDLTKKLGD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 304 RTLFKNANfTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSvwVSPSANIGYLTQEV---FDLP----LEQTPEEL- 374
Cdd:PRK13409 353 FSLEVEGG-EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPdEGE--VDPELKISYKPQYIkpdYDGTvedlLRSITDDLg 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 375 ---FENETFKARGhVQNLMRHlgftaaqwtePIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQ 451
Cdd:PRK13409 430 ssyYKSEIIKPLQ-LERLLDK----------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 498
|
490 500
....*....|....*....|
gi 2828494 452 Y----SGTLLAVSHDRYFLE 467
Cdd:PRK13409 499 IaeerEATALVVDHDIYMID 518
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-159 |
3.65e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.31 E-value: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKD-IKLALVEQE----- 74
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGkLRIGYVPQKlyldt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 75 ------------TAAYSFADQTPAEKKlLEKWHVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD---EKSL 139
Cdd:PRK09544 81 tlpltvnrflrlRPGTKKEDILPALKR-VQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvngQVAL 159
|
170 180
....*....|....*....|.
gi 2828494 140 QFLIQQLKH-YNGTVILVSHD 159
Cdd:PRK09544 160 YDLIDQLRReLDCAVLMVSHD 180
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
292-349 |
4.64e-17 |
|
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: 80.79 E-value: 4.64e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV 349
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPdSGEILV 64
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
292-438 |
4.87e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.69 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV-------SPSANIGYLtqevf 363
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPdSGEVLWdgepldpEDRRRIGYL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 364 dlpleqtPEE--LFENETfkarghVQNLMRHL----GFTAAQ-----------------WTEPIKHMSMGERVKIKLMAY 420
Cdd:COG4152 77 -------PEErgLYPKMK------VGEQLVYLarlkGLSKAEakrradewlerlglgdrANKKVEELSKGNQQKVQLIAA 143
|
170
....*....|....*...
gi 2828494 421 ILEEKDVLILDEPTNHLD 438
Cdd:COG4152 144 LLHDPELLILDEPFSGLD 161
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-167 |
4.94e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 80.57 E-value: 4.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 6 TLTNVSYEVKDQTvfKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDI--------KLALVEQET 75
Cdd:COG3840 3 RLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILwnGQDLtalppaerPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 76 ---AAYSFADQ-----------TPAEKK----LLEKwhVPLRDF-----HQLSGGEKLKARLAKGLSEDADLLLLDEPTN 132
Cdd:COG3840 81 nlfPHLTVAQNiglglrpglklTAEQRAqveqALER--VGLAGLldrlpGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 2828494 133 HLD----EKSLQFLIQQLKHYNGTVILVSHDryfLDEAA 167
Cdd:COG3840 159 ALDpalrQEMLDLVDELCRERGLTVLMVTHD---PEDAA 194
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-175 |
5.39e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 79.88 E-value: 5.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDL-APAQGQILRKDIKLALVEQETAAY----- 78
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-NLLeEPDSGTIIIDGLKLTDDKKNINELrqkvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 79 ----SFA---------------------DQTPAEK---KLLEKwhVPLRDF-----HQLSGGEKLKARLAKGLSEDADLL 125
Cdd:cd03262 80 mvfqQFNlfphltvlenitlapikvkgmSKAEAEEralELLEK--VGLADKadaypAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2828494 126 LLDEPTNHLDE---KSLQFLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLED 175
Cdd:cd03262 158 LFDEPTSALDPelvGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
302-453 |
5.43e-17 |
|
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: 79.13 E-value: 5.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 302 GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ---ETAEGSVWV--------SPSANIGYLTQEVFDLPlEQT 370
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtgLGVSGEVLIngrpldkrSFRKIIGYVPQDDILHP-TLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 371 PEElfenetfkarghvqNLMrhlgFTAAqwtepIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLS 450
Cdd:cd03213 99 VRE--------------TLM----FAAK-----LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLR 155
|
...
gi 2828494 451 QYS 453
Cdd:cd03213 156 RLA 158
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-161 |
6.59e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.44 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDI----------KLALV 71
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgDKPIsmlssrqlarRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 72 EQ-----------ETAAY------------SFADQTPAEKKLlEKWHV------PLRDfhqLSGGEKLKARLAKGLSEDA 122
Cdd:PRK11231 82 PQhhltpegitvrELVAYgrspwlslwgrlSAEDNARVNQAM-EQTRInhladrRLTD---LSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 123 DLLLLDEPTNHLD---EKSLQFLIQQLKHYNGTVILVSHD-----RY 161
Cdd:PRK11231 158 PVVLLDEPTTYLDinhQVELMRLMRELNTQGKTVVTVLHDlnqasRY 204
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-164 |
1.34e-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: 78.79 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQT--VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRKDIkl 68
Cdd:cd03245 3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirqldpadLRRNI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 ALVEQE------------TAAYSFADqtpaEKKLLEKWHV----PLRDFH-------------QLSGGEKLKARLAKGLS 119
Cdd:cd03245 81 GYVPQDvtlfygtlrdniTLGAPLAD----DERILRAAELagvtDFVNKHpngldlqigergrGLSGGQRQAVALARALL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 120 EDADLLLLDEPTNHLDEKSLQFLIQQLKHYNG--TVILVSHDRYFLD 164
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLD 203
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-159 |
1.41e-16 |
|
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: 79.02 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 18 TVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDIK---------------------------- 67
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdGEDITglppheiarlgigrtfqiprlfpeltvl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 68 ----LALVEQETAAYSFADQTPAEKKLLEK-------------WHVPLRDfhqLSGGEKLKARLAKGLSEDADLLLLDEP 130
Cdd:cd03219 94 envmVAAQARTGSGLLLARARREEREARERaeellervgladlADRPAGE---LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190
....*....|....*....|....*....|..
gi 2828494 131 T---NHLDEKSLQFLIQQLKHYNGTVILVSHD 159
Cdd:cd03219 171 AaglNPEETEELAELIRELRERGITVLLVEHD 202
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
292-462 |
1.60e-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: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAE-GSVWV--------SPSA------NIG 356
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIdgedisglSEAElyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 357 YLTQE--------VFD---LPLEQTpEELFENETfkaRGHVQNLMRHLGFTAAQWTEPIKhMSMGERVKIKLMAYILEEK 425
Cdd:cd03261 81 MLFQSgalfdsltVFEnvaFPLREH-TRLSEEEI---REIVLEKLEAVGLRGAEDLYPAE-LSGGMKKRVALARALALDP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2828494 426 DVLILDEPTNHLDlPSR----EQLEETLSQYSG-TLLAVSHD 462
Cdd:cd03261 156 ELLLYDEPTAGLD-PIAsgviDDLIRSLKKELGlTSIMVTHD 196
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
292-462 |
1.61e-16 |
|
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: 78.92 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVW--------VSPSA-NIGYLTQE 361
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdSGTILfggedatdVPVQErNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 362 --------VFD---LPLEQTPEELFENETfKARGHVQNLMRHLGFTAAQWTEPiKHMSMGERVKIKLMAYILEEKDVLIL 430
Cdd:cd03296 83 yalfrhmtVFDnvaFGLRVKPRSERPPEA-EIRAKVHELLKLVQLDWLADRYP-AQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 2828494 431 DEPTNHLDLPSREQLEETLSQY----SGTLLAVSHD 462
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLhdelHVTTVFVTHD 196
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-172 |
2.18e-16 |
|
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: 76.26 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 29 QGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDiklalveqetaaysfADQTPAEKKLLEKWHVPLRDFHQLSGGE 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID---------------GEDILEEVLDQLLLIIVGGKKASGSGEL 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 109 KLKARLAKGLSEDADLLLLDEPTNHLDEKS---------LQFLIQQLKHYNGTVILVSHDRYFLDEAATKIWS 172
Cdd:smart00382 66 RLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
292-462 |
2.20e-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: 78.32 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLF----KNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWVSPsanigyltQEVFDLP 366
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGlLKPTSGSIIFDG--------KDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 367 LEQtpeelfenetFKARGHV-----QNLMRHL--GFT-AAQWTEPIKHMSMGERVKIKLMAYILEEK------------- 425
Cdd:cd03257 74 RRL----------RKIRRKEiqmvfQDPMSSLnpRMTiGEQIAEPLRIHGKLSKKEARKEAVLLLLVgvglpeevlnryp 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2828494 426 ---------------------DVLILDEPTNHLDLPSREQLEETL----SQYSGTLLAVSHD 462
Cdd:cd03257 144 helsggqrqrvaiaralalnpKLLIADEPTSALDVSVQAQILDLLkklqEELGLTLLFITHD 205
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-164 |
2.31e-16 |
|
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: 77.57 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 6 TLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLI--HNDLAPAQGQILRK--DIKLALVEQETAAYSF- 80
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKgeDITDLPPEERARLGIFl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 81 ADQTPAEkkllekwhVP-------LRDFHQ-LSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFL---IQQLKHY 149
Cdd:cd03217 82 AFQYPPE--------IPgvknadfLRYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVaevINKLREE 153
|
170
....*....|....*
gi 2828494 150 NGTVILVSHDRYFLD 164
Cdd:cd03217 154 GKSVLIITHYQRLLD 168
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
292-467 |
2.40e-16 |
|
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: 77.57 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ---ETAEGSVWvspsanigYLTQEVFDLPLE 368
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkyEVTEGEIL--------FKGEDITDLPPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 369 -----------QTPEELfenetfkaRG-HVQNLMRHL--GFtaaqwtepikhmSMGERVKIKLMAYILEEKDVLILDEPT 434
Cdd:cd03217 73 erarlgiflafQYPPEI--------PGvKNADFLRYVneGF------------SGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 2828494 435 NHLDLPSREQLEETLSQYSG---TLLAVSHDRYFLE 467
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREegkSVLIITHYQRLLD 168
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-159 |
2.64e-16 |
|
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: 78.69 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYEVK--DQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL----------RKDI--KLALVEQE 74
Cdd:COG1124 8 SVSYGQGgrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfdgrpvtrrrRKAFrrRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 75 TAAySF-----ADQTPAE--------------KKLLEKWHVPlRDF-----HQLSGGEKLKARLAKGLSEDADLLLLDEP 130
Cdd:COG1124 88 PYA-SLhprhtVDRILAEplrihglpdreeriAELLEQVGLP-PSFldrypHQLSGGQRQRVAIARALILEPELLLLDEP 165
|
170 180 190
....*....|....*....|....*....|....
gi 2828494 131 TNHLDeKSLQF----LIQQLKH-YNGTVILVSHD 159
Cdd:COG1124 166 TSALD-VSVQAeilnLLKDLREeRGLTYLFVSHD 198
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-179 |
3.20e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.44 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 23 VNASVQQGDIIGIIGKNGAGKSTLLHLIHNdLAPAQGQILRKDIKLA-------------LVEQETAAY----------S 79
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEawsaaelarhrayLSQQQTPPFampvfqyltlH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 FADQTPAEK------------KLLEKWHVPLrdfHQLSGGEKLKARLA-------KGLSEDADLLLLDEPTNHLD---EK 137
Cdd:PRK03695 94 QPDKTRTEAvasalnevaealGLDDKLGRSV---NQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDvaqQA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2828494 138 SLQFLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLI 179
Cdd:PRK03695 171 ALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-181 |
3.29e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.20 E-value: 3.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYeVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVE-------- 72
Cdd:COG1134 24 LKELLLRRRRTR-REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLElgagfhpe 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 73 ------------------QETAAY-----SFADqtpaekklLEKW-HVPLRDFhqlSGGekLKARLAKGLSE--DADLLL 126
Cdd:COG1134 103 ltgreniylngrllglsrKEIDEKfdeivEFAE--------LGDFiDQPVKTY---SSG--MRARLAFAVATavDPDILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 127 LDEPTN----HLDEKSLQFlIQQLKHYNGTVILVSHDRYFLDEAATK-IWsLEDQTLIEF 181
Cdd:COG1134 170 VDEVLAvgdaAFQKKCLAR-IRELRESGRTVIFVSHSMGAVRRLCDRaIW-LEKGRLVMD 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-166 |
3.62e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 80.14 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIhndlA----PAQGQIL--RKDI-------- 66
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMI----AgfetPDSGRILldGRDVtglppekr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 67 KLALVEQETA-----------AY--SFADQTPAEKK-----LLEKwhVPLRDF-----HQLSGGEKLKARLAKGLSEDAD 123
Cdd:COG3842 78 NVGMVFQDYAlfphltvaenvAFglRMRGVPKAEIRarvaeLLEL--VGLEGLadrypHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 124 LLLLDEPTNHLDEK---SLQFLIQQL-KHYNGTVILVSHDRyflDEA 166
Cdd:COG3842 156 VLLLDEPLSALDAKlreEMREELRRLqRELGITFIYVTHDQ---EEA 199
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-180 |
3.93e-16 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 77.26 E-value: 3.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKL-----------ALVEQ 73
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqkniealrrigALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 -------------ETAA------YSFADQTPAEKKLLEKWHVPLRDFhqlSGGEKLKARLAKGLSEDADLLLLDEPTNHL 134
Cdd:cd03268 81 pgfypnltarenlRLLArllgirKKRIDEVLDVVGLKDSAKKKVKGF---SLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2828494 135 DE---KSLQFLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:cd03268 158 DPdgiKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
288-452 |
3.96e-16 |
|
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: 77.70 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 288 GKRFLEVQNVTKafgERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ----ETAEGSVWVSPSA--------NI 355
Cdd:cd03234 7 WDVGLKAKNWNK---YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRveggGTTSGQILFNGQPrkpdqfqkCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 356 GYLTQEVFDLPLEQTPEELFENETFKARGH----------VQNLMRHLGFTaaqwtePIKHM-----SMGERVKIKLMAY 420
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLTYTAILRLPRKssdairkkrvEDVLLRDLALT------RIGGNlvkgiSGGERRRVSIAVQ 157
|
170 180 190
....*....|....*....|....*....|..
gi 2828494 421 ILEEKDVLILDEPTNHLDLPSREQLEETLSQY 452
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVSTLSQL 189
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
292-468 |
5.10e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 77.40 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAF-GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV--------SPSA------NI 355
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPtSGQVLVngqdlsrlKRREipylrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 356 GYLTQE--------VFD---LPLE---QTPEElfenetfkARGHVQNLMRHLGFTAAQWTEPIkHMSMGE--RVKIklmA 419
Cdd:COG2884 82 GVVFQDfrllpdrtVYEnvaLPLRvtgKSRKE--------IRRRVREVLDLVGLSDKAKALPH-ELSGGEqqRVAI---A 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2828494 420 Y-ILEEKDVLILDEPTNHLDlP--SRE--QLEETLSQYSGTLLAVSHDRYFLEK 468
Cdd:COG2884 150 RaLVNRPELLLADEPTGNLD-PetSWEimELLEEINRRGTTVLIATHDLELVDR 202
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
292-462 |
5.72e-16 |
|
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: 77.47 E-value: 5.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGER----TLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWVSP--------------- 351
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPtSGTVRLAGqdlfaldedararlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 352 SANIGYLTQEvFDL-P----LE--QTPEELfenetfkaRGHvqnlmRHLGFTAAQWTE-----------PiKHMSMGE-- 411
Cdd:COG4181 89 ARHVGFVFQS-FQLlPtltaLEnvMLPLEL--------AGR-----RDARARARALLErvglghrldhyP-AQLSGGEqq 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2828494 412 RVKIKlMAYILEEKdVLILDEPTNHLDLPSREQLEETL----SQYSGTLLAVSHD 462
Cdd:COG4181 154 RVALA-RAFATEPA-ILFADEPTGNLDAATGEQIIDLLfelnRERGTTLVLVTHD 206
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
18-159 |
9.64e-16 |
|
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: 76.84 E-value: 9.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 18 TVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-----------------LRKDI-----KLALVEQET 75
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinklkgkalrqLRRQIgmifqQFNLIERLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 76 AA--------------YSFADQ-TPAEK----KLLEKwhVPLRDFH-----QLSGGEKLKARLAKGLSEDADLLLLDEPT 131
Cdd:cd03256 95 VLenvlsgrlgrrstwRSLFGLfPKEEKqralAALER--VGLLDKAyqradQLSGGQQQRVAIARALMQQPKLILADEPV 172
|
170 180 190
....*....|....*....|....*....|..
gi 2828494 132 NHLDEKS----LQFLIQQLKHYNGTVILVSHD 159
Cdd:cd03256 173 ASLDPASsrqvMDLLKRINREEGITVIVSLHQ 204
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
293-438 |
1.29e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.15 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 293 EVQNVTKAFG------ERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETaegsvwvspsaniGYLTQEVFDLP 366
Cdd:COG2401 26 RVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK-------------GTPVAGCVDVP 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2828494 367 LEQTPEELFENETFKARGHVQNLMRHLGF----TAAQWTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLD 438
Cdd:COG2401 93 DNQFGREASLIDAIGRKGDFKDAVELLNAvglsDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
292-461 |
1.35e-15 |
|
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: 74.56 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFG--ERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWV--------SPSA---NIGY 357
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGlLRPTSGRVRLdgadisqwDPNElgdHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 358 LTQEVfdlpleqtpeELFEnetfkarGHVqnlmrhlgftaaqwTEPIkhMSMGERVKIKLMAYILEEKDVLILDEPTNHL 437
Cdd:cd03246 81 LPQDD----------ELFS-------GSI--------------AENI--LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180
....*....|....*....|....*..
gi 2828494 438 DLPSREQLEETLSQYS---GTLLAVSH 461
Cdd:cd03246 128 DVEGERALNQAIAALKaagATRIVIAH 154
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
292-347 |
1.36e-15 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 76.32 E-value: 1.36e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSV 347
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPtSGSV 57
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-159 |
1.59e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 76.22 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 13 EVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-------------LRKDIKLALVEQET---- 75
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvaglvpwkrrkkFLRRIGVVFGQKTQlwwd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 76 --AAYSFA------DQTPAE-KKLLEKW----------HVPLRdfhQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD- 135
Cdd:cd03267 110 lpVIDSFYllaaiyDLPPARfKKRLDELselldleellDTPVR---QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDv 186
|
170 180
....*....|....*....|....*..
gi 2828494 136 ---EKSLQFLIQQLKHYNGTVILVSHD 159
Cdd:cd03267 187 vaqENIRNFLKEYNRERGTTVLLTSHY 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
292-453 |
1.95e-15 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 75.31 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGeKVAIIGPNGSGKTTLLNIILG-QETAEGSVWV---SPSAN-------IGYLTQ 360
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATlTPPSSGTIRIdgqDVLKQpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 361 EvFDLPLEQTPEELFE---------NETFKARghVQNLMRHLGFTAAQwTEPIKHMSMGERVKIKLMAYILEEKDVLILD 431
Cdd:cd03264 80 E-FGVYPNFTVREFLDyiawlkgipSKEVKAR--VDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180
....*....|....*....|..
gi 2828494 432 EPTNHLDLPSREQLEETLSQYS 453
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELG 177
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
292-485 |
2.04e-15 |
|
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: 75.37 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVW--------VSPSA-NIGYLTQE 361
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPtSGRIYiggrdvtdLPPKDrDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 362 --------VFD-----LPLEQTPEelfenETFKARghVQNLMRHLGFTAAQWTEPiKHMSMGERVKIKLMAYILEEKDVL 428
Cdd:cd03301 81 yalyphmtVYDniafgLKLRKVPK-----DEIDER--VREVAELLQIEHLLDRKP-KQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2828494 429 ILDEPTNHLDLPSREQLEETLS----QYSGTLLAVSHDRyfLEKTT-NSKLVISNNGIEKQL 485
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKrlqqRLGTTTIYVTHDQ--VEAMTmADRIAVMNDGQIQQI 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
296-466 |
2.18e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 78.78 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 296 NVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ-ETAEGSVWVSPSANIGYLTQE--------VFD-- 364
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDlEPSAGNVSLDPNERLGKLRQDqfafeeftVLDtv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 365 -------------------LPlEQTPE----------ELFENETFKARGHVQNLMRHLGFTAAQWTEPIKHMSMGERVKI 415
Cdd:PRK15064 86 imghtelwevkqerdriyaLP-EMSEEdgmkvadlevKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2828494 416 KLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYSGTLLAVSHDRYFL 466
Cdd:PRK15064 165 LLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFL 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-167 |
2.24e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.59 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVKDQT--VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRK 64
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvggmvlseetvwdVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 65 DIKL-----------ALVEQETaAYSFADQTPAEKKLLEKWH-----VPLRDF-----HQLSGGEKLKARLAKGLSEDAD 123
Cdd:PRK13635 82 QVGMvfqnpdnqfvgATVQDDV-AFGLENIGVPREEMVERVDqalrqVGMEDFlnrepHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2828494 124 LLLLDEPTNHLDEKSLQFL---IQQLKHYNG-TVILVSHDryfLDEAA 167
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVletVRQLKEQKGiTVLSITHD---LDEAA 205
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
292-462 |
2.84e-15 |
|
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: 75.29 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLL------NIILGQETAEGSVWVSPSaNIGYLTQEVFDL 365
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLrllnrlNDLIPGAPDEGEVLLDGK-DIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 366 PLE-----QTPEEL----FENETF--KARG-----HVQNLMRHLGFTAAQWTE-----PIKHMSMGERVKIKLMAYILEE 424
Cdd:cd03260 80 RRRvgmvfQKPNPFpgsiYDNVAYglRLHGiklkeELDERVEEALRKAALWDEvkdrlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2828494 425 KDVLILDEPTNHLDLPSREQLEETLSQYSG--TLLAVSHD 462
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
292-461 |
3.25e-15 |
|
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: 74.45 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWVSPSA----------NIGYLTQ 360
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGlSPPLAGRVLLNGGPldfqrdsiarGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 361 evfdLPLEQTPEELFENETFKARGH----VQNLMRHLGFTAAQwTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNH 436
Cdd:cd03231 81 ----APGIKTTLSVLENLRFWHADHsdeqVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|....*...
gi 2828494 437 LDLPSREQLEETLSQYS---GTLLAVSH 461
Cdd:cd03231 156 LDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
292-461 |
3.85e-15 |
|
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: 73.23 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWVSpsanigylTQEV-FDLPLEq 369
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPdSGEILVD--------GKEVsFASPRD- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 370 tpeelfenetfkarghvqnlMRHLG-FTAAQwtepikhMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEET 448
Cdd:cd03216 72 --------------------ARRAGiAMVYQ-------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKV 124
|
170
....*....|....*.
gi 2828494 449 LSQY--SG-TLLAVSH 461
Cdd:cd03216 125 IRRLraQGvAVIFISH 140
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-167 |
4.10e-15 |
|
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: 78.02 E-value: 4.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYE-----VKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI----------------- 61
Cdd:COG1123 260 LLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltklsrrslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 62 LRKDIKL-------ALVEQETAAYSFAD-------QTPAEKK-----LLEKWHVPlRDF-----HQLSGGEKLKARLAKG 117
Cdd:COG1123 340 LRRRVQMvfqdpysSLNPRMTVGDIIAEplrlhglLSRAERRervaeLLERVGLP-PDLadrypHELSGGQRQRVAIARA 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2828494 118 LSEDADLLLLDEPTNHLDEkSLQF----LIQQLKH-YNGTVILVSHD----RYFLDEAA 167
Cdd:COG1123 419 LALEPKLLILDEPTSALDV-SVQAqilnLLRDLQReLGLTYLFISHDlavvRYIADRVA 476
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
292-463 |
4.74e-15 |
|
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: 73.93 E-value: 4.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-----------QETAEGSVWVSPSANIGYLTQ 360
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGllrpdsgevrwNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 361 evfdLPLEQTPEELFENETFKARGH------VQNLMRHLGFTAAQWTePIKHMSMGERVKIKLMAYILEEKDVLILDEPT 434
Cdd:TIGR01189 81 ----LPGLKPELSALENLHFWAAIHggaqrtIEDALAAVGLTGFEDL-PAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|...
gi 2828494 435 NHLDLPSREQLEETLSQYSG----TLLAVSHDR 463
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLArggiVLLTTHQDL 188
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
291-463 |
4.99e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 76.68 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 291 FLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWVSpsaniGyltQEVFDLPleq 369
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPdSGRILLD-----G---RDVTGLP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 370 tPEE-----------LF------ENETF--KARGH--------VQNLMRHLGFTA------AQwtepikhMSMGERVKIK 416
Cdd:COG3842 74 -PEKrnvgmvfqdyaLFphltvaENVAFglRMRGVpkaeirarVAELLELVGLEGladrypHQ-------LSGGQQQRVA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2828494 417 L---MAYileEKDVLILDEPTNHLDLPSREQLEETLSQY---SG-TLLAVSHDR 463
Cdd:COG3842 146 LaraLAP---EPRVLLLDEPLSALDAKLREEMREELRRLqreLGiTFIYVTHDQ 196
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
292-462 |
5.34e-15 |
|
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: 74.64 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGE-RTLFKNANFTIQHGEKVAIIGPNGSGKTTLLN-------------IILGQETAEgsvwVSPSA---N 354
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKminrlieptsgeiFIDGEDIRE----QDPVElrrK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 355 IGYLTQEVFDLP-------------LEQTPEElfenetfKARGHVQNLMRHLGFTAAQWTEPIKH-MSMGERVKIKLMAY 420
Cdd:cd03295 77 IGYVIQQIGLFPhmtveenialvpkLLKWPKE-------KIRERADELLALVGLDPAEFADRYPHeLSGGQQQRVGVARA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2828494 421 ILEEKDVLILDEPTNHLDLPSREQLEE---TLSQYSG-TLLAVSHD 462
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEefkRLQQELGkTIVFVTHD 195
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-158 |
7.18e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 77.51 E-value: 7.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVS--YEvKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDIK----------LAL 70
Cdd:COG1132 340 IEFENVSfsYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidGVDIRdltleslrrqIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 71 VEQETA----------AYSFADQTPAE--------------KKLLEKWHVPLRDF-HQLSGGEKLK---AR-LAKglseD 121
Cdd:COG1132 419 VPQDTFlfsgtireniRYGRPDATDEEveeaakaaqahefiEALPDGYDTVVGERgVNLSGGQRQRiaiARaLLK----D 494
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2828494 122 ADLLLLDEPTNHLD---EKSLQFLIQQLKHyNGTVILVSH 158
Cdd:COG1132 495 PPILILDEATSALDtetEALIQEALERLMK-GRTTIVIAH 533
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-166 |
7.69e-15 |
|
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: 73.69 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 12 YEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI------LRKDIKLAL--------------- 70
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysIRTDRKAARqslgycpqfdalfde 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 71 --VEQ------------ETAAYSFADQTPAEKKLLEKWHVPLRDfhqLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDE 136
Cdd:cd03263 90 ltVREhlrfyarlkglpKSEIKEEVELLLRVLGLTDKANKRART---LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190
....*....|....*....|....*....|...
gi 2828494 137 KSLQF---LIQQLKHyNGTVILVSHDryfLDEA 166
Cdd:cd03263 167 ASRRAiwdLILEVRK-GRSIILTTHS---MDEA 195
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
292-348 |
8.99e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 74.30 E-value: 8.99e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVW 348
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPtSGRIL 62
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
292-462 |
1.02e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 73.64 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLfkNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWVspsanigyLTQEVFDLPLEQT 370
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGfLPPDSGRILW--------NGQDLTALPPAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 371 P-EELF-ENetfkarghvqNLMRHL--------GF------TAAQWTEpIKHM-----------------SMGERVKIKL 417
Cdd:COG3840 72 PvSMLFqEN----------NLFPHLtvaqniglGLrpglklTAEQRAQ-VEQAlervglaglldrlpgqlSGGQRQRVAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2828494 418 MAYILEEKDVLILDEPTNHLDLPSREQ----LEETLSQYSGTLLAVSHD 462
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPALRQEmldlVDELCRERGLTVLMVTHD 189
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-158 |
1.20e-14 |
|
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: 73.08 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVEQETAAY---------- 78
Cdd:cd03269 5 NVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYlpeerglypk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 79 -----------SFADQTPAEKK-----------LLEKWHVPLRdfhQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDE 136
Cdd:cd03269 85 mkvidqlvylaQLKGLKKEEARrridewlerleLSEYANKRVE---ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180
....*....|....*....|....*
gi 2828494 137 KSLQFL---IQQLKHYNGTVILVSH 158
Cdd:cd03269 162 VNVELLkdvIRELARAGKTVILSTH 186
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-190 |
1.74e-14 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 73.03 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVS--YEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR-----KDIKL-------AL 70
Cdd:cd03251 1 VEFKNVTfrYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdvRDYTLaslrrqiGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 71 VEQET----------AAYSFADQTPAE--------------KKLLEKWHVPLRDFH-QLSGGEKLKARLAKGLSEDADLL 125
Cdd:cd03251 81 VSQDVflfndtvaenIAYGRPGATREEveeaaraanahefiMELPEGYDTVIGERGvKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2828494 126 LLDEPTNHLD---EKSLQFLIQQLKHyNGTVILVSHdRYFLDEAATKIWSLEDQTLIEfKGNYSGYMK 190
Cdd:cd03251 161 ILDEATSALDtesERLVQAALERLMK-NRTTFVIAH-RLSTIENADRIVVLEDGKIVE-RGTHEELLA 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-159 |
2.68e-14 |
|
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: 72.18 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 13 EVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI------------------------------- 61
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVtvrgrvssllglgggfnpeltgreniylngr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 62 ----LRKDIKlaLVEQETaaYSFADqtpaekkLLEKWHVPLRdfhQLSGGekLKARLAKGLS--EDADLLLLDEPT---- 131
Cdd:cd03220 111 llglSRKEID--EKIDEI--IEFSE-------LGDFIDLPVK---TYSSG--MKARLAFAIAtaLEPDILLIDEVLavgd 174
|
170 180
....*....|....*....|....*...
gi 2828494 132 NHLDEKSLQFLIQQLKHyNGTVILVSHD 159
Cdd:cd03220 175 AAFQEKCQRRLRELLKQ-GKTVILVSHD 201
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
292-434 |
3.05e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.06 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV--------SPS----ANIGYL 358
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPdSGEILIdgkpvrirSPRdaiaLGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQE--VFD---------LPLEQTPEELFENEtfKARGHVQNLMRHLGFtAAQWTEPIKHMSMGE--RVKI-KLmayILEE 424
Cdd:COG3845 86 HQHfmLVPnltvaenivLGLEPTKGGRLDRK--AARARIRELSERYGL-DVDPDAKVEDLSVGEqqRVEIlKA---LYRG 159
|
170
....*....|
gi 2828494 425 KDVLILDEPT 434
Cdd:COG3845 160 ARILILDEPT 169
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-181 |
3.29e-14 |
|
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: 72.33 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKD-QTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRKDIKLA 69
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedireqdpveLRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 70 L----------VEQETAAYSFADQTPAEKK------LLEKWHVPLRDF-----HQLSGGEKLKARLAKGLSEDADLLLLD 128
Cdd:cd03295 81 IqqiglfphmtVEENIALVPKLLKWPKEKIreradeLLALVGLDPAEFadrypHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 129 EPTNHLD---EKSLQFLIQQLKHYNG-TVILVSHDryfLDEA---ATKIWSLEDQTLIEF 181
Cdd:cd03295 161 EPFGALDpitRDQLQEEFKRLQQELGkTIVFVTHD---IDEAfrlADRIAIMKNGEIVQV 217
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-159 |
3.30e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 73.96 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVS--YEVKDQTV--FKHVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDL-APAQGQIL---------------- 62
Cdd:COG1135 1 MIELENLSktFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI-NLLeRPTSGSVLvdgvdltalserelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 63 -RKDIKL-----ALVEQETA----AYSF--ADQTPAEKK-----LLEKwhVPLRDFH-----QLSGGEKLKARLAKGLSE 120
Cdd:COG1135 80 aRRKIGMifqhfNLLSSRTVaenvALPLeiAGVPKAEIRkrvaeLLEL--VGLSDKAdaypsQLSGGQKQRVGIARALAN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2828494 121 DADLLLLDEPTNHLDEKS----LQfLIQQL-KHYNGTVILVSHD 159
Cdd:COG1135 158 NPKVLLCDEATSALDPETtrsiLD-LLKDInRELGLTIVLITHE 200
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
291-462 |
3.72e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.49 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 291 FLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ-ETAEGSVWV------SPSAN-----IGYL 358
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTlTPTAGTVLVagddveALSARaasrrVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQEV---FDLPLEQTPE-------ELFENETFKARGHVQNLMRHLGfTAAQWTEPIKHMSMGERVKIKLMAYILEEKDVL 428
Cdd:PRK09536 83 PQDTslsFEFDVRQVVEmgrtphrSRFDTWTETDRAAVERAMERTG-VAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 2828494 429 ILDEPTNHLDLPSREQ---LEETLSQYSGTLLAVSHD 462
Cdd:PRK09536 162 LLDEPTASLDINHQVRtleLVRRLVDDGKTAVAAIHD 198
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-183 |
3.99e-14 |
|
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: 71.98 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 21 KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDI--------KLALVEQETA-----------AYS 79
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlnGKDItnlppekrDISYVPQNYAlfphmtvykniAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 FADQTPAEKKLLEKW----------HVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLK-- 147
Cdd:cd03299 96 LKKRKVDKKEIERKVleiaemlgidHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKki 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 2828494 148 --HYNGTVILVSHDryfLDEAatkiWSLEDQTLIEFKG 183
Cdd:cd03299 176 rkEFGVTVLHVTHD---FEEA----WALADKVAIMLNG 206
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
292-461 |
4.08e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 74.82 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTkaF---GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ-ETAEGSVWV--------SPSA---NIG 356
Cdd:COG1132 340 IEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFyDPTSGRILIdgvdirdlTLESlrrQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 357 YLTQEVFdlpleqtpeeLF-----ENETFkARGH-----VQNLMRhlgftAAQWTEPIKHM---------------SMGE 411
Cdd:COG1132 418 VVPQDTF----------LFsgtirENIRY-GRPDatdeeVEEAAK-----AAQAHEFIEALpdgydtvvgergvnlSGGQ 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2828494 412 RVKIKLM-AyILEEKDVLILDEPTNHLDLPSREQLEETLSQYSG--TLLAVSH 461
Cdd:COG1132 482 RQRIAIArA-LLKDPPILILDEATSALDTETEALIQEALERLMKgrTTIVIAH 533
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
299-484 |
4.44e-14 |
|
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: 71.56 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 299 KAFGERTLfkNANFTIQhGEKVAIIGPNGSGKTTLLNIILGQETAE-------GSVWVSPSAN---------IGYLTQEV 362
Cdd:cd03297 8 KRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDggtivlnGTVLFDSRKKinlppqqrkIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 363 fdlpleqtpeELF------ENETFKARGHVQNLMR-------------HLGFtaaqwtEPIKHMSMGERVKIKLMAYILE 423
Cdd:cd03297 85 ----------ALFphlnvrENLAFGLKRKRNREDRisvdelldllgldHLLN------RYPAQLSGGEKQRVALARALAA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2828494 424 EKDVLILDEPTNHLDLPSREQ----LEETLSQYSGTLLAVSHDRYFLEKTTNSKLVISNNGIEKQ 484
Cdd:cd03297 149 QPELLLLDEPFSALDRALRLQllpeLKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
292-349 |
4.54e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 71.95 E-value: 4.54e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV 349
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPdSGTITV 60
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
290-499 |
4.81e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 74.90 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 290 RFLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNI---------------------ILGQETA----- 343
Cdd:PLN03073 176 KDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYmamhaidgipkncqilhveqeVVGDDTTalqcv 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 344 --------------------------EGSVWVSPSANIGYLTQEVFDLPLEQTPEELFENETFKARGHVQNLMRHLGFTA 397
Cdd:PLN03073 256 lntdiertqlleeeaqlvaqqrelefETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTP 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 398 AQWTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYSGTLLAVSHDRYFLEKTTNSKLVIS 477
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLH 415
|
250 260
....*....|....*....|...
gi 2828494 478 NNGIEKQLNDVPS-ERNEREELR 499
Cdd:PLN03073 416 GQKLVTYKGDYDTfERTREEQLK 438
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
292-462 |
5.60e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.33 E-value: 5.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSVWVSP-----------SANIGYLT 359
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGehiqhyaskevARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 360 QEVfDLPLEQTPEELFenetfkARGH-----------------VQNLMRHLGFTAAQwTEPIKHMSMGERVKIKLMAYIL 422
Cdd:PRK10253 88 QNA-TTPGDITVQELV------ARGRyphqplftrwrkedeeaVTKAMQATGITHLA-DQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2828494 423 EEKDVLILDEPTNHLDLPSREQLEETLSQYSG----TLLAVSHD 462
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNRekgyTLAAVLHD 203
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-159 |
5.94e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 70.97 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 6 TLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAP---AQGQILRKDIKLAL--VEQETAAYSF 80
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAlpAEQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 81 ADQ---------------TP-----AEKKL-----LEKW---HVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTN 132
Cdd:COG4136 83 QDDllfphlsvgenlafaLPptigrAQRRArveqaLEEAglaGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190
....*....|....*....|....*....|..
gi 2828494 133 HLDeKSL-----QFLIQQLKHYNGTVILVSHD 159
Cdd:COG4136 163 KLD-AALraqfrEFVFEQIRQRGIPALLVTHD 193
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-159 |
6.29e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 74.32 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 16 DQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVEQE--TAAYSFADQTP-------- 85
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevRRRVSVCAQDAhlfdttvr 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 86 ------------------AEKKLLEKWHVPLRDFHQ---------LSGGEKLKARLAKGLSEDADLLLLDEPTNHLD-EK 137
Cdd:TIGR02868 427 enlrlarpdatdeelwaaLERVGLADWLRALPDGLDtvlgeggarLSGGERQRLALARALLADAPILLLDEPTEHLDaET 506
|
170 180
....*....|....*....|...
gi 2828494 138 SLQFLIQQLKHYNG-TVILVSHD 159
Cdd:TIGR02868 507 ADELLEDLLAALSGrTVVLITHH 529
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
294-474 |
8.03e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.30 E-value: 8.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 294 VQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ-ETAEGSVWVSPSANIGYLTQEV-FDLPLEQTP 371
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLvAPDEGVIKRNGKLRIGYVPQKLyLDTTLPLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 372 EELFeneTFKARGHVQNLMRHLGFTAAQ--WTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETL 449
Cdd:PRK09544 87 NRFL---RLRPGTKKEDILPALKRVQAGhlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLI 163
|
170 180
....*....|....*....|....*....
gi 2828494 450 SQYSGTL----LAVSHDRYFLEKTTNSKL 474
Cdd:PRK09544 164 DQLRRELdcavLMVSHDLHLVMAKTDEVL 192
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
293-462 |
8.17e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.43 E-value: 8.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 293 EVQNVTKAF-----------GERTLF----------KNANFTIQHGEKVAIIGPNGSGKTTLLNIILG--QETAeGSVWV 349
Cdd:COG4586 3 EVENLSKTYrvyekepglkgALKGLFrreyreveavDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGilVPTS-GEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 350 ---SPS-------ANIGYL----TQEVFDLPLEQT----------PEELFEN--ETFKARGHVQNLMrhlgftaaqwTEP 403
Cdd:COG4586 82 lgyVPFkrrkefaRRIGVVfgqrSQLWWDLPAIDSfrllkaiyriPDAEYKKrlDELVELLDLGELL----------DTP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 404 IKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYS----GTLLAVSHD 462
Cdd:COG4586 152 VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNrergTTILLTSHD 214
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-164 |
1.03e-13 |
|
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: 73.67 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 26 SVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIlRKDIKLA------------LVEQ--ETAAYSFADQTPAE---- 87
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDLKISykpqyispdydgTVEEflRSANTDDFGSSYYKteii 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 88 -----KKLLEKwhvPLRDfhqLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD-EKSLQF--LIQQLKHYNG-TVILVSH 158
Cdd:COG1245 441 kplglEKLLDK---NVKD---LSGGELQRVAIAACLSRDADLYLLDEPSAHLDvEQRLAVakAIRRFAENRGkTAMVVDH 514
|
....*.
gi 2828494 159 DRYFLD 164
Cdd:COG1245 515 DIYLID 520
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-168 |
1.03e-13 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 70.36 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL----------RKDIKLALVEQE 74
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdlpPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 75 TAAY---------SFA----DQTPAE--------KKLLEKWHVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNH 133
Cdd:cd03301 81 YALYphmtvydniAFGlklrKVPKDEidervrevAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2828494 134 LDEK-------SLQFLIQQLKHyngTVILVSHDRyflDEAAT 168
Cdd:cd03301 161 LDAKlrvqmraELKRLQQRLGT---TTIYVTHDQ---VEAMT 196
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-339 |
1.06e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 73.51 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 27 VQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI---LRKDIKLA------LVEQE------------------TAAYS 79
Cdd:PRK10938 26 LNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsqFSHITRLSfeqlqkLVSDEwqrnntdmlspgeddtgrTTAEI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 FADQTPAE---KKLLEKWHV-PL--RDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKS---LQFLIQQLKHYN 150
Cdd:PRK10938 106 IQDEVKDParcEQLAQQFGItALldRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASrqqLAELLASLHQSG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 151 GTVILVSHDRYFLDEAATKIWSLEDQTLIEfkgnysgymkfrekkrlTQQREYEKQQKMVerieAQMnglaswsekAHAQ 230
Cdd:PRK10938 186 ITLVLVLNRFDEIPDFVQFAGVLADCTLAE-----------------TGEREEILQQALV----AQL---------AHSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 231 stkkegfkeyhrvkaKRTDAQIkskqkrleKELEKAKAEPVTPEYTVRFsidtthktgkrflEVQNVTKAFGERTLFKNA 310
Cdd:PRK10938 236 ---------------QLEGVQL--------PEPDEPSARHALPANEPRI-------------VLNNGVVSYNDRPILHNL 279
|
330 340
....*....|....*....|....*....
gi 2828494 311 NFTIQHGEKVAIIGPNGSGKTTLLNIILG 339
Cdd:PRK10938 280 SWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
276-478 |
1.31e-13 |
|
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: 70.25 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 276 TVRFSIDTTHKTGKRFLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWV--SPS 352
Cdd:cd03220 7 SKSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiYPPDSGTVTVrgRVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 353 ANIGY-------LTQEvfdlpleqtpeelfENETFKAR--GHVQNLMRH-----LGFTA--AQWTEPIKHMSMGERVKIK 416
Cdd:cd03220 87 SLLGLgggfnpeLTGR--------------ENIYLNGRllGLSRKEIDEkideiIEFSElgDFIDLPVKTYSSGMKARLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2828494 417 LMAYILEEKDVLILDEPT----NHLDLPSREQLEETLSQySGTLLAVSHDRYFLEKTTNSKLVISN 478
Cdd:cd03220 153 FAIATALEPDILLIDEVLavgdAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEK 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-168 |
1.43e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.56 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 3 EIVTLTNvSYEvkDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLAL------------ 70
Cdd:PRK11607 21 EIRNLTK-SFD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvppyqrpinmmf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 71 ----------VEQETAAYSFADQTP-AE-----KKLLEKWHV---PLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPT 131
Cdd:PRK11607 98 qsyalfphmtVEQNIAFGLKQDKLPkAEiasrvNEMLGLVHMqefAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2828494 132 NHLDEK---SLQF-LIQQLKHYNGTVILVSHDRyflDEAAT 168
Cdd:PRK11607 178 GALDKKlrdRMQLeVVDILERVGVTCVMVTHDQ---EEAMT 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-166 |
1.54e-13 |
|
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: 70.75 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 21 KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL----------RKDI------KLALVEQ----------- 73
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLidgqdiaamsRKELrelrrkKISMVFQsfallphrtvl 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 ETAAYSFADQTPAEKKLLEKW-----HVPLRDF-----HQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD---EKSLQ 140
Cdd:cd03294 121 ENVAFGLEVQGVPRAEREERAaealeLVGLEGWehkypDELSGGMQQRVGLARALAVDPDILLMDEAFSALDpliRREMQ 200
|
170 180
....*....|....*....|....*...
gi 2828494 141 --FLIQQLKHYNgTVILVSHDryfLDEA 166
Cdd:cd03294 201 deLLRLQAELQK-TIVFITHD---LDEA 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-166 |
1.89e-13 |
|
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: 69.80 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 21 KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL----------------------------RKDIKLALVE 72
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIlegkqitepgpdrmvvfqnysllpwltvRENIALAVDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 73 qetaaySFADQTPAEKKLLEKWHVPL--------RDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD---EKSLQF 141
Cdd:TIGR01184 82 ------VLPDLSKSERRAIVEEHIALvglteaadKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDaltRGNLQE 155
|
170 180
....*....|....*....|....*.
gi 2828494 142 LIQQLKHYNG-TVILVSHDryfLDEA 166
Cdd:TIGR01184 156 ELMQIWEEHRvTVLMVTHD---VDEA 178
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
292-462 |
1.98e-13 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 69.96 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEgsvwvspSANIGYLTQEVFDLPLEQTP 371
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT-------SGEILLDGKDITNLPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 372 -------------EELFENETF------------KARghVQNLMRHLGFTAAQWTEPiKHMSMGERVKIKLMAYILEEKD 426
Cdd:cd03300 74 vntvfqnyalfphLTVFENIAFglrlkklpkaeiKER--VAEALDLVQLEGYANRKP-SQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2828494 427 VLILDEPTNHLDLPSREQLEETLSQYSG----TLLAVSHD 462
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHD 190
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-147 |
2.06e-13 |
|
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: 69.88 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKD------------------- 65
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlgigyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 66 -------IKLAlVEQ------ETAAYSFADQTPAEKKLLEKWHV-PLRD--FHQLSGGEKLKARLAKGLSEDADLLLLDE 129
Cdd:cd03218 81 pqeasifRKLT-VEEnilavlEIRGLSKKEREEKLEELLEEFHItHLRKskASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180
....*....|....*....|.
gi 2828494 130 PTNHLDEKS---LQFLIQQLK 147
Cdd:cd03218 160 PFAGVDPIAvqdIQKIIKILK 180
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
292-461 |
2.06e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.13 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWVSPSANIgyltqevFDLPLEQT 370
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGlLPPAAGTIKLDGGDID-------DPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 371 ----------PE-ELFENETFKAR------------------GHVQNLmrhlgftaaqwtePIKHMSMGE--RVKI-KLM 418
Cdd:PRK13539 76 hylghrnamkPAlTVAENLEFWAAflggeeldiaaaleavglAPLAHL-------------PFGYLSAGQkrRVALaRLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2828494 419 AYileEKDVLILDEPTNHLDLPSREQLEETLSQYS---GTLLAVSH 461
Cdd:PRK13539 143 VS---NRPIWILDEPTAALDAAAVALFAELIRAHLaqgGIVIAATH 185
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-183 |
2.46e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 70.53 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVK---DQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--------------R 63
Cdd:PRK13650 1 MSNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIidgdllteenvwdiR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 64 KDIKL-----------ALVEQETaAYSFADQTPAEKKLLEKWH-----VPLRDFH-----QLSGGEKLKARLAKGLSEDA 122
Cdd:PRK13650 81 HKIGMvfqnpdnqfvgATVEDDV-AFGLENKGIPHEEMKERVNealelVGMQDFKerepaRLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2828494 123 DLLLLDEPTNHLDEKSLQFLIQQLK----HYNGTVILVSHDryfLDEAAtkiwsLEDQTLIEFKG 183
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKgirdDYQMTVISITHD---LDEVA-----LSDRVLVMKNG 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
292-461 |
2.54e-13 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 68.11 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGE--RTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWVSP----------SANIGYL 358
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPqQGEITLDGvpvsdlekalSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQEVFdlpleqtpeeLFENetfkarghvqNLMRHLGftaaqwtepiKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLD 438
Cdd:cd03247 81 NQRPY----------LFDT----------TLRNNLG----------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180
....*....|....*....|....*
gi 2828494 439 LPSREQLEETLSQY--SGTLLAVSH 461
Cdd:cd03247 131 PITERQLLSLIFEVlkDKTLIWITH 155
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
292-349 |
2.86e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 71.26 E-value: 2.86e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV 349
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPtSGEILI 62
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-171 |
3.44e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 69.89 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYEVKDQT--VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKL-------ALVEQETA--- 76
Cdd:COG4525 10 SVRYPGGGQPqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadrGVVFQKDAllp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 77 ----------AYSFADQTPAEKK-----LLEKwhVPLRDFH-----QLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD- 135
Cdd:COG4525 90 wlnvldnvafGLRLRGVPKAERRaraeeLLAL--VGLADFArrriwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDa 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2828494 136 --EKSLQFLIQQLKHYNG-TVILVSHDryfLDEA---ATKIW 171
Cdd:COG4525 168 ltREQMQELLLDVWQRTGkGVFLITHS---VEEAlflATRLV 206
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
292-478 |
3.48e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.34 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAF----------------------GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVW 348
Cdd:COG1134 5 IEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPtSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 349 VSpsaniGYLTQevfdlPLeqtpeEL---FENEtFKARghvQNLM---RHLGFTAAQWTE-----------------PIK 405
Cdd:COG1134 85 VN-----GRVSA-----LL-----ELgagFHPE-LTGR---ENIYlngRLLGLSRKEIDEkfdeivefaelgdfidqPVK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2828494 406 HMSMGERVKIKL-MAYILEEkDVLILDEPTNHLDLP----SREQLEEtLSQYSGTLLAVSHDRYFLEKTTNSKLVISN 478
Cdd:COG1134 146 TYSSGMRARLAFaVATAVDP-DILLVDEVLAVGDAAfqkkCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-164 |
3.71e-13 |
|
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: 69.36 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 26 SVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVEQetaaYSFADQTPAEKKLLEK----------WH 95
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQ----YIKADYEGTVRDLLSSitkdfythpyFK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 96 V----PL-------RDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLKHY----NGTVILVSHDR 160
Cdd:cd03237 97 TeiakPLqieqildREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHDI 176
|
....
gi 2828494 161 YFLD 164
Cdd:cd03237 177 IMID 180
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
292-468 |
4.70e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.22 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAE-GSVWVS----PS------ANIGYLTQ 360
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDaGSISLCgepvPSrarharQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 361 evfdlpleqtpeelFEN--ETFKARGHVQNLMRHLGFTAAQWTE-----------------PIKHMSMGERVKIKLMAYI 421
Cdd:PRK13537 88 --------------FDNldPDFTVRENLLVFGRYFGLSAAAARAlvppllefaklenkadaKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2828494 422 LEEKDVLILDEPTNHLDLPSR----EQLEETLSQySGTLLAVSHdryFLEK 468
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARhlmwERLRSLLAR-GKTILLTTH---FMEE 200
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
5-167 |
4.96e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.84 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVfkHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI----------------------- 61
Cdd:PRK10771 2 LKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdhtttppsrrpvsmlfqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 62 --------LRKDIKLAL-------VEQETAAYSFADQTPAEkKLLEKwhVPlrdfHQLSGGEKLKARLAKGLSEDADLLL 126
Cdd:PRK10771 80 nnlfshltVAQNIGLGLnpglklnAAQREKLHAIARQMGIE-DLLAR--LP----GQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2828494 127 LDEPTNHLD----EKSLQFLIQQLKHYNGTVILVSHDryfLDEAA 167
Cdd:PRK10771 153 LDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHS---LEDAA 194
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
292-451 |
5.01e-13 |
|
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: 68.55 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNII--LGQETAeGSVWVSP----------SANIGYLT 359
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLttLLKPTS-GRATVAGhdvvreprevRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 360 QevfDLPLEqtpEEL--FEN-ETF---------KARGHVQNLMRHLGFTAAQwTEPIKHMSMGERVKIKLMAYILEEKDV 427
Cdd:cd03265 80 Q---DLSVD---DELtgWENlYIHarlygvpgaERRERIDELLDFVGLLEAA-DRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180
....*....|....*....|....
gi 2828494 428 LILDEPTNHLDLPSREQLEETLSQ 451
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEK 176
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
22-159 |
5.34e-13 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 68.91 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 22 HVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDI--------------------------------K 67
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdGRDItglpphriarlgiartfqnprlfpeltvlenvL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 68 LAL------------------VEQETAAYSFADQTPAEKKLLEKWHVPLRDfhqLSGGEKLKARLAKGLSEDADLLLLDE 129
Cdd:COG0411 102 VAAharlgrgllaallrlpraRREEREARERAEELLERVGLADRADEPAGN---LSYGQQRRLEIARALATEPKLLLLDE 178
|
170 180 190
....*....|....*....|....*....|....
gi 2828494 130 PT---NHLDEKSLQFLIQQLKHYNG-TVILVSHD 159
Cdd:COG0411 179 PAaglNPEETEELAELIRRLRDERGiTILLIEHD 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-434 |
5.67e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.20 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 21 KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------RKDIKLAL------VEQETAAysFADQTPAE 87
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILldgepvrFRSPRDAQaagiaiIHQELNL--VPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 88 -----------------------KKLLEKWHV------PLRDfhqLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEK- 137
Cdd:COG1129 99 niflgreprrgglidwramrrraRELLARLGLdidpdtPVGD---LSVAQQQLVEIARALSRDARVLILDEPTASLTERe 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 138 --SLQFLIQQLKHYNGTVILVSHdryFLDEaatkIWSLEDQTLIeFK-GNYSGYMKFREkkrLTQqreyekqqkmvERIE 214
Cdd:COG1129 176 veRLFRIIRRLKAQGVAIIYISH---RLDE----VFEIADRVTV-LRdGRLVGTGPVAE---LTE-----------DELV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 215 AQMNGlaswsekahaqstkkegfkeyhrvkakrtdaqikskqkrleKELEKakaepvtpEYTVRfsidtTHKTGKRFLEV 294
Cdd:COG1129 234 RLMVG-----------------------------------------RELED--------LFPKR-----AAAPGEVVLEV 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 295 QNVTKafgeRTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV--------SPS----ANIGYLTQE 361
Cdd:COG1129 260 EGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPAdSGEIRLdgkpvrirSPRdairAGIAYVPED 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 362 ------VFDLPLEqtpeelfENETF---------------KARGHVQNLMRHLGFTAAQWTEPIKHMSMGERVKI---KL 417
Cdd:COG1129 336 rkgeglVLDLSIR-------ENITLasldrlsrgglldrrRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVvlaKW 408
|
490
....*....|....*..
gi 2828494 418 MAyilEEKDVLILDEPT 434
Cdd:COG1129 409 LA---TDPKVLILDEPT 422
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-165 |
6.61e-13 |
|
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: 67.07 E-value: 6.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 2 KEIVTLTNVSyeVKDQtvFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR--KDIK-----------L 68
Cdd:cd03215 2 EPVLEVRGLS--VKGA--VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdgKPVTrrsprdairagI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 ALVEQETAAYS-FADQTPAEKKLLEkwhvplrdfHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQF---LIQ 144
Cdd:cd03215 78 AYVPEDRKREGlVLDLSVAENIALS---------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEiyrLIR 148
|
170 180
....*....|....*....|.
gi 2828494 145 QLKHYNGTVILVSHDryfLDE 165
Cdd:cd03215 149 ELADAGKAVLLISSE---LDE 166
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-160 |
7.46e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.20 E-value: 7.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKE---IVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVEQET-- 75
Cdd:PRK10247 1 MQEnspLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 76 --AAYS------FAD--------------QTPAEKKL---LEKWHVPL----RDFHQLSGGEKLKARLAKGLSEDADLLL 126
Cdd:PRK10247 81 qqVSYCaqtptlFGDtvydnlifpwqirnQQPDPAIFlddLERFALPDtiltKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 2828494 127 LDEPTNHLDEKSLQFLIQQLKHYNG----TVILVSHDR 160
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVReqniAVLWVTHDK 198
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-183 |
8.88e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 67.78 E-value: 8.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 21 KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDI-----------KLALVEQETAAYS---------- 79
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFdvvkepaearrRLGFVSDSTGLYDrltarenley 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 FAD--------QTPAEKKLLEKWHV-PLRD--FHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLKH 148
Cdd:cd03266 102 FAGlyglkgdeLTARLEELADRLGMeELLDrrVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQ 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 2828494 149 YN--GTVILVSHDRyfLDEAAtkiwSLEDQTLIEFKG 183
Cdd:cd03266 182 LRalGKCILFSTHI--MQEVE----RLCDRVVVLHRG 212
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-159 |
9.59e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.17 E-value: 9.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVEQETAAYsFADQ- 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLM-FQDAr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 84 -------------------TPAEKKLLEKwhVPLRDFHQ-----LSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKS- 138
Cdd:PRK11247 92 llpwkkvidnvglglkgqwRDAALQALAA--VGLADRANewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALTr 169
|
170 180
....*....|....*....|....
gi 2828494 139 --LQFLIQQL-KHYNGTVILVSHD 159
Cdd:PRK11247 170 ieMQDLIESLwQQHGFTVLLVTHD 193
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-158 |
1.01e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 67.13 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 18 TVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVEQETA-AYSFADQTPAEKKLLEK--- 93
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIArGLLYLGHAPGIKTTLSVlen 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 94 ---WH--------------VPLRDF-----HQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLKHY-- 149
Cdd:cd03231 94 lrfWHadhsdeqveealarVGLNGFedrpvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHca 173
|
170
....*....|
gi 2828494 150 -NGTVILVSH 158
Cdd:cd03231 174 rGGMVVLTTH 183
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
292-492 |
1.27e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.81 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEG--------SVwVSPSANIGYLTQEV- 362
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSgdlivdglKV-NDPKVDERLIRQEAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 363 -----FDLPLEQTPeelFENETF-----------KARGHVQNLMRHLGFTAAQWTEPiKHMSMG--ERVKIklmAYILEE 424
Cdd:PRK09493 81 mvfqqFYLFPHLTA---LENVMFgplrvrgaskeEAEKQARELLAKVGLAERAHHYP-SELSGGqqQRVAI---ARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2828494 425 KDVLIL-DEPTNHLDLPSRE---QLEETLSQYSGTLLAVSHDRYFLEKTTNSKLVISNNGI------EKQLNDVPSER 492
Cdd:PRK09493 154 KPKLMLfDEPTSALDPELRHevlKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIaedgdpQVLIKNPPSQR 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-180 |
1.34e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 67.71 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDL-APAQGQILRKDIKLALVEQETAAYS--- 79
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI-NLLeEPDSGTITVDGEDLTDSKKDINKLRrkv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 ---------FADQT--------P----------AEKK---LLEKwhVPLRDF-----HQLSGGEKLKARLAKGLSEDADL 124
Cdd:COG1126 80 gmvfqqfnlFPHLTvlenvtlaPikvkkmskaeAEERameLLER--VGLADKadaypAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 125 LLLDEPTNHLD-EKS---LQfLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:COG1126 158 MLFDEPTSALDpELVgevLD-VMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVE 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
292-462 |
1.55e-12 |
|
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: 70.08 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAF-GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWVS-----------PSANIGYL 358
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlLDPLQGEVTLDgvpvssldqdeVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQE--VFDLPL---------EQTPEELfenETFKARGHVQNLMRHLGFTAAQW-TEPIKHMSMGERVKIKLMAYILEEKD 426
Cdd:TIGR02868 415 AQDahLFDTTVrenlrlarpDATDEEL---WAALERVGLADWLRALPDGLDTVlGEGGARLSGGERQRLALARALLADAP 491
|
170 180 190
....*....|....*....|....*....|....*...
gi 2828494 427 VLILDEPTNHLDLPSREQLEETLSQ-YSG-TLLAVSHD 462
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLEDLLAaLSGrTVVLITHH 529
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
313-461 |
1.71e-12 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 66.75 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 313 TIQHGEKVAIIGPNGSGKTTLLNIILGQETAE-GSVWVSpsaNIGYLTQEVFDLPLEQTPEE--LFENETFKA------- 382
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQsGRVLIN---GVDVTAAPPADRPVSMLFQEnnLFAHLTVEQnvglgls 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 383 ---------RGHVQNLMRHLGFTAAQWTEPiKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLS--- 450
Cdd:cd03298 97 pglkltaedRQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLdlh 175
|
170
....*....|..
gi 2828494 451 -QYSGTLLAVSH 461
Cdd:cd03298 176 aETKMTVLMVTH 187
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
292-438 |
1.72e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.80 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFG-----ERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWVSpSANIGYLTQE---- 361
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPdSGSILID-GKDVTKLPEYkrak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 362 ----VFDLPLEQTPEEL--FENETF-KARGHVQNLmrHLGFTAAQ---WTEPIKHMSMG--ERVKIK------------- 416
Cdd:COG1101 81 yigrVFQDPMMGTAPSMtiEENLALaYRRGKRRGL--RRGLTKKRrelFRELLATLGLGleNRLDTKvgllsggqrqals 158
|
170 180
....*....|....*....|...
gi 2828494 417 -LMAyILEEKDVLILDEPTNHLD 438
Cdd:COG1101 159 lLMA-TLTKPKLLLLDEHTAALD 180
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
292-452 |
1.79e-12 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 66.62 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNA----NFTIQHGEKVAIIGPNGSGKTTLLNIILGQetaegsvwVSPSAniGYLTQEVFDlpL 367
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAvdgvSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL--------LEPDA--GFATVDGFD--V 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 368 EQTPEEL-------------------FENETFKARGH----------VQNLMRHLGFtAAQWTEPIKHMSMGERVKIKLM 418
Cdd:cd03266 70 VKEPAEArrrlgfvsdstglydrltaRENLEYFAGLYglkgdeltarLEELADRLGM-EELLDRRVGGFSTGMRQKVAIA 148
|
170 180 190
....*....|....*....|....*....|....
gi 2828494 419 AYILEEKDVLILDEPTNHLDLPSREQLEETLSQY 452
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQL 182
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
292-370 |
1.95e-12 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 67.21 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGE-RTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWV--------------SPSANI 355
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlVEPTSGSVLIdgtdinklkgkalrQLRRQI 80
|
90
....*....|....*
gi 2828494 356 GYLTQEvFDLPLEQT 370
Cdd:cd03256 81 GMIFQQ-FNLIERLS 94
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-180 |
2.20e-12 |
|
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: 66.74 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVS--YEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVE---------- 72
Cdd:cd03252 1 ITFEHVRfrYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADpawlrrqvgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 73 --QETAAYS--------FADQTPAEKKLLEKwhVPLRDFHQ-------------------LSGGEKLKARLAKGLSEDAD 123
Cdd:cd03252 81 vlQENVLFNrsirdniaLADPGMSMERVIEA--AKLAGAHDfiselpegydtivgeqgagLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2828494 124 LLLLDEPTNHLDEKSLQFLIQQLKHY--NGTVILVSHdRYFLDEAATKIWSLEDQTLIE 180
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAH-RLSTVKNADRIIVMEKGRIVE 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
292-465 |
2.32e-12 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 66.40 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV------SPSANIGYLTQEV-- 362
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPdSGTIIIdglkltDDKKNINELRQKVgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 363 ----FDlpleqtpeeLFENETFKarghvQNLM----RHLGFTAAQWTEpiKHMSMGERVKI--KLMAYILE--------- 423
Cdd:cd03262 81 vfqqFN---------LFPHLTVL-----ENITlapiKVKGMSKAEAEE--RALELLEKVGLadKADAYPAQlsggqqqrv 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2828494 424 --------EKDVLILDEPTNHLDlPS--REQLE--ETLSQYSGTLLAVSHDRYF 465
Cdd:cd03262 145 aiaralamNPKVMLFDEPTSALD-PElvGEVLDvmKDLAEEGMTMVVVTHEMGF 197
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
291-449 |
2.79e-12 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 66.48 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 291 FLEVQNVTKAFGE-RTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWV-----------SPSANIGY 357
Cdd:cd03254 2 EIEFENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfYDPQKGQILIdgidirdisrkSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 358 LTQEVF----------DLPLEQTPEELFENETFKARGHvqNLMRHL--GFtAAQWTEPIKHMSMGERVKIKLMAYILEEK 425
Cdd:cd03254 82 VLQDTFlfsgtimeniRLGRPNATDEEVIEAAKEAGAH--DFIMKLpnGY-DTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180
....*....|....*....|....
gi 2828494 426 DVLILDEPTNHLDLPSREQLEETL 449
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEAL 182
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-184 |
2.79e-12 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 66.48 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 8 TNVSYEvKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDI------------KLALVEQET 75
Cdd:cd03254 8 VNFSYD-EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrsMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 76 AAYS--------FADQTPAEKKLLEKWH-VPLRDF----------------HQLSGGEKLKARLAKGLSEDADLLLLDEP 130
Cdd:cd03254 87 FLFSgtimenirLGRPNATDEEVIEAAKeAGAHDFimklpngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 131 TNHLD---EKSLQFLIQQLKHyNGTVILVSHdRYFLDEAATKIWSLEDQTLIEfKGN 184
Cdd:cd03254 167 TSNIDtetEKLIQEALEKLMK-GRTSIIIAH-RLSTIKNADKILVLDDGKIIE-EGT 220
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
173-279 |
3.19e-12 |
|
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: 62.21 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 173 LEDQTLIEFKGNYSGYMKFREKKRLTQQREYEKQQKMVERIEAqmnglaswsekahaqstkkegFKEYHRVKAKRTdAQI 252
Cdd:pfam12848 3 LERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEE---------------------FIDRFRAKASKA-KQA 60
|
90 100
....*....|....*....|....*..
gi 2828494 253 KSKQKRLEKeLEKAKAePVTPEYTVRF 279
Cdd:pfam12848 61 QSRIKALEK-MERIEK-PERDKPKLRF 85
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
23-131 |
3.35e-12 |
|
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: 65.92 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 23 VNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR--KDIK-----------LALVEQ--------------ET 75
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgRDITglppheraragIGYVPEgrrifpeltveenlLL 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2828494 76 AAYSFADQTPAEK---------KLLEKWHvplRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPT 131
Cdd:cd03224 99 GAYARRRAKRKARlervyelfpRLKERRK---QLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
292-480 |
3.56e-12 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 64.48 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGE-RTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGqetaegsVWVSPSANIGYLTQE-VFDLPleQ 369
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-------LWPWGSGRIGMPEGEdLLFLP--Q 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 370 TPeelfenetFKARGhvqNLMRHLGFTaaqWTepiKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETL 449
Cdd:cd03223 72 RP--------YLPLG---TLREQLIYP---WD---DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
170 180 190
....*....|....*....|....*....|.
gi 2828494 450 SQYSGTLLAVSHdRYFLEKTTNSKLVISNNG 480
Cdd:cd03223 135 KELGITVISVGH-RPSLWKFHDRVLDLDGEG 164
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
293-439 |
4.63e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 66.26 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 293 EVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV-------SPSA----NIGYLTQ 360
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPdSGEVLVdgldvatTPSRelakRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 361 E--------VFDL------PLEQ---TPEElfenetfkaRGHVQNLMRHLGFtaaqwtEPIKH-----MSMGERvkikLM 418
Cdd:COG4604 83 EnhinsrltVRELvafgrfPYSKgrlTAED---------REIIDEAIAYLDL------EDLADryldeLSGGQR----QR 143
|
170 180
....*....|....*....|....*
gi 2828494 419 AYI----LEEKDVLILDEPTNHLDL 439
Cdd:COG4604 144 AFIamvlAQDTDYVLLDEPLNNLDM 168
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
292-462 |
5.33e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 65.95 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVwvspsanigyltqEVFDLPLEQ- 369
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEV-------------RLNGRPLADw 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 370 TPEELfenetfkARghvqnlMR-------HLGFT----------AAQWTEPIKH------------------------MS 408
Cdd:PRK13548 70 SPAEL-------AR------RRavlpqhsSLSFPftveevvamgRAPHGLSRAEddalvaaalaqvdlahlagrdypqLS 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2828494 409 MGERVKIKLmAYIL-------EEKDVLILDEPTNHLDLPSREQLEETLSQYS----GTLLAVSHD 462
Cdd:PRK13548 137 GGEQQRVQL-ARVLaqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhergLAVIVVLHD 200
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
306-361 |
5.54e-12 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 65.18 E-value: 5.54e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 306 LFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWVSPSanIGYLTQE 361
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKlSGSVSVPGS--IAYVSQE 74
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-180 |
6.74e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.21 E-value: 6.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEV---KDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDI--------- 66
Cdd:TIGR00958 475 LEGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldGVPLvqydhhylh 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 67 -KLALVEQETAAYSFA---------DQTPAEKKLLEKWHVPLRDF----------------HQLSGGEKLKARLAKGLSE 120
Cdd:TIGR00958 555 rQVALVGQEPVLFSGSvreniayglTDTPDEEIMAAAKAANAHDFimefpngydtevgekgSQLSGGQKQRIAIARALVR 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 121 DADLLLLDEPTNHLDEKSLQFLIQQLKHYNGTVILVSHdRYFLDEAATKIWSLEDQTLIE 180
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVE 693
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-159 |
6.89e-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: 65.34 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDI--------KLALVEQE 74
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILldGKDItnlpphkrPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 75 TAAY---------SFA------DQTPAEKKLLEKWH-VPLRDF-----HQLSGGEKLKARLAKGLSEDADLLLLDEPTNH 133
Cdd:cd03300 81 YALFphltvfeniAFGlrlkklPKAEIKERVAEALDlVQLEGYanrkpSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190
....*....|....*....|....*....|
gi 2828494 134 LDEK---SLQFLIQQLKHYNG-TVILVSHD 159
Cdd:cd03300 161 LDLKlrkDMQLELKRLQKELGiTFVFVTHD 190
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
280-348 |
7.37e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 65.52 E-value: 7.37e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 280 SIDTTHKTgkrFLEVQNVTKAFGErtlFK---NANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ-ETAEGSVW 348
Cdd:COG4674 2 SLDTMHGP---ILYVEDLTVSFDG---FKalnDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKtRPDSGSVL 68
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
292-433 |
7.88e-12 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 65.37 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAE-GSVWV-------SP-----SANIGYL 358
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDaGKILIdgqdithLPmheraRLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQE--VF-DLPLEQTPE---ELFENETFKARGH-VQNLMRHLGFTAAQwTEPIKHMSMGERVKIKLMAYILEEKDVLILD 431
Cdd:TIGR04406 82 PQEasIFrKLTVEENIMavlEIRKDLDRAEREErLEALLEEFQISHLR-DNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
..
gi 2828494 432 EP 433
Cdd:TIGR04406 161 EP 162
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-167 |
8.08e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.88 E-value: 8.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSY------EVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKD--------- 65
Cdd:PRK13633 1 MNEMIKCKNVSYkyesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 66 -----------------IKLALVEQETA------------AYSFADQTPAEKKLLE-KWHVPlrdfHQLSGGEKLKARLA 115
Cdd:PRK13633 81 wdirnkagmvfqnpdnqIVATIVEEDVAfgpenlgippeeIRERVDESLKKVGMYEyRRHAP----HLLSGGQKQRVAIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2828494 116 KGLSEDADLLLLDEPTNHLDEKSLQFLIQQLKHYNG----TVILVSHdryFLDEAA 167
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkygiTIILITH---YMEEAV 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-187 |
8.50e-12 |
|
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: 64.11 E-value: 8.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVK------DQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQ--GQILRKDIKL-------- 68
Cdd:cd03213 4 LSFRNLTVTVKsspsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLdkrsfrki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 -ALVEQETAAYsfADQTPAEKKLLekwHVPLRdfhQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLK 147
Cdd:cd03213 84 iGYVPQDDILH--PTLTVRETLMF---AAKLR---GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2828494 148 HY---NGTVILVSHdryfldEAATKIWSLEDQTLIEFKGN--YSG 187
Cdd:cd03213 156 RLadtGRTIICSIH------QPSSEIFELFDKLLLLSQGRviYFG 194
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
292-363 |
8.76e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.05 E-value: 8.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVW-----VSP-------SANIGYL 358
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGRIFldgedITHlpmhkraRLGIGYL 83
|
....*..
gi 2828494 359 TQE--VF 363
Cdd:COG1137 84 PQEasIF 90
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-170 |
9.51e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.11 E-value: 9.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDLAPAQGQILRKD--------IKLALVEQET 75
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITSGDLIVDglkvndpkVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 76 AA-----YSFADQTPAE---------------------KKLLEKWHVPLRDFH---QLSGGEKLKARLAKGLSEDADLLL 126
Cdd:PRK09493 80 GMvfqqfYLFPHLTALEnvmfgplrvrgaskeeaekqaRELLAKVGLAERAHHypsELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 127 LDEPTNHLD-EKSLQFL--IQQLKHYNGTVILVSHDRYFLDEAATKI 170
Cdd:PRK09493 160 FDEPTSALDpELRHEVLkvMQDLAEEGMTMVIVTHEIGFAEKVASRL 206
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
291-451 |
9.78e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.44 E-value: 9.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 291 FLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNII--LGQeTAEGSV-WVSPSAN------------I 355
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILagLAR-PDAGEVlWQGEPIRrqrdeyhqdllyL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 356 GYLTqevfDLPLEQTPEelfENETFKARGHvqnlmrHLGFTAAQWT----------E--PIKHMSMGERVKIKLMAYILE 423
Cdd:PRK13538 80 GHQP----GIKTELTAL---ENLRFYQRLH------GPGDDEALWEalaqvglagfEdvPVRQLSAGQQRRVALARLWLT 146
|
170 180
....*....|....*....|....*...
gi 2828494 424 EKDVLILDEPTNHLDLPSREQLEETLSQ 451
Cdd:PRK13538 147 RAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-158 |
1.10e-11 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 64.44 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 22 HVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------------------------------RKDIKLAL 70
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLingvdvtaappadrpvsmlfqennlfahltvEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 71 V-------EQETAAYSFADQTPAEKKLlekwhvpLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD---EKSLQ 140
Cdd:cd03298 96 SpglkltaEDRQAIEVALARVGLAGLE-------KRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalRAEML 168
|
170
....*....|....*....
gi 2828494 141 FLIQQLKHYNG-TVILVSH 158
Cdd:cd03298 169 DLVLDLHAETKmTVLMVTH 187
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-180 |
1.15e-11 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 67.05 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVS--YEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR-----KDIKL-------ALVEQ- 73
Cdd:TIGR02203 335 NVTfrYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLdghdlADYTLaslrrqvALVSQd 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 ---------ETAAYSFADQTPAEKKLLEKWHVPLRDF--------HQ--------LSGGEKLKARLAKGLSEDADLLLLD 128
Cdd:TIGR02203 415 vvlfndtiaNNIAYGRTEQADRAEIERALAAAYAQDFvdklplglDTpigengvlLSGGQRQRLAIARALLKDAPILILD 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2828494 129 EPTNHLDEKSLQFLIQQLKHY--NGTVILVSHdRYFLDEAATKIWSLEDQTLIE 180
Cdd:TIGR02203 495 EATSALDNESERLVQAALERLmqGRTTLVIAH-RLSTIEKADRIVVMDDGRIVE 547
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
287-463 |
1.37e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.90 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 287 TGKRFLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSVWV---------------- 349
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKpTEGQIFIdgedvthrsiqqrdic 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 350 ------------SPSANIGYlTQEVFDLPLEQTPE------ELFENETFKARGhvqnlmrhlgftaaqwtepIKHMSMGE 411
Cdd:PRK11432 82 mvfqsyalfphmSLGENVGY-GLKMLGVPKEERKQrvkealELVDLAGFEDRY-------------------VDQISGGQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 412 RVKIKLM-AYILEEKdVLILDEPTNHLDL----PSREQLEETLSQYSGTLLAVSHDR 463
Cdd:PRK11432 142 QQRVALArALILKPK-VLLFDEPLSNLDAnlrrSMREKIRELQQQFNITSLYVTHDQ 197
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-159 |
1.50e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.17 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-----------------RKdi 66
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILfdgenipamsrsrlytvRK-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 67 KLALVEQ-----------ETAAYSFADQTPAEKKLLEKW------HVPLRDFHQ-----LSGGEKLKARLAKGLSEDADL 124
Cdd:PRK11831 85 RMSMLFQsgalftdmnvfDNVAYPLREHTQLPAPLLHSTvmmkleAVGLRGAAKlmpseLSGGMARRAALARAIALEPDL 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 2828494 125 LLLDEPTNHLDEKS---LQFLIQQLKHYNG-TVILVSHD 159
Cdd:PRK11831 165 IMFDEPFVGQDPITmgvLVKLISELNSALGvTCVVVSHD 203
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
289-491 |
1.53e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 65.04 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 289 KRFLEVQNVTKAF--GERTLFKNANFTIQHGEKVAIIGPNGSGKTTL---LNIIL----------GQETAEGSVWvSPSA 353
Cdd:PRK13635 3 EEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLaklLNGLLlpeagtitvgGMVLSEETVW-DVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 354 NIGYLTQE--------------VFDLPLEQTP-EELFEnetfkargHVQNLMRHLGFTAAQWTEPiKHMSMGERVKIKLM 418
Cdd:PRK13635 82 QVGMVFQNpdnqfvgatvqddvAFGLENIGVPrEEMVE--------RVDQALRQVGMEDFLNREP-HRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 419 AYILEEKDVLILDEPTNHLDLPSREQLEET---LSQYSG-TLLAVSHDryfLEKTTNSKLVISNNGIEKQLNDVPSE 491
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETvrqLKEQKGiTVLSITHD---LDEAAQADRVIVMNKGEILEEGTPEE 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-158 |
1.64e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 65.59 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVS--YEVKDQTV--FKHVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDL-APAQGQIL----------RKDIKLA 69
Cdd:PRK11153 2 IELKNISkvFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCI-NLLeRPTSGRVLvdgqdltalsEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 70 ------------LVEQETAAYSFA-----DQTPAEK------KLLEKwhVPLRDFH-----QLSGGEKLKARLAKGLSED 121
Cdd:PRK11153 81 rrqigmifqhfnLLSSRTVFDNVAlplelAGTPKAEikarvtELLEL--VGLSDKAdrypaQLSGGQKQRVAIARALASN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2828494 122 ADLLLLDEPTNHLDEKSLQFLIQQLKHYNG----TVILVSH 158
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRelglTIVLITH 199
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
292-461 |
1.76e-11 |
|
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: 64.17 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFG--ERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWV-----------SPSANIGY 357
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRfYDVDSGRILIdghdvrdytlaSLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 358 LTQEVFdlpleqtpeeLF-----ENETFKARGHVQNLMRHLGfTAAQWTEPIKHM---------------SMGERVKIKL 417
Cdd:cd03251 81 VSQDVF----------LFndtvaENIAYGRPGATREEVEEAA-RAANAHEFIMELpegydtvigergvklSGGQRQRIAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2828494 418 MAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYSG--TLLAVSH 461
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERLMKnrTTFVIAH 195
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-159 |
1.85e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.49 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 21 KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------RKDIKLA----LV-EQET-------AAYSF- 80
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvpfKRRKEFArrigVVfGQRSqlwwdlpAIDSFr 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 81 ------------ADQTPAE-KKLL---EKWHVPLRdfhQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD----EKSLQ 140
Cdd:COG4586 119 llkaiyripdaeYKKRLDElVELLdlgELLDTPVR---QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDvvskEAIRE 195
|
170
....*....|....*....
gi 2828494 141 FLIQQLKHYNGTVILVSHD 159
Cdd:COG4586 196 FLKEYNRERGTTILLTSHD 214
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
292-461 |
2.18e-11 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 63.79 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFG-ERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWV-----------SPSANIGYL 358
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRfYDVSSGSILIdgqdirevtldSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQevfDLPL--------------EQTPEELFEnetfKARghvqnlmrhlgftAAQWTEPIKHM---------------SM 409
Cdd:cd03253 81 PQ---DTVLfndtigynirygrpDATDEEVIE----AAK-------------AAQIHDKIMRFpdgydtivgerglklSG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2828494 410 GERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYSG--TLLAVSH 461
Cdd:cd03253 141 GEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAH 194
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-199 |
2.31e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.80 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVF-----KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDI------------- 66
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqaiHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDItithktkdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 67 ---KLALVEQETAAYSFADQTPAE------------KKLLEKWHVPLRDF-----------HQLSGGEKLKARLAKGLSE 120
Cdd:PRK13646 83 vrkRIGMVFQFPESQLFEDTVEREiifgpknfkmnlDEVKNYAHRLLMDLgfsrdvmsqspFQMSGGQMRKIAIVSILAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 121 DADLLLLDEPTNHLDEKSLQFLIQQLKHY----NGTVILVSHDRYFLDEAATKIWSLEDQTLIEfkgNYSGYMKFREKKR 196
Cdd:PRK13646 163 NPDIIVLDEPTAGLDPQSKRQVMRLLKSLqtdeNKTIILVSHDMNEVARYADEVIVMKEGSIVS---QTSPKELFKDKKK 239
|
...
gi 2828494 197 LTQ 199
Cdd:PRK13646 240 LAD 242
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-158 |
2.36e-11 |
|
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: 63.83 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 15 KDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHN---DLAPAQGQIL-------RKDIK--LALVEQ--------- 73
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILfngqprkPDQFQkcVAYVRQddillpglt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 --ETAAYSFADQTPAEKK------------LLEKWHVPLRD--FHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEK 137
Cdd:cd03234 98 vrETLTYTAILRLPRKSSdairkkrvedvlLRDLALTRIGGnlVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180
....*....|....*....|....
gi 2828494 138 SLQFLIQQLKHY---NGTVILVSH 158
Cdd:cd03234 178 TALNLVSTLSQLarrNRIVILTIH 201
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-175 |
2.64e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 63.20 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 23 VNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-----------------LRKDIKLALVEQ---------ETA 76
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqdvsdlrgraipyLRRKIGVVFQDFrllpdrnvyENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 77 AYSF--ADQTPAE-----KKLLEKwhVPLRDFH-----QLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQ 144
Cdd:cd03292 100 AFALevTGVPPREirkrvPAALEL--VGLSHKHralpaELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMN 177
|
170 180 190
....*....|....*....|....*....|....
gi 2828494 145 QLKHYN---GTVILVSHDRYFLDEAATKIWSLED 175
Cdd:cd03292 178 LLKKINkagTTVVVATHAKELVDTTRHRVIALER 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
292-478 |
2.80e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 63.20 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTL-FKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSVWVS-------PSANIGYLTQEV 362
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNgqdvsdlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 363 ------FDLPLEQTpeeLFENETF----------KARGHVQNLMRHLGFTAAQWTEPiKHMSMGERVKIKLMAYILEEKD 426
Cdd:cd03292 81 gvvfqdFRLLPDRN---VYENVAFalevtgvpprEIRKRVPAALELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2828494 427 VLILDEPTNHLDLP-SREQLE--ETLSQYSGTLLAVSHDRYFLEKTTNSKLVISN 478
Cdd:cd03292 157 ILIADEPTGNLDPDtTWEIMNllKKINKAGTTVVVATHAKELVDTTRHRVIALER 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
292-462 |
2.98e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.93 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEGSVWVSPSA-------NIGYLTQEVFD 364
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAplaeareDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 365 LPLEQtpeeLFENETFKARGHVQNLMRH------LGFTAAQWTEPikhMSMGERVKIKLMAYILEEKDVLILDEPTNHLD 438
Cdd:PRK11247 93 LPWKK----VIDNVGLGLKGQWRDAALQalaavgLADRANEWPAA---LSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180
....*....|....*....|....*...
gi 2828494 439 LPSR---EQLEETLSQYSG-TLLAVSHD 462
Cdd:PRK11247 166 ALTRiemQDLIESLWQQHGfTVLLVTHD 193
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-159 |
3.05e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.30 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 19 VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVEQETAA----------YSFADQTPaEK 88
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqklgfiYQFHHLLP-DF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 89 KLLEKWHVPL-------------------------RDFH---QLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEK--- 137
Cdd:PRK11629 103 TALENVAMPLligkkkpaeinsralemlaavglehRANHrpsELSGGERQRVAIARALVNNPRLVLADEPTGNLDARnad 182
|
170 180
....*....|....*....|...
gi 2828494 138 SLQFLIQQLKHYNGTVIL-VSHD 159
Cdd:PRK11629 183 SIFQLLGELNRLQGTAFLvVTHD 205
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
292-462 |
3.13e-11 |
|
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: 63.68 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEGSVwVSPSA-------------NIGYL 358
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGT-VDLAGvdlhglsrrararRVALV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQEV-FDLPLE--------QTP-EELFENETFKARGHVQNLMRHLGFTAAQwTEPIKHMSMGERVKIKLMAYILEEKDVL 428
Cdd:TIGR03873 81 EQDSdTAVPLTvrdvvalgRIPhRSLWAGDSPHDAAVVDRALARTELSHLA-DRDMSTLSGGERQRVHVARALAQEPKLL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 2828494 429 ILDEPTNHLDLpsREQLE-----ETLSQYSGTLLAVSHD 462
Cdd:TIGR03873 160 LLDEPTNHLDV--RAQLEtlalvRELAATGVTVVAALHD 196
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-183 |
3.31e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.76 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 7 LTNVSYEVKDQTV-FKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVEQEtaAYS------ 79
Cdd:PRK10522 325 LRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE--DYRklfsav 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 FAD-----------QTPAEKKLLEKW--HVPLRDFHQLSGGEKLKARLAKG----------LSEDADLLLLDE------P 130
Cdd:PRK10522 403 FTDfhlfdqllgpeGKPANPALVEKWleRLKMAHKLELEDGRISNLKLSKGqkkrlalllaLAEERDILLLDEwaadqdP 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2828494 131 tnHLDEKSLQFLIQQLKHYNGTVILVSH-DRYFldEAATKIWSLEDQTLIEFKG 183
Cdd:PRK10522 483 --HFRREFYQVLLPLLQEMGKTIFAISHdDHYF--IHADRLLEMRNGQLSELTG 532
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
292-483 |
3.98e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 64.72 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEG----------SVWVSPSANIGYLTQE 361
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSghirfhgtdvSRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 362 --------VFD--------LPLEQTPeelfenETFKARGHVQNL--MRHLGFTAAQWTepiKHMSMGERVKIKLMAYILE 423
Cdd:PRK10851 83 yalfrhmtVFDniafgltvLPRRERP------NAAAIKAKVTQLleMVQLAHLADRYP---AQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2828494 424 EKDVLILDEPTNHLDLPSREQLEETLSQ----YSGTLLAVSHDRYFLEKTTNSKLVISNNGIEK 483
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQlheeLKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQ 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
292-376 |
5.29e-11 |
|
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: 65.15 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAF--GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSV---------WvSPSA---NIG 356
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGvWPPTAGSVrldgadlsqW-DREElgrHIG 409
|
90 100
....*....|....*....|
gi 2828494 357 YLTQEVfdlpleqtpeELFE 376
Cdd:COG4618 410 YLPQDV----------ELFD 419
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-167 |
5.48e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 63.23 E-value: 5.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQTVF--KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRKDIK 67
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfekLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 68 LALVEQET----------AAYSFADQTPAEKKLLEKWHVPLRDF----------HQLSGGEKLKARLAKGLSEDADLLLL 127
Cdd:PRK13648 87 IVFQNPDNqfvgsivkydVAFGLENHAVPYDEMHRRVSEALKQVdmleradyepNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2828494 128 DEPTNHLD---EKSLQFLIQQLK-HYNGTVILVSHDryfLDEAA 167
Cdd:PRK13648 167 DEATSMLDpdaRQNLLDLVRKVKsEHNITIISITHD---LSEAM 207
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-159 |
5.83e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 63.33 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQT-VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI----------------LRKDI 66
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkglmkLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 67 KL-----------ALVEQETAAYSFADQTPAE------KKLLEKWHV-PLRD--FHQLSGGEKLKARLAKGLSEDADLLL 126
Cdd:PRK13636 85 GMvfqdpdnqlfsASVYQDVSFGAVNLKLPEDevrkrvDNALKRTGIeHLKDkpTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 2828494 127 LDEPTNHLDEKS----LQFLIQQLKHYNGTVILVSHD 159
Cdd:PRK13636 165 LDEPTAGLDPMGvseiMKLLVEMQKELGLTIIIATHD 201
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-159 |
6.16e-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: 62.45 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQ----TVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKL-ALVEQETAAY 78
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 79 -----SFADQ---------------TPAE-----------KKLLEKW-------HVPlrdfHQLSGGEKLKARLAKGLSE 120
Cdd:COG4181 88 rarhvGFVFQsfqllptltalenvmLPLElagrrdararaRALLERVglghrldHYP----AQLSGGEQQRVALARAFAT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2828494 121 DADLLLLDEPTNHLDEKSLQFLIQQL----KHYNGTVILVSHD 159
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLfelnRERGTTLVLVTHD 206
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
287-463 |
6.16e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.20 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 287 TGKRFLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEgsvwvspSANIGYLTQEVFDLP 366
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPD-------SGRIMLDGQDITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 367 LEQTP-------------EELFENETF------------KARGHVQNLMRHLGFTAAQwtePIKHMSMGERVKIKLMAYI 421
Cdd:PRK09452 83 AENRHvntvfqsyalfphMTVFENVAFglrmqktpaaeiTPRVMEALRMVQLEEFAQR---KPHQLSGGQQQRVAIARAV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2828494 422 LEEKDVLILDEPTNHLDLPSREQLEETLSQYSGTL----LAVSHDR 463
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQ 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-135 |
6.62e-11 |
|
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: 65.32 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 19 VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-------------------LRKDIKLALVEQETAAYS 79
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIkhsgrisfspqtswimpgtIKDNIIFGLSYDEYRYTS 520
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 FADQTPAEK---KLLEKWHVPLRDFH-QLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD 135
Cdd:TIGR01271 521 VIKACQLEEdiaLFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
292-464 |
7.13e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.72 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNII-------LGQETAEGSVWVSPSANigYLTQEVFD 364
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFarlltpqSGTVFLGDKPISMLSSR--QLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 365 LPLEQ-TPE----------------ELFENETFKARGHVQNLMRHLGFTA-AQwtEPIKHMSMGERVKIKLMAYILEEKD 426
Cdd:PRK11231 81 LPQHHlTPEgitvrelvaygrspwlSLWGRLSAEDNARVNQAMEQTRINHlAD--RRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2828494 427 VLILDEPTNHLDLpsREQLE-----ETLSQYSGTLLAVSHD-----RY 464
Cdd:PRK11231 159 VVLLDEPTTYLDI--NHQVElmrlmRELNTQGKTVVTVLHDlnqasRY 204
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
311-462 |
8.56e-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: 8.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 311 NFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEGSVWVS-------PSANI----GYLTQE---VFDLPLEQ-----TP 371
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNgrplsdwSAAELarhrAYLSQQqspPFAMPVFQylalhQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 372 EELFENETFKArghVQNLMRHLGFTaAQWTEPIKHMSMGERVKIKLMAYILE-------EKDVLILDEPTNHLDLPSREQ 444
Cdd:COG4138 96 AGASSEAVEQL---LAQLAEALGLE-DKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAA 171
|
170 180
....*....|....*....|.
gi 2828494 445 LEETLSQYS---GTLLAVSHD 462
Cdd:COG4138 172 LDRLLRELCqqgITVVMSSHD 192
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
308-461 |
1.29e-10 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 61.36 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 308 KNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVW---VSPSA--------NIGYLTQEVF----------Dl 365
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRlVELSSGSILidgVDISKiglhdlrsRISIIPQDPVlfsgtirsnlD- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 366 PLEQ-TPEELFEN-ETFKARGHVQNLMRHLGFTAaqwTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSRE 443
Cdd:cd03244 100 PFGEySDEELWQAlERVGLKEFVESLPGGLDTVV---EEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDA 176
|
170 180
....*....|....*....|
gi 2828494 444 QLEETL-SQYSG-TLLAVSH 461
Cdd:cd03244 177 LIQKTIrEAFKDcTVLTIAH 196
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-179 |
1.32e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 62.40 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQT-VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRK------DIKLALVEQETA 76
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepikyDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 77 AYSFA---DQTPA---------------------EKKLLEKWH-VPLRDF-----HQLSGGEKLKARLAKGLSEDADLLL 126
Cdd:PRK13639 81 GIVFQnpdDQLFAptveedvafgplnlglskeevEKRVKEALKaVGMEGFenkppHHLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2828494 127 LDEPTNHLDEKSLQFLIQQLKHYNG---TVILVSHDRYFLDEAATKIWSLEDQTLI 179
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
311-461 |
1.36e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.52 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 311 NFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAE-GSVWV--------SPSAN-IGYLTQE--VFD-LPLEQ-------- 369
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPAsGSLTLngqdhtttPPSRRpVSMLFQEnnLFShLTVAQniglglnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 370 ----TPEelfENETFKARGHVQNLMRHLGFTAAQwtepikhMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQ- 444
Cdd:PRK10771 99 glklNAA---QREKLHAIARQMGIEDLLARLPGQ-------LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEm 168
|
170 180
....*....|....*....|
gi 2828494 445 ---LEETLSQYSGTLLAVSH 461
Cdd:PRK10771 169 ltlVSQVCQERQLTLLMVSH 188
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
292-433 |
1.40e-10 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 61.40 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVW-----VSP-------SANIGYL 358
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGKILldgqdITKlpmhkraRLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQEvfdlpleqtpEELFENETFKarghvQNLM---RHLGFTAAQWTEPIKHM-----------------SMGERVKIKLM 418
Cdd:cd03218 81 PQE----------ASIFRKLTVE-----ENILavlEIRGLSKKEREEKLEELleefhithlrkskasslSGGERRRVEIA 145
|
170
....*....|....*
gi 2828494 419 AYILEEKDVLILDEP 433
Cdd:cd03218 146 RALATNPKFLLLDEP 160
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-159 |
1.60e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.93 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQT-VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDI------KLA------- 69
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsKLQgirklvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 70 -------------LVEQETA------------AYSFADQTPAEKKLLEKWHvplRDFHQLSGGEKLKARLAKGLSEDADL 124
Cdd:PRK13644 81 ivfqnpetqfvgrTVEEDLAfgpenlclppieIRKRVDRALAEIGLEKYRH---RSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 2828494 125 LLLDEPTNHLDEKSLQFLIQQLK--HYNG-TVILVSHD 159
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKklHEKGkTIVYITHN 195
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-158 |
1.63e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.99 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 21 KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDI--------------KLALVEQ--------ETAAY 78
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVditdkkvklsdirkKVGLVFQypeyqlfeETIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 79 SFA--------DQTPAEKKLLEKWHVPLRDFH--------QLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKS---L 139
Cdd:PRK13637 104 DIAfgpinlglSEEEIENRVKRAMNIVGLDYEdykdkspfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGrdeI 183
|
170 180
....*....|....*....|
gi 2828494 140 QFLIQQL-KHYNGTVILVSH 158
Cdd:PRK13637 184 LNKIKELhKEYNMTIILVSH 203
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-158 |
1.86e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 61.68 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFK-----HVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-----------RKDIK- 67
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitstskNKDIKq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 68 ----LALVEQETAAYSFAD----------------QTPAEKKLLEKWHV-----PLRDFH--QLSGGEKLKARLAKGLSE 120
Cdd:PRK13649 83 irkkVGLVFQFPESQLFEEtvlkdvafgpqnfgvsQEEAEALAREKLALvgiseSLFEKNpfELSGGQMRRVAIAGILAM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2828494 121 DADLLLLDEPTNHLD---EKSLQFLIQQLKHYNGTVILVSH 158
Cdd:PRK13649 163 EPKILVLDEPTAGLDpkgRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-162 |
1.88e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 63.28 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 6 TLTNVSY---EVKDQTVFK--HVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIklALVEQETAAYS- 79
Cdd:COG4615 329 ELRGVTYrypGEDGDEGFTlgPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ--PVTADNREAYRq 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 -----FAD-------------QTPAE-KKLLEKWH----VPLRD--FH--QLSGGEKlKaRLAKGLS--EDADLLLLDE- 129
Cdd:COG4615 407 lfsavFSDfhlfdrllgldgeADPARaRELLERLEldhkVSVEDgrFSttDLSQGQR-K-RLALLVAllEDRPILVFDEw 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2828494 130 -----PtnhldekslQF-------LIQQLKHYNGTVILVSHD-RYF 162
Cdd:COG4615 485 aadqdP---------EFrrvfyteLLPELKARGKTVIAISHDdRYF 521
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-159 |
2.16e-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: 60.67 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGdIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDI-----------KLALVEQ 73
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 E------TAAYSFAD-----------QTPAE-KKLLEKwhVPLRDFH-----QLSGGEKLKARLAKGLSEDADLLLLDEP 130
Cdd:cd03264 80 EfgvypnFTVREFLDyiawlkgipskEVKARvDEVLEL--VNLGDRAkkkigSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190
....*....|....*....|....*....|..
gi 2828494 131 TNHLD-EKSLQF--LIQQLKHyNGTVILVSHD 159
Cdd:cd03264 158 TAGLDpEERIRFrnLLSELGE-DRIVILSTHI 188
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-174 |
2.17e-10 |
|
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: 60.95 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVK---DQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDI--------- 66
Cdd:cd03248 8 LKGIVKFQNVTFAYPtrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldGKPIsqyehkylh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 67 -KLALVEQETA----------AYSFADQTPAE-KKLLEKWHVplRDF----------------HQLSGGEKLKARLAKGL 118
Cdd:cd03248 88 sKVSLVGQEPVlfarslqdniAYGLQSCSFECvKEAAQKAHA--HSFiselasgydtevgekgSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2828494 119 SEDADLLLLDEPTNHLDEKSLQFLIQQLK--HYNGTVILVSHdRYFLDEAATKIWSLE 174
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYdwPERRTVLVIAH-RLSTVERADQILVLD 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-166 |
2.21e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.74 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-----------RKDIKLALVE 72
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsrarHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 73 Q------------------ETAAYSFADQTPAEKKLLE------KWHVPLRDfhqLSGGEKLKARLAKGLSEDADLLLLD 128
Cdd:PRK13537 87 QfdnldpdftvrenllvfgRYFGLSAAAARALVPPLLEfaklenKADAKVGE---LSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2828494 129 EPTNHLDEKSLQFLIQQLKHY---NGTVILVSHdryFLDEA 166
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLlarGKTILLTTH---FMEEA 201
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
311-462 |
2.34e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.10 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 311 NFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEGSVWVS-------PSANI----GYLTQE---VFDLPLEQ-----TP 371
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAgqpleawSAAELarhrAYLSQQqtpPFAMPVFQyltlhQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 372 EelfENETFKARGHVQNLMRHLGFTaAQWTEPIKHMSMGERVKIKLMAYILE-------EKDVLILDEPTNHLDLPSREQ 444
Cdd:PRK03695 96 D---KTRTEAVASALNEVAEALGLD-DKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAA 171
|
170 180
....*....|....*....|.
gi 2828494 445 LEETLSQYSGTLLAV---SHD 462
Cdd:PRK03695 172 LDRLLSELCQQGIAVvmsSHD 192
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
292-499 |
2.49e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 60.92 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLL------------NIILGQETAEGSVWVSPSAN-IGYL 358
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLrcinlleqpeagTIRVGDITIDTARSLSQQKGlIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQEV------FDL-PLEQTPEELFE---------NETFKARGhvQNLMRHLGFTAAQWTEPiKHMSMGERVKIKLMAYIL 422
Cdd:PRK11264 84 RQHVgfvfqnFNLfPHRTVLENIIEgpvivkgepKEEATARA--RELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 423 EEKDVLILDEPTNHLDLPSREQLEET---LSQYSGTLLAVSHDRYFLEKTTN-----SKLVISNNGIEKQLNDVPSERNE 494
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTirqLAQEKRTMVIVTHEMSFARDVADraifmDQGRIVEQGPAKALFADPQQPRT 240
|
....*
gi 2828494 495 REELR 499
Cdd:PRK11264 241 RQFLE 245
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-159 |
2.73e-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: 60.82 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------RKDIK---LALVEQE 74
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILfggedatDVPVQernVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 75 TAAY---------SF------ADQTPAEKKLLEKWH-----VPLRDF-----HQLSGGEKLKARLAKGLSEDADLLLLDE 129
Cdd:cd03296 83 YALFrhmtvfdnvAFglrvkpRSERPPEAEIRAKVHellklVQLDWLadrypAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190
....*....|....*....|....*....|....
gi 2828494 130 PTNHLD---EKSLQFLIQQLKHYNG-TVILVSHD 159
Cdd:cd03296 163 PFGALDakvRKELRRWLRRLHDELHvTTVFVTHD 196
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-186 |
2.97e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 62.67 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEV--KDQTVFkHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRKDIkl 68
Cdd:PRK13657 335 VEFDDVSFSYdnSRQGVE-DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIlidgtdirtvtrasLRRNI-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 ALVEQEtaAYSFA------------DQTPAE----KKLLEKWHVPLR-----DFH------QLSGGEKLKARLAKGLSED 121
Cdd:PRK13657 412 AVVFQD--AGLFNrsiednirvgrpDATDEEmraaAERAQAHDFIERkpdgyDTVvgergrQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2828494 122 ADLLLLDEPTNHLD---EKSLQFLIQQLKHyNGTVILVSHdRYFLDEAATKIWSLEDQTLIEfKGNYS 186
Cdd:PRK13657 490 PPILILDEATSALDvetEAKVKAALDELMK-GRTTFIIAH-RLSTVRNADRILVFDNGRVVE-SGSFD 554
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
9-158 |
3.00e-10 |
|
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: 59.68 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLA-LVEQETAAYSFADQTPAE 87
Cdd:TIGR01189 5 NLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAeQRDEPHENILYLGHLPGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 88 KKLLEK------WH----------------VPLRDF-----HQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQ 140
Cdd:TIGR01189 85 KPELSAlenlhfWAaihggaqrtiedalaaVGLTGFedlpaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|.
gi 2828494 141 FLIQQLK---HYNGTVILVSH 158
Cdd:TIGR01189 165 LLAGLLRahlARGGIVLLTTH 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
16-158 |
3.16e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.82 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 16 DQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI------LRKD----------------IKLALVEQ 73
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgepIRRQrdeyhqdllylghqpgIKTELTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 ETAAYSFADQTPAEK----KLLEKwhVPLRDF-----HQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQ 144
Cdd:PRK13538 93 ENLRFYQRLHGPGDDealwEALAQ--VGLAGFedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEA 170
|
170
....*....|....*..
gi 2828494 145 QLKHY---NGTVILVSH 158
Cdd:PRK13538 171 LLAQHaeqGGMVILTTH 187
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-159 |
3.24e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.68 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVEQETAAYSFADQ 83
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 84 TPAE--------------------------------KKLLEKWHVP-LRDF--HQLSGGEKLKARLAKGLSEDADLLLLD 128
Cdd:PRK10895 83 LPQEasifrrlsvydnlmavlqirddlsaeqredraNELMEEFHIEhLRDSmgQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190
....*....|....*....|....*....|....
gi 2828494 129 EPTNHLDEKS---LQFLIQQLKHYNGTVILVSHD 159
Cdd:PRK10895 163 EPFAGVDPISvidIKRIIEHLRDSGLGVLITDHN 196
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-179 |
3.27e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.77 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 18 TVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQG-------QILR---KDI--KLALVEQEtaAYSFADQTP 85
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGhvwldgeHIQHyasKEVarRIGLLAQN--ATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 86 AE---------KKLLEKW------------------HVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD--- 135
Cdd:PRK10253 99 QElvargryphQPLFTRWrkedeeavtkamqatgitHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDish 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2828494 136 EKSLQFLIQQLKHYNG-TVILVSHDryfLDEA---ATKIWSLEDQTLI 179
Cdd:PRK10253 179 QIDLLELLSELNREKGyTLAAVLHD---LNQAcryASHLIALREGKIV 223
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-185 |
3.29e-10 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 59.09 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVF-KHVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDLAPA-QGQILR-KDIKLALVEQETaaY--- 78
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPWgSGRIGMpEGEDLLFLPQRP--Ylpl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 79 -SFADQtpaekkLLEKWHvplrdfHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLKHYNGTVILVS 157
Cdd:cd03223 78 gTLREQ------LIYPWD------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVG 145
|
170 180
....*....|....*....|....*....
gi 2828494 158 HdRyfldeaaTKIWSLEDQTL-IEFKGNY 185
Cdd:cd03223 146 H-R-------PSLWKFHDRVLdLDGEGGW 166
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-158 |
3.30e-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: 60.63 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSY---EVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDIK----------LA 69
Cdd:cd03249 1 IEFKNVSFrypSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldGVDIRdlnlrwlrsqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 70 LVEQETA----------AYSFADQTPAE--------------KKLLEKWHVPLRDF-HQLSGGEKLKARLAKGLSEDADL 124
Cdd:cd03249 81 LVSQEPVlfdgtiaeniRYGKPDATDEEveeaakkanihdfiMSLPDGYDTLVGERgSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 2828494 125 LLLDEPTNHLD---EKSLQFLIQQLKHyNGTVILVSH 158
Cdd:cd03249 161 LLLDEATSALDaesEKLVQEALDRAMK-GRTTIVIAH 196
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
17-180 |
3.89e-10 |
|
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: 60.59 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 17 QTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-----------------LRKDIKL-------ALVE 72
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsfrgqdlyqldrkqrraFRRDVQLvfqdspsAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 73 QETAAYSFA---------DQTPAEKKLLEKWH-VPLRDFH------QLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD- 135
Cdd:TIGR02769 104 RMTVRQIIGeplrhltslDESEQKARIAELLDmVGLRSEDadklprQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDm 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2828494 136 --EKSLQFLIQQLKHYNGTV-ILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:TIGR02769 184 vlQAVILELLRKLQQAFGTAyLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
259-480 |
3.95e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.52 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 259 LEKELEKAKAEPVTPEytvrfSIDTTHKTGkrfLEVQNVTKAFGE-RTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNII 337
Cdd:COG4178 338 FEEALEAADALPEAAS-----RIETSEDGA---LALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 338 LG-QETAEGSVWVSPSANIGYLTQEVFdLPL----EQ----TPEELFENETFKA---RGHVQNLMRHLGfTAAQWTepiK 405
Cdd:COG4178 410 AGlWPYGSGRIARPAGARVLFLPQRPY-LPLgtlrEAllypATAEAFSDAELREaleAVGLGHLAERLD-EEADWD---Q 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2828494 406 HMSMGERVKIKLmAYILEEK-DVLILDEPTNHLDLPSREQLEETLSQ--YSGTLLAVSHdRYFLEKTTNSKLVISNNG 480
Cdd:COG4178 485 VLSLGEQQRLAF-ARLLLHKpDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGDG 560
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
9-131 |
4.19e-10 |
|
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: 60.00 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYevKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDIK-----------LALVEQ-- 73
Cdd:COG0410 10 HAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdGEDITglpphriarlgIGYVPEgr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 ------------ETAAYSFADQTPAEK----------KLLEKWHVPLRdfhQLSGGEK--LkArLAKGLSEDADLLLLDE 129
Cdd:COG0410 88 rifpsltveenlLLGAYARRDRAEVRAdlervyelfpRLKERRRQRAG---TLSGGEQqmL-A-IGRALMSRPKLLLLDE 162
|
..
gi 2828494 130 PT 131
Cdd:COG0410 163 PS 164
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-186 |
4.28e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.17 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 10 VSYEVKDQTVFKH--------VNASVQQGDIIGIIGKNGAGKSTLLHLIH----------------NDLAPAQ------- 58
Cdd:PRK11174 348 VTIEAEDLEILSPdgktlagpLNFTLPAGQRIALVGPSGAGKTSLLNALLgflpyqgslkingielRELDPESwrkhlsw 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 59 -GQ-------ILRKDIKLALVE-QETAAYSFADQTPAE---KKLLEKWHVPLRDfhQ---LSGGEKLKARLAKGLSEDAD 123
Cdd:PRK11174 428 vGQnpqlphgTLRDNVLLGNPDaSDEQLQQALENAWVSeflPLLPQGLDTPIGD--QaagLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2828494 124 LLLLDEPTNHLDEKSLQFLIQQLKHY--NGTVILVSHDRYFLdEAATKIWSLEDQTLIEfKGNYS 186
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQLEDL-AQWDQIWVMQDGQIVQ-QGDYA 568
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-453 |
5.16e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDI-------KLA---- 69
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhKLAaqlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 70 --LVEQEtaaYSFADQTPAEK-----KLLEK--WHVPLRDFHQ------------------------LSGGEKLKARLAK 116
Cdd:PRK09700 82 igIIYQE---LSVIDELTVLEnlyigRHLTKkvCGVNIIDWREmrvraammllrvglkvdldekvanLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 117 GLSEDADLLLLDEPTNHLDEKSLQFL---IQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIefkgnYSGYMKFRE 193
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV-----CSGMVSDVS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 194 KKRLTQQreyekqqkMVERieaqmnglaswsekahaqstkkegfkeyhrvkakrtdaQIKSKQKRLEKELEKAKAEPVtp 273
Cdd:PRK09700 234 NDDIVRL--------MVGR--------------------------------------ELQNRFNAMKENVSNLAHETV-- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 274 eytvrfsidtthktgkrfLEVQNVTKAfgERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSVW---- 348
Cdd:PRK09700 266 ------------------FEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKrAGGEIRlngk 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 349 -VSPSA-------NIGYLTQEV--------FDLPLEQTPEELFENETFKA----------RGHVQNLMRHLGFTAAQWTE 402
Cdd:PRK09700 326 dISPRSpldavkkGMAYITESRrdngffpnFSIAQNMAISRSLKDGGYKGamglfhevdeQRTAENQRELLALKCHSVNQ 405
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2828494 403 PIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYS 453
Cdd:PRK09700 406 NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA 456
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
32-167 |
5.63e-10 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 61.28 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 32 IIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL---------RKDI-------KLALVEQETA-----------AYSFADQT 84
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtlfdsRKGIflppekrRIGYVFQEARlfphlsvrgnlRYGMKRAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 85 PAEKK--------LLEKWHVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKS----LQFLIQQLKHYNGT 152
Cdd:TIGR02142 105 PSERRisfervieLLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRkyeiLPYLERLHAEFGIP 184
|
170
....*....|....*
gi 2828494 153 VILVSHDryfLDEAA 167
Cdd:TIGR02142 185 ILYVSHS---LQEVL 196
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
286-463 |
5.81e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.34 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 286 KTGKRFLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIIlgqetaegSVWVSP-SANIGYLTQEVFD 364
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIV--------ASLISPtSGTLLFEGEDIST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 365 LPLE----------QTP----EELFENETF--KARGH-------VQNLMRhLGFTAAQWTEPIKHMSMGERVKIKLMAYI 421
Cdd:PRK10247 74 LKPEiyrqqvsycaQTPtlfgDTVYDNLIFpwQIRNQqpdpaifLDDLER-FALPDTILTKNIAELSGGEKQRISLIRNL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2828494 422 LEEKDVLILDEPTNHLDLPSREQLEETLSQYSG----TLLAVSHDR 463
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVReqniAVLWVTHDK 198
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
35-174 |
6.28e-10 |
|
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: 59.16 E-value: 6.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 35 IIGKNGAGKSTLLHLI----HNDLAPA--QGQILRKDIKlalvEQETAAYSFADQTPAEKKlleKWHVpLRDF------- 101
Cdd:cd03240 27 IVGQNGAGKTTIIEALkyalTGELPPNskGGAHDPKLIR----EGEVRAQVKLAFENANGK---KYTI-TRSLailenvi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 102 --HQ-------------LSGGEKLKA----RLA--KGLSEDADLLLLDEPTNHLDE----KSLQFLIQ-QLKHYNGTVIL 155
Cdd:cd03240 99 fcHQgesnwplldmrgrCSGGEKVLAsliiRLAlaETFGSNCGILALDEPTTNLDEenieESLAEIIEeRKSQKNFQLIV 178
|
170
....*....|....*....
gi 2828494 156 VSHDRYFLDeAATKIWSLE 174
Cdd:cd03240 179 ITHDEELVD-AADHIYRVE 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
291-434 |
6.30e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.57 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 291 FLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV--------SP----SANIGY 357
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPdSGEILLdgepvrfrSPrdaqAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 358 LTQEvFDLPLEQTPEE-LFENETFKARGHV---------QNLMRHLGFTAAQWTePIKHMSMGER--VKI-KlmAYILEE 424
Cdd:COG1129 84 IHQE-LNLVPNLSVAEnIFLGREPRRGGLIdwramrrraRELLARLGLDIDPDT-PVGDLSVAQQqlVEIaR--ALSRDA 159
|
170
....*....|
gi 2828494 425 KdVLILDEPT 434
Cdd:COG1129 160 R-VLILDEPT 168
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-170 |
7.21e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 60.86 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIvTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIH-----------------NDLAPAQgqilR 63
Cdd:COG3839 1 MASL-ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAgledptsgeiliggrdvTDLPPKD----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 64 kDIklALVEQETAAY---------SF----ADQTPAEK--------KLLEkwhvpLRDF-----HQLSGGEKLKARLAKG 117
Cdd:COG3839 76 -NI--AMVFQSYALYphmtvyeniAFplklRKVPKAEIdrrvreaaELLG-----LEDLldrkpKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 118 LSEDADLLLLDEPTNHLDEKS-------LQFLIQQLKHyngTVILVSHDryfLDEA---ATKI 170
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLrvemraeIKRLHRRLGT---TTIYVTHD---QVEAmtlADRI 204
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
305-461 |
7.28e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.40 E-value: 7.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 305 TLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEGSVWVSpsanigylTQEVFDLPLE----------QTPeEL 374
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKIN--------GIELRELDPEswrkhlswvgQNP-QL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 375 F-----ENETFkARGH-----VQNLMRHLG---FTAAQ---WTEPIKH----MSMGERVKIKLMAYILEEKDVLILDEPT 434
Cdd:PRK11174 435 PhgtlrDNVLL-GNPDasdeqLQQALENAWvseFLPLLpqgLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180
....*....|....*....|....*....
gi 2828494 435 NHLDLPSREQLEETLSQYSG--TLLAVSH 461
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAASRrqTTLMVTH 542
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-159 |
7.42e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.71 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKL-------ALVEQ--- 73
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegpgaerGVVFQneg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 ---------------ETAAYSFADQTPAEKKLLEKwhVPLRDFH-----QLSGGEKLKARLAKGLSEDADLLLLDEPTNH 133
Cdd:PRK11248 81 llpwrnvqdnvafglQLAGVEKMQRLEIAHQMLKK--VGLEGAEkryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190
....*....|....*....|....*....|
gi 2828494 134 LD---EKSLQFLIQQLKHYNGT-VILVSHD 159
Cdd:PRK11248 159 LDaftREQMQTLLLKLWQETGKqVLLITHD 188
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-159 |
7.87e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.12 E-value: 7.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL----------RKDI------- 66
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgepldpedRRRIgylpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 67 ----KLALVEQetAAYsFA---DQTPAE-----KKLLEK------WHVPLRDfhqLSGGEKLKARLAKGLSEDADLLLLD 128
Cdd:COG4152 81 glypKMKVGEQ--LVY-LArlkGLSKAEakrraDEWLERlglgdrANKKVEE---LSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190
....*....|....*....|....*....|....*
gi 2828494 129 EPTNHLDEKSLQFL---IQQLKHyNG-TVILVSHD 159
Cdd:COG4152 155 EPFSGLDPVNVELLkdvIRELAA-KGtTVIFSSHQ 188
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-170 |
7.98e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.75 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVKDQT-VFKHVNASVQQGDIIGIIGKNGAGKST-LLHL--IHndlAPAQGQI--------------L 62
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTlLLHLngIY---LPQRGRVkvmgrevnaenekwV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 63 RKdiKLALVEQ------------ETAAYSFADQTPAEKKLLEKWHVPLR-----DF-----HQLSGGEKLKARLAKGLSE 120
Cdd:PRK13647 78 RS--KVGLVFQdpddqvfsstvwDDVAFGPVNMGLDKDEVERRVEEALKavrmwDFrdkppYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2828494 121 DADLLLLDEPTNHLDEKSLQFLIQQLK--HYNG-TVILVSHDRYFLDEAATKI 170
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDrlHNQGkTVIVATHDVDLAAEWADQV 208
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
292-348 |
8.42e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 59.31 E-value: 8.42e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG---QETAEGSVW 348
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkYEVTSGSIL 60
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-438 |
9.96e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 23 VNASVQQGDIIGIIGKNGAGKSTLLHLI-----HNDLapaQGQIL---------------RKDI-----KLALVEQETAA 77
Cdd:PRK13549 24 VSLKVRAGEIVSLCGENGAGKSTLMKVLsgvypHGTY---EGEIIfegeelqasnirdteRAGIaiihqELALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 78 --------------YSFADQTPAEKKLLEKWHV---PLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQ 140
Cdd:PRK13549 101 eniflgneitpggiMDYDAMYLRAQKLLAQLKLdinPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 141 FL---IQQLKHYNGTVILVSHDryfLDEA---ATKIWSLEDqtliefkGNYSGYmkfREKKRLTQqreyekqqkmvERIE 214
Cdd:PRK13549 181 VLldiIRDLKAHGIACIYISHK---LNEVkaiSDTICVIRD-------GRHIGT---RPAAGMTE-----------DDII 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 215 AQMNGlaswsekahaqstkkegfkeyhrvkakrtdaqikskqkRLEKELekakaEPVTPeytvrfsidttHKTGKRFLEV 294
Cdd:PRK13549 237 TMMVG--------------------------------------RELTAL-----YPREP-----------HTIGEVILEV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 295 QNVT---KAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG--QETAEGSVWV--------SPS----ANIGY 357
Cdd:PRK13549 263 RNLTawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGayPGRWEGEIFIdgkpvkirNPQqaiaQGIAM 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 358 LTQE----------------------------VFDLPLEQTpeelfenetfkargHVQNLMRHLGFTAAQWTEPIKHMSM 409
Cdd:PRK13549 343 VPEDrkrdgivpvmgvgknitlaaldrftggsRIDDAAELK--------------TILESIQRLKVKTASPELAIARLSG 408
|
490 500
....*....|....*....|....*....
gi 2828494 410 GERVKIKLMAYILEEKDVLILDEPTNHLD 438
Cdd:PRK13549 409 GNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
296-462 |
1.01e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.43 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 296 NVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSVW--------VSPSA-NIGYLTQEVFDL 365
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGDLFigekrmndVPPAErGVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 366 PleqtPEELFENETF--------KA--RGHVQNLMRHLGFTAAQWTEPiKHMSMGERVKIKLMAYILEEKDVLILDEPTN 435
Cdd:PRK11000 88 P----HLSVAENMSFglklagakKEeiNQRVNQVAEVLQLAHLLDRKP-KALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190
....*....|....*....|....*....|.
gi 2828494 436 HLDLPSREQLEETLS----QYSGTLLAVSHD 462
Cdd:PRK11000 163 NLDAALRVQMRIEISrlhkRLGRTMIYVTHD 193
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-166 |
1.08e-09 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 58.54 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQ-------ILRKDIK----LALVEQETAA 77
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdVVREPREvrrrIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 78 ----------YSFA--------------DQTPAEKKLLEKWHVPLRDFhqlSGGEKLKARLAKGLSEDADLLLLDEPTNH 133
Cdd:cd03265 85 ddeltgwenlYIHArlygvpgaerreriDELLDFVGLLEAADRLVKTY---SGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 2828494 134 LDEKSLQFL---IQQLKHYNG-TVILVSHdryFLDEA 166
Cdd:cd03265 162 LDPQTRAHVweyIEKLKEEFGmTILLTTH---YMEEA 195
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
292-462 |
1.14e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.33 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWVS------PSANIGYLTQEVFD 364
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGfVPYQHGSITLDgkpvegPGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 365 LPLEQTPE------ELFENETFKARGHVQNLMRHLGFTAAQwTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLD 438
Cdd:PRK11248 82 LPWRNVQDnvafglQLAGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180
....*....|....*....|....*...
gi 2828494 439 LPSREQLEETLSQ-YSGT---LLAVSHD 462
Cdd:PRK11248 161 AFTREQMQTLLLKlWQETgkqVLLITHD 188
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
292-347 |
1.15e-09 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 58.60 E-value: 1.15e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSV 347
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPrSGSI 57
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-166 |
1.18e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI------LRKD------------ 65
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlferqsIKKDlctyqkqlcfvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 66 ----IKLALVEQETAAYSFADQTPAEK-----KLLEKWHvpLRDF--HQLSGGEKLKARLAKGLSEDADLLLLDEPTNHL 134
Cdd:PRK13540 81 hrsgINPYLTLRENCLYDIHFSPGAVGitelcRLFSLEH--LIDYpcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 2828494 135 DEKSLQFLIQQLKHY---NGTVILVSHDRYFLDEA 166
Cdd:PRK13540 159 DELSLLTIITKIQEHrakGGAVLLTSHQDLPLNKA 193
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
311-465 |
1.20e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.58 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 311 NFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWVS----PSANIG-------------YLTQEVFDLPLEQTPE 372
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGlYRPESGEILLDgqpvTADNREayrqlfsavfsdfHLFDRLLGLDGEADPA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 373 ElfenetfkarghVQNLMRHLGftaaqwtepIKH-------------MSMGERvkiK----LMAYiLEEKDVLILDE--- 432
Cdd:COG4615 432 R------------ARELLERLE---------LDHkvsvedgrfsttdLSQGQR---KrlalLVAL-LEDRPILVFDEwaa 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2828494 433 ---PT------NHLdLPS-REQleetlsqysG-TLLAVSHD-RYF 465
Cdd:COG4615 487 dqdPEfrrvfyTEL-LPElKAR---------GkTVIAISHDdRYF 521
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
292-480 |
1.27e-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: 58.50 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLfKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAE-GSVW--------VSPSA-NIGYLTQE 361
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDsGKILlngkditnLPPEKrDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 362 VFDLPleqtPEELFENETFKAR----------GHVQNLMRHLGFTAAQWTEPiKHMSMGERVKIKL-MAYILEEKdVLIL 430
Cdd:cd03299 80 YALFP----HMTVYKNIAYGLKkrkvdkkeieRKVLEIAEMLGIDHLLNRKP-ETLSGGEQQRVAIaRALVVNPK-ILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2828494 431 DEPTNHLDLPSREQLEETLS----QYSGTLLAVSHDryFLE-KTTNSKLVISNNG 480
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKkirkEFGVTVLHVTHD--FEEaWALADKVAIMLNG 206
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-164 |
1.28e-09 |
|
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: 58.92 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 26 SVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQG-------------------------QILRKDIKLALVEQetaaysF 80
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeildefrgselqnyftKLLEGDVKVIVKPQ------Y 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 81 ADQTPAEKK-----LLEKW----------------HVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEK-- 137
Cdd:cd03236 96 VDLIPKAVKgkvgeLLKKKdergkldelvdqlelrHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqr 175
|
170 180
....*....|....*....|....*...
gi 2828494 138 -SLQFLIQQLKHYNGTVILVSHDRYFLD 164
Cdd:cd03236 176 lNAARLIRELAEDDNYVLVVEHDLAVLD 203
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
286-503 |
1.30e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 60.23 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 286 KTGKRF---LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETaegsvwvsPSA-NIGYLTQE 361
Cdd:PRK11607 11 KTRKALtplLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQ--------PTAgQIMLDGVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 362 VFDLPLEQTP-------EELFENETFK---ARGHVQNLMRHlGFTAAQWTEPIK--HM-----------SMGERVKIKLM 418
Cdd:PRK11607 83 LSHVPPYQRPinmmfqsYALFPHMTVEqniAFGLKQDKLPK-AEIASRVNEMLGlvHMqefakrkphqlSGGQRQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 419 AYILEEKDVLILDEPTNHLD--LPSREQLE--ETLSQYSGTLLAVSHDRyflEK--TTNSKLVISNNGIEKQLNDvPSER 492
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQ---EEamTMAGRIAIMNRGKFVQIGE-PEEI 237
|
250
....*....|.
gi 2828494 493 NEREELRLKLE 503
Cdd:PRK11607 238 YEHPTTRYSAE 248
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
292-461 |
1.33e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 60.89 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERT---LFKNANFTIQHGEKVAIIGPNGSGKTT----LLNI---------------------------- 336
Cdd:TIGR00958 479 IEFQDVSFSYPNRPdvpVLKGLTFTLHPGEVVALVGPSGSGKSTvaalLQNLyqptggqvlldgvplvqydhhylhrqva 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 337 ILGQETA--EGSVwvspSANIGYltqevfdlPLEQTPEELFENETFKARGHvqNLMrhLGFTAAQWTEPIKH---MSMGE 411
Cdd:TIGR00958 559 LVGQEPVlfSGSV----RENIAY--------GLTDTPDEEIMAAAKAANAH--DFI--MEFPNGYDTEVGEKgsqLSGGQ 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2828494 412 RVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYSGTLLAVSH 461
Cdd:TIGR00958 623 KQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-181 |
1.43e-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: 60.53 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEV--KDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------------- 61
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdreelgrhigy 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 62 LRKDIKL--ALVEQETAaySFADQTPAE--------------KKLLEKWHVPLRDF-HQLSGGEKLKARLAKGLSEDADL 124
Cdd:COG4618 411 LPQDVELfdGTIAENIA--RFGDADPEKvvaaaklagvhemiLRLPDGYDTRIGEGgARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 125 LLLDEPTNHLD---EKSLQFLIQQLKHYNGTVILVSHDRYFLdEAATKIWSLEDQTLIEF 181
Cdd:COG4618 489 VVLDEPNSNLDdegEAALAAAIRALKARGATVVVITHRPSLL-AAVDKLLVLRDGRVQAF 547
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
292-512 |
1.56e-09 |
|
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: 60.20 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG---QETAEGSV-----------WVSPSANIG- 356
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqYEPTSGRIiyhvalcekcgYVERPSKVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 357 -------YLTQEVFDL----------------PLEQTPEELFENETFKArgHVQNLMRHLGFTA-------------AQW 400
Cdd:TIGR03269 81 pcpvcggTLEPEEVDFwnlsdklrrrirkriaIMLQRTFALYGDDTVLD--NVLEALEEIGYEGkeavgravdliemVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 401 TEPIKH----MSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPS----REQLEETLSQYSGTLLAVSHDRYFLEKTTNS 472
Cdd:TIGR03269 159 SHRITHiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTaklvHNALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2828494 473 KLVISNNGIEKQLNdvPSERNER-EELRLKLETERQEVLGK 512
Cdd:TIGR03269 239 AIWLENGEIKEEGT--PDEVVAVfMEGVSEVEKECEVEVGE 277
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-135 |
1.82e-09 |
|
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: 58.71 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 19 VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-------------------LRKDIKLALVEQETAAYS 79
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkhsgrisfssqfswimpgtIKENIIFGVSYDEYRYKS 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 FADQTPAEK---KLLEKWHVPLRDFH-QLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD 135
Cdd:cd03291 132 VVKACQLEEditKFPEKDNTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
292-499 |
1.94e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.69 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGE--RTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEGSV------WVSPSAN-----IGYL 358
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIqidgvsWNSVTLQtwrkaFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQEVFDL---------PLEQ-TPEELFE-NETFKARGHVQNLMRHLGFtaaQWTEPIKHMSMGERVKIKLMAYILEEKDV 427
Cdd:TIGR01271 1298 PQKVFIFsgtfrknldPYEQwSDEEIWKvAEEVGLKSVIEQFPDKLDF---VLVDGGYVLSNGHKQLMCLARSILSKAKI 1374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 428 LILDEPTNHLDLPSREQLEETLSQ-YSGTLLAVSHDRYFLEKTTNSKLVISNNGIeKQLNDVPSERNEREELR 499
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQIIRKTLKQsFSNCTVILSEHRVEALLECQQFLVIEGSSV-KQYDSIQKLLNETSLFK 1446
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-451 |
2.20e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.84 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHL-------------IHNDLAPAQGQILR----KDI 66
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIlsgvyphgtwdgeIYWSGSPLKASNIRdterAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 67 -----KLALVEQETAA---------------YSFADQTPAEKKLLEKWHVPL----RDFHQLSGGEKLKARLAKGLSEDA 122
Cdd:TIGR02633 81 viihqELTLVPELSVAeniflgneitlpggrMAYNAMYLRAKNLLRELQLDAdnvtRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 123 DLLLLDEPTNHLDEKSLQFL---IQQLKHYNGTVILVSHDryfLDEAAtkiwSLEDQTLIEFKGNYSGYmkfREKKRLTQ 199
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILldiIRDLKAHGVACVYISHK---LNEVK----AVCDTICVIRDGQHVAT---KDMSTMSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 200 qreyekqqkmvERIEAQMNGlaswsekahaqstkKEGFKEYHRvkakrtdaqikskqkrlekelekakaEPvtpeytvrf 279
Cdd:TIGR02633 231 -----------DDIITMMVG--------------REITSLYPH--------------------------EP--------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 280 sidttHKTGKRFLEVQNVTKAFGERTLFK---NANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA--EGSVWVSPSAN 354
Cdd:TIGR02633 251 -----HEIGDVILEARNLTCWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGkfEGNVFINGKPV 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 355 IGYLTQEVFDLPLEQTPEE-------------------LFENETFKAR-------GHVQNLMRHLGFTAAQWTEPIKHMS 408
Cdd:TIGR02633 326 DIRNPAQAIRAGIAMVPEDrkrhgivpilgvgknitlsVLKSFCFKMRidaaaelQIIGSAIQRLKVKTASPFLPIGRLS 405
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2828494 409 MGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQ 451
Cdd:TIGR02633 406 GGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQ 448
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
296-449 |
2.20e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.28 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 296 NVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAE---GSVWVS---PSANI----GYLTQEVFDL 365
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnftGTILANnrkPTKQIlkrtGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 366 P------------LEQTPEELFENETFKArghVQNLMRHLGFTAAQWT----EPIKHMSMGERVKIKLMAYILEEKDVLI 429
Cdd:PLN03211 153 PhltvretlvfcsLLRLPKSLTKQEKILV---AESVISELGLTKCENTiignSFIRGISGGERKRVSIAHEMLINPSLLI 229
|
170 180
....*....|....*....|
gi 2828494 430 LDEPTNHLDLPSREQLEETL 449
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTL 249
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
5-166 |
2.38e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 59.73 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDI------------KLALVE 72
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpltklqldswrsRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 73 Q------ETAAYSFA----DQTPAEKKLLEKwhvpLRDFHQ-------------------LSGGEKLKARLAKGLSEDAD 123
Cdd:PRK10789 396 QtpflfsDTVANNIAlgrpDATQQEIEHVAR----LASVHDdilrlpqgydtevgergvmLSGGQKQRISIARALLLNAE 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2828494 124 LLLLDEPTNHLDEKSLQFLIQQLKHY--NGTVILVSHDRYFLDEA 166
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWgeGRTVIISAHRLSALTEA 516
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
14-176 |
2.40e-09 |
|
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: 56.81 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 14 VKDQTVFkHVN---ASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGqilrkDIKLALVeqetaaysfadqTPAEKKl 90
Cdd:cd03222 7 VKRYGVF-FLLvelGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD-----NDEWDGI------------TPVYKP- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 91 lekwhvplrDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLKHY----NGTVILVSHDRYFLDEA 166
Cdd:cd03222 68 ---------QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYL 138
|
170
....*....|
gi 2828494 167 ATKIWSLEDQ 176
Cdd:cd03222 139 SDRIHVFEGE 148
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
292-468 |
2.42e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 59.07 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV----------SPSANIGYLTQ 360
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPdAGKITVlgvpvpararLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 361 evFD-LPLEQTPEE-------LFENETFKARGHVQNLMrHLGFTAAQWTEPIKHMSMGERVKIKLMAYILEEKDVLILDE 432
Cdd:PRK13536 122 --FDnLDLEFTVREnllvfgrYFGMSTREIEAVIPSLL-EFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2828494 433 PTNHLDLPSR----EQLEETLSQySGTLLAVSHdryFLEK 468
Cdd:PRK13536 199 PTTGLDPHARhliwERLRSLLAR-GKTILLTTH---FMEE 234
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-158 |
3.02e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 23 VNASVQQGDIIGIIGKNGAGKSTLLHL-------------IHNDlapaqGQILR-KDIK-------------LALVEQ-- 73
Cdd:NF040905 20 VNLSVREGEIHALCGENGAGKSTLMKVlsgvyphgsyegeILFD-----GEVCRfKDIRdsealgiviihqeLALIPYls 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 ---------ETAAYSFAD--QTPAE-KKLLEKwhVPLRDFHQ-----LSGGEKLKARLAKGLSEDADLLLLDEPT---NH 133
Cdd:NF040905 95 iaeniflgnERAKRGVIDwnETNRRaRELLAK--VGLDESPDtlvtdIGVGKQQLVEIAKALSKDVKLLILDEPTaalNE 172
|
170 180
....*....|....*....|....*
gi 2828494 134 LDEKSLQFLIQQLKHYNGTVILVSH 158
Cdd:NF040905 173 EDSAALLDLLLELKAQGITSIIISH 197
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-462 |
3.30e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLA----------- 69
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArltpakahqlg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 70 --LVEQEtaAYSFADQT---------PAEKKLLEKWHVPLRdfhQLSGGEKLKARLA-------------KGLSEDADLL 125
Cdd:PRK15439 88 iyLVPQE--PLLFPNLSvkenilfglPKRQASMQKMKQLLA---ALGCQLDLDSSAGslevadrqiveilRGLMRDSRIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 126 LLDEPTNHLDEKSLQFLIQQLKHYNGT---VILVSHDryfLDEaatkIWSLEDqtliefkgnysgymkfrekkrltqqre 202
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQgvgIVFISHK---LPE----IRQLAD--------------------------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 203 yekqqkmveRIEAQMNGLASWSEKAhAQSTKKEGFKEYHRVKakrTDAQIKSKQKrLEKELEKAKaepvtpeytvrfsid 282
Cdd:PRK15439 209 ---------RISVMRDGTIALSGKT-ADLSTDDIIQAITPAA---REKSLSASQK-LWLELPGNR--------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 283 TTHKTGKRFLEVQNVTkafGERtlFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWVSPSANIGYLTQE 361
Cdd:PRK15439 260 RQQAAGAPVLTVEDLT---GEG--FRNISLEVRAGEILGLAGVVGAGRTELAETLYGlRPARGGRIMLNGKEINALSTAQ 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 362 VFDLPLEQTPEE-------------------LFENETF-----KARGHVQNLMRHLGFTAAQWTEPIKHMSMGERVKIkL 417
Cdd:PRK15439 335 RLARGLVYLPEDrqssglyldaplawnvcalTHNRRGFwikpaRENAVLERYRRALNIKFNHAEQAARTLSGGNQQKV-L 413
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2828494 418 MAYILE-EKDVLILDEPTNHLDLPSRE---QLEETLSQYSGTLLAVSHD 462
Cdd:PRK15439 414 IAKCLEaSPQLLIVDEPTRGVDVSARNdiyQLIRSIAAQNVAVLFISSD 462
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-186 |
3.68e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 59.26 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVS--YEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR-----KDIKL-------AL 70
Cdd:PRK11176 342 IEFRNVTftYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdghdlRDYTLaslrnqvAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 71 VEQE----------TAAYSFADQTPAEK--KLLEKWHVplRDFHQ----------------LSGGEKLKARLAKGLSEDA 122
Cdd:PRK11176 422 VSQNvhlfndtianNIAYARTEQYSREQieEAARMAYA--MDFINkmdngldtvigengvlLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 123 DLLLLDEPTNHLD---EKSLQFLIQQLKHyNGTVILVSHdRYFLDEAATKIWSLEDQTLIEfKGNYS 186
Cdd:PRK11176 500 PILILDEATSALDtesERAIQAALDELQK-NRTSLVIAH-RLSTIEKADEILVVEDGEIVE-RGTHA 563
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
292-462 |
4.11e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.10 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGER----TLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWV--SP------------- 351
Cdd:PRK10584 7 VEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGlDDGSSGEVSLvgQPlhqmdeearaklr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 352 SANIGYLTQEVFDLP----LE--QTPEELFENETFKARGHVQNLMRHLGFtaaqwTEPIKHM----SMGERVKIKLMAYI 421
Cdd:PRK10584 87 AKHVGFVFQSFMLIPtlnaLEnvELPALLRGESSRQSRNGAKALLEQLGL-----GKRLDHLpaqlSGGEQQRVALARAF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2828494 422 LEEKDVLILDEPTNHLDLPSREQLEETL----SQYSGTLLAVSHD 462
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
292-445 |
4.19e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.89 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAF-GERTLFKNANFTIQHGEKVAIIGPNGSGKTTL---LNIILGQETAEGSVWVSP--SANI-------GYL 358
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLfrhFNGILKPTSGSVLIRGEPitKENIrevrkfvGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQ----EVFDLPLEQT----PEEL-FENETFKARghVQNLMRHLGFTAAQWTEPiKHMSMGERVKIKLMAYILEEKDVLI 429
Cdd:PRK13652 84 FQnpddQIFSPTVEQDiafgPINLgLDEETVAHR--VSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170
....*....|....*.
gi 2828494 430 LDEPTNHLDLPSREQL 445
Cdd:PRK13652 161 LDEPTAGLDPQGVKEL 176
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-158 |
4.33e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.42 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 16 DQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKD--------------------IKLALVEQET 75
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeachylghrnaMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 76 ----AAYSFADQTPAEKKL--LEKWHVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKS---LQFLIQQL 146
Cdd:PRK13539 94 lefwAAFLGGEELDIAAALeaVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAvalFAELIRAH 173
|
170
....*....|..
gi 2828494 147 KHYNGTVILVSH 158
Cdd:PRK13539 174 LAQGGIVIAATH 185
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
292-347 |
4.59e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.24 E-value: 4.59e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSV 347
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPdAGEV 63
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-174 |
4.63e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.51 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVK-DQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--------------RKDIKL 68
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgepitkenirevRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 AL-----------VEQETA---------AYSFADQTPAEKKLLEKWHVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLD 128
Cdd:PRK13652 83 VFqnpddqifsptVEQDIAfgpinlgldEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2828494 129 EPTNHLDEKSLQFLIQQL----KHYNGTVILVSHDRYFLDEAATKIWSLE 174
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLndlpETYGMTVIFSTHQLDLVPEMADYIYVMD 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-166 |
5.51e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 57.92 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDI-----------KLALVEQ 73
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlaraRIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 -ETAAYSFadqTPAEKKL------------LEKWHVPLRDF-----------HQLSGGEKLKARLAKGLSEDADLLLLDE 129
Cdd:PRK13536 122 fDNLDLEF---TVRENLLvfgryfgmstreIEAVIPSLLEFarleskadarvSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2828494 130 PTNHLDEKSLQFLIQQLKHY---NGTVILVSHdryFLDEA 166
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLlarGKTILLTTH---FMEEA 235
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-159 |
5.85e-09 |
|
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: 57.76 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYEVKDQTVF--KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAP---AQGQIL--RKDI--------------K 67
Cdd:COG0444 8 KVYFPTRRGVVKavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILfdGEDLlklsekelrkirgrE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 68 LALVEQE---------TAAYSFAD----QTPAEKK--------LLEKWHVP-----LRDF-HQLSGGEKLKARLAKGLSE 120
Cdd:COG0444 88 IQMIFQDpmtslnpvmTVGDQIAEplriHGGLSKAeareraieLLERVGLPdperrLDRYpHELSGGMRQRVMIARALAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2828494 121 DADLLLLDEPTNHLDeKSLQF----LIQQLKH-YNGTVILVSHD 159
Cdd:COG0444 168 EPKLLIADEPTTALD-VTIQAqilnLLKDLQReLGLAILFITHD 210
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-159 |
6.16e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.81 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDIK----------- 67
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVfdGKDITdwqtakimrea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 68 LALVEQETAAYS-------------FADQTPAEKKLLEKWHVPLRDFHQ-------LSGGEKLKARLAKGLSEDADLLLL 127
Cdd:PRK11614 82 VAIVPEGRRVFSrmtveenlamggfFAERDQFQERIKWVYELFPRLHERriqragtMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 2828494 128 DEPTNHLDEKSLQFL---IQQLKHYNGTVILVSHD 159
Cdd:PRK11614 162 DEPSLGLAPIIIQQIfdtIEQLREQGMTIFLVEQN 196
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
278-438 |
6.18e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 58.52 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 278 RFSIDTTHKTGKRFLEVQNVTKAfGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQEtaEGSVWVSPSANI-- 355
Cdd:TIGR00955 13 RVAQDGSWKQLVSRLRGCFCRER-PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRS--PKGVKGSGSVLLng 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 356 ------------GYLTQEVFDLPLEQTPEELF--------ENETFKARGH-VQNLMRHLGFTAAQWT-----EPIKHMSM 409
Cdd:TIGR00955 90 mpidakemraisAYVQQDDLFIPTLTVREHLMfqahlrmpRRVTKKEKRErVDEVLQALGLRKCANTrigvpGRVKGLSG 169
|
170 180
....*....|....*....|....*....
gi 2828494 410 GERVKIKLMAYILEEKDVLILDEPTNHLD 438
Cdd:TIGR00955 170 GERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-159 |
6.20e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.02 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 18 TVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDI----------KLALVEQETAAYSFADQTP 85
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILidGKDVtklpeykrakYIGRVFQDPMMGTAPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 86 AE-------------------KKLLEKWHVPLRDFH------------QLSGGEK-----LKARLAKglsedADLLLLDE 129
Cdd:COG1101 100 EEnlalayrrgkrrglrrgltKKRRELFRELLATLGlglenrldtkvgLLSGGQRqalslLMATLTK-----PKLLLLDE 174
|
170 180 190
....*....|....*....|....*....|....
gi 2828494 130 PTNHLDEKSLQFLIQ---QL-KHYNGTVILVSHD 159
Cdd:COG1101 175 HTAALDPKTAALVLElteKIvEENNLTTLMVTHN 208
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
292-461 |
6.48e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 57.36 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLF-----KNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ-ETAEGSVWV------SPSANIGYLT 359
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkalDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLlKPTSGKIIIdgvditDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 360 QE---VFdlpleQTPE-ELFENETFK--ARG-------------HVQNLMRHLGFTAAQWTE--PIKhMSMGERVKIKLM 418
Cdd:PRK13637 83 KKvglVF-----QYPEyQLFEETIEKdiAFGpinlglseeeienRVKRAMNIVGLDYEDYKDksPFE-LSGGQKRRVAIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 419 AYILEEKDVLILDEPTNHLDLPSREQLEETLS----QYSGTLLAVSH 461
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKelhkEYNMTIILVSH 203
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-174 |
7.81e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 57.73 E-value: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIH-----------------NDLAPAQGQIlrkdik 67
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAgleditsgdlfigekrmNDVPPAERGV------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 68 lALVEQETAAY---------SF------ADQTPAEKK------LLEKWHVPLRDFHQLSGGEKLKARLAKGLSEDADLLL 126
Cdd:PRK11000 78 -GMVFQSYALYphlsvaenmSFglklagAKKEEINQRvnqvaeVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2828494 127 LDEPTNHLDEK---SLQFLIQQL-KHYNGTVILVSHDRYfldEAAT---KIWSLE 174
Cdd:PRK11000 157 LDEPLSNLDAAlrvQMRIEISRLhKRLGRTMIYVTHDQV---EAMTladKIVVLD 208
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-267 |
8.14e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.77 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 10 VSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNdLAPAQGQI---------------------------- 61
Cdd:TIGR01271 1225 AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLR-LLSTEGEIqidgvswnsvtlqtwrkafgvipqkvfi 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 62 ----LRK---------DIKLALVEQETAAYSFADQTPaekkllEKWHVPLRDF-HQLSGGEKLKARLAKGLSEDADLLLL 127
Cdd:TIGR01271 1304 fsgtFRKnldpyeqwsDEEIWKVAEEVGLKSVIEQFP------DKLDFVLVDGgYVLSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 128 DEPTNHLDEKSLQFLIQQLKHY--NGTVILVSHDRYFLdeaatkiwsLEDQTLIEFKGNysgymkfrekkrltQQREYEK 205
Cdd:TIGR01271 1378 DEPSAHLDPVTLQIIRKTLKQSfsNCTVILSEHRVEAL---------LECQQFLVIEGS--------------SVKQYDS 1434
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 206 QQKMVERieaqmnglASWSEKAHAQSTKKEGFKEYHRVKAKR-TDAQIKSKQKRLEKELEKAK 267
Cdd:TIGR01271 1435 IQKLLNE--------TSLFKQAMSAADRLKLFPLHRRNSSKRkPQPKITALREEAEEEVQNTR 1489
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-166 |
8.18e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 55.55 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-LRKDIklalveqetaaySFADQ 83
Cdd:cd03250 6 ASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVsVPGSI------------AYVSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 84 TPaekkllekWHVP--LRD---FHQ-------------------------------------LSGGEklKAR--LAKGLS 119
Cdd:cd03250 74 EP--------WIQNgtIREnilFGKpfdeeryekvikacalepdleilpdgdlteigekginLSGGQ--KQRisLARAVY 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2828494 120 EDADLLLLDEPTNHLDEKSLQFLIQQ-----LKHyNGTVILVSHDRYFLDEA 166
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFENcilglLLN-NKTRILVTHQLQLLPHA 194
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-159 |
8.32e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.20 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNV--SYEVKDQT--VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQG--QILRKDI------KL 68
Cdd:PRK10535 1 MTALLELKDIrrSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyRVAGQDVatldadAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 ALVEQETAAYSF----------ADQT---PA-----EKK--------LLEKWHVPLR-DFH--QLSGGEKLKARLAKGLS 119
Cdd:PRK10535 81 AQLRREHFGFIFqryhllshltAAQNvevPAvyaglERKqrllraqeLLQRLGLEDRvEYQpsQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2828494 120 EDADLLLLDEPTNHLDEKS---LQFLIQQLKHYNGTVILVSHD 159
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-169 |
8.54e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 56.30 E-value: 8.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKL----------ALVEQE 74
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqqkGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 75 TAAYSFADQ-----------------------TPAE------KKLLEKWHV-------PLRdfhqLSGGEKLKARLAKGL 118
Cdd:PRK11264 84 RQHVGFVFQnfnlfphrtvleniiegpvivkgEPKEeataraRELLAKVGLagketsyPRR----LSGGQQQRVAIARAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2828494 119 SEDADLLLLDEPTNHLD-EKSLQFL--IQQLKHYNGTVILVSHDRYFLDEAATK 169
Cdd:PRK11264 160 AMRPEVILFDEPTSALDpELVGEVLntIRQLAQEKRTMVIVTHEMSFARDVADR 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-349 |
8.86e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.73 E-value: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 21 KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLA--------------------LVE-------- 72
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprdaialgigmvhqhfmLVPnltvaeni 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 73 ---QETAAYSFADQTPAEKKLLE-----KWHVPLRDF-HQLSGGEK-----LKArlakgLSEDADLLLLDEPTNHL--DE 136
Cdd:COG3845 102 vlgLEPTKGGRLDRKAARARIRElseryGLDVDPDAKvEDLSVGEQqrveiLKA-----LYRGARILILDEPTAVLtpQE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 137 -KSLQFLIQQLKHYNGTVILVSHdryfldeaatkiwsledqtliefkgnysgymKFREKKRLTQQ----ReyekQQKMVE 211
Cdd:COG3845 177 aDELFEILRRLAAEGKSIIFITH-------------------------------KLREVMAIADRvtvlR----RGKVVG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 212 RIEAqmnglaswsekahAQSTKKE------GfkeyhrvkakrtdaqikskqKRLEKELEKAKAEPvtpeytvrfsidtth 285
Cdd:COG3845 222 TVDT-------------AETSEEElaelmvG--------------------REVLLRVEKAPAEP--------------- 253
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2828494 286 ktGKRFLEVQNVT-KAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAE-GSVWV 349
Cdd:COG3845 254 --GEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAsGSIRL 317
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-168 |
1.30e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.88 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 2 KEIVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVEQE-----TA 76
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEnrhvnTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 77 AYSFA-----------------DQTPA---EKKLLEKWH-VPLRDF-----HQLSGGEKLKARLAKGLSEDADLLLLDEP 130
Cdd:PRK09452 92 FQSYAlfphmtvfenvafglrmQKTPAaeiTPRVMEALRmVQLEEFaqrkpHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2828494 131 TNHLD---EKSLQFLIQQLKHYNG-TVILVSHDRyflDEAAT 168
Cdd:PRK09452 172 LSALDyklRKQMQNELKALQRKLGiTFVFVTHDQ---EEALT 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
292-462 |
1.51e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.90 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAF--GERTLfKNANFTIQHGEKVAIIGPNGSGKTTLL---NII----------LGQE-TAEGSVWVSpsANI 355
Cdd:PRK13647 5 IEVEDLHFRYkdGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLlhlNGIylpqrgrvkvMGREvNAENEKWVR--SKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 356 GYLTQE---------VFD------LPLEQTPEELFE--NETFKARGhVQNLmRHlgftaaqwtEPIKHMSMGERVKIKLM 418
Cdd:PRK13647 82 GLVFQDpddqvfsstVWDdvafgpVNMGLDKDEVERrvEEALKAVR-MWDF-RD---------KPPYHLSYGQKKRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 419 AYILEEKDVLILDEPTNHLDLPSREQLEETL---SQYSGTLLAVSHD 462
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILdrlHNQGKTVIVATHD 197
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-177 |
1.55e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.12 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 16 DQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDLAP-AQGQILR-KDIKLALVEQ----------ETAAYSFADQ 83
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI-AGLWPyGSGRIARpAGARVLFLPQrpylplgtlrEALLYPATAE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 84 TPAEKKL---LEKwhVPLRDF-----------HQLSGGEKLK---AR--LAKglsedADLLLLDEPTNHLDEKSLQFLIQ 144
Cdd:COG4178 454 AFSDAELreaLEA--VGLGHLaerldeeadwdQVLSLGEQQRlafARllLHK-----PDWLFLDEATSALDEENEAALYQ 526
|
170 180 190
....*....|....*....|....*....|....*
gi 2828494 145 QLKH--YNGTVILVSHdRYFLDEAATKIWSLEDQT 177
Cdd:COG4178 527 LLREelPGTTVISVGH-RSTLAAFHDRVLELTGDG 560
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
292-349 |
1.63e-08 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 55.28 E-value: 1.63e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 292 LEVQNVTKAFGER----TLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSVWV 349
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERpTSGSVLV 64
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
292-348 |
1.70e-08 |
|
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: 55.37 E-value: 1.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVW 348
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPrSGSIR 61
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
292-339 |
1.76e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.42 E-value: 1.76e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG 339
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-183 |
1.82e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.96 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKD--QTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAP---AQGQILRKDIKL---------- 68
Cdd:PRK13640 5 IVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLtaktvwdire 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 ---------------ALVEQETAAYSFADQTPAEK------KLLEKwhVPLRDFHQ-----LSGGEKLKARLAKGLSEDA 122
Cdd:PRK13640 85 kvgivfqnpdnqfvgATVGDDVAFGLENRAVPRPEmikivrDVLAD--VGMLDYIDsepanLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2828494 123 DLLLLDEPTNHLD----EKSLQFLIQQLKHYNGTVILVSHDryfLDEAatkiwSLEDQTLIEFKG 183
Cdd:PRK13640 163 KIIILDESTSMLDpagkEQILKLIRKLKKKNNLTVISITHD---IDEA-----NMADQVLVLDDG 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-159 |
1.83e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.78 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFK-----HVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI------------------ 61
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdyaipanlkkikevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 62 -LRKDIKLAL------VEQETAAYSFA--------DQTPAEKK---LLEKWHVPlRDF-----HQLSGGEKLKARLAKGL 118
Cdd:PRK13645 87 rLRKEIGLVFqfpeyqLFQETIEKDIAfgpvnlgeNKQEAYKKvpeLLKLVQLP-EDYvkrspFELSGGQKRRVALAGII 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2828494 119 SEDADLLLLDEPTNHLDEKS----LQFLIQQLKHYNGTVILVSHD 159
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHN 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
9-180 |
1.85e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.99 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYEVKDQTVFK-----HVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI------------------LRKD 65
Cdd:PRK13641 7 NVDYIYSPGTPMEkkgldNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyhitpetgnknlkkLRKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 66 IKLAL---------------VEQETAAYSFADQTPAEKKLleKW--HVPLRD-------FhQLSGGEKLKARLAKGLSED 121
Cdd:PRK13641 87 VSLVFqfpeaqlfentvlkdVEFGPKNFGFSEDEAKEKAL--KWlkKVGLSEdliskspF-ELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2828494 122 ADLLLLDEPTNHLDEKSLQFLIQQLKHYNG---TVILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
281-437 |
1.97e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 281 IDTTHKTGKRFLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEGSVWVSPSANIGYLT- 359
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 360 QEVFDLPLEQTPEE--LFENETFK------------ARGHVQNLMRHLGFTAAQwtepikHMSMG-----ERVKIKLMAY 420
Cdd:PRK15439 81 AKAHQLGIYLVPQEplLFPNLSVKenilfglpkrqaSMQKMKQLLAALGCQLDL------DSSAGslevaDRQIVEILRG 154
|
170
....*....|....*..
gi 2828494 421 ILEEKDVLILDEPTNHL 437
Cdd:PRK15439 155 LMRDSRILILDEPTASL 171
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-166 |
2.32e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.38 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 7 LTNV--SYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRKDIKL-- 68
Cdd:PRK13632 10 VENVsfSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkidgitiskenlkeIRKKIGIif 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 ---------ALVEQETA----------------AYSFADQTPAEKkLLEkwhvplRDFHQLSGGEKLKARLAKGLSEDAD 123
Cdd:PRK13632 90 qnpdnqfigATVEDDIAfglenkkvppkkmkdiIDDLAKKVGMED-YLD------KEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 124 LLLLDEPTNHLDEKS----LQFLIQQLKHYNGTVILVSHDryfLDEA 166
Cdd:PRK13632 163 IIIFDESTSMLDPKGkreiKKIMVDLRKTRKKTLISITHD---MDEA 206
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
12-170 |
2.41e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.87 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 12 YEVKDQTV--FKHVNASVQQGDIIGIIGKNGAGKSTLLHlihndlapaqgQILRKDIKLALVEQETAAYS----FADQTP 85
Cdd:cd03238 1 LTVSGANVhnLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------EGLYASGKARLISFLPKFSRnkliFIDQLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 86 AEKKL-LEkwHVPL-RDFHQLSGGEKLKARLAK--GLSEDADLLLLDEPTNHLDEKSLQFLIQQLK---HYNGTVILVSH 158
Cdd:cd03238 70 FLIDVgLG--YLTLgQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLEVIKgliDLGNTVILIEH 147
|
170
....*....|..
gi 2828494 159 DRYFLDEAATKI 170
Cdd:cd03238 148 NLDVLSSADWII 159
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-187 |
2.45e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 2 KEIVTLTNVSYEVkdqtvFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-----------RKDIKLAL 70
Cdd:PRK15439 266 APVLTVEDLTGEG-----FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMlngkeinalstAQRLARGL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 71 V-----EQETAAY-----------------SFADQTPAEKKLLEKWH----VPLRDFHQ----LSGGEKLKARLAKGLSE 120
Cdd:PRK15439 341 VylpedRQSSGLYldaplawnvcalthnrrGFWIKPARENAVLERYRralnIKFNHAEQaartLSGGNQQKVLIAKCLEA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 121 DADLLLLDEPTNHLD---EKSLQFLIQQLKHYNGTVILVSHDryfLDEaatkIWSLEDQTLIEFKGNYSG 187
Cdd:PRK15439 421 SPQLLIVDEPTRGVDvsaRNDIYQLIRSIAAQNVAVLFISSD---LEE----IEQMADRVLVMHQGEISG 483
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-199 |
2.73e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.98 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 19 VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLALVEQETAAYSFAD---------------- 82
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADknqlrllrtrltmvfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 83 ---------------QTPAEKKLLEKWHVPLRDFH-----------------QLSGGEKLKARLAKGLSEDADLLLLDEP 130
Cdd:PRK10619 100 hfnlwshmtvlenvmEAPIQVLGLSKQEARERAVKylakvgideraqgkypvHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2828494 131 TNHLDEK---SLQFLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEdQTLIEFKGNYSGYMKFREKKRLTQ 199
Cdd:PRK10619 180 TSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLH-QGKIEEEGAPEQLFGNPQSPRLQQ 250
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
303-462 |
2.86e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 55.17 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 303 ERTLFKNANFTIQHGEKVAIIGPNGSGKTTL---LNIILGQETaeGSVWVSpSANIGYLTQEVFDLPLEQT-------PE 372
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLiqnINALLKPTT--GTVTVD-DITITHKTKDKYIRPVRKRigmvfqfPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 373 -ELFEN-----------------ETFKARGHvqNLMRHLGFTAAQWTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPT 434
Cdd:PRK13646 96 sQLFEDtvereiifgpknfkmnlDEVKNYAH--RLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190
....*....|....*....|....*....|..
gi 2828494 435 NHLDLPSREQLEETLSQY----SGTLLAVSHD 462
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLqtdeNKTIILVSHD 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-173 |
3.39e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.01 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 8 TNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--------RKDIKLALVEQETAAYS 79
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwqgkpldySKRGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 FADQT------------------PAEKK----------LLEKWHVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPT 131
Cdd:PRK13638 85 DPEQQifytdidsdiafslrnlgVPEAEitrrvdealtLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2828494 132 NHLDEKSLQFLIQQLKHYNGT---VILVSHDRYFLDEAATKIWSL 173
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVL 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-348 |
3.46e-08 |
|
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: 56.23 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 17 QTVFKHVNASVQQGDIIGIIGKNGAGKS----TLLHLIHNDLAPAQGQI--------------LRK----DIklALVEQE 74
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSIlfdgqdllglsereLRRirgnRI--AMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 75 --TA---AYSFADQ-------------TPAEKK---LLEKWHVP-----LRDF-HQLSGGEKLKARLAKGLSEDADLLLL 127
Cdd:COG4172 101 pmTSlnpLHTIGKQiaevlrlhrglsgAAARARaleLLERVGIPdperrLDAYpHQLSGGQRQRVMIAMALANEPDLLIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 128 DEPTNHLD----EKSLQfLIQQLKHYNGT-VILVSHD----RYFLDEAATkiwsledqtliefkgnysgyMKfrekkrlt 198
Cdd:COG4172 181 DEPTTALDvtvqAQILD-LLKDLQRELGMaLLLITHDlgvvRRFADRVAV--------------------MR-------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 199 qqreyekQQKMVERIEAQmnglASWSEKAHAqstkkegfkeYhrvkakrTDAQIKSKQKRLEKELEkAKAEPVtpeytvr 278
Cdd:COG4172 232 -------QGEIVEQGPTA----ELFAAPQHP----------Y-------TRKLLAAEPRGDPRPVP-PDAPPL------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 279 fsidtthktgkrfLEVQNVTKAF-GERTLF----------KNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEGSV 347
Cdd:COG4172 276 -------------LEARDLKVWFpIKRGLFrrtvghvkavDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEI 342
|
.
gi 2828494 348 W 348
Cdd:COG4172 343 R 343
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
289-462 |
3.58e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 54.74 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 289 KRFLEVQNVTKAFG---ERTLFKNANFTIQHGEKVAIIGPNGSGKTT-------LLN------IILGQETAEGSVWvsps 352
Cdd:PRK13650 2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrlidgLLEaesgqiIIDGDLLTEENVW---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 353 aNIGYLTQEVFDLPLEQ----TPEEL----FEN-----ETFKARghVQNLMRHLGFTAAQWTEPIKhMSMGERVKIKLMA 419
Cdd:PRK13650 78 -DIRHKIGMVFQNPDNQfvgaTVEDDvafgLENkgiphEEMKER--VNEALELVGMQDFKEREPAR-LSGGQKQRVAIAG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 420 YILEEKDVLILDEPTNHLDLPSREQLEETL----SQYSGTLLAVSHD 462
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIkgirDDYQMTVISITHD 200
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-166 |
3.61e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.81 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 2 KEIVTLTNVSYEVKDQTVfkhvnaSVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDI--------------- 66
Cdd:PRK10070 32 EQILEKTGLSLGVKDASL------AIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiakisdaelrevrr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 67 -KLALVEQETAA---YSFADQT---------PA----EKKLLEKWHVPLRDF-----HQLSGGEKLKARLAKGLSEDADL 124
Cdd:PRK10070 106 kKIAMVFQSFALmphMTVLDNTafgmelagiNAeerrEKALDALRQVGLENYahsypDELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 125 LLLDEPTNHLD-----EKSLQFLIQQLKHYNgTVILVSHDryfLDEA 166
Cdd:PRK10070 186 LLMDEAFSALDplirtEMQDELVKLQAKHQR-TIVFISHD---LDEA 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
285-348 |
3.66e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.77 E-value: 3.66e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2828494 285 HKTGKRFLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAE-GSVW 348
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDhGEIL 65
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
292-462 |
3.71e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 54.61 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG--QETAeGSVWVSPSANIGYLTQEVFDLPLEQ 369
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfyKPTG-GTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 370 TpeelFEN-ETFKARGHVQNLM----RHL--GF-------------------TAAQWTEPIKHMSMGERVKIKLmAY--- 420
Cdd:PRK11300 85 T----FQHvRLFREMTVIENLLvaqhQQLktGLfsgllktpafrraesealdRAATWLERVGLLEHANRQAGNL-AYgqq 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2828494 421 --------ILEEKDVLILDEPTNHLDLPSREQLEETLS----QYSGTLLAVSHD 462
Cdd:PRK11300 160 rrleiarcMVTQPEILMLDEPAAGLNPKETKELDELIAelrnEHNVTVLLIEHD 213
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
292-461 |
3.86e-08 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 54.01 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERT---LFKNANFTIQHGEKVAIIGPNGSGKTTLLNIIL-------GQETAEG---------------- 345
Cdd:cd03248 12 VKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLEnfyqpqgGQVLLDGkpisqyehkylhskvs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 346 SVWVSP-------SANIGYltqevfdlPLEQTPEELFENETFKARGHvQNLMrhlGFTAAQWT---EPIKHMSMGERVKI 415
Cdd:cd03248 92 LVGQEPvlfarslQDNIAY--------GLQSCSFECVKEAAQKAHAH-SFIS---ELASGYDTevgEKGSQLSGGQKQRV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2828494 416 KLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQY--SGTLLAVSH 461
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH 207
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-187 |
4.23e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.42 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVK----DQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPA---QGQILRKDI---KLALVEQ 73
Cdd:cd03233 3 TLSWRNISFTTGkgrsKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIpykEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 ETAAYSFADQtpaekkllekWHVP------LRDF------HQ----LSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEK 137
Cdd:cd03233 83 GEIIYVSEED----------VHFPtltvreTLDFalrckgNEfvrgISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2828494 138 S-LQFL--IQQLKHYNGTVILVShdryfLDEAATKIWSLEDQTLIEFKGN--YSG 187
Cdd:cd03233 153 TaLEILkcIRTMADVLKTTTFVS-----LYQASDEIYDLFDKVLVLYEGRqiYYG 202
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-184 |
4.26e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.11 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 2 KEIVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL------------RKDIklA 69
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFidgedvthrsiqQRDI--C 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 70 LVEQETAAY---SFADQT---------PAE------KKLLEKwhVPLRDFH-----QLSGGEKLKARLAKGLSEDADLLL 126
Cdd:PRK11432 82 MVFQSYALFphmSLGENVgyglkmlgvPKEerkqrvKEALEL--VDLAGFEdryvdQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2828494 127 LDEPTNHLD---EKSLQFLIQQL-KHYNGTVILVSHDRyfldeaaTKIWSLEDQTLIEFKGN 184
Cdd:PRK11432 160 FDEPLSNLDanlRRSMREKIRELqQQFNITSLYVTHDQ-------SEAFAVSDTVIVMNKGK 214
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-159 |
4.60e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 54.31 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 17 QTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-----------------LRKDIKLALVEQETA--- 76
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplaklnraqrkaFRRDIQMVFQDSISAvnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 77 ----------------AYSFADQTPAEKKLLEKwhVPLRDFH------QLSGGEKLKARLAKGLSEDADLLLLDEPTNHL 134
Cdd:PRK10419 105 rktvreiireplrhllSLDKAERLARASEMLRA--VDLDDSVldkrppQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190
....*....|....*....|....*....|
gi 2828494 135 DeKSLQF-LIQQLK---HYNGTVIL-VSHD 159
Cdd:PRK10419 183 D-LVLQAgVIRLLKklqQQFGTACLfITHD 211
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
282-462 |
4.84e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.41 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 282 DTTHKTGKRFlEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNiILG--QETAEGSV---------WVS 350
Cdd:PRK10575 3 EYTNHSDTTF-ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGrhQPPSEGEIlldaqplesWSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 351 PS--ANIGYLTQEvfdLPLEQ--TPEEL--------------FENETfkaRGHVQNLMRHLGFTaaqwtePIKH-----M 407
Cdd:PRK10575 81 KAfaRKVAYLPQQ---LPAAEgmTVRELvaigrypwhgalgrFGAAD---REKVEEAISLVGLK------PLAHrlvdsL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2828494 408 SMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQ---LEETLSQYSG-TLLAVSHD 462
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDvlaLVHRLSQERGlTVIAVLHD 207
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
5-167 |
4.94e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 54.64 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVF-----KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI------------------ 61
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerralYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervitagkknkklkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 62 LRKdiKLALVEQ--------ETAA--YSFADQ----TPAEKKLLEKWHVPL---------RDFHQLSGGEKLKARLAKGL 118
Cdd:PRK13634 83 LRK--KVGIVFQfpehqlfeETVEkdICFGPMnfgvSEEDAKQKAREMIELvglpeellaRSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2828494 119 SEDADLLLLDEPTNHLD---EKSLQFLIQQLKHYNG-TVILVSHDryfLDEAA 167
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDpkgRKEMMEMFYKLHKEKGlTTVLVTHS---MEDAA 210
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
311-454 |
5.38e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 311 NFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEGSVWVSPSANIGYLTQEVFDLPLEQ-------------------TP 371
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDewqrnntdmlspgeddtgrTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 372 EELFENETfKARGHVQNLMRHLGFTAAqWTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQ 451
Cdd:PRK10938 103 AEIIQDEV-KDPARCEQLAQQFGITAL-LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLAS 180
|
...
gi 2828494 452 YSG 454
Cdd:PRK10938 181 LHQ 183
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-158 |
5.77e-08 |
|
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: 53.77 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKD-QTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRKDIklA 69
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlidgqdirevtldsLRRAI--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 70 LVEQETA----------AYSFADQTPAE--------------KKLLEKWH--VPLRDFhQLSGGEKLKARLAKGLSEDAD 123
Cdd:cd03253 79 VVPQDTVlfndtigyniRYGRPDATDEEvieaakaaqihdkiMRFPDGYDtiVGERGL-KLSGGEKQRVAIARAILKNPP 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 2828494 124 LLLLDEPTNHLDEKSLQFLIQQLKHY--NGTVILVSH 158
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAH 194
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
35-170 |
6.70e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 52.36 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 35 IIGKNGAGKSTLLhlihndlapaqgqilrKDIKLALVEQETAAYSFADQTPAEKKLLEKWHVPLRdFHQLSGGEKLKARL 114
Cdd:cd03227 26 ITGPNGSGKSTIL----------------DAIGLALGGAQSATRRRSGVKAGCIVAAVSAELIFT-RLQLSGGEKELSAL 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 115 AKGLSE----DADLLLLDEPTNHLDEKSLQFLIQQLKHYNG---TVILVSHDRYFLDEAATKI 170
Cdd:cd03227 89 ALILALaslkPRPLYILDEIDRGLDPRDGQALAEAILEHLVkgaQVIVITHLPELAELADKLI 151
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
17-181 |
7.01e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 53.48 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 17 QTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIH--------------------NDLAPAQGQILRKdiKLALVEQE-- 74
Cdd:COG4161 15 HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNlletpdsgqlniaghqfdfsQKPSEKAIRLLRQ--KVGMVFQQyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 75 ------------TAAYSFADQTPAE-----KKLLEKwhVPLRDFH-----QLSGGEKLKARLAKGLSEDADLLLLDEPTN 132
Cdd:COG4161 93 lwphltvmenliEAPCKVLGLSKEQarekaMKLLAR--LRLTDKAdrfplHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2828494 133 HLD-EKSLQF--LIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIEF 181
Cdd:COG4161 171 ALDpEITAQVveIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
321-468 |
7.29e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 52.99 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 321 AIIGPNGSGKTTLLNIILGQETAEGSvwvsPSANIGYLTQEVFdlpleqtpeelFENETfkaRGHVqnlmrHLGFTAA-- 398
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYALTGELP----PNSKGGAHDPKLI-----------REGEV---RAQV-----KLAFENAng 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 399 -----------------------QW--TEPIKHMSMGERVKIKL-----MAYILEEK-DVLILDEPTNHLDLPSREQ--- 444
Cdd:cd03240 83 kkytitrslailenvifchqgesNWplLDMRGRCSGGEKVLASLiirlaLAETFGSNcGILALDEPTTNLDEENIEEsla 162
|
170 180
....*....|....*....|....*.
gi 2828494 445 --LEETLSQYSGTLLAVSHDRYFLEK 468
Cdd:cd03240 163 eiIEERKSQKNFQLIVITHDEELVDA 188
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-159 |
8.31e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.94 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVKDQTVFK---HVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--LRKDIKL------- 68
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNkkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 -----ALVEQET---------------------AAYSFADQT---------------PAEKKLLEKWHVPL--------- 98
Cdd:PRK13651 81 ekvleKLVIQKTrfkkikkikeirrrvgvvfqfAEYQLFEQTiekdiifgpvsmgvsKEEAKKRAAKYIELvgldesylq 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2828494 99 RDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQLKHYN---GTVILVSHD 159
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNkqgKTIILVTHD 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-158 |
8.62e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 22 HVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRK-------------DIKLALVEQE-------TAAYS-F 80
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqemrfasttaalAAGVAIIYQElhlvpemTVAENlY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 81 ADQTPA-----EKKLLEKW--------------HVPLRDfhqLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQF 141
Cdd:PRK11288 102 LGQLPHkggivNRRLLNYEareqlehlgvdidpDTPLKY---LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQ 178
|
170 180
....*....|....*....|.
gi 2828494 142 L---IQQLKHyNGTVIL-VSH 158
Cdd:PRK11288 179 LfrvIRELRA-EGRVILyVSH 198
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
9-180 |
1.08e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.09 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYEVkDQTVFKhVNASVQQGDIIGIIGKNGAGKSTLLHLI----------------HNDLA----PAQGQILRKDIKL 68
Cdd:PRK11124 9 NCFYGA-HQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprsgtlniagnHFDFSktpsDKAIRELRRNVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 A---------------LVEQETAAYSFADQTPAE--KKLLEKWHvpLRDFH-----QLSGGEKLKARLAKGLSEDADLLL 126
Cdd:PRK11124 87 VfqqynlwphltvqqnLIEAPCRVLGLSKDQALAraEKLLERLR--LKPYAdrfplHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 127 LDEPTNHLD-EKSLQF--LIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:PRK11124 165 FDEPTAALDpEITAQIvsIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-159 |
1.17e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.07 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 22 HVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLA-------------------------------L 70
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpghqiarmgvvrtfqhvrlfremtvienlL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 71 VEQ----ETAAYSFADQTPA----EKKLLEK---W--HVPLRDFHQ-----LSGGEKLKARLAKGLSEDADLLLLDEPT- 131
Cdd:PRK11300 103 VAQhqqlKTGLFSGLLKTPAfrraESEALDRaatWleRVGLLEHANrqagnLAYGQQRRLEIARCMVTQPEILMLDEPAa 182
|
170 180 190
....*....|....*....|....*....|.
gi 2828494 132 --NHLDEKSLQFLIQQLK-HYNGTVILVSHD 159
Cdd:PRK11300 183 glNPKETKELDELIAELRnEHNVTVLLIEHD 213
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
316-466 |
1.42e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 316 HGEKVAIIGPNGSGKTTLLNIILGQ--ETAEGSVWVSPSANIGYLTQEVFDLPleqtpeelfenetfkarghvqnlmrhl 393
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARElgPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2828494 394 gftaaqwTEPIKHMSMGERVKIKLMAYILEEK-DVLILDEPTNHLDLPSREQLEETLSQYSGTLLAVSHDRYFL 466
Cdd:smart00382 54 -------VGGKKASGSGELRLRLALALARKLKpDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-165 |
1.66e-07 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 54.04 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 2 KEIVTLTNVS--YEVKDQTVFKHVNA---SVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-------------LR 63
Cdd:TIGR03269 277 EPIIKVRNVSkrYISVDRGVVKAVDNvslEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 64 KDIK------LALVEQETAAYSFAD-----------QTPAE--------------------KKLLEKWHvplrdfHQLSG 106
Cdd:TIGR03269 357 PDGRgrakryIGILHQEYDLYPHRTvldnlteaiglELPDElarmkavitlkmvgfdeekaEEILDKYP------DELSE 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 107 GEKLKARLAKGLSEDADLLLLDEPTNHLDE----KSLQFLIQQLKHYNGTVILVSHDRYFLDE 165
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPitkvDVTHSILKAREEMEQTFIIVSHDMDFVLD 493
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
292-349 |
1.89e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 53.16 E-value: 1.89e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 292 LEVQNVTKAF----GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWV 349
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPtSGSVLV 64
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-159 |
2.14e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.09 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 18 TVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIH--NDLAPAQGQILRKDIKlALVEQETAAY----------SFA---- 81
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAglDDGSSGEVSLVGQPLH-QMDEEARAKLrakhvgfvfqSFMlipt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 82 ------DQTPA-------------EKKLLEKWHVPLRDFH---QLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD---- 135
Cdd:PRK10584 103 lnalenVELPAllrgessrqsrngAKALLEQLGLGKRLDHlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDrqtg 182
|
170 180
....*....|....*....|....
gi 2828494 136 EKSLQFLIQQLKHYNGTVILVSHD 159
Cdd:PRK10584 183 DKIADLLFSLNREHGTTLILVTHD 206
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
313-465 |
2.15e-07 |
|
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: 52.03 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 313 TIQHGEKVAIIGPNGSGKTTLLNIILGQETAEGSVWVSPSANIGYLTQEVfdlpleqtpeelfeneTFKARGHVQNLMRH 392
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYI----------------KADYEGTVRDLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 393 L---GFTAAQW-TEPIKHMSM-------------GERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQY--- 452
Cdd:cd03237 85 ItkdFYTHPYFkTEIAKPLQIeqildrevpelsgGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaen 164
|
170
....*....|....
gi 2828494 453 -SGTLLAVSHDRYF 465
Cdd:cd03237 165 nEKTAFVVEHDIIM 178
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-206 |
2.27e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.51 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYE----------VKDQTVFKHVNA----------SVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQ 60
Cdd:PRK13546 1 MNVSVNIKNVTKEyriyrtnkerMKDALIPKHKNKtffalddislKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 61 ILRKD------IKLALVEQETAAYSFADQ------TPAEKKLL-----------EKWHVPLRDFhqlSGGEKLKARLAKG 117
Cdd:PRK13546 81 VDRNGevsviaISAGLSGQLTGIENIEFKmlcmgfKRKEIKAMtpkiiefselgEFIYQPVKKY---SSGMRAKLGFSIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 118 LSEDADLLLLDEPTNHLDE----KSLQfLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKG------NYSG 187
Cdd:PRK13546 158 ITVNPDILVIDEALSVGDQtfaqKCLD-KIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGElddvlpKYEA 236
|
250
....*....|....*....
gi 2828494 188 YMKFREKKRLTQQREYEKQ 206
Cdd:PRK13546 237 FLNDFKKKSKAEQKEFRNK 255
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
272-468 |
2.46e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 53.29 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 272 TPEytVRFSIDTTHKTGKRFLEVQNVTKAFGERTL--FKNANFTIQHGEKVAIIGPNGSGKTTLLNIIlgqeTAEgsvWv 349
Cdd:PRK11160 321 KPE--VTFPTTSTAAADQVSLTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL----TRA---W- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 350 spSANIGYLTqeVFDLPLEQTPEE-LFENETF-KARGHV------QNL---------------MRHLGFTA--------A 398
Cdd:PRK11160 391 --DPQQGEIL--LNGQPIADYSEAaLRQAISVvSQRVHLfsatlrDNLllaapnasdealievLQQVGLEKlleddkglN 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 399 QWT-EPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYSG--TLLAVSHDRYFLEK 468
Cdd:PRK11160 467 AWLgEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQnkTVLMITHRLTGLEQ 539
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-434 |
2.47e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.59 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--LRKDIK-------------- 67
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevLGGDMAdarhrravcpriay 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 68 ------------LALVE------------------------QETAAYSFADQtPAEKkllekwhvplrdfhqLSGGEKLK 111
Cdd:NF033858 81 mpqglgknlyptLSVFEnldffgrlfgqdaaerrrridellRATGLAPFADR-PAGK---------------LSGGMKQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 112 ARLAKGLSEDADLLLLDEPTNHLDEKS-LQF--LIQQLKHYNG--TVILvshdryfldeaATkiwsledqtliefkgnys 186
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTGVDPLSrRQFweLIDRIRAERPgmSVLV-----------AT------------------ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 187 GYMKfrekkrltqqreyekqqkmveriEAQ-------MNG---LASWSE---KAHAQSTKKEgfkeyhrvkakrtDAQIk 253
Cdd:NF033858 196 AYME-----------------------EAErfdwlvaMDAgrvLATGTPaelLARTGADTLE-------------AAFI- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 254 skqkRLEKELEKAKAEPVT-PEYTVRFSIDTThktgkrfLEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTT 332
Cdd:NF033858 239 ----ALLPEEKRRGHQPVViPPRPADDDDEPA-------IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKST 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 333 LLNIILG-QETAEGSVW-----VSPS-----ANIGYLTQEvFDLPLEQTPEE-------LFENETFKARGHVQNLMRHLG 394
Cdd:NF033858 308 TMKMLTGlLPASEGEAWlfgqpVDAGdiatrRRVGYMSQA-FSLYGELTVRQnlelharLFHLPAAEIAARVAEMLERFD 386
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2828494 395 FTAAQWTEPIKhMSMGERVKIKLMAYILEEKDVLILDEPT 434
Cdd:NF033858 387 LADVADALPDS-LPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-157 |
2.81e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.19 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 17 QTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI----------LRKDIKLALVEQETAAYSF------ 80
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrqaLQKNLVAYVPQSEEVDWSFpvlved 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 81 -----------------------ADQTPAEKKLLEKWHvplRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEK 137
Cdd:PRK15056 100 vvmmgryghmgwlrrakkrdrqiVTAALARVDMVEFRH---RQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180
....*....|....*....|..
gi 2828494 138 SLQFLIQQLKHY--NGTVILVS 157
Cdd:PRK15056 177 TEARIISLLRELrdEGKTMLVS 198
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
292-462 |
3.37e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 53.19 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAF--GERTL--FKNANFTIQHGEKVAIIGPNGSGKTTLLNII--LGQETAeGSVWVSpsanigylTQEVFDL 365
Cdd:PRK10535 5 LELKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcLDKPTS-GTYRVA--------GQDVATL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 366 ---PLEQTPEELFeNETFKaRGHvqnLMRHLgfTAAQWTE-P------------------IKHMSMGERV---------- 413
Cdd:PRK10535 76 dadALAQLRREHF-GFIFQ-RYH---LLSHL--TAAQNVEvPavyaglerkqrllraqelLQRLGLEDRVeyqpsqlsgg 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2828494 414 ---KIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYSG---TLLAVSHD 462
Cdd:PRK10535 149 qqqRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrghTVIIVTHD 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-159 |
3.79e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 23 VNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------------------------RKD---IKLALVEQE 74
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYldgkpidirsprdairagimlcpedRKAegiIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 75 TAAYSFADQTPAEKKLLEKWHVPLRDFH----------------QLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD--E 136
Cdd:PRK11288 352 INISARRHHLRAGCLINNRWEAENADRFirslniktpsreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDvgA 431
|
170 180
....*....|....*....|....
gi 2828494 137 KSLQF-LIQQLKHYNGTVILVSHD 159
Cdd:PRK11288 432 KHEIYnVIYELAAQGVAVLFVSSD 455
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
293-463 |
3.82e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 52.66 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 293 EVQNVTKAF-GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNII-LGQETAEGSVWV-----------SPSANIGYLT 359
Cdd:PRK13657 336 EFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqRVFDPQSGRILIdgtdirtvtraSLRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 360 QE--VFDLPLEQ---------TPEELFEnETFKARGHVQNLMRHLGFtAAQWTEPIKHMSMGERVKIKLMAYILEEKDVL 428
Cdd:PRK13657 416 QDagLFNRSIEDnirvgrpdaTDEEMRA-AAERAQAHDFIERKPDGY-DTVVGERGRQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190
....*....|....*....|....*....|....*
gi 2828494 429 ILDEPTNHLDLPSREQLEETLSqysgtllAVSHDR 463
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALD-------ELMKGR 521
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
292-461 |
3.92e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 51.31 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNII-----LGQE-TAEGSV------WVSPSANIGYLT 359
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEvTITGSIvynghnIYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 360 QE---VFDLPlEQTPEELFENETFKAR-----------GHVQNLMRhlgfTAAQWTEPIKH-------MSMGERVKIKLM 418
Cdd:PRK14239 86 KEigmVFQQP-NPFPMSIYENVVYGLRlkgikdkqvldEAVEKSLK----GASIWDEVKDRlhdsalgLSGGQQQRVCIA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 419 AYILEEKDVLILDEPTNHLDLPSREQLEETL----SQYsgTLLAVSH 461
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLlglkDDY--TMLLVTR 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
306-448 |
4.61e-07 |
|
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: 52.99 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 306 LFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ-ETAEGSvwVSPSANIGYLTQEVFDLPLEQTPEELF--ENETFKA 382
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGElEPSEGK--IKHSGRISFSPQTSWIMPGTIKDNIIFglSYDEYRY 518
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2828494 383 RGHVQ--NLMRHLGFTAAQWTEPIKH----MSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEET 448
Cdd:TIGR01271 519 TSVIKacQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFES 590
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
302-438 |
5.17e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 50.32 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 302 GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA---EGSVWVSPSAN-------IGYLTQEVFDLPlEQTP 371
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgviTGEILINGRPLdknfqrsTGYVEQQDVHSP-NLTV 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 372 EELFEnetFKArghvqnLMRHLGftaaqwTEPIKHMSMGervkIKLMAyileEKDVLILDEPTNHLD 438
Cdd:cd03232 97 REALR---FSA------LLRGLS------VEQRKRLTIG----VELAA----KPSILFLDEPTSGLD 140
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
306-448 |
5.24e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 51.40 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 306 LFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ-ETAEGSvwVSPSANIGYLTQEVFDLpleqtPEELFENETFkarG 384
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGElEPSEGK--IKHSGRISFSSQFSWIM-----PGTIKENIIF---G 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 385 HVQNLMRHLG-FTAAQWTEPIKH---------------MSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEET 448
Cdd:cd03291 122 VSYDEYRYKSvVKACQLEEDITKfpekdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFES 201
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
295-438 |
5.59e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 295 QNVTKAFGE---RTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ-ETAEGSVWVSPSanIGYLTQEVFDLPLEQT 370
Cdd:PTZ00243 661 KMKTDDFFElepKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQfEISEGRVWAERS--IAYVPQQAWIMNATVR 738
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2828494 371 PEELFENETFKARghVQNLMR--HLGFTAAQWT--------EPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLD 438
Cdd:PTZ00243 739 GNILFFDEEDAAR--LADAVRvsQLEADLAQLGggleteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
292-461 |
6.14e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 50.81 E-value: 6.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLL---N----IILGQETaEGSVWV------SPSAN---- 354
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNrmndLIPGARV-EGEILLdgediyDPDVDvvel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 355 ---IGYltqeVFdlpleQTPEEL----FENETFKARGH-----------VQNLMRHlgftAAQWTEpikhmsmgerVKIK 416
Cdd:COG1117 91 rrrVGM----VF-----QKPNPFpksiYDNVAYGLRLHgikskseldeiVEESLRK----AALWDE----------VKDR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2828494 417 LMAYILE-----------------EKDVLILDEPTNHLDLPSREQLEETL----SQYsgTLLAVSH 461
Cdd:COG1117 148 LKKSALGlsggqqqrlciaralavEPEVLLMDEPTSALDPISTAKIEELIlelkKDY--TIVIVTH 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
292-361 |
6.23e-07 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 51.64 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVqNVTKAFGERTLfkNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAE-------GSVWVSPSAN---------I 355
Cdd:COG4148 3 LEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDsgrirlgGEVLQDSARGiflpphrrrI 79
|
....*.
gi 2828494 356 GYLTQE 361
Cdd:COG4148 80 GYVFQE 85
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
292-480 |
9.14e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 50.26 E-value: 9.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETA-EGSVWVSPSANIGYLTQEVFDLPLEQT 370
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRAtSGRIVFDGKDITDWQTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 371 PeelfENETFKARGHVQNLMRHLGFTA--AQWTEPIKH------------------MSMGERVKIKLMAYILEEKDVLIL 430
Cdd:PRK11614 86 P----EGRRVFSRMTVEENLAMGGFFAerDQFQERIKWvyelfprlherriqragtMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2828494 431 DEPTNHLDLPSREQLEETLSQYSGTLLAVshdrYFLEKTTNSKLVISNNG 480
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTI----FLVEQNANQALKLADRG 207
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
274-465 |
9.79e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.51 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 274 EYTVRFSIDTTHKTGKRfLEVQNVTKAFGERTL-FKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVW--- 348
Cdd:PRK10522 306 PYKAEFPRPQAFPDWQT-LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGlYQPQSGEILldg 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 349 --VSPSANIGY--LTQEVF-DLPLEQtpeELFENETFKARGH-VQNLMRHLGF----TAAQWTEPIKHMSMGERVKIKLM 418
Cdd:PRK10522 385 kpVTAEQPEDYrkLFSAVFtDFHLFD---QLLGPEGKPANPAlVEKWLERLKMahklELEDGRISNLKLSKGQKKRLALL 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2828494 419 AYILEEKDVLILDEPTNHLDLPSR----EQLEETLSQYSGTLLAVSH-DRYF 465
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDPHFRrefyQVLLPLLQEMGKTIFAISHdDHYF 513
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
295-478 |
9.92e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.87 E-value: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 295 QNVTKAF-GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQE-TAEGSVWVS-------PSANIGYLTQEV--- 362
Cdd:PRK10908 5 EHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIErPSAGKIWFSghditrlKNREVPFLRRQIgmi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 363 ---FDLPLEQT-------PEELFENETFKARGHVQNLMRHLGFTAAQWTEPIKhMSMGERVKIKLMAYILEEKDVLILDE 432
Cdd:PRK10908 85 fqdHHLLMDRTvydnvaiPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2828494 433 PTNHLDLPSRE---QLEETLSQYSGTLLAVSHDRYFLEKTTNSKLVISN 478
Cdd:PRK10908 164 PTGNLDDALSEgilRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
301-461 |
1.01e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.50 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 301 FGERTLFkNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ-ETAEGSVWVSPSANIGYLTQE-----------VFDLPLE 368
Cdd:PRK13643 17 FASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlQPTEGKVTVGDIVVSSTSKQKeikpvrkkvgvVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 369 QTPEEL------FENETF-----KARGHVQNLMRHLGFTAAQWTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHL 437
Cdd:PRK13643 96 QLFEETvlkdvaFGPQNFgipkeKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180
....*....|....*....|....*..
gi 2828494 438 DLPSR---EQLEETLSQYSGTLLAVSH 461
Cdd:PRK13643 176 DPKARiemMQLFESIHQSGQTVVLVTH 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
98-462 |
1.10e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.24 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 98 LRDF-HQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDeKSLQFLIQQLkhyngtvilvshdryfldeaatkiwsledq 176
Cdd:PRK15134 150 LTDYpHQLSGGERQRVMIAMALLTRPELLIADEPTTALD-VSVQAQILQL------------------------------ 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 177 tLIEFKGNYSGYMKFrekkrLTQQREYEKqqKMVERIEAQMNGLAswsekahaqstkkegfkeyhrVKAKRTDAQIKSKQ 256
Cdd:PRK15134 199 -LRELQQELNMGLLF-----ITHNLSIVR--KLADRVAVMQNGRC---------------------VEQNRAATLFSAPT 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 257 KRLEKELekAKAEPVTpeYTVRFSIDTThktgkRFLEVQNVTKAF-----------GERTLFKNANFTIQHGEKVAIIGP 325
Cdd:PRK15134 250 HPYTQKL--LNSEPSG--DPVPLPEPAS-----PLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 326 NGSGKTT----LLNIIlgqeTAEGSVWVSPSANIGYLTQEVfdLPLEQTPEELFE--NETFKARGHVQNLM------RHL 393
Cdd:PRK15134 321 SGSGKSTtglaLLRLI----NSQGEIWFDGQPLHNLNRRQL--LPVRHRIQVVFQdpNSSLNPRLNVLQIIeeglrvHQP 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 394 GFTAAQWTEP-IKHM-----------------SMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQ---LEETLSQ- 451
Cdd:PRK15134 395 TLSAAQREQQvIAVMeevgldpetrhrypaefSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQilaLLKSLQQk 474
|
410
....*....|.
gi 2828494 452 YSGTLLAVSHD 462
Cdd:PRK15134 475 HQLAYLFISHD 485
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-158 |
1.15e-06 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 49.80 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRKdiKLALVEQE 74
Cdd:cd03244 9 SLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIlidgvdiskiglhdLRS--RISIIPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 75 TAAYS---------FADQTPAE-KKLLEKwhVPLRDFHQ----------------LSGGEKLKARLAKGLSEDADLLLLD 128
Cdd:cd03244 87 PVLFSgtirsnldpFGEYSDEElWQALER--VGLKEFVEslpggldtvveeggenLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190
....*....|....*....|....*....|....
gi 2828494 129 EPTNHLD---EKSLQFLIQQ-LKHYngTVILVSH 158
Cdd:cd03244 165 EATASVDpetDALIQKTIREaFKDC--TVLTIAH 196
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
292-461 |
1.17e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.91 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNI------------ILGQETAEG-SVWVSPSANIGYL 358
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGEVYLDGqDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQEVFDLPLEQTPEELFENETF--------KARGHVQNLMRHLGFTAAQWTE-------PIKHMSMGERVKIKLMAYILE 423
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALglklnrlvKSKKELQERVRWALEKAQLWDEvkdrldaPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2828494 424 EKDVLILDEPTNHLDLPSREQLEETLSQYSG--TLLAVSH 461
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
292-438 |
1.20e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.89 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEGSVWVSPS------------ANIGYL 358
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGiVPRDAGNIIIDDEdisllplhararRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQE--------VF-----------DLPLEQTPEELFE-NETFkargHVQNLMRHLGftaaqwtepiKHMSMGERVKIKLM 418
Cdd:PRK10895 84 PQEasifrrlsVYdnlmavlqirdDLSAEQREDRANElMEEF----HIEHLRDSMG----------QSLSGGERRRVEIA 149
|
170 180
....*....|....*....|
gi 2828494 419 AYILEEKDVLILDEPTNHLD 438
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVD 169
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-168 |
1.27e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.09 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVKDQTVFKHVNA---SVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LR 63
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGvsfSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVkidgelltaenvwnLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 64 KDIKL-----------ALVEQETaAYSFADQTPAEKKLLEK-----WHVPLRDFH-----QLSGGEKLKARLAKGLSEDA 122
Cdd:PRK13642 81 RKIGMvfqnpdnqfvgATVEDDV-AFGMENQGIPREEMIKRvdealLAVNMLDFKtrepaRLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2828494 123 DLLLLDEPTNHLD---EKSLQFLIQQLK-HYNGTVILVSHDryfLDEAAT 168
Cdd:PRK13642 160 EIIILDESTSMLDptgRQEIMRVIHEIKeKYQLTVLSITHD---LDEAAS 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
292-484 |
1.33e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.97 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNII-LGQETAEGSVWVSpSANIGYLTQ-----EVFD- 364
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInFLEKPSEGSIVVN-GQTINLVRDkdgqlKVADk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 365 --LPLEQT------------------------PEELFENETFKARGHVQNLMRHLGFTAAQWTEPIKHMSMGERVKIKLM 418
Cdd:PRK10619 85 nqLRLLRTrltmvfqhfnlwshmtvlenvmeaPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2828494 419 AYILEEKDVLILDEPTNHLD---LPSREQLEETLSQYSGTLLAVSHDRYFLEKTTNSKLVISNNGIEKQ 484
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-180 |
1.38e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.05 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 2 KEIVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHL------IHNDLAPAQGQIL------------- 62
Cdd:PRK14246 8 EDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLyfgkdifqidaik 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 63 -RKDIKLALVEQ---------ETAAYSFADQTPAEKKLLEK-----------WHVPLRDFH----QLSGGEKLKARLAKG 117
Cdd:PRK14246 88 lRKEVGMVFQQPnpfphlsiyDNIAYPLKSHGIKEKREIKKiveeclrkvglWKEVYDRLNspasQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2828494 118 LSEDADLLLLDEPTNHLD---EKSLQFLIQQLKHyNGTVILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDivnSQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-158 |
1.49e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 49.65 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVKDQTVF-------KHVNASVQQGDIIGIIGKNGAGKSTLLHLIH--NDLAP---AQGQIL--RKDI 66
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYygdkqalKDINLDIPENKVTALIGPSGCGKSTLLRCLNrmNDLIPgarVEGEILldGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 67 ------------KLALVEQ----------ETAAYSFADQTPAEKKLLEK-----------W-HVplRD-FHQ----LSGG 107
Cdd:COG1117 81 ydpdvdvvelrrRVGMVFQkpnpfpksiyDNVAYGLRLHGIKSKSELDEiveeslrkaalWdEV--KDrLKKsalgLSGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 108 EKLkaRL--AKGLSEDADLLLLDEPTNHLDEKSLQF---LIQQLK-HYngTVILVSH 158
Cdd:COG1117 159 QQQ--RLciARALAVEPEVLLMDEPTSALDPISTAKieeLILELKkDY--TIVIVTH 211
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
292-499 |
1.50e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.85 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGE--RTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIIL------GQETAEGSVWVSPSAN-----IGYL 358
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQIDGVSWNSVPLQkwrkaFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 359 TQEVFDL---------PLEQ-TPEELFE-NETFKARGHVQNLMRHLGFTAAQWTEPIKHmsmGERVKIKLMAYILEEKDV 427
Cdd:cd03289 83 PQKVFIFsgtfrknldPYGKwSDEEIWKvAEEVGLKSVIEQFPGQLDFVLVDGGCVLSH---GHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 428 LILDEPTNHLDLPSREQLEETLSQ-YSGTLLAVSHDRYFLEKTTNSKLVISNNGIeKQLNDVPSERNEREELR 499
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQaFADCTVILSEHRIEAMLECQRFLVIEENKV-RQYDSIQKLLNEKSHFK 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-179 |
1.65e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.12 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 23 VNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDI----------------KLALVEQETAAYSFAD---- 82
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsstskqkeikpvrkKVGVVFQFPESQLFEEtvlk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 83 ------------QTPAEKKLLEKWHVP--LRDF-----HQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKS---LQ 140
Cdd:PRK13643 105 dvafgpqnfgipKEKAEKIAAEKLEMVglADEFwekspFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKArieMM 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 2828494 141 FLIQQLKHYNGTVILVSHDRYFLDEAATKIWSLEDQTLI 179
Cdd:PRK13643 185 QLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
291-445 |
1.69e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 291 FLEVQNVTKAF-GERTLfKNANFTIQHGEKVAIIGPNGSGKTTLLNI-------------ILGQETAEGSVWVSPSANIG 356
Cdd:PRK11288 4 YLSFDGIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKIlsgnyqpdagsilIDGQEMRFASTTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 357 YLTQEVFDLP---------LEQTPEEL-FENETfKARGHVQNLMRHLGFTAAQWTePIKHMSMGERVKIKLMAYILEEKD 426
Cdd:PRK11288 83 IIYQELHLVPemtvaenlyLGQLPHKGgIVNRR-LLNYEAREQLEHLGVDIDPDT-PLKYLSIGQRQMVEIAKALARNAR 160
|
170
....*....|....*....
gi 2828494 427 VLILDEPTNHLDLPSREQL 445
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQL 179
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-175 |
1.88e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.10 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 23 VNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-----------------LRKDIKLALVEQE----------- 74
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditrlknrevpfLRRQIGMIFQDHHllmdrtvydnv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 75 -----TAAYSFADQTPAEKKLLEKwhVPLRDFH-----QLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQ 144
Cdd:PRK10908 101 aipliIAGASGDDIRRRVSAALDK--VGLLDKAknfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR 178
|
170 180 190
....*....|....*....|....*....|....
gi 2828494 145 QLKHYNG---TVILVSHDRYFLDEAATKIWSLED 175
Cdd:PRK10908 179 LFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
293-461 |
2.02e-06 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 49.08 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 293 EVQNVTKAFGER---TLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIIL-------------GQETAEGSV-WVspSANI 355
Cdd:cd03249 2 EFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfydptsgeilldGVDIRDLNLrWL--RSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 356 GYLTQE--VFD--------LPLEQTPEELFENETFKARGH--VQNLMR----HLGFTAAQwtepikhMSMGERVKIKLMA 419
Cdd:cd03249 80 GLVSQEpvLFDgtiaenirYGKPDATDEEVEEAAKKANIHdfIMSLPDgydtLVGERGSQ-------LSGGQKQRIAIAR 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2828494 420 YILEEKDVLILDEPTNHLDLPSREQLEETLSQYSG--TLLAVSH 461
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESEKLVQEALDRAMKgrTTIVIAH 196
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
292-460 |
2.38e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 49.24 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLL----NIILGQETAEGSVWV----------------SP 351
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIELlgrtvqregrlardirKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 352 SANIGYLTQEvFDLPLEQTpeeLFENETFKARGHV---QNLMRHlgFTAAQWTEPIKH----------------MSMGER 412
Cdd:PRK09984 85 RANTGYIFQQ-FNLVNRLS---VLENVLIGALGSTpfwRTCFSW--FTREQKQRALQAltrvgmvhfahqrvstLSGGQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2828494 413 VKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETL---SQYSGTLLAVS 460
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLrdiNQNDGITVVVT 209
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-167 |
3.11e-06 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 49.33 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 23 VNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL---------RKDI-------KLALVEQETA---------- 76
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsARGIflpphrrRIGYVFQEARlfphlsvrgn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 77 ---AYSFADQTPAEKK------------LLEKWhvPlrdfHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKS--- 138
Cdd:COG4148 98 llyGRKRAPRAERRISfdevvellgighLLDRR--P----ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkae 171
|
170 180 190
....*....|....*....|....*....|...
gi 2828494 139 ----LQFLIQQLkhyNGTVILVSHDryfLDEAA 167
Cdd:COG4148 172 ilpyLERLRDEL---DIPILYVSHS---LDEVA 198
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
292-462 |
3.27e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 48.27 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTL----FKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSVW--------VSPSA----- 353
Cdd:PRK11629 6 LQCDNLCKRYQEGSVqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTpTSGDVIfngqpmskLSSAAkaelr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 354 --NIGYLTQEVFDLP----LEQTPEELFENEtfKARGHVQNLMRHLgFTAAQWTEPIKH----MSMGERVKIKLMAYILE 423
Cdd:PRK11629 86 nqKLGFIYQFHHLLPdftaLENVAMPLLIGK--KKPAEINSRALEM-LAAVGLEHRANHrpseLSGGERQRVAIARALVN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2828494 424 EKDVLILDEPTNHLDLPSRE---QLEETLSQYSGT-LLAVSHD 462
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADsifQLLGELNRLQGTaFLVVTHD 205
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-158 |
3.38e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.62 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIH--NDLAP---AQGQI-------------- 61
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIvynghniysprtdt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 62 --LRKDIklALVEQ----------ETAAYSFADQTPAEKKLLEK-----------WHVPLRDFHQ----LSGGEKLKARL 114
Cdd:PRK14239 82 vdLRKEI--GMVFQqpnpfpmsiyENVVYGLRLKGIKDKQVLDEavekslkgasiWDEVKDRLHDsalgLSGGQQQRVCI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 115 AKGLSEDADLLLLDEPTNHLDEKS---LQFLIQQLKHyNGTVILVSH 158
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISagkIEETLLGLKD-DYTMLLVTR 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
286-339 |
3.98e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.45 E-value: 3.98e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2828494 286 KTGKRFLEVQNVTKAFG--ERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG 339
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTG 57
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
292-445 |
4.73e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 48.25 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERT-LF--------KNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ-ETAEGSVWV------------ 349
Cdd:PRK15112 5 LEVRNLSKTFRYRTgWFrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMiEPTSGELLIddhplhfgdysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 350 ------------SPSANIGYLTQEVFDLPL----EQTPEELfENETFKARGHVQNLMRHLGFtaaqwtepIKHM-SMGER 412
Cdd:PRK15112 85 rsqrirmifqdpSTSLNPRQRISQILDFPLrlntDLEPEQR-EKQIIETLRQVGLLPDHASY--------YPHMlAPGQK 155
|
170 180 190
....*....|....*....|....*....|....
gi 2828494 413 VKIKLM-AYILEEKdVLILDEPTNHLDLPSREQL 445
Cdd:PRK15112 156 QRLGLArALILRPK-VIIADEALASLDMSMRSQL 188
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
10-174 |
5.00e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.54 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 10 VSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIlRKDIKLALVEQETAAYSFADQTPAEKK 89
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI-QIDGKTATRGDRSRFMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 90 ---LLEKWH--------------------VPLRDF-----HQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQF 141
Cdd:PRK13543 96 dlsTLENLHflcglhgrrakqmpgsalaiVGLAGYedtlvRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITL 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 2828494 142 LIQQLK---HYNGTVILVSHDRYFLDEAATKIWSLE 174
Cdd:PRK13543 176 VNRMISahlRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
8-261 |
5.98e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 8 TNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDL---------------APAQGQI----LRKDIkL 68
Cdd:PTZ00243 664 TDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFeisegrvwaersiayVPQQAWImnatVRGNI-L 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 ALVEQETAaySFAD-----QTPAEKKLL---------EKWHvplrdfhQLSGGEKLKARLAKGLSEDADLLLLDEPTNHL 134
Cdd:PTZ00243 743 FFDEEDAA--RLADavrvsQLEADLAQLgggleteigEKGV-------NLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 135 DEKSLQFLIQQ--LKHYNG-TVILVSHDRYFLDEaATKIWSLEDQTlIEFKGNYSGYMKFREKKRLTQQREYEKQQK--M 209
Cdd:PTZ00243 814 DAHVGERVVEEcfLGALAGkTRVLATHQVHVVPR-ADYVVALGDGR-VEFSGSSADFMRTSLYATLAAELKENKDSKegD 891
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2828494 210 VERIEAQMN---GLASWSEKAHAQSTKKEGfkeyhRVKAKRTDAQIKSKQKRLEK 261
Cdd:PTZ00243 892 ADAEVAEVDaapGGAVDHEPPVAKQEGNAE-----GGDGAALDAAAGRLMTREEK 941
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
292-438 |
6.66e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.76 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTL-FKNANFTIQHGEKVAIIGPNGSGKTTL---LNIILgqETAEGSVWVSpSANIGYLTQE------ 361
Cdd:PRK13639 2 LETRDLKYSYPDGTEaLKGINFKAEKGEMVALLGPNGAGKSTLflhFNGIL--KPTSGEVLIK-GEPIKYDKKSllevrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 362 ----VFDLPLEQ----TPEE----------LFENETFKargHVQNLMRHLGFTAAQWTEPiKHMSMGERVKIKLMAYILE 423
Cdd:PRK13639 79 tvgiVFQNPDDQlfapTVEEdvafgplnlgLSKEEVEK---RVKEALKAVGMEGFENKPP-HHLSGGQKKRVAIAGILAM 154
|
170
....*....|....*
gi 2828494 424 EKDVLILDEPTNHLD 438
Cdd:PRK13639 155 KPEIIVLDEPTSGLD 169
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
292-339 |
7.67e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 7.67e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG 339
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
19-170 |
7.81e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 48.16 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 19 VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL----------RKDIKLALVEQETAAY---------S 79
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgtdvsrlhARDRKVGFVFQHYALFrhmtvfdniA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 FA------DQTPAEK-------KLLEKW---HVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD---EKSLQ 140
Cdd:PRK10851 97 FGltvlprRERPNAAaikakvtQLLEMVqlaHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDaqvRKELR 176
|
170 180 190
....*....|....*....|....*....|.
gi 2828494 141 FLIQQL-KHYNGTVILVSHDRYFLDEAATKI 170
Cdd:PRK10851 177 RWLRQLhEELKFTSVFVTHDQEEAMEVADRV 207
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-164 |
7.98e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.33 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 2 KEIVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLI--HNDLAPAQGQILRKDIKLALVEQETAAYS 79
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 ---FADQTPAE-----------------KKLLEKWHVPLRDFHQL-----------------------SGGEKLKARLAK 116
Cdd:CHL00131 85 gifLAFQYPIEipgvsnadflrlaynskRKFQGLPELDPLEFLEIineklklvgmdpsflsrnvnegfSGGEKKRNEILQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2828494 117 GLSEDADLLLLDEPTNHLDEKSLQFL---IQQLKHYNGTVILVSHDRYFLD 164
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIaegINKLMTSENSIILITHYQRLLD 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
292-462 |
1.03e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.08 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLL------NIILGQETAEGSVW----------VSPSA-- 353
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIPGFRVEGKVTfhgknlyapdVDPVEvr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 354 -NIGYltqeVFDLPlEQTPEELFENETFKAR-----GHVQNLMRHLGFTAAQWTEpIK--------HMSMGERVKIKLMA 419
Cdd:PRK14243 91 rRIGM----VFQKP-NPFPKSIYDNIAYGARingykGDMDELVERSLRQAALWDE-VKdklkqsglSLSGGQQQRLCIAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 420 YILEEKDVLILDEPTNHLDLPSREQLEETL----SQYsgTLLAVSHD 462
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMhelkEQY--TIIIVTHN 209
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-159 |
1.14e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 21 KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------------------------RKDIKLAL---VE 72
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTldghevvtrspqdglangivyisedRKRDGLVLgmsVK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 73 QE---TAAYSFADQTPAEKKLLEKWHV-----------PLRD--FHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD- 135
Cdd:PRK10762 349 ENmslTALRYFSRAGGSLKHADEQQAVsdfirlfniktPSMEqaIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDv 428
|
170 180
....*....|....*....|....*.
gi 2828494 136 --EKSLQFLIQQLKHYNGTVILVSHD 159
Cdd:PRK10762 429 gaKKEIYQLINQFKAEGLSIILVSSE 454
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-131 |
1.17e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.09 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 13 EVKD---QTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-----------RKDIK--LALVEQETA 76
Cdd:COG1129 258 EVEGlsvGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvrirspRDAIRagIAYVPEDRK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 77 AYS-FADQT---------------------PAEKKLLEKWhvpLRDFH-----------QLSGGEKLKARLAKGLSEDAD 123
Cdd:COG1129 338 GEGlVLDLSirenitlasldrlsrgglldrRRERALAEEY---IKRLRiktpspeqpvgNLSGGNQQKVVLAKWLATDPK 414
|
....*...
gi 2828494 124 LLLLDEPT 131
Cdd:COG1129 415 VLILDEPT 422
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
313-442 |
1.46e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 313 TIQHGEKVAIIGPNGSGKTTLLNII-------LGQETAEGSvW-----------------------VSPSANIGYLTQ-- 360
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILsgelipnLGDYEEEPS-WdevlkrfrgtelqnyfkklyngeIKVVHKPQYVDLip 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 361 EVF-----DLpLEQTPEelfenetfkaRGHVQNLMRHLGFTAAqWTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTN 435
Cdd:PRK13409 174 KVFkgkvrEL-LKKVDE----------RGKLDEVVERLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
....*..
gi 2828494 436 HLDLPSR 442
Cdd:PRK13409 242 YLDIRQR 248
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-158 |
2.43e-05 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 45.48 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 19 VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RKDI----------KLALVEQETAAYS------- 79
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidGIDIstipledlrsSLTIIPQDPTLFSgtirsnl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 --FADQTpaEKKLLEKWHVPlRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSlQFLIQQLKH---YNGTVI 154
Cdd:cd03369 103 dpFDEYS--DEEIYGALRVS-EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT-DALIQKTIReefTNSTIL 178
|
....
gi 2828494 155 LVSH 158
Cdd:cd03369 179 TIAH 182
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-180 |
2.60e-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: 47.04 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 19 VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRKDI----------------KL 68
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIllngfslkdidrhtLRQFInylpqepyifsgsileNL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 69 AL-----VEQET--AAYSFADQTPAEKKLLEKWHVPL-RDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQ 140
Cdd:TIGR01193 569 LLgakenVSQDEiwAACEIAEIKDDIENMPLGYQTELsEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEK 648
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2828494 141 FLIQQLKHYN-GTVILVSHdRYFLDEAATKIWSLEDQTLIE 180
Cdd:TIGR01193 649 KIVNNLLNLQdKTIIFVAH-RLSVAKQSDKIIVLDHGKIIE 688
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
292-462 |
2.78e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 46.13 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERT-LFKNANFTIQHGEKVAIIGPNGSGKTTL---LN----------IILGQETAE-----------GS 346
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLalhLNgllrpqkgkvLVSGIDTGDfsklqgirklvGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 347 VWVSPSAN-IGYLTQEvfDLPLeqTPEELFENETfKARGHVQNLMRHLGFTAAQWTEPiKHMSMGERVKIKLMAYILEEK 425
Cdd:PRK13644 82 VFQNPETQfVGRTVEE--DLAF--GPENLCLPPI-EIRKRVDRALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2828494 426 DVLILDEPTNHLDLPSREQLEET---LSQYSGTLLAVSHD 462
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERikkLHEKGKTIVYITHN 195
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
309-462 |
3.83e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 45.59 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 309 NANFTIQHGEKVAIIGPNGSGKTTLL--------------NIILGQETAEGSvwvspSANIGYLTQEV---FDLPLEQtp 371
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMqhfnallkpssgtiTIAGYHITPETG-----NKNLKKLRKKVslvFQFPEAQ-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 372 eeLFENETFKargHVQNLMRHLGFT-------AAQW-------TEPIKH----MSMGE--RVKIK-LMAYileEKDVLIL 430
Cdd:PRK13641 98 --LFENTVLK---DVEFGPKNFGFSedeakekALKWlkkvglsEDLISKspfeLSGGQmrRVAIAgVMAY---EPEILCL 169
|
170 180 190
....*....|....*....|....*....|....*
gi 2828494 431 DEPTNHLDLPSREQLEETLSQYSG---TLLAVSHD 462
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHN 204
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-158 |
3.91e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.00 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 3 EIVTLTNVSYevkdqtvfkhvnaSVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIK--------------- 67
Cdd:PRK13631 38 ELVALNNISY-------------TFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYigdkknnhelitnpy 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 68 -------------LALVEQETAAYSFAD--------------QTPAEKKLLEKWHVPL---------RDFHQLSGGEKLK 111
Cdd:PRK13631 105 skkiknfkelrrrVSMVFQFPEYQLFKDtiekdimfgpvalgVKKSEAKKLAKFYLNKmglddsyleRSPFGLSGGQKRR 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2828494 112 ARLAKGLSEDADLLLLDEPTNHLD---EKSLQFLIQQLKHYNGTVILVSH 158
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDpkgEHEMMQLILDAKANNKTVFVITH 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-158 |
4.03e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 7 LTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------RKDIKLAL------VEQ 73
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILfqgkeidFKSSKEALengismVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 74 E--------------TAAYS----FADQTPA---EKKLLEKWHV---PLRDFHQLSGGEKLKARLAKGLSEDADLLLLDE 129
Cdd:PRK10982 81 ElnlvlqrsvmdnmwLGRYPtkgmFVDQDKMyrdTKAIFDELDIdidPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190
....*....|....*....|....*....|..
gi 2828494 130 PTNHLDEKSLQFL---IQQLKHYNGTVILVSH 158
Cdd:PRK10982 161 PTSSLTEKEVNHLftiIRKLKERGCGIVYISH 192
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-187 |
4.12e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 46.19 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 21 KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPA---QGQIL-------RKDIKL--ALVEQE-------------- 74
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLlngmpidAKEMRAisAYVQQDdlfiptltvrehlm 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 75 -TAAYSFADQTPAEKK------LLEKwhVPLRDFHQ-----------LSGGEKLKARLAKGLSEDADLLLLDEPTNHLDE 136
Cdd:TIGR00955 122 fQAHLRMPRRVTKKEKrervdeVLQA--LGLRKCANtrigvpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2828494 137 KSLQFLIQQLKHY--NG-TVILVSHdryfldEAATKIWSLEDQTLIEFKGN--YSG 187
Cdd:TIGR00955 200 FMAYSVVQVLKGLaqKGkTIICTIH------QPSSELFELFDKIILMAEGRvaYLG 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
292-483 |
4.36e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 45.46 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERT-----LFKNANFTIQHGEKVAIIGPNGSGKTTL---LNIILGQETaeGSV-WVSPSANigylTQEV 362
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLLPDT--GTIeWIFKDEK----NKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 363 FDLPLEQTPEELFENETFKARGHVQNLMRHLG--FTAAQWT---EPIKH------MSMG-------ERVK--IKL----- 417
Cdd:PRK13651 77 TKEKEKVLEKLVIQKTRFKKIKKIKEIRRRVGvvFQFAEYQlfeQTIEKdiifgpVSMGvskeeakKRAAkyIELvglde 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 418 -------------------MAYILE-EKDVLILDEPTNHLDlP--SREQLE--ETLSQYSGTLLAVSHDRYFLEKTTNSK 473
Cdd:PRK13651 157 sylqrspfelsggqkrrvaLAGILAmEPDFLVFDEPTAGLD-PqgVKEILEifDNLNKQGKTIILVTHDLDNVLEWTKRT 235
|
250
....*....|
gi 2828494 474 LVISNNGIEK 483
Cdd:PRK13651 236 IFFKDGKIIK 245
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
303-491 |
4.79e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 45.46 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 303 ERTLFKNANFTIQHGEKVAIIGPNGSGKTTL---LNIILgqETAEGSVWV-----SPSANIGYLTQE---VFDLPLEQT- 370
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL--IPSEGKVYVdgldtSDEENLWDIRNKagmVFQNPDNQIv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 371 -----------PEEL-FENETFKARghVQNLMRHLGFTAAQWTEPikHM-SMGERVKIKLMAYILEEKDVLILDEPTNHL 437
Cdd:PRK13633 100 ativeedvafgPENLgIPPEEIRER--VDESLKKVGMYEYRRHAP--HLlSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2828494 438 DLPSREQLEETL----SQYSGTLLAVSHdryFLEKTTNSKLVISNNGIEKQLNDVPSE 491
Cdd:PRK13633 176 DPSGRREVVNTIkelnKKYGITIILITH---YMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
292-434 |
5.06e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAF-GERTLfKNANFTIQHGEKVAIIGPNGSGKTTLLNI-------------IL--GQETAEGSVWVSPSANI 355
Cdd:NF040905 2 LEMRGITKTFpGVKAL-DDVNLSVREGEIHALCGENGAGKSTLMKVlsgvyphgsyegeILfdGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 356 GYLTQEVFDLPLEQTPEELF---E---------NETFKargHVQNLMRHLGFTAAQWTePIKHMSMGER--VKI-KLMAy 420
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFlgnErakrgvidwNETNR---RARELLAKVGLDESPDT-LVTDIGVGKQqlVEIaKALS- 155
|
170
....*....|....*.
gi 2828494 421 ileeKDV--LILDEPT 434
Cdd:NF040905 156 ----KDVklLILDEPT 167
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
32-159 |
5.74e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 32 IIGIIGKNGAGKSTLLHLIH--------------NDLAP-----------------------AQGQI------------- 61
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIRyalygkarsrsklrSDLINvgseeasvelefehggkryrierRQGEFaefleakpserke 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 62 -------------LRKDIKLALVEQETAAYSFADQTPAEKKLLEKWHVpLRDFHQLSGGEklkaRLAKGLSEDADlLLLD 128
Cdd:COG0419 105 alkrllgleiyeeLKERLKELEEALESALEELAELQKLKQEILAQLSG-LDPIETLSGGE----RLRLALADLLS-LILD 178
|
170 180 190
....*....|....*....|....*....|.
gi 2828494 129 epTNHLDEKSLQFLIQQLKhyngTVILVSHD 159
Cdd:COG0419 179 --FGSLDEERLERLLDALE----ELAIITHV 203
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-159 |
8.18e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.83 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNV--SYEVKDQTVfKHVNASVQQGDIIGIIGKNGAGKSTLLHLIH-----------------NDLAPAQgqilrKD 65
Cdd:PRK11650 4 LKLQAVrkSYDGKTQVI-KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAgleritsgeiwiggrvvNELEPAD-----RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 66 IklALVEQETAAY---SFADQ---------TPAEK---------KLLEkwhvpLRDF-----HQLSGGEklKARLAKG-- 117
Cdd:PRK11650 78 I--AMVFQNYALYphmSVRENmayglkirgMPKAEieervaeaaRILE-----LEPLldrkpRELSGGQ--RQRVAMGra 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2828494 118 LSEDADLLLLDEPTNHLDEK---SLQFLIQQL-KHYNGTVILVSHD 159
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKlrvQMRLEIQRLhRRLKTTSLYVTHD 194
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
292-349 |
9.59e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.83 E-value: 9.59e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTL-FKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSVWV 349
Cdd:PRK11650 4 LKLQAVRKSYDGKTQvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERiTSGEIWI 63
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
279-486 |
9.73e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 45.01 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 279 FSI---DTTHKTGKRF-------LEVQNVTKAF-GERTL-FKNANFTIQHGEKVAIIGPNGSGKTTLLNIILG-QETAEG 345
Cdd:PRK11176 319 FAIldlEQEKDEGKRVierakgdIEFRNVTFTYpGKEVPaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRfYDIDEG 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 346 SVWV-----------SPSANIGYLTQEVfdlpleqtpeELFeNET-----------FKARGHVQNLMRhlgftAAQWTEP 403
Cdd:PRK11176 399 EILLdghdlrdytlaSLRNQVALVSQNV----------HLF-NDTianniayarteQYSREQIEEAAR-----MAYAMDF 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 404 IKHM---------------SMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLS--QYSGTLLAVSH----- 461
Cdd:PRK11176 463 INKMdngldtvigengvllSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDelQKNRTSLVIAHrlsti 542
|
250 260 270
....*....|....*....|....*....|....*
gi 2828494 462 ----------DRYFLEKTTNSKLvISNNGIEKQLN 486
Cdd:PRK11176 543 ekadeilvveDGEIVERGTHAEL-LAQNGVYAQLH 576
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-183 |
1.01e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.23 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 9 NVSYEVKDQTV--FKHVNASVQQGDIIGIIGKNGAGKS----TLLHLIH-----------------------NDLAPAQG 59
Cdd:PRK10261 19 NIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEqagglvqcdkmllrrrsrqvielSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 60 QILR-KDIKLALVEQETA-------------------AYSFADQTPAEKKLLEKWHVP------LRDFHQLSGGEKLKAR 113
Cdd:PRK10261 99 RHVRgADMAMIFQEPMTSlnpvftvgeqiaesirlhqGASREEAMVEAKRMLDQVRIPeaqtilSRYPHQLSGGMRQRVM 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2828494 114 LAKGLSEDADLLLLDEPTNHLDeKSLQFLIQQL-----KHYNGTVILVSHDRYFLDEAAtkiwsleDQTLIEFKG 183
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALD-VTIQAQILQLikvlqKEMSMGVIFITHDMGVVAEIA-------DRVLVMYQG 245
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
313-462 |
1.05e-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: 45.16 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 313 TIQHGEKVAIIGPNGSGKTTLLNIILGQET-------------------------------AEGSVWVSpsanigYLTQE 361
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKpnlgdydeepswdevlkrfrgtelqdyfkklANGEIKVA------HKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 362 VFDLP--LEQTPEELFE--NETFKARGHVQNL-MRHLgftaaqWTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNH 436
Cdd:COG1245 169 VDLIPkvFKGTVRELLEkvDERGKLDELAEKLgLENI------LDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190
....*....|....*....|....*....|.
gi 2828494 437 LDLpsREQLE-----ETLSQYSGTLLAVSHD 462
Cdd:COG1245 243 LDI--YQRLNvarliRELAEEGKYVLVVEHD 271
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
286-462 |
1.07e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 44.27 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 286 KTGKRFLEVQNVTKAF---GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIiLGQETAEGSVWVSPSANIGYLTQEV 362
Cdd:PRK14246 2 EAGKSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKV-LNRLIEIYDSKIKVDGKVLYFGKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 363 FDLPLEQTPEE---------------LFENETFKARGH-------VQNLMRHLGFTAAQWTE-------PIKHMSMGERV 413
Cdd:PRK14246 81 FQIDAIKLRKEvgmvfqqpnpfphlsIYDNIAYPLKSHgikekreIKKIVEECLRKVGLWKEvydrlnsPASQLSGGQQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2828494 414 KIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYSG--TLLAVSHD 462
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
292-437 |
1.15e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.61 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAF-GERTLfKNANFTIQHGEKVAIIGPNGSGKTTLLNII-------------LGQETAEGSVWVSPSANIGY 357
Cdd:PRK10762 5 LQLKGIDKAFpGVKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLtgiytrdagsilyLGKEVTFNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 358 LTQEVFDLPLEQTPEELFENETFKAR-GHVQ---------NLMRHLGFTAAQWTePIKHMSMGER--VKI-KLMAYileE 424
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGREFVNRfGRIDwkkmyaeadKLLARLNLRFSSDK-LVGELSIGEQqmVEIaKVLSF---E 159
|
170
....*....|...
gi 2828494 425 KDVLILDEPTNHL 437
Cdd:PRK10762 160 SKVIIMDEPTDAL 172
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
292-438 |
1.17e-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: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFG----ERTLFKNANFTIQHGEKVAIIGPNGSGKT-TLLNII--LGQETAEgsvwvsPSANIGYLTQEVFD 364
Cdd:COG4172 7 LSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrlLPDPAAH------PSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 365 LPleqtpeelfENETFKARGH-----------------------VQNLMRHLGFTAAQWT-------------EPIK--- 405
Cdd:COG4172 81 LS---------ERELRRIRGNriamifqepmtslnplhtigkqiAEVLRLHRGLSGAAARaralellervgipDPERrld 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 2828494 406 ---H-MSMGE--RVKIKlMAyILEEKDVLILDEPTNHLD 438
Cdd:COG4172 152 aypHqLSGGQrqRVMIA-MA-LANEPDLLIADEPTTALD 188
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-163 |
1.20e-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: 45.32 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 26 SVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDiKLALVEQ----------ETAAYSFADQTPAEKKLLEKWH 95
Cdd:TIGR00957 660 SIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVPQqawiqndslrENILFGKALNEKYYQQVLEACA 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 96 VpLRDFH---------------QLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSLQFLIQQ-------LKhyNGTV 153
Cdd:TIGR00957 739 L-LPDLEilpsgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHvigpegvLK--NKTR 815
|
170
....*....|
gi 2828494 154 ILVSHDRYFL 163
Cdd:TIGR00957 816 ILVTHGISYL 825
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
314-462 |
1.47e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 314 IQHGEKVAIIGPNGSGKTTLLNIILGQETAEGSVWVSPSANIGYLTQEVfdlpleqtpeelfenetfkarghvqnlmrhl 393
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 394 gftaaqwtepikHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYS----GTLLAVSHD 462
Cdd:cd03222 71 ------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeegkKTALVVEHD 131
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
292-480 |
1.48e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 43.46 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEgsvwvSPSANIgylTQEVFDlpLEQTP 371
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPR-----SGTLNI---AGNHFD--FSKTP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 372 EelfENETFKARGHV----------------QNL----MRHLGFTAAQWTEPIK-----------------HMSMGE--R 412
Cdd:PRK11124 73 S---DKAIRELRRNVgmvfqqynlwphltvqQNLieapCRVLGLSKDQALARAEkllerlrlkpyadrfplHLSGGQqqR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2828494 413 VKI--KLMAyileEKDVLILDEPTNHLDLPSREQ----LEEtLSQYSGTLLAVSHDRYFLEKTTnSKLVISNNG 480
Cdd:PRK11124 150 VAIarALMM----EPQVLLFDEPTAALDPEITAQivsiIRE-LAETGITQVIVTHEVEVARKTA-SRVVYMENG 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-158 |
1.55e-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: 44.94 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 19 VFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDI------------KLALVEQETAAYS------- 79
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLniakiglhdlrfKITIIPQDPVLFSgslrmnl 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 80 --FADQTPAEKKL-LEKWHvpLRDF---------HQLS-GGEKLKAR------LAKGLSEDADLLLLDEPTNHLDEKSlQ 140
Cdd:TIGR00957 1381 dpFSQYSDEEVWWaLELAH--LKTFvsalpdkldHECAeGGENLSVGqrqlvcLARALLRKTKILVLDEATAAVDLET-D 1457
|
170 180
....*....|....*....|.
gi 2828494 141 FLIQ---QLKHYNGTVILVSH 158
Cdd:TIGR00957 1458 NLIQstiRTQFEDCTVLTIAH 1478
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
292-344 |
1.65e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.63 E-value: 1.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAE 344
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYE 54
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
102-170 |
1.68e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.96 E-value: 1.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2828494 102 HQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLD----EKSLQFLIQQLKHYNGTVILVSHDRYFLDEAATKI 170
Cdd:PRK11022 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiqAQIIELLLELQQKENMALVLITHDLALVAEAAHKI 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-158 |
1.70e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 43.69 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNdLAPAQGQI----------------------- 61
Cdd:cd03289 5 VKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLR-LLNTEGDIqidgvswnsvplqkwrkafgvip 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 62 ---------LRK---------DIKLALVEQETAAYSFADQTPAEKK--LLEKWHVplrdfhqLSGGEKLKARLAKGLSED 121
Cdd:cd03289 84 qkvfifsgtFRKnldpygkwsDEEIWKVAEEVGLKSVIEQFPGQLDfvLVDGGCV-------LSHGHKQLMCLARSVLSK 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 2828494 122 ADLLLLDEPTNHLDEKSLQFLIQQLKH--YNGTVILVSH 158
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQafADCTVILSEH 195
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
104-159 |
3.88e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.24 E-value: 3.88e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2828494 104 LSGGEKLKARLAKGLSEDAD--LLLLDEPTNHLDEKSLQFLIQQLKH---YNGTVILVSHD 159
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRlrdLGNTVLVVEHD 198
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4-158 |
4.19e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.78 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 4 IVTLTNVSYEVKDQTVFKhVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDI----------------- 66
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCninniakpyctyighnl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 67 --KLALVEQE-----TAAYSFADQTPAEKKLLEKWHVPLRDFHQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKS- 138
Cdd:PRK13541 80 glKLEMTVFEnlkfwSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENr 159
|
170 180
....*....|....*....|..
gi 2828494 139 --LQFLIQQLKHYNGTVILVSH 158
Cdd:PRK13541 160 dlLNNLIVMKANSGGIVLLSSH 181
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
30-62 |
4.47e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 42.22 E-value: 4.47e-04
10 20 30
....*....|....*....|....*....|...
gi 2828494 30 GDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL 62
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-158 |
4.58e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.09 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 15 KDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL------RKDI-------KLALVEQET------ 75
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIindshnLKDInlkwwrsKIGVVSQDPllfsns 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 76 -------AAYSFAD-------------------------------------QTPAEKKLLE----------------KWH 95
Cdd:PTZ00265 476 iknnikySLYSLKDlealsnyynedgndsqenknkrnscrakcagdlndmsNTTDSNELIEmrknyqtikdsevvdvSKK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 96 VPLRDF----------------HQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLDEKSlQFLIQQ----LK-HYNGTVI 154
Cdd:PTZ00265 556 VLIHDFvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-EYLVQKtinnLKgNENRITI 634
|
....
gi 2828494 155 LVSH 158
Cdd:PTZ00265 635 IIAH 638
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
100-164 |
4.89e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.38 E-value: 4.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2828494 100 DFHQLSGGEKLKARLAKGLSEDAD---LLLLDEPTNHLDEKSLQFLIQQLKH---YNGTVILVSHDRYFLD 164
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKElsrNGAQLILTTHSPLLLD 303
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
257-438 |
5.27e-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: 43.01 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 257 KRLEKELEKAKAEPVTPEytvRFSIdtthKTGKRF-LEVQN--VTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTL 333
Cdd:TIGR00957 608 KRLRIFLSHEELEPDSIE---RRTI----KPGEGNsITVHNatFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 334 LNIILGQ-ETAEGSVWVSPSanIGYLTQE------------VFDLPLeqtpEELFENETFKARGHVQNLMRHLGFTAAQW 400
Cdd:TIGR00957 681 LSALLAEmDKVEGHVHMKGS--VAYVPQQawiqndslreniLFGKAL----NEKYYQQVLEACALLPDLEILPSGDRTEI 754
|
170 180 190
....*....|....*....|....*....|....*...
gi 2828494 401 TEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLD 438
Cdd:TIGR00957 755 GEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
302-438 |
5.44e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.19 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 302 GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ--ETAEGSVWVSPSanIGYLTQ-------EVFDLPLEQTPe 372
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGElpPRSDASVVIRGT--VAYVPQvswifnaTVRDNILFGSP- 704
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 373 elFENETFKARGHVQNLMRHL----GFTAAQWTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLD 438
Cdd:PLN03130 705 --FDPERYERAIDVTALQHDLdllpGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
104-158 |
6.03e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 6.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2828494 104 LSGGEKLKARLAKGLSEDAD---LLLLDEPTNHL---DEKSLQFLIQQLKHYNGTVILVSH 158
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLhfdDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
312-462 |
6.14e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 42.26 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 312 FTIQHGEKVAIIGPNGSGKTTL---LNIIlgQETAEGS-------VWVSPSANIGYLTQE---VFDLP---------LEQ 369
Cdd:PRK11308 36 FTLERGKTLAVVGESGCGKSTLarlLTMI--ETPTGGElyyqgqdLLKADPEAQKLLRQKiqiVFQNPygslnprkkVGQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 370 TPEE-LFENETFKA---RGHVQNLMRHLGFTAAQWTE-PikHM-SMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSRE 443
Cdd:PRK11308 114 ILEEpLLINTSLSAaerREKALAMMAKVGLRPEHYDRyP--HMfSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQA 191
|
170 180
....*....|....*....|...
gi 2828494 444 Q---LEETLSQYSGT-LLAVSHD 462
Cdd:PRK11308 192 QvlnLMMDLQQELGLsYVFISHD 214
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
9-53 |
6.62e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 6.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2828494 9 NVSYEvkDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHND 53
Cdd:PRK10938 267 VVSYN--DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD 309
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-158 |
9.32e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 40.98 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 1 MKEIVTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIH-----NDLAPAQGQI-------------- 61
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelNEEARVEGEVrlfgrniyspdvdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 62 --LRKDI-----------KLALVEQETAAYSFADQTPAEKKLLE--KWHVP-----------LRDF-HQLSGGEKLKARL 114
Cdd:PRK14267 81 ieVRREVgmvfqypnpfpHLTIYDNVAIGVKLNGLVKSKKELDErvEWALKkaalwdevkdrLNDYpSNLSGGQRQRLVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2828494 115 AKGLSEDADLLLLDEPTNHLD---EKSLQFLIQQLKHyNGTVILVSH 158
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-EYTIVLVTH 206
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
309-349 |
9.75e-04 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 40.80 E-value: 9.75e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2828494 309 NANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEGSVWV 349
Cdd:pfam00006 6 DGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYA 46
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
303-461 |
1.01e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 41.16 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 303 ERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLN------------IILGQETAEGSVwvsPSANIGYLTQE---VFDLPL 367
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQhlngllqptsgtVTIGERVITAGK---KNKKLKPLRKKvgiVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 368 EQTPEELFENE------TF-----KARGHVQNLMRHLGFTAAQWTEPIKHMSMGE--RVKIklmAYILE-EKDVLILDEP 433
Cdd:PRK13634 96 HQLFEETVEKDicfgpmNFgvseeDAKQKAREMIELVGLPEELLARSPFELSGGQmrRVAI---AGVLAmEPEVLVLDEP 172
|
170 180 190
....*....|....*....|....*....|..
gi 2828494 434 TNHLDLPSREQLEE---TLSQYSG-TLLAVSH 461
Cdd:PRK13634 173 TAGLDPKGRKEMMEmfyKLHKEKGlTTVLVTH 204
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
303-438 |
1.28e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.89 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 303 ERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEGSVWVSPSANIGYLTQE--VFDLPLEQTP--EELFENE 378
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVPQVswIFNATVRENIlfGSDFESE 708
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2828494 379 TFKARGHVQNLMRHLGFTAAQWTEPIK----HMSMGERVKIKLMAYILEEKDVLILDEPTNHLD 438
Cdd:PLN03232 709 RYWRAIDVTALQHDLDLLPGRDLTEIGergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
10-46 |
1.29e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 40.66 E-value: 1.29e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2828494 10 VSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTL 46
Cdd:cd03288 27 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSL 63
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
95-159 |
1.44e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2828494 95 HVPL-RDFHQLSGGEKLKARLAKGL---SEDADLLLLDEPTNHL---DEKSLQFLIQQLKHYNGTVILVSHD 159
Cdd:PRK00635 800 YLPLgRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQGHTVVIIEHN 871
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
102-170 |
1.45e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.94 E-value: 1.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2828494 102 HQLSGGEKLKARLAKGLSEDADLLLLDEPTNHLdEKSLQFLIQQL-----KHYNGTVILVSHDRYFLDEAATKI 170
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAM-EPTTQAQIFRLltrlnQNNNTTILLISHDLQMLSQWADKI 229
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
292-462 |
1.54e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 40.58 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET---AEGSVWVS--------PSANIGYLTQ 360
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggAPRGARVTgdvtlngePLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 361 EVFDLPLEQTPEELFeneTFKARG--------HVQN---LMRHLGFTAAQWTE----------PIKHMSMGE--RVKI-K 416
Cdd:PRK13547 82 ARLRAVLPQAAQPAF---AFSAREivllgrypHARRagaLTHRDGEIAWQALAlagatalvgrDVTTLSGGElaRVQFaR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2828494 417 LMAYILEEKDV------LILDEPTNHLDLPSREQLEETLSQYSGT----LLAVSHD 462
Cdd:PRK13547 159 VLAQLWPPHDAaqppryLLLDEPTAALDLAHQHRLLDTVRRLARDwnlgVLAIVHD 214
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
7-67 |
1.68e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.03 E-value: 1.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2828494 7 LTNVSYEVkdqtvfkhvnasvQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIlrkDIK 67
Cdd:PRK13545 40 LNNISFEV-------------PEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV---DIK 84
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
303-340 |
1.69e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 41.24 E-value: 1.69e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2828494 303 ERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQ 340
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRH 364
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
293-349 |
1.71e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 40.55 E-value: 1.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2828494 293 EVQNVTKAF----GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSVWV 349
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERpTSGRVLV 64
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-158 |
1.88e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 40.28 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 5 VTLTNVSYEVKDQTVFKHVNASVQQGDIIGIIGKNGAGKSTLLHLIHN--DLAP---AQGQI--------------LRKD 65
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPearVSGEVyldgqdifkmdvieLRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 66 IK-----------LALVEQETAAYSFADQTPAEKKLLEKWHVPLRDFH--------------QLSGGEKLKARLAKGLSE 120
Cdd:PRK14247 84 VQmvfqipnpipnLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQlwdevkdrldapagKLSGGQQQRLCIARALAF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2828494 121 DADLLLLDEPTNHLDEKS---LQFLIQQLKHyNGTVILVSH 158
Cdd:PRK14247 164 QPEVLLADEPTANLDPENtakIESLFLELKK-DMTIVLVTH 203
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
299-347 |
2.12e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 39.55 E-value: 2.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2828494 299 KAFGERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAEGSV 347
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSV 63
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
320-542 |
2.13e-03 |
|
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: 40.45 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 320 VAIIGPNGSGKTTLLNII---------LGQETAEGSVWVSPSANIGYLTQEVFDLPLEqtpeelFENETFKARGHVQNLM 390
Cdd:pfam13304 2 NVLIGPNGSGKSNLLEALrfladfdalVIGLTDERSRNGGIGGIPSLLNGIDPKEPIE------FEISEFLEDGVRYRYG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 391 rhLGFTAAQWTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQ----LEETLSQYSGTLLAVSHDRYFL 466
Cdd:pfam13304 76 --LDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERielsLSELSDLISGLLLLSIISPLSF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2828494 467 EKTTNSKLVISNNGIEKQLNDVpSERNEREELRLKLETERQEVLGKLSFMTPNDKGYKELDQAFNELTKRIKELDH 542
Cdd:pfam13304 154 LLLLDEGLLLEDWAVLDLAADL-ALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGG 228
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
97-159 |
2.30e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 97 PLRDFHQLSGGEKLKARLAKGLSedADLL----LLDEPTNHL---DEKSLQFLIQQLKHYNGTVILVSHD 159
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHLG--AELIgityILDEPSIGLhpqDTHKLINVIKKLRDQGNTVLLVEHD 537
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
237-370 |
2.34e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.86 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 237 FKEYHRVKAKRTDAQIKSKQKRLEKELEKAKAEPVTPEYTVRFSIDTTHKTGKRFLEVQNVTKAFG----ERTLFKNANF 312
Cdd:TIGR00956 705 FRRGSLKRAKKAGETSASNKNDIEAGEVLGSTDLTDESDDVNDEKDMEKESGEDIFHWRNLTYEVKikkeKRVILNNVDG 784
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2828494 313 TIQHGEKVAIIGPNGSGKTTLLNIILGQETA----EGSVWV-------SPSANIGYLTQEvfDLPLEQT 370
Cdd:TIGR00956 785 WVKPGTLTALMGASGAGKTTLLNVLAERVTTgvitGGDRLVngrpldsSFQRSIGYVQQQ--DLHLPTS 851
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
292-337 |
2.41e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.98 E-value: 2.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2828494 292 LEVQNVtKAFGERTLF--KNANFTIqhgekvaIIGPNGSGKTTLLNII 337
Cdd:COG3950 6 LTIENF-RGFEDLEIDfdNPPRLTV-------LVGENGSGKTTLLEAI 45
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
294-541 |
2.87e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 39.99 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 294 VQNVTKAFGERTLFK-----NANFTIQHGEKVAIIGPNGSGKTTLL---NIILGQETAEGSV--WVSPsANIGYLtQEVF 363
Cdd:PRK13645 9 LDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIqltNGLIISETGQTIVgdYAIP-ANLKKI-KEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 364 DLPLE-----QTPE-ELFENETFK--ARGHVqnlmrHLGFTAAQWTEPIK------------------HMSMGERVKIKL 417
Cdd:PRK13645 87 RLRKEiglvfQFPEyQLFQETIEKdiAFGPV-----NLGENKQEAYKKVPellklvqlpedyvkrspfELSGGQKRRVAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 418 MAYILEEKDVLILDEPTNHLDLPSREQ----LEETLSQYSGTLLAVSHDRYFLEKTTNSKLVISnngiEKQLNDV--PSE 491
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDfinlFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMH----EGKVISIgsPFE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2828494 492 RNEREELRLKLETERQEVLGKLsfmtpndkgYKELDQAFNELTKRIKELD 541
Cdd:PRK13645 238 IFSNQELLTKIEIDPPKLYQLM---------YKLKNKGIDLLNKNIRTIE 278
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-69 |
3.61e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 39.39 E-value: 3.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2828494 21 KHVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRKDIKLA 69
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH 78
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
292-481 |
3.76e-03 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 39.28 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 292 LEVQNVTKAF---------GERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQET-AEGSV-W------------ 348
Cdd:PRK10419 4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVsWrgeplaklnraq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 349 ------------------VSPSANIGYLTQEvfdlPLEQTpEELFENETfKARghVQNLMRHLGFTAAQWTEPIKHMSMG 410
Cdd:PRK10419 84 rkafrrdiqmvfqdsisaVNPRKTVREIIRE----PLRHL-LSLDKAER-LAR--ASEMLRAVDLDDSVLDKRPPQLSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2828494 411 ERVKIKLMAYILEEKDVLILDEPTNHLDLPSREQ---LEETLSQYSGT-LLAVSHDRYFLEKTTNSKLVISNNGI 481
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGvirLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
303-461 |
3.77e-03 |
|
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: 39.01 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 303 ERTLFKNANFTIQHGEKVAIIGPNGSGKTTLLNIILGQETAE-GSVWV-----------SPSANIGYLTQE--VFD---- 364
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPEnGRVLVdghdlaladpaWLRRQVGVVLQEnvLFNrsir 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 365 ----LPLEQTPEELFENETFKARGHVQNLMRHLGFTAAQwTEPIKHMSMGERVKIKLMAYILEEKDVLILDEPTNHLDLP 440
Cdd:cd03252 94 dniaLADPGMSMERVIEAAKLAGAHDFISELPEGYDTIV-GEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180
....*....|....*....|...
gi 2828494 441 SREQLEETLSQYSG--TLLAVSH 461
Cdd:cd03252 173 SEHAIMRNMHDICAgrTVIIIAH 195
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
309-339 |
3.98e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.87 E-value: 3.98e-03
10 20 30
....*....|....*....|....*....|.
gi 2828494 309 NANFTIQHGEKVAIIGPNGSGKTTLLNIILG 339
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAG 72
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
320-462 |
4.14e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.84 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 320 VAIIGPNGSGKTTLLNII---LGQETAEGSVWVSPSANIGYLTQEV-------------------FDLPLEQTPEE---- 373
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIryaLYGKARSRSKLRSDLINVGSEEASVelefehggkryrierrqgeFAEFLEAKPSErkea 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2828494 374 ---LFENETF-KARGHVQNLMRHLGFTAAQWTE----------------PIKHMSMGERVKIKLMAYIleekdVLILDep 433
Cdd:COG0419 106 lkrLLGLEIYeELKERLKELEEALESALEELAElqklkqeilaqlsgldPIETLSGGERLRLALADLL-----SLILD-- 178
|
170 180
....*....|....*....|....*....
gi 2828494 434 TNHLDLPSREQLEETLSQysgtLLAVSHD 462
Cdd:COG0419 179 FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
104-174 |
6.16e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.75 E-value: 6.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 104 LSGGEKLKARLAKGLSEDAD---LLLLDEPTNHL---DEKSLQFLIQQLKHYNGTVILVSHDryfLDEAATKIWSLE 174
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfhDVKKLLEVLQRLVDKGNTVVVIEHN---LDVIKCADWIID 243
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
99-159 |
6.41e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 6.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2828494 99 RDFHQLSGGEKLKARLAK----GLSedADLLLLDEPTNHLDEKSLQFLIQQLKHYN---GTVILVSHD 159
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLATqigsGLT--GVLYVLDEPSIGLHQRDNRRLINTLKRLRdlgNTLIVVEHD 549
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
104-157 |
7.17e-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: 39.04 E-value: 7.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2828494 104 LSGGEKLKARLAKGLSEDADLLLLDEPTNHLD---EKSLQFLIQQLKHYNGTVILVS 157
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDvgaKYEIYKLINQLAQEGVAIIVVS 460
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
315-343 |
8.27e-03 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 37.09 E-value: 8.27e-03
10 20 30
....*....|....*....|....*....|
gi 2828494 315 QHGEKVAIIG-PNgSGKTTLLNIILGQETA 343
Cdd:cd04164 1 REGIKVVIAGkPN-VGKSSLLNALAGRDRA 29
|
|
| VirB4_CagE |
TIGR00929 |
type IV secretion/conjugal transfer ATPase, VirB4 family; Type IV secretion systems are found ... |
320-340 |
9.14e-03 |
|
type IV secretion/conjugal transfer ATPase, VirB4 family; Type IV secretion systems are found in Gram-negative pathogens. They export proteins, DNA, or complexes in different systems and are related to plasmid conjugation systems. This model represents related ATPases that include VirB4 in Agrobacterium tumefaciens (DNA export) CagE in Helicobacter pylori (protein export) and plasmid TraB (conjugation).
Pssm-ID: 273346 [Multi-domain] Cd Length: 785 Bit Score: 38.84 E-value: 9.14e-03
|
| |
