|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-532 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 705.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 5 ATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYLRQINNVDSTLSIID 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 85 ELYTVIEPILDMEKRILKMQNEMrhltgEKLEKLYSSYTALTHNYELMDGYAAKSKVVGILKGLGFEEADFDRKINTLSG 164
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKL-----AEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 165 GQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNVQMYLGNYT 244
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 245 DFSNKKQMLLDAKMKEYLNQQQEIRHQEAVITKLKQfnREKSIKRAESRQKQLEKIERVDAPQTyTENMRLSLDIAKESG 324
Cdd:COG0488 236 AYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRA--KARKAKQAQSRIKALEKLEREEPPRR-DKTVEIRFPPPERLG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 325 KDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQEHQVLHM 404
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 405 DKTLFDEISDTYPEMTNTRIRNILAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLE 484
Cdd:COG0488 393 DKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 496028547 485 NALNSFPGTVCYVSHDRYFINKTATRILDLTENRLLNYIGNYDYYIEK 532
Cdd:COG0488 473 EALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-535 |
8.60e-117 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 358.82 E-value: 8.60e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSN---EIIkSATFliNEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYLRQINNVDS 78
Cdd:PRK15064 1 MLSTANITMQFGAKplfENI-SVKF--GGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 79 TLSIID-------ELYTVIEpildmEKRILKMQNEMRHLTGEKLEKLYSSYTAlthnyelMDGYAAKSKVVGILKGLGFE 151
Cdd:PRK15064 78 EFTVLDtvimghtELWEVKQ-----ERDRIYALPEMSEEDGMKVADLEVKFAE-------MDGYTAEARAGELLLGVGIP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 152 EADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDI 231
Cdd:PRK15064 146 EEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 232 ENGNVQMYLGNYTDFsnkkqMLLDAKMKEylNQQQEIRHQEAVITKLKQF------NREKSiKRAESRQKQLEKIERVDA 305
Cdd:PRK15064 226 DYGELRVYPGNYDEY-----MTAATQARE--RLLADNAKKKAQIAELQSFvsrfsaNASKA-KQATSRAKQIDKIKLEEV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 306 PQTYTENMRLSLDIAKESGKDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVI 385
Cdd:PRK15064 298 KPSSRQNPFIRFEQDKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 386 YGSNVSVAYYDQEHQV-LHMDKTLFDEISD-TYPEMTNTRIRNILAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKA 463
Cdd:PRK15064 378 WSENANIGYYAQDHAYdFENDLTLFDWMSQwRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKP 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496028547 464 NFLLLDEPTNHLDIVSKDVLENALNSFPGTVCYVSHDRYFINKTATRILDLTENRLLNYIGNYDYYIEKREA 535
Cdd:PRK15064 458 NVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQGI 529
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-541 |
2.61e-114 |
|
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: 353.09 E-value: 2.61e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSN-EIIK--SATFLINEheKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYLRQINNVDSTLSII 83
Cdd:TIGR03719 9 RVSKVVPPKkEILKdiSLSFFPGA--KIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 84 DELYTVIEPILDMEKRIlkmqNEMRHLTGE---KLEKLYSSYTALTHNYELMDGYAAKSKVvgilkglgfEEA------- 153
Cdd:TIGR03719 87 ENVEEGVAEIKDALDRF----NEISAKYAEpdaDFDKLAAEQAELQEIIDAADAWDLDSQL---------EIAmdalrcp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 154 DFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIEN 233
Cdd:TIGR03719 154 PWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 234 GNVQMYLGNYTDFSNKKQmlldAKMKeylnqqQEIRHQEAvitklkqfnREKSIKR--------AESRQKQ----LEKIE 301
Cdd:TIGR03719 234 GRGIPWEGNYSSWLEQKQ----KRLE------QEEKEESA---------RQKTLKRelewvrqsPKGRQAKskarLARYE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 302 RVDAPQTYTENMRLSLDI--AKESGKDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEP 379
Cdd:TIGR03719 295 ELLSQEFQKRNETAEIYIppGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 380 DTGEVIYGSNVSVAYYDQEHQVLHMDKTLFDEISDTYPEMT--NTRI--RNILAAFLFTGEDVYKKISDLSGGERGRVSL 455
Cdd:TIGR03719 375 DSGTIEIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKlgKREIpsRAYVGRFNFKGSDQQKKVGQLSGGERNRVHL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 456 VKLMLSKANFLLLDEPTNHLDIVSKDVLENALNSFPGTVCYVSHDRYFINKTATRILDLT-ENRLLNYIGNYDYYIE--K 532
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEYEEdkK 534
|
....*....
gi 496028547 533 REAVEEAAN 541
Cdd:TIGR03719 535 RRLGEDADQ 543
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-541 |
2.32e-108 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 337.86 E-value: 2.32e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 30 KAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYLRQinnvdstlsiidelytviEPILDMEKRILKMQNEMRH 109
Cdd:PRK11819 35 KIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ------------------EPQLDPEKTVRENVEEGVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 110 LTGEKLEKLYSSYTALTHNYELMDGYAAK-SKVVGILKGLGFEEAD--------------FDRKINTLSGGQKTRVFLAK 174
Cdd:PRK11819 97 EVKAALDRFNEIYAAYAEPDADFDALAAEqGELQEIIDAADAWDLDsqleiamdalrcppWDAKVTKLSGGERRRVALCR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 175 LLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNVQMYLGNYTDFSNKKQMLL 254
Cdd:PRK11819 177 LLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAKRL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 255 dakmkeylnqQQEIRHQEAvitklkqfnREKSIKR--------AESRQ-KQLEKIERVDAPQTYTENMRLS-LDI----A 320
Cdd:PRK11819 257 ----------AQEEKQEAA---------RQKALKRelewvrqsPKARQaKSKARLARYEELLSEEYQKRNEtNEIfippG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 321 KESGKDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQEHQ 400
Cdd:PRK11819 318 PRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 401 VLHMDKTLFDEISDTYPEMT--NTRI--RNILAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLD 476
Cdd:PRK11819 398 ALDPNKTVWEEISGGLDIIKvgNREIpsRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 477 IVSKDVLENALNSFPGTVCYVSHDRYFINKTATRILDLT-ENRLLNYIGNYDYYIE--KREAVEEAAN 541
Cdd:PRK11819 478 VETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEgDSQVEWFEGNFQEYEEdkKRRLGADAAR 545
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-639 |
7.67e-98 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 313.04 E-value: 7.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYLRQinnvDSTLS 81
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQ----DPPRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 82 IIDELYTVIEPILDMEKRILKMQNEMRHLTG-EKLEKLYSSYTALTHNYELMDGYAAKSKVVGILKGLGFeeaDFDRKIN 160
Cdd:PRK11147 79 VEGTVYDFVAEGIEEQAEYLKRYHDISHLVEtDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGL---DPDAALS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 161 TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNVQMYL 240
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 241 GNYtdfsnkkQMLLDAKmKEYLNQQQEirhQEAvitklkQFNRE---------KSIK----RAESRQKQL-----EKIER 302
Cdd:PRK11147 236 GNY-------DQYLLEK-EEALRVEEL---QNA------EFDRKlaqeevwirQGIKarrtRNEGRVRALkalrrERSER 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 303 VDAPQTytenMRLSLDIAKESGKDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTG 382
Cdd:PRK11147 299 REVMGT----AKMQVEEASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 383 EVIYGSNVSVAYYDQEHQVLHMDKTLFDEISDTYPE-MTNTRIRNILA---AFLFTGEDVYKKISDLSGGERGRVSLVKL 458
Cdd:PRK11147 375 RIHCGTKLEVAYFDQHRAELDPEKTVMDNLAEGKQEvMVNGRPRHVLGylqDFLFHPKRAMTPVKALSGGERNRLLLARL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 459 MLSKANFLLLDEPTNHLDIVSKDVLENALNSFPGTVCYVSHDRYFINKTATRILDLTENRLLN-YIGNYdyyiekREAVE 537
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGrYVGGY------HDARQ 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 538 EAANLSNIEQAQKgidvsESKQEWMDNKTAQAQKKKIKNTLNkcekeiseieselqtvdeefanpknssnvgklmeLQKQ 617
Cdd:PRK11147 529 QQAQYLALKQPAV-----KKKEEAAAPKAETVKRSSKKLSYK----------------------------------LQRE 569
|
650 660
....*....|....*....|..
gi 496028547 618 KEALEERLDKLMADWEELTLQM 639
Cdd:PRK11147 570 LEQLPQLLEDLEAEIEALQAQV 591
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-641 |
1.83e-86 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 283.21 E-value: 1.83e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 13 GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYlrqINNVDSTLSIidelyTVIEP 92
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAW---VNQETPALPQ-----PALEY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 93 ILDMEKRILKMQNEMRHLTgeklEKLYSSYTALTH-NYELMDGYAAKSKVVGILKGLGFEEADFDRKINTLSGGQKTRVF 171
Cdd:PRK10636 84 VIDGDREYRQLEAQLHDAN----ERNDGHAIATIHgKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 172 LAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNVQMYLGNYTDFSNKKQ 251
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 252 MLLDAKMKEYLNQQQEIRHQEAVITKLKQfnREKSIKRAESRQKQLEKIERVdAPQTYTENMRLSLDIAKESGKDVLSVH 331
Cdd:PRK10636 240 TRLAQQQAMYESQQERVAHLQSYIDRFRA--KATKAKQAQSRIKMLERMELI-APAHVDNPFHFSFRAPESLPNPLLKME 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 332 NLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQeHQV--LHMDKTLF 409
Cdd:PRK10636 317 KVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ-HQLefLRADESPL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 410 DEISDTYPEMTNTRIRNILAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENALNS 489
Cdd:PRK10636 396 QHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 490 FPGTVCYVSHDRYFINKTATRILDLTENRLLNYIGNYDYYIEKREAVEEAANLSNIEQAQKGidvSESKQEWMDNKTAQA 569
Cdd:PRK10636 476 FEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQENQTDEAPKENN---ANSAQARKDQKRREA 552
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 570 ----QKKKIKNTLNKCEKEISEIESELQTVDEEFANPK--NSSNVGKLME-LQKQKEALEERLDKLMAdWEELTLQMEE 641
Cdd:PRK10636 553 elrtQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSElyDQSRKAELTAcLQQQASAKSGLEECEMA-WLEAQEQLEQ 630
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
7-529 |
5.49e-75 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 254.40 E-value: 5.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILtGEEQADGgsvtLAKDAKLGYLRQINNVDSTLSIIDEL 86
Cdd:PLN03073 182 NFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYM-AMHAIDG----IPKNCQILHVEQEVVGDDTTALQCVL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 87 YTVIE--PILDMEKRILKMQNEM------------------RHLTGEKLEKLYSsytalthNYELMDGYAAKSKVVGILK 146
Cdd:PLN03073 257 NTDIErtQLLEEEAQLVAQQRELefetetgkgkgankdgvdKDAVSQRLEEIYK-------RLELIDAYTAEARAASILA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 147 GLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGAVVIVSHDRYFLDKIVS 226
Cdd:PLN03073 330 GLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVT 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 227 KVIDIENGNVQMYLGNYTDFSNKKQMLLDAKMKEYLNQQQEIRHQEAVITKLKQFNREKSIkrAESRQKQLEKIERVDA- 305
Cdd:PLN03073 410 DILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASL--VQSRIKALDRLGHVDAv 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 306 --PQTYTENMRLSLDiakESGKDVLSVHNLSKSFDRKK-LFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTG 382
Cdd:PLN03073 488 vnDPDYKFEFPTPDD---RPGPPIISFSDASFGYPGGPlLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 383 EVIYGSNVSVAYYDQEH-QVLHMDKTLFDEISDTYPEMTNTRIRNILAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLS 461
Cdd:PLN03073 565 TVFRSAKVRMAVFSQHHvDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFK 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 462 KANFLLLDEPTNHLDIVSKDVLENALNSFPGTVCYVSHDRYFINKTATRILDLTENRLLNYIGNYDYY 529
Cdd:PLN03073 645 KPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDY 712
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
330-573 |
4.18e-72 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 241.51 E-value: 4.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 330 VHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQEHQvLHMDKTLF 409
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPP-LDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 410 DEISDTYPEMT--------------------------------------NTRIRNILAAFLFTGEDVYKKISDLSGGERG 451
Cdd:COG0488 80 DTVLDGDAELRaleaeleeleaklaepdedlerlaelqeefealggweaEARAEEILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 452 RVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENALNSFPGTVCYVSHDRYFINKTATRILDLTENRLLNYIGNYDYYIE 531
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 496028547 532 KREAVEEAANLSNiEQAQKGIdvsESKQEWMDNKTAQAQKKK 573
Cdd:COG0488 240 QRAERLEQEAAAY-AKQQKKI---AKEEEFIRRFRAKARKAK 277
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-246 |
1.14e-68 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 232.65 E-value: 1.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYLRQINNVdstls 81
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEE----- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 82 iidelytviepiLDMEKRILkmqNEMRhltgekleklyssytalthnyELMDGyAAKSKVVGILKGLGFEEADFDRKINT 161
Cdd:COG0488 390 ------------LDPDKTVL---DELR---------------------DGAPG-GTEQEVRGYLGRFLFSGDDAFKPVGV 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 162 LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNVQMYLG 241
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPG 512
|
....*
gi 496028547 242 NYTDF 246
Cdd:COG0488 513 GYDDY 517
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
328-518 |
4.29e-59 |
|
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: 194.59 E-value: 4.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQehqvlhmdkt 407
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 408 lfdeisdtypemtntrirnilaaflftgedvykkisdLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENAL 487
Cdd:cd03221 71 -------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL 113
|
170 180 190
....*....|....*....|....*....|.
gi 496028547 488 NSFPGTVCYVSHDRYFINKTATRILDLTENR 518
Cdd:cd03221 114 KEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-234 |
3.33e-52 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 176.10 E-value: 3.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYLRQinnvdstlsi 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 idelytviepildmekrilkmqnemrhltgekleklyssytalthnyelmdgyaakskvvgilkglgfeeadfdrkintL 162
Cdd:cd03221 71 -------------------------------------------------------------------------------L 71
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496028547 163 SGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENG 234
Cdd:cd03221 72 SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
328-519 |
1.67e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 149.58 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVS----------VAYYD 396
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdGKPLSampppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 397 QEHQVLHMdkTLFDEISDTY----PEMTNTRIRNILAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPT 472
Cdd:COG4619 81 QEPALWGG--TVRDNLPFPFqlreRKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496028547 473 NHLDIVSKDVLENALNSFP----GTVCYVSHDRYFINKTATRILDLTENRL 519
Cdd:COG4619 159 SALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-512 |
1.40e-39 |
|
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: 152.36 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSF--GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADG---GSVTLAKDAKLGYlrqinnv 76
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLEL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 77 dstlsiidelytviePILDMEKRI-LKMQNEMRHLTGEKLEKLYssytALTHNYELMDGYAAKSKVVGILKGLGFEEAdF 155
Cdd:COG1123 77 ---------------SEALRGRRIgMVFQDPMTQLNPVTVGDQI----AEALENLGLSRAEARARVLELLEAVGLERR-L 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 156 DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD----LRSIEWLESYLLNYNGAVVIVSHDryfldkiVSKVIDI 231
Cdd:COG1123 137 DRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHD-------LGVVAEI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 232 ENGNVQMYLGnytdfsnkkQMLLDAKMKEYLNQQQeirhqeavitklkqfnreksikraesrqkQLEKIERVDAPqtyte 311
Cdd:COG1123 210 ADRVVVMDDG---------RIVEDGPPEEILAAPQ-----------------------------ALAAVPRLGAA----- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 312 nmRLSLDIAKESGKDVLSVHNLSKSFDRKKLFY-----DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY 386
Cdd:COG1123 247 --RGRAAPAAAAAEPLLEVRNLSKRYPVRGKGGvravdDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 387 G----------------SNVSVAYYDQEHQVLHMDkTLFDEISDTY-------PEMTNTRIRNILAAFLFTGEDVYKKIS 443
Cdd:COG1123 325 DgkdltklsrrslrelrRRVQMVFQDPYSSLNPRM-TVGDIIAEPLrlhgllsRAERRERVAELLERVGLPPDLADRYPH 403
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496028547 444 DLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDiVS-----KDVLENALNSFPGTVCYVSHDRYFINKTATRIL 512
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALD-VSvqaqiLNLLRDLQRELGLTYLFISHDLAVVRYIADRVA 476
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-253 |
5.96e-39 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 151.04 E-value: 5.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 5 ATNISKSFGSNEIIKSATFLInehEKAAIVGV---NGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYlrqinnVDSTLS 81
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSL---PPGGIVGIigpNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAY------VDQSRD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 82 IIDELYTVIEPI---LDmekrILKM-QNEM--RhltgekleklyssytalthnyelmdGYAAKskvvgilkgLGFEEADF 155
Cdd:PRK11819 398 ALDPNKTVWEEIsggLD----IIKVgNREIpsR-------------------------AYVGR---------FNFKGGDQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 156 DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD---LRSiewLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIE 232
Cdd:PRK11819 440 QKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDvetLRA---LEEALLEFPGCAVVISHDRWFLDRIATHILAFE 516
|
250 260
....*....|....*....|...
gi 496028547 233 -NGNVQMYLGNYTDF-SNKKQML 253
Cdd:PRK11819 517 gDSQVEWFEGNFQEYeEDKKRRL 539
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-253 |
2.06e-37 |
|
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: 146.62 E-value: 2.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLInehEKAAIVGV---NGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYlrqinnVDS 78
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKL---PPGGIVGVigpNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAY------VDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 79 TLSIIDELYTVIEPILDmekrilkmqnemrhltGEKLEKLyssytaltHNYELMD-GYAAKskvvgilkgLGFEEADFDR 157
Cdd:TIGR03719 393 SRDALDPNKTVWEEISG----------------GLDIIKL--------GKREIPSrAYVGR---------FNFKGSDQQK 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 158 KINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIE-NGNV 236
Cdd:TIGR03719 440 KVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHV 519
|
250
....*....|....*...
gi 496028547 237 QMYLGNYTDF-SNKKQML 253
Cdd:TIGR03719 520 EWFEGNFSEYeEDKKRRL 537
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
327-572 |
1.17e-35 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 141.79 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKK-LFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQEHQvLHMD 405
Cdd:PRK11819 6 IYTMNRVSKVVPPKKqILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQ-LDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 406 KTL-----------------FDEISDTY-----------PEMTntRIRNILAAFlfTGEDVYKK---------------- 441
Cdd:PRK11819 85 KTVrenveegvaevkaaldrFNEIYAAYaepdadfdalaAEQG--ELQEIIDAA--DAWDLDSQleiamdalrcppwdak 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 442 ISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENALNSFPGTVCYVSHDRYFINKTATRILDLTENRLLN 521
Cdd:PRK11819 161 VTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 522 YIGNYDYYIE---KREAVEEAAnlsniEQA-QKGIdvsESKQEW--MDNKTAQAQKK 572
Cdd:PRK11819 241 WEGNYSSWLEqkaKRLAQEEKQ-----EAArQKAL---KRELEWvrQSPKARQAKSK 289
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-249 |
5.72e-35 |
|
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: 132.67 E-value: 5.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVtlakdaklgylrQINNVDStlsi 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSI------------LIDGEDV---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 idelytVIEPILDMEK-RILKMQNEMR-HLTGEKleklYSSYTALTHNyelMDGYAAKSKVVGILKGLGFEEaDFDRKIN 160
Cdd:COG4555 66 ------RKEPREARRQiGVLPDERGLYdRLTVRE----NIRYFAELYG---LFDEELKKRIEELIELLGLEE-FLDRRVG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 161 TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNY---NGAVVIVSHDRYFLDKIVSKVIDIENGNVQ 237
Cdd:COG4555 132 ELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKVV 211
|
250
....*....|..
gi 496028547 238 mYLGNYTDFSNK 249
Cdd:COG4555 212 -AQGSLDELREE 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-510 |
7.47e-35 |
|
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: 138.78 E-value: 7.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQ--ADGGSVT--LAKDAKLGYL-------RQINN 75
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhVALCEKCGYVerpskvgEPCPV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 76 VDSTLSIID-ELYTVIEPIL-DMEKRILKMQNEMRHLTGEKleklyssyTALTHNYELMD--GYAAKSKVVGILKGLgfE 151
Cdd:TIGR03269 85 CGGTLEPEEvDFWNLSDKLRrRIRKRIAIMLQRTFALYGDD--------TVLDNVLEALEeiGYEGKEAVGRAVDLI--E 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 152 EADFDRKI----NTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLL----NYNGAVVIVSHDRYFLDK 223
Cdd:TIGR03269 155 MVQLSHRIthiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeavkASGISMVLTSHWPEVIED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 224 IVSKVIDIENGNVQMyLGNYTDFSNKkqmlldakmkeYLNQQQEIRHQEAVitklkqfnreksikraesrqkqlekierv 303
Cdd:TIGR03269 235 LSDKAIWLENGEIKE-EGTPDEVVAV-----------FMEGVSEVEKECEV----------------------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 304 dapqtytenmrlsldiakESGKDVLSVHNLSK---SFDRK--KLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILE 378
Cdd:TIGR03269 274 ------------------EVGEPIIKVRNVSKryiSVDRGvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 379 PDTGEViygsNVSVA--YYDQEHQ-------------VLHMDKTLF----------DEISDTYP-EMTNTRIRNILAAFL 432
Cdd:TIGR03269 336 PTSGEV----NVRVGdeWVDMTKPgpdgrgrakryigILHQEYDLYphrtvldnltEAIGLELPdELARMKAVITLKMVG 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 433 FT---GEDVYKKISD-LSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSK-DVLENALNS---FPGTVCYVSHDRYFI 504
Cdd:TIGR03269 412 FDeekAEEILDKYPDeLSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKvDVTHSILKAreeMEQTFIIVSHDMDFV 491
|
....*.
gi 496028547 505 NKTATR 510
Cdd:TIGR03269 492 LDVCDR 497
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
327-516 |
2.95e-34 |
|
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: 129.52 E-value: 2.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVS---VAYYDQEHQVL 402
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWnGEPIRdarEDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 403 HMDktlfdeisDTYPEMT-----------------NTRIRNILAAFLFTG-EDvyKKISDLSGGERGRVSLVKLMLSKAN 464
Cdd:COG4133 82 HAD--------GLKPELTvrenlrfwaalyglradREAIDEALEAVGLAGlAD--LPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 465 FLLLDEPTNHLDIVSKDVLENALNSFP---GTVCYVSHDRYFInkTATRILDLTE 516
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLEL--AAARVLDLGD 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-225 |
5.07e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.13 E-value: 5.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL------AKDAKLGYLRQIN 74
Cdd:COG1121 5 PAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 75 NVDSTLSIidelyTVIEPILdmekrilkmqneMRHLTGEKLEKLYSSytalthnyelmdgyAAKSKVVGILK--GLgfee 152
Cdd:COG1121 85 EVDWDFPI-----TVRDVVL------------MGRYGRRGLFRRPSR--------------ADREAVDEALErvGL---- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 153 ADF-DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNG-AVVIVSHD-----RYFlDK 223
Cdd:COG1121 130 EDLaDRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLreLRREGkTILVVTHDlgavrEYF-DR 208
|
..
gi 496028547 224 IV 225
Cdd:COG1121 209 VL 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
328-512 |
1.39e-32 |
|
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: 123.66 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVSvayyDQEHQVLHMDK 406
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkVLGKDIK----KEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 407 TLFDEISdTYPEMtntrirnilaaflfTGEDVYKkisdLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENA 486
Cdd:cd03230 77 YLPEEPS-LYENL--------------TVRENLK----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWEL 137
|
170 180
....*....|....*....|....*....
gi 496028547 487 LNSF---PGTVCYVSHDRYFINKTATRIL 512
Cdd:cd03230 138 LRELkkeGKTILLSSHILEEAERLCDRVA 166
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-233 |
4.79e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 120.28 E-value: 4.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL----AKDAKLGYLRQINNV 76
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngepIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 77 DSTLSIIDELyTVIEpILDMEKRILKMqnemrHLTGEKLEklyssytalthnyELMDgyaakskVVGILkglGFEeadfD 156
Cdd:COG4133 81 GHADGLKPEL-TVRE-NLRFWAALYGL-----RADREAID-------------EALE-------AVGLA---GLA----D 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 157 RKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYN---GAVVIVSHDRYFLDKIvsKVIDIEN 233
Cdd:COG4133 127 LPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA--RVLDLGD 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
329-518 |
5.61e-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: 118.50 E-value: 5.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 329 SVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVSvayydqehqvlhmdkt 407
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIlIDGKDIA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 408 lfdeisdtypEMTNTRIRNILAAflftgedvykkISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENAL 487
Cdd:cd00267 65 ----------KLPLEELRRRIGY-----------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELL 123
|
170 180 190
....*....|....*....|....*....|....
gi 496028547 488 NSFPG---TVCYVSHDRYFINKTATRILDLTENR 518
Cdd:cd00267 124 RELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
327-548 |
6.72e-31 |
|
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: 121.12 E-value: 6.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYgSNVSVAYYDQEHQ----VL 402
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI-DGEDVRKEPREARrqigVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 403 HMDKTLFD------------EISDTYPEMTNTRIRNILAAFLFtGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDE 470
Cdd:COG4555 80 PDERGLYDrltvreniryfaELYGLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 471 PTNHLDIVSKDVLENALNSF---PGTVCYVSHDRYFINKTATRILDLTENRLLnyignydyYIEKREAVEEAANLSNIEQ 547
Cdd:COG4555 159 PTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKVV--------AQGSLDELREEIGEENLED 230
|
.
gi 496028547 548 A 548
Cdd:COG4555 231 A 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
329-512 |
1.24e-30 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 119.11 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 329 SVHNLSKSFDR--KKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-------------GSNVSVA 393
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdgkdltklslkelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 394 YYDQEHQVLHMdkTLFDEIS------DTYPEMTNTRIRNILAAFLFTG-EDvyKKISDLSGGERGRVSLVKLMLSKANFL 466
Cdd:cd03225 81 FQNPDDQFFGP--TVEEEVAfglenlGLPEEEIEERVEEALELVGLEGlRD--RSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496028547 467 LLDEPTNHLDIVSKDVLENALNSFPG---TVCYVSHDRYFINKTATRIL 512
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVI 205
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-225 |
2.29e-30 |
|
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: 119.76 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL-------------AKdaKLG 68
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgrdlaslsrrelAR--RIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 69 YLRQINNVDSTLsiidelyTVIEpildmekrILKM-----QNEMRHLTGEKLEKLYSsytALthnyelmdgyaaksKVVG 143
Cdd:COG1120 79 YVPQEPPAPFGL-------TVRE--------LVALgryphLGLFGRPSAEDREAVEE---AL--------------ERTG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 144 IlkglgfeeADF-DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS-IEWLEsyLL-----NYNGAVVIVSH 216
Cdd:COG1120 127 L--------EHLaDRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHqLEVLE--LLrrlarERGRTVVMVLH 196
|
250
....*....|....
gi 496028547 217 D-----RYFlDKIV 225
Cdd:COG1120 197 DlnlaaRYA-DRLV 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-512 |
3.07e-30 |
|
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: 125.67 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 32 AIVGVNGAGKTTLLKILTGEEQADGGSVT--LAKDAKLGYLRQInnvdstlsiidELYTVIEPILDMEKRI-LKMQNEmr 108
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKPNLGDYDeePSWDEVLKRFRGT-----------ELQDYFKKLANGEIKVaHKPQYV-- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 109 hltgEKLEKLYSSYTAlthnyELMDGYAAKSKVVGILKGLGFEEAdFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEP 188
Cdd:COG1245 170 ----DLIPKVFKGTVR-----ELLEKVDERGKLDELAEKLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 189 TNHLDLRsiEWLESY-----LLNYNGAVVIVSHDRYFLDKIvSKVIDIengnvqMY--LGNYTDFSNKKQMlldakmKEY 261
Cdd:COG1245 240 SSYLDIY--QRLNVArlireLAEEGKYVLVVEHDLAILDYL-ADYVHI------LYgePGVYGVVSKPKSV------RVG 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 262 LNQQqeirhqeavitkLKQFNREKSIKraeSRQkqlEKIE-RVDAPQTYTEnmrlsldiakesGKDVLSVHNLSKSFDRK 340
Cdd:COG1245 305 INQY------------LDGYLPEENVR---IRD---EPIEfEVHAPRREKE------------EETLVEYPDLTKSYGGF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 341 KLFYDINfEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIygSNVSVAY---Y---DQEHQVlhmDKTLFDEISD 414
Cdd:COG1245 355 SLEVEGG-EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKISYkpqYispDYDGTV---EEFLRSANTD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 415 TYPE-MTNTRIRNILAAflftgEDVY-KKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDI-----VSKdVLENAL 487
Cdd:COG1245 429 DFGSsYYKTEIIKPLGL-----EKLLdKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlaVAK-AIRRFA 502
|
490 500
....*....|....*....|....*
gi 496028547 488 NSFPGTVCYVSHDRYFINKTATRIL 512
Cdd:COG1245 503 ENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
327-512 |
7.73e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.88 E-value: 7.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS-----VAYYDQEHQ 400
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrLFGKPPRrarrrIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 401 VlhmDK----TLFDEI-SDTYPEMTNTRIRN------ILAAFLFTG-EDVYKK-ISDLSGGERGRVSLVKLMLSKANFLL 467
Cdd:COG1121 86 V---DWdfpiTVRDVVlMGRYGRRGLFRRPSradreaVDEALERVGlEDLADRpIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496028547 468 LDEPTNHLDIVSKDVLEN---ALNSFPGTVCYVSHDRYFINKTATRIL 512
Cdd:COG1121 163 LDEPFAGVDAATEEALYEllrELRREGKTILVVTHDLGAVREYFDRVL 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-236 |
1.12e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.45 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDA-----------KLGYLR 71
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 72 QinnvdstlsiidelytviEPILdMEKRIlkmqnemrhltgekleklyssYTALTHNYELMDGYAAKSKVVGILKGLGFE 151
Cdd:COG4619 81 Q------------------EPAL-WGGTV---------------------RDNLPFPFQLRERKFDRERALELLERLGLP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 152 EADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS----IEWLESYLLNYNGAVVIVSHDRYFLDKIVSK 227
Cdd:COG4619 121 PDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADR 200
|
....*....
gi 496028547 228 VIDIENGNV 236
Cdd:COG4619 201 VLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-236 |
1.13e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 117.47 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-KD---------AKLGYLRQ 72
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgEDvardpaevrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 73 INNVDSTLsiidelyTVIEpildmekrILKMQNEMRHltgekleklyssytalthnyelMDGYAAKSKVVGILKGLGFEE 152
Cdd:COG1131 81 EPALYPDL-------TVRE--------NLRFFARLYG----------------------LPRKEARERIDELLELFGLTD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 153 AdFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNG---AVVIVSHDRYFLDKIVSKVI 229
Cdd:COG1131 124 A-ADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVA 202
|
....*..
gi 496028547 230 DIENGNV 236
Cdd:COG1131 203 IIDKGRI 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
328-520 |
5.97e-29 |
|
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: 115.12 E-value: 5.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSF-DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVSVAYYDQ-------- 397
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdGKDITKKNLRElrrkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 398 ----EHQVLHMdkTLFDEISdtY--------PEMTNTRIRNILAAFlftG-EDVYKK-ISDLSGGERGRVSLVKLMLSKA 463
Cdd:COG1122 81 fqnpDDQLFAP--TVEEDVA--FgpenlglpREEIRERVEEALELV---GlEHLADRpPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 464 NFLLLDEPTNHLDIVSKDVLENALNSFPG---TVCYVSHDRYFINKTATRILDLTENRLL 520
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-236 |
6.86e-29 |
|
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: 114.55 E-value: 6.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 5 ATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA------KDAKLGYLRQINNVDS 78
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgkplekERKRIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 79 TLSIidelyTVIEPILdmekrilkmqnemrhltgekleklyssyTALTHNYELMDGY--AAKSKVVGILKGLGFEeaDF- 155
Cdd:cd03235 82 DFPI-----SVRDVVL----------------------------MGLYGHKGLFRRLskADKAKVDEALERVGLS--ELa 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 156 DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNG-AVVIVSHDRYFLDKIVSKVIDIE 232
Cdd:cd03235 127 DRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLreLRREGmTILVVTHDLGLVLEYFDRVLLLN 206
|
....
gi 496028547 233 NGNV 236
Cdd:cd03235 207 RTVV 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-512 |
1.61e-28 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 120.68 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 33 IVGVNGAGKTTLLKILTGEEQADggsvtlakdakLGylrqinNVDSTLS---IID-----ELYTVIEPILDMEKR-ILKM 103
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELIPN-----------LG------DYEEEPSwdeVLKrfrgtELQNYFKKLYNGEIKvVHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 104 QNEmrhltgEKLEKLYSSYTAlthnyELMDGYAAKSKVVGILKGLGFEEAdFDRKINTLSGGQKTRVFLAKLLLEEPDII 183
Cdd:PRK13409 167 QYV------DLIPKVFKGKVR-----ELLKKVDERGKLDEVVERLGLENI-LDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 184 LLDEPTNHLDL-------RSIEWLESyllnyNGAVVIVSHDRYFLDKIvSKVIDIengnvqMY--LGNYTDFSNKKqmll 254
Cdd:PRK13409 235 FFDEPTSYLDIrqrlnvaRLIRELAE-----GKYVLVVEHDLAVLDYL-ADNVHI------AYgePGAYGVVSKPK---- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 255 daKMKEYLNQQqeirhqeavitkLKQFNREKSIKraeSRQKQLEKIERvdAPQTytenmrlsldiaKESGKDVLSVHNLS 334
Cdd:PRK13409 299 --GVRVGINEY------------LKGYLPEENMR---IRPEPIEFEER--PPRD------------ESERETLVEYPDLT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 335 KSFDRKKLFYDiNFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEViyGSNVSVAY---Y---DQEHQVLHMDKTL 408
Cdd:PRK13409 348 KKLGDFSLEVE-GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYkpqYikpDYDGTVEDLLRSI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 409 FDEISDTY--PEMTNT-RIRNILAaflftgedvyKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDI-----VSK 480
Cdd:PRK13409 425 TDDLGSSYykSEIIKPlQLERLLD----------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlaVAK 494
|
490 500 510
....*....|....*....|....*....|..
gi 496028547 481 dVLENALNSFPGTVCYVSHDRYFINKTATRIL 512
Cdd:PRK13409 495 -AIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-236 |
4.11e-28 |
|
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: 110.99 E-value: 4.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 5 ATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKdaklgylrqinnvdstlsiid 84
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG--------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 85 elytviEPILDMEKRILKmqnemRHLtgekleklysSY--TALthnyelmdgyaaksKVVGIlkglgfeeADF-DRKINT 161
Cdd:cd03214 61 ------KDLASLSPKELA-----RKI----------AYvpQAL--------------ELLGL--------AHLaDRPFNE 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 162 LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS----IEWLESYLLNYNGAVVIVSHD-----RYFldkivSKVIDIE 232
Cdd:cd03214 98 LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHqielLELLRRLARERGKTVVMVLHDlnlaaRYA-----DRVILLK 172
|
....
gi 496028547 233 NGNV 236
Cdd:cd03214 173 DGRI 176
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
327-520 |
4.75e-28 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 113.21 E-value: 4.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVS----------VAYY 395
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLAslsrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 396 DQEHQVlHMDKTLFD---------------------EISDTYPEMTNtrirniLAAFlftgedVYKKISDLSGGERGRVS 454
Cdd:COG1120 81 PQEPPA-PFGLTVRElvalgryphlglfgrpsaedrEAVEEALERTG------LEHL------ADRPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 455 LVKLMLSKANFLLLDEPTNHLDIVSK-DVLE--NALNSFPG-TVCYVSHD-----RYfinktATRILDLTENRLL 520
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQlEVLEllRRLARERGrTVVMVLHDlnlaaRY-----ADRLVLLKDGRIV 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
328-520 |
5.75e-28 |
|
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: 111.84 E-value: 5.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS--------VAYYDQE 398
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlIDGRDVTgvpperrnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 399 HQVL-HMdkTLFDEISdtYP--------EMTNTRIRNILAAFLFTGEdVYKKISDLSGGERGRVSLVKLMLSKANFLLLD 469
Cdd:cd03259 81 YALFpHL--TVAENIA--FGlklrgvpkAEIRARVRELLELVGLEGL-LNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 470 EPTNHLDIVSKDVLENAL----NSFPGTVCYVSHDRYFINKTATRILDLTENRLL 520
Cdd:cd03259 156 EPLSALDAKLREELREELkelqRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
345-473 |
7.68e-28 |
|
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: 109.27 E-value: 7.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYG-----------SNVSVAYYDQEHQVLhMDKTLFDEI- 412
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQDPQLF-PRLTVRENLr 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 413 --------SDTYPEMTNTRIRNILAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTN 473
Cdd:pfam00005 82 lglllkglSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-236 |
8.71e-28 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 109.79 E-value: 8.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqINNVDstlsi 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK------------VLGKD----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 idelytVIEPILDMEKRILKMQNEMRhltgeklekLYSSYTAlthnYELMDgyaakskvvgilkglgfeeadfdrkintL 162
Cdd:cd03230 64 ------IKKEPEEVKRRIGYLPEEPS---------LYENLTV----RENLK----------------------------L 96
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 163 SGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYN---GAVVIVSHDRYFLDKIVSKVIDIENGNV 236
Cdd:cd03230 97 SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
329-500 |
1.28e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 109.83 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 329 SVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS----------VAYYdq 397
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlLDGKDLAslspkelarkIAYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 398 eHQVLhmdktlfdeisdtypEMTNtrirniLAAFLftgedvYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDI 477
Cdd:cd03214 79 -PQAL---------------ELLG------LAHLA------DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180
....*....|....*....|....*..
gi 496028547 478 VSK-DVLE--NALN-SFPGTVCYVSHD 500
Cdd:cd03214 131 AHQiELLEllRRLArERGKTVVMVLHD 157
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
328-500 |
2.54e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.54 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS---------VAYYDQ 397
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrVLGEDVArdpaevrrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 398 EHqVLHMDKT------LFDEISDTYPEMTNTRIRNILAAF-LftGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDE 470
Cdd:COG1131 81 EP-ALYPDLTvrenlrFFARLYGLPRKEARERIDELLELFgL--TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190
....*....|....*....|....*....|...
gi 496028547 471 PTNHLDIVSKDVLENALNSFPG---TVCYVSHD 500
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAegkTVLLSTHY 190
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
328-518 |
2.41e-26 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 105.54 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFD--RKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGsNVSVAYYDQEHqvlhmd 405
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID-GVDLRDLDLES------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 406 ktlfdeisdtypemtntrIRNILA-----AFLFTGeDVYKKIsdLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSK 480
Cdd:cd03228 74 ------------------LRKNIAyvpqdPFLFSG-TIRENI--LSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496028547 481 DVLENALNSFPG--TVCYVSHdRYFINKTATRILDLTENR 518
Cdd:cd03228 133 ALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-305 |
2.70e-26 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 113.89 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVtlakdaKLGYLRQINNVDSTL 80
Cdd:PRK11147 318 IVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------HCGTKLEVAYFDQHR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 SIIDELYTVIEPILDMEKRIlkMQN-EMRHLTGEKLEKLYSSYTALThnyelmdgyaakskvvgilkglgfeeadfdrKI 159
Cdd:PRK11147 392 AELDPEKTVMDNLAEGKQEV--MVNgRPRHVLGYLQDFLFHPKRAMT-------------------------------PV 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 160 NTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIE-NGNVQM 238
Cdd:PRK11147 439 KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIGR 518
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 239 YLGNYTDfsNKKQmlldaKMKEYLNQQQEIRHQEAVITKLKQFNREKSIKRAESRQKQLE----KIERVDA 305
Cdd:PRK11147 519 YVGGYHD--ARQQ-----QAQYLALKQPAVKKKEEAAAPKAETVKRSSKKLSYKLQRELEqlpqLLEDLEA 582
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-234 |
5.96e-26 |
|
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: 106.01 E-value: 5.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNE--IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-KDAKLGYLRQIN--------N 75
Cdd:cd03225 4 NLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgKDLTKLSLKELRrkvglvfqN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 76 VDS---TLSIIDELytviepildmekrILKMQNemRHLTGEKLEKlyssytalthnyelmdgyaaksKVVGILKGLGFEE 152
Cdd:cd03225 84 PDDqffGPTVEEEV-------------AFGLEN--LGLPEEEIEE----------------------RVEEALELVGLEG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 153 ADfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGA---VVIVSHDRYFLDKIVSKVI 229
Cdd:cd03225 127 LR-DRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLELADRVI 205
|
....*
gi 496028547 230 DIENG 234
Cdd:cd03225 206 VLEDG 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
328-512 |
1.97e-25 |
|
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: 103.42 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGsnvsvayydqehqvlhmDKT 407
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-----------------GED 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 408 LFDEISDTYPEmtNTRIRNILAAF-LFTGEDVYKKIS-DLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLEN 485
Cdd:cd03229 64 LTDLEDELPPL--RRRIGMVFQDFaLFPHLTVLENIAlGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRA 141
|
170 180 190
....*....|....*....|....*....|.
gi 496028547 486 ALNS----FPGTVCYVSHDRYFINKTATRIL 512
Cdd:cd03229 142 LLKSlqaqLGITVVLVTHDLDEAARLADRVV 172
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
297-533 |
3.02e-25 |
|
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: 111.08 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 297 LEKIERV-DAPqtyTENMRLSLDIAKESGKDVLSVHNLSKSF--DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKII 373
Cdd:COG2274 445 LERLDDIlDLP---PEREEGRSKLSLPRLKGDIELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 374 NGILEPDTGEVIY-GSNV----------SVAYYDQEHQVLHMdkTLFDEISDTYPEMTNTRIRNI--LAAFLftgEDVYK 440
Cdd:COG2274 522 LGLYEPTSGRILIdGIDLrqidpaslrrQIGVVLQDVFLFSG--TIRENITLGDPDATDEEIIEAarLAGLH---DFIEA 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 441 -------KISD----LSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENALNSFPG--TVCYVSHDRYFINKt 507
Cdd:COG2274 597 lpmgydtVVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL- 675
|
250 260
....*....|....*....|....*.
gi 496028547 508 ATRILDLTENRLLNyIGNYDYYIEKR 533
Cdd:COG2274 676 ADRIIVLDKGRIVE-DGTHEELLARK 700
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
328-520 |
3.08e-25 |
|
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: 104.51 E-value: 3.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVSVAyydQEHQVLHMDK 406
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlIDGEDISGL---SEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 407 ---------------TLFDEISdtYP--EMTN---TRIRNILAAFL-FTG--EDVYKKISDLSGGERGRVSLVKLMLSKA 463
Cdd:cd03261 78 rmgmlfqsgalfdslTVFENVA--FPlrEHTRlseEEIREIVLEKLeAVGlrGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 464 NFLLLDEPTNHLDIVSKDVLENALNS----FPGTVCYVSHDRYFINKTATRILDLTENRLL 520
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSlkkeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
328-514 |
3.78e-25 |
|
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: 104.89 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSF----DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVSVAYY-DQEHQV 401
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdGRPVTRRRRkAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 402 ----------LHMDKTLFDEISDTYPEMTNTRIRNILAAFLftgEDV-------YKKISDLSGGERGRVSLVKLMLSKAN 464
Cdd:COG1124 82 qmvfqdpyasLHPRHTVDRILAEPLRIHGLPDREERIAELL---EQVglppsflDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 465 FLLLDEPTNHLD-IVSKDVLeNALNS----FPGTVCYVSHDRYFINKTATRILDL 514
Cdd:COG1124 159 LLLLDEPTSALDvSVQAEIL-NLLKDlreeRGLTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
329-500 |
4.41e-25 |
|
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: 103.38 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 329 SVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS-----VAYYDQEHQVL 402
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrVFGKPLEkerkrIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 403 H-MDKTLFDEIS-DTYPEM------TNTRIRNILAAFLFTGEDVYKK--ISDLSGGERGRVSLVKLMLSKANFLLLDEPT 472
Cdd:cd03235 81 RdFPISVRDVVLmGLYGHKglfrrlSKADKAKVDEALERVGLSELADrqIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190
....*....|....*....|....*....|.
gi 496028547 473 NHLDIVS-KDVLE--NALNSFPGTVCYVSHD 500
Cdd:cd03235 161 AGVDPKTqEDIYEllRELRREGMTILVVTHD 191
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
327-519 |
1.71e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 102.05 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKL-FYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVS------VAYY--- 395
Cdd:COG2884 1 MIRFENVSKRYPGGREaLSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVnGQDLSrlkrreIPYLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 396 ----DQEHQVLhMDKTLFD------EISDTYPEMTNTRIRNILA-------AFLFTGEdvykkisdLSGGERGRVSLVKL 458
Cdd:COG2884 81 igvvFQDFRLL-PDRTVYEnvalplRVTGKSRKEIRRRVREVLDlvglsdkAKALPHE--------LSGGEQQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496028547 459 MLSKANFLLLDEPTNHLD-IVSKDVLE--NALNSFPGTVCYVSHDRYFINKTATRILDLTENRL 519
Cdd:COG2884 152 LVNRPELLLADEPTGNLDpETSWEIMEllEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-236 |
2.20e-24 |
|
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: 101.80 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSN----EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-------KDAKLGYLR 71
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisklSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 72 --QINNVDSTLSIIDELyTVIEPILdmekriLKMqnemrHLTGEKLEKlyssytalthnyelmdgyaAKSKVVGILKGLG 149
Cdd:cd03255 81 rrHIGFVFQSFNLLPDL-TALENVE------LPL-----LLAGVPKKE-------------------RRERAEELLERVG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 150 FEEAdFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS----IEWLESYLLNYNGAVVIVSHDRyFLDKIV 225
Cdd:cd03255 130 LGDR-LNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP-ELAEYA 207
|
250
....*....|.
gi 496028547 226 SKVIDIENGNV 236
Cdd:cd03255 208 DRIIELRDGKI 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-190 |
2.64e-24 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 99.26 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 18 IKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDA-----------KLGYLRQINNVDSTLSIIDEL 86
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrkEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 87 YTViepildmekriLKMQNEMRHLTGEKLEKlyssytalthnyelmdgyaakskvvgILKGLGFEEAD---FDRKINTLS 163
Cdd:pfam00005 81 RLG-----------LLLKGLSKREKDARAEE--------------------------ALEKLGLGDLAdrpVGERPGTLS 123
|
170 180
....*....|....*....|....*..
gi 496028547 164 GGQKTRVFLAKLLLEEPDIILLDEPTN 190
Cdd:pfam00005 124 GGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
327-512 |
3.60e-24 |
|
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: 101.43 E-value: 3.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFY----DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYgsnvsvayydQEHQVL 402
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkaldDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIF----------DGKDLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 403 HMDKTLFD----EIS----DTY----PEMT----------------NTRIRNILAAFLFTG----EDVYKK-ISDLSGGE 449
Cdd:cd03257 71 KLSRRLRKirrkEIQmvfqDPMsslnPRMTigeqiaeplrihgklsKKEARKEAVLLLLVGvglpEEVLNRyPHELSGGQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 450 RGRVSLVKLMLSKANFLLLDEPTNHLDIVSK----DVLENALNSFPGTVCYVSHDRYFINKTATRIL 512
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQaqilDLLKKLQEELGLTLLFITHDLGVVAKIADRVA 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-234 |
5.41e-24 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 98.47 E-value: 5.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 5 ATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqINNVDSTLSIID 84
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL------------IDGKDIAKLPLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 85 ELytviepildmEKRIlkmqnemrhltgekleklyssytalthnyelmdGYaakskvvgilkglgfeeadfdrkINTLSG 164
Cdd:cd00267 70 EL----------RRRI---------------------------------GY-----------------------VPQLSG 83
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 165 GQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNG---AVVIVSHDRYFLDKIVSKVIDIENG 234
Cdd:cd00267 84 GQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
323-519 |
6.06e-24 |
|
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: 106.38 E-value: 6.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 323 SGKDVLSVHNLSKSF-DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS--------- 391
Cdd:COG4988 332 AGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlINGVDLSdldpaswrr 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 392 -VAYYDQEHQVLHMdkTLFDEISDTYPEMTNTRIRNILAA-----FLFTGEDVYK-KISD----LSGGERGRVSLVKLML 460
Cdd:COG4988 412 qIAWVPQNPYLFAG--TIRENLRLGRPDASDEELEAALEAagldeFVAALPDGLDtPLGEggrgLSGGQAQRLALARALL 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 461 SKANFLLLDEPTNHLDIVSKDVLENALNSFPG--TVCYVSHDRYFINKtATRILDLTENRL 519
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALLAQ-ADRILVLDDGRI 549
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
327-511 |
9.43e-24 |
|
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: 100.44 E-value: 9.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGsNVSVAYYDQEHQVLHMDK 406
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-GQDITGLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 407 T--------LFDEIS---------DTYPEMTNTRIRNI----LAAFlftG-EDVYKK-ISDLSGGERGRVSLVKLMLSKA 463
Cdd:COG1127 84 IgmlfqggaLFDSLTvfenvafplREHTDLSEAEIRELvlekLELV---GlPGAADKmPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496028547 464 NFLLLDEPTNHLDIVSKDVLEN---ALN-SFPGTVCYVSHDRYFINKTATRI 511
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDElirELRdELGLTSVVVTHDLDSAFAIADRV 212
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
330-520 |
1.99e-23 |
|
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: 99.33 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 330 VHNLSKSFDR-----------KKLFY----------DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGS 388
Cdd:cd03267 3 VSNLSKSYRVyskepgligslKSLFKrkyrevealkGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 389 NVSvayYDQEHQVLHM------DKT-------------LFDEISDTYPEMTNTRIRNiLAAFLFTGEDVYKKISDLSGGE 449
Cdd:cd03267 83 LVP---WKRRKKFLRRigvvfgQKTqlwwdlpvidsfyLLAAIYDLPPARFKKRLDE-LSELLDLEELLDTPVRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 450 RGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENALNSF----PGTVCYVSHDRYFINKTATRILDLTENRLL 520
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-234 |
2.00e-23 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 98.48 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFG-SNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKdaklgylRQINNVDSTLSIide 85
Cdd:cd03226 4 NISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-------KPIKAKERRKSI--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 86 lYTViepildmekrilkMQNEMRHLTGE--KLEKLYSsytalthnyeLMDGYAAKSKVVGILKGLGFEEADfDRKINTLS 163
Cdd:cd03226 74 -GYV-------------MQDVDYQLFTDsvREELLLG----------LKELDAGNEQAETVLKDLDLYALK-ERHPLSLS 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 164 GGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIE----WLESyLLNYNGAVVIVSHDRYFLDKIVSKVIDIENG 234
Cdd:cd03226 129 GGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMErvgeLIRE-LAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
328-500 |
3.06e-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: 98.31 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFD----RKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY------GSNVSVAYYDQ 397
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 398 EHQVLH----MDKTLFD-EISDTYPEMTNTRIRNILAAFLFTG-EDVYkkISDLSGGERGRVSLVKLMLSKANFLLLDEP 471
Cdd:cd03293 81 QDALLPwltvLDNVALGlELQGVPKAEARERAEELLELVGLSGfENAY--PHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190
....*....|....*....|....*....|...
gi 496028547 472 TNHLDIVSK----DVLENALNSFPGTVCYVSHD 500
Cdd:cd03293 159 FSALDALTReqlqEELLDIWRETGKTVLLVTHD 191
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-480 |
3.25e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.56 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAkdaklGYLRQINNV-DST 79
Cdd:COG1129 3 PLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD-----GEPVRFRSPrDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 80 ----------LSIIDELyTVIEPI-LDMEKRILKM--QNEMRHLTGEkleklyssytalthnyelmdgyaakskvvgILK 146
Cdd:COG1129 78 aagiaiihqeLNLVPNL-SVAENIfLGREPRRGGLidWRAMRRRARE------------------------------LLA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 147 GLGFEEaDFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLesyllnYN--------G-AVVIVSHd 217
Cdd:COG1129 127 RLGLDI-DPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERL------FRiirrlkaqGvAIIYISH- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 218 ryFLD---KIVSKVIDIENGnvqmylgnytdfsnkkQMLLDAKMKEyLNQQQEIRHqeavIT--KLKQFNREKsikraes 292
Cdd:COG1129 199 --RLDevfEIADRVTVLRDG----------------RLVGTGPVAE-LTEDELVRL----MVgrELEDLFPKR------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 293 rqkqlekiervdapqtytenmrlsldiAKESGKDVLSVHNLSksfdRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKI 372
Cdd:COG1129 249 ---------------------------AAAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARA 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 373 INGILEPDTGEVIYG------------------------------------SNVSVAYYDQEHQVLHMDKTLFDEISDTY 416
Cdd:COG1129 298 LFGADPADSGEIRLDgkpvrirsprdairagiayvpedrkgeglvldlsirENITLASLDRLSRGGLLDRRRERALAEEY 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496028547 417 peMTNTRIRnilaaflfTGeDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSK 480
Cdd:COG1129 378 --IKRLRIK--------TP-SPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAK 430
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
32-217 |
3.29e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.30 E-value: 3.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 32 AIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYLRQINNVDSTLSIidelyTVIEpILDM---EKRILkmqneMR 108
Cdd:NF040873 22 AVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPL-----TVRD-LVAMgrwARRGL-----WR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 109 HLTGEkleklyssytalthnyelmdgyaAKSKVVGILKGLGFeeADF-DRKINTLSGGQKTRVFLAKLLLEEPDIILLDE 187
Cdd:NF040873 91 RLTRD-----------------------DRAAVDDALERVGL--ADLaGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|...
gi 496028547 188 PTNHLDLRSIEWLESYLLNYNG---AVVIVSHD 217
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
328-518 |
6.31e-23 |
|
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: 98.02 E-value: 6.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSF-DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVSVAYYDQEHQVLHMD 405
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 406 KTLFDEISDTyPEMtnTRIRNILAAFL------------FTGED----------------VYKKISDLSGGERGRVSLVK 457
Cdd:cd03256 81 GMIFQQFNLI-ERL--SVLENVLSGRLgrrstwrslfglFPKEEkqralaalervglldkAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 458 LMLSKANFLLLDEPTNHLD-IVSKDVLE--NALNSFPGTVCYVS-HDRYFINKTATRILDLTENR 518
Cdd:cd03256 158 ALMQQPKLILADEPVASLDpASSRQVMDllKRINREEGITVIVSlHQVDLAREYADRIVGLKDGR 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
328-519 |
6.53e-23 |
|
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: 102.92 E-value: 6.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFD--RKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGsNVSVAYYDQEHQ----- 400
Cdd:COG4987 334 LELEDVSFRYPgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG-GVDLRDLDEDDLrrria 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 401 VLHMDKTLFDeisDTY--------PEMTNTRIRNILAA-----FLFT---------GEDVYKkisdLSGGERGRVSLVKL 458
Cdd:COG4987 413 VVPQRPHLFD---TTLrenlrlarPDATDEELWAALERvglgdWLAAlpdgldtwlGEGGRR----LSGGERRRLALARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 459 MLSKANFLLLDEPTNHLDIVS-KDVLENALNSFPG-TVCYVSHDRYFINKtATRILDLTENRL 519
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATeQALLADLLEALAGrTVLLITHRLAGLER-MDRILVLEDGRI 547
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-225 |
1.02e-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: 97.19 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSF----GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYLRQINNVd 77
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 78 stlsiidelytviepildMEKRI-LKMQNEMRHLT-----GEKLEKlyssytALTHNYELMDGYAAKSKVVGILKGLGFE 151
Cdd:cd03257 80 ------------------RRKEIqMVFQDPMSSLNprmtiGEQIAE------PLRIHGKLSKKEARKEAVLLLLVGVGLP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 152 EADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDlRSIEWLESYLL-----NYNGAVVIVSHD----RYFLD 222
Cdd:cd03257 136 EEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALD-VSVQAQILDLLkklqeELGLTLLFITHDlgvvAKIAD 214
|
...
gi 496028547 223 KIV 225
Cdd:cd03257 215 RVA 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-234 |
1.13e-22 |
|
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: 97.57 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGS----NEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-----KDAKLGYLRQI 73
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDgrpvtRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 74 NNV--DSTLSI-----IDElyTVIEPIldmekRILKMQNEMRhltgekleklyssytalthnyelmdgyaaksKVVGILK 146
Cdd:COG1124 82 QMVfqDPYASLhprhtVDR--ILAEPL-----RIHGLPDREE-------------------------------RIAELLE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 147 GLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDL----RSIEWLESYLLNYNGAVVIVSHDRYFLD 222
Cdd:COG1124 124 QVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVA 203
|
250
....*....|..
gi 496028547 223 KIVSKVIDIENG 234
Cdd:COG1124 204 HLCDRVAVMQNG 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
329-517 |
2.01e-22 |
|
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: 95.79 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 329 SVHNLSKSFDRK-KLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNV-------SVAYY---DQ 397
Cdd:cd03226 1 RIENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPikakerrKSIGYvmqDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 398 EHQvLHMDkTLFDE--ISDTYPEMTNTRIRNILAAF-LFTGEDVYKKisDLSGGERGRVSLVKLMLSKANFLLLDEPTNH 474
Cdd:cd03226 81 DYQ-LFTD-SVREEllLGLKELDAGNEQAETVLKDLdLYALKERHPL--SLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496028547 475 LDIVSKDVLENALNSFPG---TVCYVSHDRYFINKTATRILDLTEN 517
Cdd:cd03226 157 LDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
328-519 |
2.83e-22 |
|
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: 95.63 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFY----DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS----------- 391
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalkGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrVDGTDISklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 392 ---VAYYDQEHQVLhmdktlfdeisdtyPEMtnTRIRNILAAFLFTG--------------------EDVYKKISDLSGG 448
Cdd:cd03255 81 rrhIGFVFQSFNLL--------------PDL--TALENVELPLLLAGvpkkerreraeellervglgDRLNHYPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 449 ERGRVSLVKLMLSKANFLLLDEPTNHLDIV-SKDVLE--NALNSFPG-TVCYVSHDRyFINKTATRILDLTENRL 519
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSEtGKEVMEllRELNKEAGtTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-236 |
4.29e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 95.11 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNE----IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-------KDAKLGYL 70
Cdd:COG1136 4 LLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgqdisslSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 71 RQiNNV-----DSTLsiIDELyTVIEPIldmekrilkmqnemrhltgekleklyssytALTHNYELMDGYAAKSKVVGIL 145
Cdd:COG1136 84 RR-RHIgfvfqFFNL--LPEL-TALENV------------------------------ALPLLLAGVSRKERRERARELL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 146 KGLGFEEADfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS----IEWLESYLLNYNGAVVIVSHDRyFL 221
Cdd:COG1136 130 ERVGLGDRL-DHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDP-EL 207
|
250
....*....|....*
gi 496028547 222 DKIVSKVIDIENGNV 236
Cdd:COG1136 208 AARADRVIRLRDGRI 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
328-520 |
5.07e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 94.59 E-value: 5.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVSVAYYDQEH------- 399
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItFDGKSYQKNIEALRRigaliea 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 400 QVLHMDKTLFD--EISDTYPEMTNTRIRNILAAFLFTGEDvYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDI 477
Cdd:cd03268 81 PGFYPNLTAREnlRLLARLLGIRKKRIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496028547 478 VS-KDVLE--NALNSFPGTVCYVSHDRYFINKTATRILDLTENRLL 520
Cdd:cd03268 160 DGiKELREliLSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
325-514 |
6.67e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 94.73 E-value: 6.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 325 KDVLSVHNLSKSFDRKKL----FYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVS-------- 391
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGevtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdGQDISslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 392 ------VAYYDQEHQVL-HMdkTLFD------EISDTYPEMTNTRIRNILAAF-LftGEDVYKKISDLSGGERGRVSLVK 457
Cdd:COG1136 82 rlrrrhIGFVFQFFNLLpEL--TALEnvalplLLAGVSRKERRERARELLERVgL--GDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 458 LMLSKANFLLLDEPTNHLDIV-SKDVLE--NALNSFPG-TVCYVSHDRyFINKTATRILDL 514
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKtGEEVLEllRELNRELGtTIVMVTHDP-ELAARADRVIRL 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-234 |
7.81e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 93.82 E-value: 7.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLakDAKlGYLRQINNVDSTLSIIDEl 86
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF--DGK-SYQKNIEALRRIGALIEA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 87 ytviePILDMekrilkmqnemrHLTGEKLEKLYSSYTALThnyelmdgyaaKSKVVGILKGLGFEEADfDRKINTLSGGQ 166
Cdd:cd03268 81 -----PGFYP------------NLTARENLRLLARLLGIR-----------KKRIDEVLDVVGLKDSA-KKKVKGFSLGM 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 167 KTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYN---GAVVIVSHDRYFLDKIVSKVIDIENG 234
Cdd:cd03268 132 KQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRdqgITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
328-500 |
8.43e-22 |
|
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: 94.71 E-value: 8.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLfYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVS--------VAYYDQE 398
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDITnlppekrdISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 399 HQVL-HMdkTLFDEIS-----DTYPEMT-NTRIRNIlAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEP 471
Cdd:cd03299 80 YALFpHM--TVYKNIAyglkkRKVDKKEiERKVLEI-AEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190
....*....|....*....|....*....|...
gi 496028547 472 TNHLDIVSKDVLENAL----NSFPGTVCYVSHD 500
Cdd:cd03299 157 FSALDVRTKEKLREELkkirKEFGVTVLHVTHD 189
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
328-515 |
1.05e-21 |
|
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: 94.17 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILE-----PDTGEV-IYGSNVsvayYDQEHQV 401
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVlLDGKDI----YDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 402 LHM--------------DKTLFDEISdtYP----EMTNTRIRNILAAFLFTGEDVYKKISD------LSGGERGRVSLVK 457
Cdd:cd03260 77 LELrrrvgmvfqkpnpfPGSIYDNVA--YGlrlhGIKLKEELDERVEEALRKAALWDEVKDrlhalgLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 458 LMLSKANFLLLDEPTNHLDIVSKDVLENALNSF--PGTVCYVSHDRyfinKTATRILDLT 515
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHNM----QQAARVADRT 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-238 |
1.22e-21 |
|
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: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 13 GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA----KDAKLGYLRQinNV-----DSTLSII 83
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkdiTKKNLRELRR--KVglvfqNPDDQLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 84 DElyTVIE-----------PILDMEKRILKmqnemrhltgekleklyssytALthnyelmdgyaaksKVVGIlkglgfee 152
Cdd:COG1122 90 AP--TVEEdvafgpenlglPREEIRERVEE---------------------AL--------------ELVGL-------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 153 ADF-DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGA---VVIVSHDRYFLDKIVSKV 228
Cdd:COG1122 125 EHLaDRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHDLDLVAELADRV 204
|
250
....*....|
gi 496028547 229 IDIENGNVQM 238
Cdd:COG1122 205 IVLDDGRIVA 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
328-499 |
1.42e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 93.11 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVSVAYYDQ-----EHQV 401
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdGKPLDIAARNRigylpEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 402 LHMDKTLFD------EISDTYPEMTNTRIRNILAAFLFtGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHL 475
Cdd:cd03269 81 LYPKMKVIDqlvylaQLKGLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180
....*....|....*....|....*..
gi 496028547 476 DIVSKDVLENALNSFPG---TVCYVSH 499
Cdd:cd03269 160 DPVNVELLKDVIRELARagkTVILSTH 186
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
327-500 |
4.00e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 93.23 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKK----LFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVS-----VAYYD 396
Cdd:COG1116 7 ALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdGKPVTgpgpdRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 397 QEHQVL----------------HMDKTLFDEISDTYPEMTNtrirniLAAFlftgEDVYkkISDLSGGERGRVSLVKLML 460
Cdd:COG1116 87 QEPALLpwltvldnvalglelrGVPKAERRERARELLELVG------LAGF----EDAY--PHQLSGGMRQRVAIARALA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496028547 461 SKANFLLLDEPTNHLDIVSK----DVLENALNSFPGTVCYVSHD 500
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRerlqDELLRLWQETGKTVLFVTHD 198
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-236 |
4.72e-21 |
|
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: 92.84 E-value: 4.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEE-QADGGSVTLakdakLGY---------L 70
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRL-----FGErrggedvweL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 71 RQ-INNVDSTLSiidELYTVIEPILDMekrIlkmqnemrhLTGeklekLYSSyTALTHNYELMDgyaaKSKVVGILKGLG 149
Cdd:COG1119 77 RKrIGLVSPALQ---LRFPRDETVLDV---V---------LSG-----FFDS-IGLYREPTDEQ----RERARELLELLG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 150 FEE-AdfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNG--AVVIVSHdryFLDKI 224
Cdd:COG1119 132 LAHlA--DRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLdkLAAEGapTLVLVTH---HVEEI 206
|
250
....*....|....*
gi 496028547 225 ---VSKVIDIENGNV 236
Cdd:COG1119 207 ppgITHVLLLKDGRV 221
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
229-315 |
5.38e-21 |
|
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: 87.63 E-value: 5.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 229 IDIENGNVQMYLGNYTDFSNKKQMLLDAKMKEYLNQQQEIRHQEAVITKLKQfnREKSIKRAESRQKQLEKIERVDAPQT 308
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRA--KASKAKQAQSRIKALEKMERIEKPER 78
|
....*..
gi 496028547 309 YTENMRL 315
Cdd:pfam12848 79 DKPKLRF 85
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
345-520 |
6.65e-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: 91.50 E-value: 6.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGsNVSVAYYDqeHQVL-------HMDKTLF-----DEI 412
Cdd:cd03245 22 NVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLD-GTDIRQLD--PADLrrnigyvPQDVTLFygtlrDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 413 SDTYPEMTNTRirnILAAFLFTGEDVYKK---------ISD----LSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVS 479
Cdd:cd03245 99 TLGAPLADDER---ILRAAELAGVTDFVNkhpngldlqIGErgrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496028547 480 KDVLENALNSFPG--TVCYVSHdryfinktATRILDLTeNRLL 520
Cdd:cd03245 176 EERLKERLRQLLGdkTLIIITH--------RPSLLDLV-DRII 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
328-499 |
7.31e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 90.45 E-value: 7.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFD--RKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGsnvsvayydqEHQVLHMD 405
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD----------GVPVSDLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 406 KTLFDEIS--DTYPEMTNTRIRNILAAflftgedvykkisDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLD-IVSKDV 482
Cdd:cd03247 71 KALSSLISvlNQRPYLFDTTLRNNLGR-------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDpITERQL 137
|
170
....*....|....*...
gi 496028547 483 LENALNSFPG-TVCYVSH 499
Cdd:cd03247 138 LSLIFEVLKDkTLIWITH 155
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
17-253 |
8.54e-21 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 96.85 E-value: 8.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 17 IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYLRQINnvdstlsiIDELYTVIEPILDM 96
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHH--------VDGLDLSSNPLLYM 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 97 ekrilkmqneMRHLTGEKLEKLYSSYTA--LTHNYELMDGYaakskvvgilkglgfeeadfdrkinTLSGGQKTRVFLAK 174
Cdd:PLN03073 596 ----------MRCFPGVPEQKLRAHLGSfgVTGNLALQPMY-------------------------TLSGGQKSRVAFAK 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 175 LLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNVQMYLGNYTDFsnkKQML 253
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDY---KKTL 716
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
314-522 |
8.73e-21 |
|
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: 91.20 E-value: 8.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 314 RLSLDIAKEsgkdvLSVHNLsksfdrkklfyDINFEIKrGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNV--- 390
Cdd:cd03297 1 MLCVDIEKR-----LPDFTL-----------KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfd 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 391 ------------SVAYYDQEHQVL-HMdkTLFDEISDTYPEMTNTRIR---NILAAFLFTGEDVYKKISDLSGGERGRVS 454
Cdd:cd03297 64 srkkinlppqqrKIGLVFQQYALFpHL--NVRENLAFGLKRKRNREDRisvDELLDLLGLDHLLNRYPAQLSGGEKQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496028547 455 LVKLMLSKANFLLLDEPTNHLDIVSKDVLENALN----SFPGTVCYVSHDRYFINKTATRILDLTENRLLNY 522
Cdd:cd03297 142 LARALAAQPELLLLDEPFSALDRALRLQLLPELKqikkNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
328-520 |
1.04e-20 |
|
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: 91.34 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGS------------------- 388
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglppheiarlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 389 --------------NVSVAyydqeHQVLHMDKTLFDEISDTYPEMTNtRIRNILaAFLFTGEDVYKKISDLSGGERGRVS 454
Cdd:cd03219 81 fqiprlfpeltvleNVMVA-----AQARTGSGLLLARARREEREARE-RAEELL-ERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 455 LVKLMLSKANFLLLDEPTNHLDIVSKDVLEN---ALNSFPGTVCYVSHDRYFINKTATRILDLTENRLL 520
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAElirELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-237 |
1.08e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 91.27 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MIlNATNISKSF-GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-------KDAKLGYLR- 71
Cdd:COG2884 1 MI-RFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlsrlKRREIPYLRr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 72 QINNVDSTLSIIDELyTVIE----P--ILDMEKRilkmqnEMRHLTGEKLEKlyssytalthnyelmdgyaakskvVGiL 145
Cdd:COG2884 80 RIGVVFQDFRLLPDR-TVYEnvalPlrVTGKSRK------EIRRRVREVLDL------------------------VG-L 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 146 KGLGfeeadfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD----LRSIEWLESylLNYNG-AVVIVSHDRYF 220
Cdd:COG2884 128 SDKA------KALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDpetsWEIMELLEE--INRRGtTVLIATHDLEL 199
|
250
....*....|....*..
gi 496028547 221 LDKIVSKVIDIENGNVQ 237
Cdd:COG2884 200 VDRMPKRVLELEDGRLV 216
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-218 |
2.09e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 92.90 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLakdaklgylrqiNNVDstl 80
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL------------NGRD--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 siideLYTVIEPildMEKRI-LKMQNE--MRHLT-------GekLEKLYSSYTAlthnyelmdgyaAKSKVVGILK--GL 148
Cdd:COG1118 66 -----LFTNLPP---RERRVgFVFQHYalFPHMTvaeniafG--LRVRPPSKAE------------IRARVEELLElvQL 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 149 -GFEeadfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD------LRSieWLESYLLNYNGAVVIVSHDR 218
Cdd:COG1118 124 eGLA----DRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDakvrkeLRR--WLRRLHDELGGTTVFVTHDQ 194
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
328-500 |
2.54e-20 |
|
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: 89.62 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVsVAYYDQEHQVLHM--- 404
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD-VTDLPPKDRDIAMvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 405 ------DKTLFDEIS------DTYPEMTNTRIRNIlAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPT 472
Cdd:cd03301 80 nyalypHMTVYDNIAfglklrKVPKDEIDERVREV-AELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190
....*....|....*....|....*....|..
gi 496028547 473 NHLDIVSKDVLENALNSF----PGTVCYVSHD 500
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLqqrlGTTTIYVTHD 190
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
288-562 |
3.01e-20 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 95.31 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 288 KRAESRQKQLEKIERVDAPQTYTENM-RLSLDIAKESG----KDVlSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDN 362
Cdd:PLN03073 134 KRKEERQREVQYQAHVAEMEAAKAGMpGVYVNHDGNGGgpaiKDI-HMENFSISVGGRDLIVDASVTLAFGRHYGLVGRN 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 363 GTGKTTLLK-----IINGIlePDTGEVIY------GSNVSV------------AYYDQEHQVLHMDKTLF---------- 409
Cdd:PLN03073 213 GTGKTTFLRymamhAIDGI--PKNCQILHveqevvGDDTTAlqcvlntdiertQLLEEEAQLVAQQRELEfetetgkgkg 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 410 --------DEISDTYPEM-----------TNTRIRNILAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDE 470
Cdd:PLN03073 291 ankdgvdkDAVSQRLEEIykrlelidaytAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 471 PTNHLDIVSKDVLENALNSFPGTVCYVSHDRYFINKTATRILDLTENRLLNYIGNYDYYIEKREaveeaanlSNIEQAQK 550
Cdd:PLN03073 371 PTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTRE--------EQLKNQQK 442
|
330
....*....|..
gi 496028547 551 GIDVSESKQEWM 562
Cdd:PLN03073 443 AFESNERSRSHM 454
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
328-514 |
3.41e-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: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSF-DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGsNVSVAYYDQEH------- 399
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN-GVPLADADADSwrdqiaw 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 400 --QVLHM-DKTLFDEISDTYPEMTNTRIRNILAA-----FLFT-GEDVYKKISD----LSGGERGRVSLVKLMLSKANFL 466
Cdd:TIGR02857 401 vpQHPFLfAGTIAENIRLARPDASDAEIREALERagldeFVAAlPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496028547 467 LLDEPTNHLDIVSKDVLENALNSFPG--TVCYVSHDRYFInKTATRILDL 514
Cdd:TIGR02857 481 LLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
328-514 |
6.11e-20 |
|
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: 87.21 E-value: 6.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLS-KSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQEhqvlhmdk 406
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 407 tlfdeisdtyPEMTNTRIRNILAaflFTGEDVykkisdLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENA 486
Cdd:cd03223 73 ----------PYLPLGTLREQLI---YPWDDV------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170 180
....*....|....*....|....*...
gi 496028547 487 LNSFPGTVCYVSHdRYFINKTATRILDL 514
Cdd:cd03223 134 LKELGITVISVGH-RPSLWKFHDRVLDL 160
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
328-499 |
7.34e-20 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 86.71 E-value: 7.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEViygsnvsvayydqehqVLHMDKT 407
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI----------------LVDGKEV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 408 LFDEISDtypeMTNTRIRNilaaflftgedVYKkisdLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENAL 487
Cdd:cd03216 65 SFASPRD----ARRAGIAM-----------VYQ----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI 125
|
170
....*....|....*
gi 496028547 488 NSFPG---TVCYVSH 499
Cdd:cd03216 126 RRLRAqgvAVIFISH 140
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
326-391 |
7.35e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.37 E-value: 7.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 326 DVLSVHNLSKSF-------------------DRKKLFY---DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGE 383
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrrTRREEFWalkDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
....*...
gi 496028547 384 VIYGSNVS 391
Cdd:COG1134 83 VEVNGRVS 90
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-225 |
7.43e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.45 E-value: 7.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL----------AKDAK-LGY 69
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLngrpladwspAELARrRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 70 LRQinnvDSTLSIIdelYTVIEpildmekrILKM--------QNEMRHLTGEKLEKlyssyTALTHnyelmdgYAakskv 141
Cdd:PRK13548 81 LPQ----HSSLSFP---FTVEE--------VVAMgraphglsRAEDDALVAAALAQ-----VDLAH-------LA----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 142 vgilkglgfeeadfDRKINTLSGGQKTRVFLAKLLL------EEPDIILLDEPTNHLDLR----SIEWLESYLLNYNGAV 211
Cdd:PRK13548 129 --------------GRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAhqhhVLRLARQLAHERGLAV 194
|
250
....*....|....*....
gi 496028547 212 VIVSHD-----RYfLDKIV 225
Cdd:PRK13548 195 IVVLHDlnlaaRY-ADRIV 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-234 |
1.11e-19 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 88.03 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEI--IKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVtlakdaklgylrQINNVDSTLsiid 84
Cdd:cd03245 7 NVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV------------LLDGTDIRQ---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 85 elytvIEPIlDMEKRILKMQNEMRHLTGekleklyssytALTHNYELMDGYAAKSKVVGILKGLGFEE------ADFDRK 158
Cdd:cd03245 71 -----LDPA-DLRRNIGYVPQDVTLFYG-----------TLRDNITLGAPLADDERILRAAELAGVTDfvnkhpNGLDLQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 159 IN----TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNG--AVVIVSHdRYFLDKIVSKVIDIE 232
Cdd:cd03245 134 IGergrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMD 212
|
..
gi 496028547 233 NG 234
Cdd:cd03245 213 SG 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
330-476 |
1.14e-19 |
|
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: 88.55 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 330 VHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYG----SNVSVayydQEHQV---- 401
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedaTDVPV----QERNVgfvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 402 ------LHMdkTLFDEI---------SDTYPEMT-NTRIRNILAAFLFTG-EDVYKkiSDLSGGERGRVSLVKLMLSKAN 464
Cdd:cd03296 81 qhyalfRHM--TVFDNVafglrvkprSERPPEAEiRAKVHELLKLVQLDWlADRYP--AQLSGGQRQRVALARALAVEPK 156
|
170
....*....|..
gi 496028547 465 FLLLDEPTNHLD 476
Cdd:cd03296 157 VLLLDEPFGALD 168
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-217 |
1.77e-19 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 87.56 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNE--IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAkdaklGY--LRQINNVDSTLSI 82
Cdd:cd03263 5 NLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN-----GYsiRTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 IdelytviepildMEKRILkmqneMRHLTGEKLEKLYSSYTALTHNYelmdgyaAKSKVVGILKGLGFEEaDFDRKINTL 162
Cdd:cd03263 80 C------------PQFDAL-----FDELTVREHLRFYARLKGLPKSE-------IKEEVELLLRVLGLTD-KANKRARTL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 163 SGGQKTRVFLAKLLLEEPDIILLDEPTNHLD--LRSIEWleSYLLNY--NGAVVIVSHD 217
Cdd:cd03263 135 SGGMKRKLSLAIALIGGPSVLLLDEPTSGLDpaSRRAIW--DLILEVrkGRSIILTTHS 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-193 |
2.65e-19 |
|
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: 86.86 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINE--HekaAIVGVNGAGKTTLLKILTGEEQADGGSVTL----------AKDAKLGYL 70
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPgmY---GLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvlkqpqKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 71 RQINNVDSTLSIIDELYtviepildmekrilkmqnemrhltgekleklyssYTALTHNyelMDGYAAKSKVVGILKGLGF 150
Cdd:cd03264 78 PQEFGVYPNFTVREFLD----------------------------------YIAWLKG---IPSKEVKARVDEVLELVNL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496028547 151 EEADfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:cd03264 121 GDRA-KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
328-487 |
3.35e-19 |
|
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: 86.26 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQEHQVLH---- 403
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 404 ---MDKTL--------FDEISDTYPEMtntrIRNILAAFLFTG-EDVykKISDLSGGERGRVSLVKLMLSKANFLLLDEP 471
Cdd:TIGR01189 81 lpgLKPELsalenlhfWAAIHGGAQRT----IEDALAAVGLTGfEDL--PAAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170
....*....|....*.
gi 496028547 472 TNHLDIVSKDVLENAL 487
Cdd:TIGR01189 155 TTALDKAGVALLAGLL 170
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
349-512 |
4.20e-19 |
|
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: 87.08 E-value: 4.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 349 EIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYgSNVSVAYYDQE---HQVLHMDKTLFDEISDTY-PEMTNTRI 424
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYikaDYEGTVRDLLSSITKDFYtHPYFKTEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 425 RNILAAflftgEDVY-KKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLD-----IVSKDVLENALNSfPGTVCYVS 498
Cdd:cd03237 100 AKPLQI-----EQILdREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrlMASKVIRRFAENN-EKTAFVVE 173
|
170
....*....|....
gi 496028547 499 HDRYFINKTATRIL 512
Cdd:cd03237 174 HDIIMIDYLADRLI 187
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-225 |
4.20e-19 |
|
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: 86.85 E-value: 4.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSN-EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL-------AKDAKLGYLR-QI 73
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdgtdinkLKGKALRQLRrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 74 NNVDSTLSIIDELyTVIEPIldmekrilkmqnemrhLTGeKLEKLySSYTALTHNYELMDGYAAKSkvvgILKGLGFEEa 153
Cdd:cd03256 81 GMIFQQFNLIERL-SVLENV----------------LSG-RLGRR-STWRSLFGLFPKEEKQRALA----ALERVGLLD- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 154 DFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYN---GAVVIVS-HD----RYFLDKIV 225
Cdd:cd03256 137 KAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreeGITVIVSlHQvdlaREYADRIV 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
328-477 |
4.43e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.90 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS----------VAYYD 396
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVlVAGDDVEalsaraasrrVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 397 QE---------HQVLHMDKTLFDEISDTYPEMTNTRIRNILAAflfTGEDVY--KKISDLSGGERGRVSLVKLMLSKANF 465
Cdd:PRK09536 84 QDtslsfefdvRQVVEMGRTPHRSRFDTWTETDRAAVERAMER---TGVAQFadRPVTSLSGGERQRVLLARALAQATPV 160
|
170
....*....|..
gi 496028547 466 LLLDEPTNHLDI 477
Cdd:PRK09536 161 LLLDEPTASLDI 172
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
336-500 |
5.31e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.36 E-value: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 336 SFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQEhqvlhmdktlfDEISDT 415
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQR-----------SEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 416 YPemtnTRIRNILAAFLF---------TGED----------------VYKKISDLSGGERGRVSLVKLMLSKANFLLLDE 470
Cdd:NF040873 70 LP----LTVRDLVAMGRWarrglwrrlTRDDraavddalervgladlAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|...
gi 496028547 471 PTNHLDIVSKDVLENALNSFPG---TVCYVSHD 500
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
327-521 |
5.32e-19 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 86.25 E-value: 5.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYD----INFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGS-------------- 388
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRvlkgVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGqslsklssnerakl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 389 -NVSVAYYDQEHQVLhMDKTLFDE------ISDTYPEMTNTRIRNILAAFLFtGEDVYKKISDLSGGERGRVSLVKLMLS 461
Cdd:TIGR02211 81 rNKKLGFIYQFHHLL-PDFTALENvampllIGKKSVKEAKERAYEMLEKVGL-EHRINHRPSELSGGERQRVAIARALVN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496028547 462 KANFLLLDEPTNHLD-----IVSKDVLEnaLNSFPGT-VCYVSHDRYFINKTaTRILDLTENRLLN 521
Cdd:TIGR02211 159 QPSLVLADEPTGNLDnnnakIIFDLMLE--LNRELNTsFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-234 |
5.80e-19 |
|
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: 85.66 E-value: 5.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYLRQINNVDSTLSI 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 IDELY------TVIEPILDMEKRILKM-QNEMRHLTGEKLEKlyssytalthnyelmdgyaakskvVGILkglgfEEADf 155
Cdd:cd03262 81 VFQQFnlfphlTVLENITLAPIKVKGMsKAEAEERALELLEK------------------------VGLA-----DKAD- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 156 dRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSI-EWLESYL-LNYNG-AVVIVSHDRYFLDKIVSKVIDIE 232
Cdd:cd03262 131 -AYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVgEVLDVMKdLAEEGmTMVVVTHEMGFAREVADRVIFMD 209
|
..
gi 496028547 233 NG 234
Cdd:cd03262 210 DG 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
326-500 |
5.86e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 86.71 E-value: 5.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 326 DVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQEhqvLHMD 405
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK---LYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 406 KTLFDEISDTYPEMTNTRIRNILAAF--LFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSK--- 480
Cdd:PRK09544 80 TTLPLTVNRFLRLRPGTKKEDILPALkrVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQval 159
|
170 180
....*....|....*....|.
gi 496028547 481 -DVLENALNSFPGTVCYVSHD 500
Cdd:PRK09544 160 yDLIDQLRRELDCAVLMVSHD 180
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
327-516 |
7.83e-19 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 85.95 E-value: 7.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSF-----DRKKL--FYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY---GSNVSVAYYD 396
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 397 qEHQVLHMDKtlfDEIS------DTYPEMT-------------------NTRIRNILAAFlftgeDVYKKISDL-----S 446
Cdd:COG4778 84 -PREILALRR---RTIGyvsqflRVIPRVSaldvvaepllergvdreeaRARARELLARL-----NLPERLWDLppatfS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 447 GGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDV----LENALNSfpGT-VCYVSHDRYFINKTATRILDLTE 516
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVvvelIEEAKAR--GTaIIGIFHDEEVREAVADRVVDVTP 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
346-519 |
1.08e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 85.31 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 346 INFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVS-------------VAYYDQEHQVLhMDKTLFDe 411
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsGHDITrlknrevpflrrqIGMIFQDHHLL-MDRTVYD- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 412 isdtypemtNTRIRNILAAflFTGEDVYKKIS-----------------DLSGGERGRVSLVKLMLSKANFLLLDEPTNH 474
Cdd:PRK10908 99 ---------NVAIPLIIAG--ASGDDIRRRVSaaldkvglldkaknfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496028547 475 LD-IVSKDVLE--NALNSFPGTVCYVSHDRYFINKTATRILDLTENRL 519
Cdd:PRK10908 168 LDdALSEGILRlfEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-218 |
1.10e-18 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 84.88 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 6 TNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKdaklgylRQINNVdstlsiide 85
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG-------RDVTGV--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 86 lytviePIldmEKRILKM--QNE--MRHLTGEK-----LEKLyssytalthnyeLMDGYAAKSKVVGILKGLGFEEaDFD 156
Cdd:cd03259 68 ------PP---ERRNIGMvfQDYalFPHLTVAEniafgLKLR------------GVPKAEIRARVRELLELVGLEG-LLN 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496028547 157 RKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGA----VVIVSHDR 218
Cdd:cd03259 126 RYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRElgitTIYVTHDQ 191
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-256 |
1.25e-18 |
|
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: 89.58 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNE-----IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVT--------LAKDAKLG 68
Cdd:COG1123 260 LLEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgkdltkLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 69 YLRQINNV--DSTLSIiDELYTViepildmeKRILkmqnemrhltGEKLeklyssytaltHNYELMDGYAAKSKVVGILK 146
Cdd:COG1123 340 LRRRVQMVfqDPYSSL-NPRMTV--------GDII----------AEPL-----------RLHGLLSRAERRERVAELLE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 147 GLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS----IEWLESYLLNYNGAVVIVSHD----R 218
Cdd:COG1123 390 RVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDlavvR 469
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 496028547 219 YFLDKIVskVID----IENGNVQMYLGN----YTdfsnkkQMLLDA 256
Cdd:COG1123 470 YIADRVA--VMYdgriVEDGPTEEVFANpqhpYT------RALLAA 507
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
328-519 |
1.47e-18 |
|
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: 83.42 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSF--DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVSVAYYDQEHQ---V 401
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrLDGADISQWDPNELGDhvgY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 402 LHMDKTLFD-EISDtypemtntrirNIlaaflftgedvykkisdLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSK 480
Cdd:cd03246 81 LPQDDELFSgSIAE-----------NI-----------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496028547 481 DVLENA---LNSFPGTVCYVSHDRYFInKTATRILDLTENRL 519
Cdd:cd03246 133 RALNQAiaaLKAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
327-485 |
1.98e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.16 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY--GSNVSVAYYDQEHQVLHM 404
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdgGDIDDPDVAEACHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 405 D--KtlfdeisdtyPEMT------------NTRIRNILAAFLFTG----EDVykKISDLSGGERGRVSLVKLMLSKANFL 466
Cdd:PRK13539 82 NamK----------PALTvaenlefwaaflGGEELDIAAALEAVGlaplAHL--PFGYLSAGQKRRVALARLLVSNRPIW 149
|
170
....*....|....*....
gi 496028547 467 LLDEPTNHLDIVSKDVLEN 485
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAE 168
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
327-499 |
2.34e-18 |
|
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: 85.14 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVI------YGsNVSV-------- 392
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRG-GEDVwelrkrig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 393 -------AYYDQEHQVLHM------DKT-LFDEISDtypEMTNtRIRNILAAF-LFTGEDvyKKISDLSGGERGRVSLVK 457
Cdd:COG1119 82 lvspalqLRFPRDETVLDVvlsgffDSIgLYREPTD---EQRE-RARELLELLgLAHLAD--RPFGTLSQGEQRRVLIAR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496028547 458 LMLSKANFLLLDEPTNHLDIVSKDVLENALNSF-----PGTVcYVSH 499
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLaaegaPTLV-LVTH 201
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
345-519 |
2.68e-18 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 84.00 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS------VAYYDQEHQV------LHMDKTLFD- 410
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrVNGQDVSdlrgraIPYLRRKIGVvfqdfrLLPDRNVYEn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 411 -----EISDTYPEMTNTRIRNILAAF-LFTGEDVYKkiSDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLE 484
Cdd:cd03292 99 vafalEVTGVPPREIRKRVPAALELVgLSHKHRALP--AELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 496028547 485 NALNSFP---GTVCYVSHDRYFINKTATRILDLTENRL 519
Cdd:cd03292 177 NLLKKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
323-500 |
2.97e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.48 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 323 SGKDVLSVHNLSKSFDRKKL----FYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGS---------- 388
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 389 -----NVSVAYYDQEHQVLHmDKTLFDE------ISDTYPEMTNTRIRNILAAFLFTgEDVYKKISDLSGGERGRVSLVK 457
Cdd:PRK11629 81 kaelrNQKLGFIYQFHHLLP-DFTALENvampllIGKKKPAEINSRALEMLAAVGLE-HRANHRPSELSGGERQRVAIAR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496028547 458 LMLSKANFLLLDEPTNHLDIVSKDV---LENALNSFPGTV-CYVSHD 500
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSifqLLGELNRLQGTAfLVVTHD 205
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-480 |
3.12e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.30 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAK------DAKLGYLRQINNVDSTL 80
Cdd:PRK09700 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynklDHKLAAQLGIGIIYQEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 SIIDELyTVIEPILdmekrilkmqnEMRHLTGEKLeklyssytalthNYELMDGYAAKSKVVGILKGLGFeEADFDRKIN 160
Cdd:PRK09700 90 SVIDEL-TVLENLY-----------IGRHLTKKVC------------GVNIIDWREMRVRAAMMLLRVGL-KVDLDEKVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 161 TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWL---ESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNvQ 237
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGS-S 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 238 MYLGNYTDFSNKK--QMLLDAKMKeylnqqqeirhqeavitklkqfNREKSIKRAESRQkqlekiervdapqtytenmrl 315
Cdd:PRK09700 224 VCSGMVSDVSNDDivRLMVGRELQ----------------------NRFNAMKENVSNL--------------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 316 sldiakeSGKDVLSVHNLSkSFDRKKLfYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVI-YGSNVS--- 391
Cdd:PRK09700 261 -------AHETVFEVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRlNGKDISprs 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 392 --------VAYYDQEHQvlhmDKTLFDEIS-----DTYPEMTNTRIRNILAAF-----LFTGED-----------VYKKI 442
Cdd:PRK09700 332 pldavkkgMAYITESRR----DNGFFPNFSiaqnmAISRSLKDGGYKGAMGLFhevdeQRTAENqrellalkchsVNQNI 407
|
490 500 510
....*....|....*....|....*....|....*...
gi 496028547 443 SDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSK 480
Cdd:PRK09700 408 TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAK 445
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
345-500 |
3.90e-18 |
|
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: 87.80 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSnVSVAYYDQEHQ-----VLHMDKTLFDeisdtypem 419
Cdd:TIGR02868 353 GVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG-VPVSSLDQDEVrrrvsVCAQDAHLFD--------- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 420 tnTRIRN--ILAAFLFTGEDVYKKISD------------------------LSGGERGRVSLVKLMLSKANFLLLDEPTN 473
Cdd:TIGR02868 423 --TTVREnlRLARPDATDEELWAALERvgladwlralpdgldtvlgeggarLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180
....*....|....*....|....*....
gi 496028547 474 HLDI-VSKDVLENALNSFPG-TVCYVSHD 500
Cdd:TIGR02868 501 HLDAeTADELLEDLLAALSGrTVVLITHH 529
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-217 |
4.90e-18 |
|
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: 83.44 E-value: 4.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL-AKD-AKLG-YLRQINNVDSTLSII 83
Cdd:cd03300 5 NVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLdGKDiTNLPpHKRPVNTVFQNYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 84 DELyTVIEPI---LDMEKR----ILKMQNEMRHLTGekleklyssytalthnyelMDGYAakskvvgilkglgfeeadfD 156
Cdd:cd03300 85 PHL-TVFENIafgLRLKKLpkaeIKERVAEALDLVQ-------------------LEGYA-------------------N 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 157 RKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGAV----VIVSHD 217
Cdd:cd03300 126 RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgitfVFVTHD 190
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-229 |
5.63e-18 |
|
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: 87.53 E-value: 5.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEI-IKSATflINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlaKDAKLGYLRQINNVDSTL 80
Cdd:COG1245 341 LVEYPDLTKSYGGFSLeVEGGE--IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKISYKPQYISPDYDG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 SIIDELYTVIEPILDmekrilkmqnemrhltgekleklySSYtaltHNYElmdgyaakskvvgILKGLGFEEAdFDRKIN 160
Cdd:COG1245 417 TVEEFLRSANTDDFG------------------------SSY----YKTE-------------IIKPLGLEKL-LDKNVK 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496028547 161 TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDL-------RSIewlESYLLNYNGAVVIVSHDRYFLDKIVSKVI 229
Cdd:COG1245 455 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlavaKAI---RRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
325-519 |
5.74e-18 |
|
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: 87.27 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 325 KDVLSVHNLSKSF--DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILePDTGEV-----IYGSNV------- 390
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRIsgevlLDGRDLlelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 391 ---SVAYYDQEHQVLHMDKTLFDEISDTY------PEMTNTRIRNILAAF-LFTGEDVYkkISDLSGGERGRVSLVKLML 460
Cdd:COG1123 81 rgrRIGMVFQDPMTQLNPVTVGDQIAEALenlglsRAEARARVLELLEAVgLERRLDRY--PHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 461 SKANFLLLDEPTNHLD-IVSKDVLE--NALNSFPG-TVCYVSHDRYFINKTATRILDLTENRL 519
Cdd:COG1123 159 LDPDLLIADEPTTALDvTTQAEILDllRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-217 |
6.81e-18 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 83.26 E-value: 6.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-KD---------AKLGYLR- 71
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgEDitglppheiARLGIGRt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 72 -QINNVDSTLSIIDEL---YTVIEPILDMEKRILKMQNEMRHLTGEKLEKLyssytalthnyelmdgyaakskvvgilkG 147
Cdd:cd03219 81 fQIPRLFPELTVLENVmvaAQARTGSGLLLARARREEREARERAEELLERV----------------------------G 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 148 LGfeeADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPT---NHLDLRSI-EWLESylLNYNG-AVVIVSHD 217
Cdd:cd03219 133 LA---DLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELaELIRE--LRERGiTVLLVEHD 202
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-218 |
6.86e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 85.53 E-value: 6.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAkdaklGylRQINNVdstls 81
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD-----G--RDVTGL----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 82 iidelytviEPildmEKRILKM--QNE--MRHLT-------GEKLEKLYSSytalthnyelmdgyAAKSKV------VGi 144
Cdd:COG3842 73 ---------PP----EKRNVGMvfQDYalFPHLTvaenvafGLRMRGVPKA--------------EIRARVaellelVG- 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 145 LKGLGfeeadfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNY----NGAVVIVSHDR 218
Cdd:COG3842 125 LEGLA------DRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqrelGITFIYVTHDQ 196
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-236 |
7.16e-18 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 83.32 E-value: 7.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL--------------AKDAKLGYLRQ 72
Cdd:cd03261 5 GLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgedisglseaelyRLRRRMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 73 INNVDSTLSIIDelyTVIEPILdmEKRILKmQNEMRHLTGEKLEklyssytalthnyelmdgyaakskVVGIlkglgfeE 152
Cdd:cd03261 85 SGALFDSLTVFE---NVAFPLR--EHTRLS-EEEIREIVLEKLE------------------------AVGL-------R 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 153 ADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGA----VVIVSHDRYFLDKIVSKV 228
Cdd:cd03261 128 GAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElgltSIMVTHDLDTAFAIADRI 207
|
....*...
gi 496028547 229 IDIENGNV 236
Cdd:cd03261 208 AVLYDGKI 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
327-519 |
7.65e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.67 E-value: 7.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEViygsnvsvayydqehqvlhmdk 406
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV---------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 407 TLFD-EISDTYP-EMtnTRIRNILA-----AFLFTGEDV--------------------------------YKKISDLSG 447
Cdd:PRK13548 60 RLNGrPLADWSPaEL--ARRRAVLPqhsslSFPFTVEEVvamgraphglsraeddalvaaalaqvdlahlaGRDYPQLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 448 GERGRVSL--VKLMLSKAN----FLLLDEPTNHLDIVSKDVLENALNSF----PGTVCYVSHD-----RYfinktATRIL 512
Cdd:PRK13548 138 GEQQRVQLarVLAQLWEPDgpprWLLLDEPTSALDLAHQHHVLRLARQLaherGLAVIVVLHDlnlaaRY-----ADRIV 212
|
....*..
gi 496028547 513 DLTENRL 519
Cdd:PRK13548 213 LLHQGRL 219
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
18-239 |
8.00e-18 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 87.61 E-value: 8.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 18 IKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqINNVDSTLsiidelytvIEPIlDME 97
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVL------------LDGVDIRQ---------IDPA-DLR 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 98 KRILKMQNEMRHLTGekleklyssytALTHNYELMDGYAAKSKVVGILKGLGFEE------ADFDRKIN----TLSGGQK 167
Cdd:TIGR03375 539 RNIGYVPQDPRLFYG-----------TLRDNIALGAPYADDEEILRAAELAGVTEfvrrhpDGLDMQIGergrSLSGGQR 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496028547 168 TRVFLAKLLLEEPDIILLDEPTNHLDLRS----IEWLESYLLNYngAVVIVSHDRYFLDkIVSKVIDIENGNVQMY 239
Cdd:TIGR03375 608 QAVALARALLRDPPILLLDEPTSAMDNRSeerfKDRLKRWLAGK--TLVLVTHRTSLLD-LVDRIIVMDNGRIVAD 680
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
332-522 |
8.88e-18 |
|
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: 83.12 E-value: 8.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 332 NLSKSF-DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNV----------SVAYYDQE- 398
Cdd:cd03295 5 NVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfIDGEDIreqdpvelrrKIGYVIQQi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 399 ----HQVLHMDKTLFDEISDTYPEMTNTRIRNILAAF-LFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTN 473
Cdd:cd03295 85 glfpHMTVEENIALVPKLLKWPKEKIRERADELLALVgLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496028547 474 HLDIVSKDVLENA---LNSFPG-TVCYVSHDRYFINKTATRILDLTENRLLNY 522
Cdd:cd03295 165 ALDPITRDQLQEEfkrLQQELGkTIVFVTHDIDEAFRLADRIAIMKNGEIVQV 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
327-484 |
9.19e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.16 E-value: 9.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVSvAYYDQEHQVL--- 402
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIR-RQRDEYHQDLlyl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 403 -HMD--KTL---------FDEISDTYpemTNTRIRNILAAFLFTG-EDVykKISDLSGGERGRVSLVKLMLSKANFLLLD 469
Cdd:PRK13538 80 gHQPgiKTEltalenlrfYQRLHGPG---DDEALWEALAQVGLAGfEDV--PVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170
....*....|....*
gi 496028547 470 EPTNHLDIVSKDVLE 484
Cdd:PRK13538 155 EPFTAIDKQGVARLE 169
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
327-487 |
9.86e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 84.00 E-value: 9.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVSVAYYDQ-------- 397
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEPLDPEDRRRigylpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 398 --------EHQV-----LH-MDKtlfDEIsdtypemtNTRIRNILAAF-LftGEDVYKKISDLSGGERGRVSLVKLMLSK 462
Cdd:COG4152 81 glypkmkvGEQLvylarLKgLSK---AEA--------KRRADEWLERLgL--GDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180
....*....|....*....|....*
gi 496028547 463 ANFLLLDEPTNHLDIVSKDVLENAL 487
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVI 172
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
327-471 |
1.07e-17 |
|
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: 82.71 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS-----------VAY 394
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIlIDGQDIThlpmherarlgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 395 YDQEhqvlhmdKTLFDEIS---------DTYPEMTNTRIRNILAAFLftgEDVY------KKISDLSGGERGRVSLVKLM 459
Cdd:TIGR04406 81 LPQE-------ASIFRKLTveenimavlEIRKDLDRAEREERLEALL---EEFQishlrdNKAMSLSGGERRRVEIARAL 150
|
170
....*....|..
gi 496028547 460 LSKANFLLLDEP 471
Cdd:TIGR04406 151 ATNPKFILLDEP 162
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-237 |
1.51e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 84.75 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL---------AKDAKLGYLR 71
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtdvsrlhARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 72 QinnvdstlsiideLYTViepildmekrilkmqneMRHLTgeKLEKLYSSYTALTHNyELMDGYAAKSKVVGILKGLGFE 151
Cdd:PRK10851 81 Q-------------HYAL-----------------FRHMT--VFDNIAFGLTVLPRR-ERPNAAAIKAKVTQLLEMVQLA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 152 EADfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD------LRSieWLESYLLNYNGAVVIVSHDRYFLDKIV 225
Cdd:PRK10851 128 HLA-DRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDaqvrkeLRR--WLRQLHEELKFTSVFVTHDQEEAMEVA 204
|
250
....*....|..
gi 496028547 226 SKVIDIENGNVQ 237
Cdd:PRK10851 205 DRVVVMSQGNIE 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
327-476 |
1.68e-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: 81.06 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDR------KKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEP--DTGEVIY-GSNVS------ 391
Cdd:cd03213 3 TLSFRNLTVTVKSspsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLInGRPLDkrsfrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 392 -VAYYDQEHQVlhmdktlfdeisdtYPEMTntrIRNilaAFLFTGedvykKISDLSGGERGRVSLVKLMLSKANFLLLDE 470
Cdd:cd03213 83 iIGYVPQDDIL--------------HPTLT---VRE---TLMFAA-----KLRGLSGGERKRVSIALELVSNPSLLFLDE 137
|
....*.
gi 496028547 471 PTNHLD 476
Cdd:cd03213 138 PTSGLD 143
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
328-518 |
1.96e-17 |
|
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: 80.98 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLS-----KSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSnvSVAYYDQEHQVL 402
Cdd:cd03250 1 ISVEDASftwdsGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 403 HM---DKTLFDEISDtyPEMTNTRIR--------NILAAFLFT--GEdvyKKISdLSGGERGRVSLVKLMLSKANFLLLD 469
Cdd:cd03250 79 NGtirENILFGKPFD--EERYEKVIKacalepdlEILPDGDLTeiGE---KGIN-LSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496028547 470 EPTNHLDI-VSKDVLENALNSF---PGTVCYVSHDRYFINKtATRILDLTENR 518
Cdd:cd03250 153 DPLSAVDAhVGRHIFENCILGLllnNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
327-472 |
2.73e-17 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 82.01 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSF------DrkklfyDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGS------------ 388
Cdd:COG0411 4 LLEVRGLTKRFgglvavD------DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrditglpphria 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 389 ---------------------NVSVAYYDQEHQVLHMDKTLFDEISDTYPEMTnTRIRNILAAF-LftGEDVYKKISDLS 446
Cdd:COG0411 78 rlgiartfqnprlfpeltvleNVLVAAHARLGRGLLAALLRLPRARREEREAR-ERAEELLERVgL--ADRADEPAGNLS 154
|
170 180
....*....|....*....|....*.
gi 496028547 447 GGERGRVSLVKLMLSKANFLLLDEPT 472
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPA 180
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-236 |
2.74e-17 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 81.26 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 5 ATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAkdaklGY--LRQINNVDSTLSI 82
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVA-----GHdvVREPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 IDElytviEPILDmekrilkmqnemRHLTG-EKLE---KLYSsytalthnyelMDGYAAKSKVVGILKGLGFEEADfDRK 158
Cdd:cd03265 78 VFQ-----DLSVD------------DELTGwENLYihaRLYG-----------VPGAERRERIDELLDFVGLLEAA-DRL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 159 INTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS----IEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENG 234
Cdd:cd03265 129 VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTrahvWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
..
gi 496028547 235 NV 236
Cdd:cd03265 209 RI 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-217 |
3.40e-17 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 80.98 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSA----TFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL------AKDAKLGYLRQ 72
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTAlediSLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 73 innvDSTLsiideL--YTVIEPILdmekrI-LKMQNemrhltgekleklyssytalthnyelMDGYAAKSKVVGILK--G 147
Cdd:cd03293 81 ----QDAL-----LpwLTVLDNVA-----LgLELQG--------------------------VPKAEARERAEELLElvG 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 148 L-GFEeadfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD--LRSI--EWLESYLLNYNGAVVIVSHD 217
Cdd:cd03293 121 LsGFE----NAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDalTREQlqEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-234 |
3.46e-17 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 79.54 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqINNVDstlsi 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL------------IDGED----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 ideLYTVIEPILDMEKRI-LKMQ--NEMRHLTgekleklyssytalthnyelmdgyaakskvvgILKGLGFeeadfdrki 159
Cdd:cd03229 64 ---LTDLEDELPPLRRRIgMVFQdfALFPHLT--------------------------------VLENIAL--------- 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 160 nTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLL----NYNGAVVIVSHDRYFLDKIVSKVIDIENG 234
Cdd:cd03229 100 -GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKslqaQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
3-196 |
4.10e-17 |
|
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: 81.40 E-value: 4.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYLRQinnVDSTLSI 82
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRR---ARARRVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 IDELYTVIEPILDMEKRILKMQNEMRHLTGekleklyssyTALTHNYELMDGYAAKSkvvgilkglgfEEADF-DRKINT 161
Cdd:TIGR03873 79 LVEQDSDTAVPLTVRDVVALGRIPHRSLWA----------GDSPHDAAVVDRALART-----------ELSHLaDRDMST 137
|
170 180 190
....*....|....*....|....*....|....*
gi 496028547 162 LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS 196
Cdd:TIGR03873 138 LSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRA 172
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
328-512 |
4.26e-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: 80.27 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYgsnvsvayydqEHQVLHMDKT 407
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII-----------DGLKLTDDKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 408 LFDEIS----------DTYPEMtnTRIRNILAAFLF-----------TGEDVYKKI----------SDLSGGERGRVSLV 456
Cdd:cd03262 70 NINELRqkvgmvfqqfNLFPHL--TVLENITLAPIKvkgmskaeaeeRALELLEKVgladkadaypAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 457 KLMLSKANFLLLDEPTNHLD--IVsKDVLE--NALNSFPGTVCYVSHDRYFINKTATRIL 512
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDpeLV-GEVLDvmKDLAEEGMTMVVVTHEMGFAREVADRVI 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2-215 |
4.58e-17 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 80.49 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNE----IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqinnvd 77
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 78 stlsiIDELYTVIEPIlDMEKRILKMQNEMR---HLTG-EKLEklyssYTALTHNyelMDGYAAKSKVVGILKGLGFEEA 153
Cdd:cd03266 64 -----VDGFDVVKEPA-EARRRLGFVSDSTGlydRLTArENLE-----YFAGLYG---LKGDELTARLEELADRLGMEEL 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496028547 154 dFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNGAVVIVS 215
Cdd:cd03266 130 -LDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIrqLRALGKCILFS 192
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
331-512 |
4.92e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.91 E-value: 4.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 331 HNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY------GSNVSVAYYDQEHQVLHM 404
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdglkvnDPKVDERLIRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 405 DKTLFdeisdtyPEMTN--------TRIR-------NILAAFLFT----GEDVYKKISDLSGGERGRVSLVKLMLSKANF 465
Cdd:PRK09493 85 QFYLF-------PHLTAlenvmfgpLRVRgaskeeaEKQARELLAkvglAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 466 LLLDEPTNHLD--------IVSKDVLENALnsfpgTVCYVSHDRYFINKTATRIL 512
Cdd:PRK09493 158 MLFDEPTSALDpelrhevlKVMQDLAEEGM-----TMVIVTHEIGFAEKVASRLI 207
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-263 |
5.66e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 80.83 E-value: 5.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAkDAKLGYLRQINNvdstl 80
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIA-GHQFDFSQKPSE----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 SIIDEL----------------YTVIEPILDMEKRILKMQNEmrhltgekleklyssytalthnyelmdgyAAKSKVVGI 144
Cdd:COG4161 75 KAIRLLrqkvgmvfqqynlwphLTVMENLIEAPCKVLGLSKE-----------------------------QAREKAMKL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 145 LKGLGFeeADF-DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNG---AVVIVSHDRYF 220
Cdd:COG4161 126 LARLRL--TDKaDRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIVTHEVEF 203
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 496028547 221 LDKIVSKVIDIENGNVQMYlGNYTDFSNKKQmlldAKMKEYLN 263
Cdd:COG4161 204 ARKVASQVVYMEKGRIIEQ-GDASHFTQPQT----EAFAHYLS 241
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-239 |
6.03e-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: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-KD-------------AKLGYLRQ 72
Cdd:COG1127 10 NLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDgQDitglsekelyelrRRIGMLFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 73 innvDSTLsiIDELyTVIEPI---LDMEKRILKmqNEMRHLTGEKLEKlyssytalthnyelmdgyaakskvVGiLKGLG 149
Cdd:COG1127 90 ----GGAL--FDSL-TVFENVafpLREHTDLSE--AEIRELVLEKLEL------------------------VG-LPGAA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 150 feeadfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD-LRSIEWLEsyLLN-----YNGAVVIVSHDRYFLDK 223
Cdd:COG1127 136 ------DKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDpITSAVIDE--LIRelrdeLGLTSVVVTHDLDSAFA 207
|
250
....*....|....*.
gi 496028547 224 IVSKVIDIENGNVQMY 239
Cdd:COG1127 208 IADRVAVLADGKIIAE 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-237 |
6.36e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 80.45 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 16 EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAK----DAKLGYLRQI-------NNVDSTLSIID 84
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwKRRKKFLRRIgvvfgqkTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 85 ELYtVIEPILDMEKRilKMQNEMRHLTgekleklyssytalthnyELMDgyaakskvvgilkglgfEEADFDRKINTLSG 164
Cdd:cd03267 115 SFY-LLAAIYDLPPA--RFKKRLDELS------------------ELLD-----------------LEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 165 GQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYN---GAVVIV-SHDRYFLDKIVSKVIDIENGNVQ 237
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNrerGTTVLLtSHYMKDIEALARRVLVIDKGRLL 233
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
328-500 |
7.25e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 82.43 E-value: 7.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNV---------SVAY---- 394
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlppkdrNIAMvfqs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 395 ---YDqehqvlHMdkTLFD------EISDTYPEMTNTRIRNI-----LAAFLftgeDvyKKISDLSGGERGRVSL----V 456
Cdd:COG3839 84 yalYP------HM--TVYEniafplKLRKVPKAEIDRRVREAaellgLEDLL----D--RKPKQLSGGQRQRVALgralV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496028547 457 KlmlsKANFLLLDEPTNHLDIVSKDVLE-------NALNSfpgTVCYVSHD 500
Cdd:COG3839 150 R----EPKVFLLDEPLSNLDAKLRVEMRaeikrlhRRLGT---TTIYVTHD 193
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
328-471 |
8.85e-17 |
|
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: 79.89 E-value: 8.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSN------------VSVAYY 395
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 396 DQEHqvlhmdkTLFDEIsdtypemtnTRIRNILAAFLFTGEDVYKKI--------------------SDLSGGERGRVSL 455
Cdd:cd03218 81 PQEA-------SIFRKL---------TVEENILAVLEIRGLSKKEREekleelleefhithlrkskaSSLSGGERRRVEI 144
|
170
....*....|....*.
gi 496028547 456 VKLMLSKANFLLLDEP 471
Cdd:cd03218 145 ARALATNPKFLLLDEP 160
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
328-520 |
1.02e-16 |
|
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: 79.16 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGeRVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS---------VAYYDQ 397
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIrIDGQDVLkqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 398 EHQVlhmdktlfdeisdtYPEMT-------------------NTRIRNILAAfLFTGEDVYKKISDLSGGERGRVSLVKL 458
Cdd:cd03264 80 EFGV--------------YPNFTvrefldyiawlkgipskevKARVDEVLEL-VNLGDRAKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496028547 459 MLSKANFLLLDEPTNHLDIVSKDVLENALNSFPGTVCYV--SHDRYFINKTATRILDLTENRLL 520
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-229 |
1.08e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 83.70 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 6 TNISKSFGSNEIIKSATFlINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlaKDAKLGYLRQinnvdstlsiide 85
Cdd:PRK13409 344 PDLTKKLGDFSLEVEGGE-IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--PELKISYKPQ------------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 86 lYtvIEPILDMEKRILKMQNEmrhltgeklEKLYSSYtaltHNYElmdgyaakskvvgILKGLGFEEAdFDRKINTLSGG 165
Cdd:PRK13409 408 -Y--IKPDYDGTVEDLLRSIT---------DDLGSSY----YKSE-------------IIKPLQLERL-LDKNVKDLSGG 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 166 QKTRVFLAKLLLEEPDIILLDEPTNHLDL-----------RSIEwlesyllNYNGAVVIVSHDRYFLDKIVSKVI 229
Cdd:PRK13409 458 ELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlavakairRIAE-------EREATALVVDHDIYMIDYISDRLM 525
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
345-488 |
1.32e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 83.29 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNV----------SVAYYDQEHQVLHMdkTLFDEIs 413
Cdd:COG1132 358 DISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlIDGVDIrdltleslrrQIGVVPQDTFLFSG--TIRENI- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 414 dTY--PEMTNTRIRNILAA-----FLFT---GED--VYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKD 481
Cdd:COG1132 435 -RYgrPDATDEEVEEAAKAaqaheFIEAlpdGYDtvVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEA 513
|
....*..
gi 496028547 482 VLENALN 488
Cdd:COG1132 514 LIQEALE 520
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
338-519 |
1.38e-16 |
|
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: 79.45 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 338 DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSN----VSVAYYDQEHQVLHMDKTLF---- 409
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlalADPAWLRRQVGVVLQENVLFnrsi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 410 -DEISDTYPEMTNTRIrnILAAFLFTGEDVYKKI------------SDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLD 476
Cdd:cd03252 93 rDNIALADPGMSMERV--IEAAKLAGAHDFISELpegydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496028547 477 IVSKDVLENALNSFPG--TVCYVSHdRYFINKTATRILDLTENRL 519
Cdd:cd03252 171 YESEHAIMRNMHDICAgrTVIIIAH-RLSTVKNADRIIVMEKGRI 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
321-505 |
1.52e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.99 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 321 KESgKDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVS-------- 391
Cdd:PRK10247 2 QEN-SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDIStlkpeiyr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 392 --VAYYDQEhQVLHMDkTLFD------EISDTYPEMtnTRIRNILAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKA 463
Cdd:PRK10247 81 qqVSYCAQT-PTLFGD-TVYDnlifpwQIRNQQPDP--AIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496028547 464 NFLLLDEPTNHLDIVSK----DVLENALNSFPGTVCYVSHDRYFIN 505
Cdd:PRK10247 157 KVLLLDEITSALDESNKhnvnEIIHRYVREQNIAVLWVTHDKDEIN 202
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
327-472 |
1.52e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.77 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSF------DrkklfyDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNV--------- 390
Cdd:COG3845 5 ALELRGITKRFggvvanD------DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEIlIDGKPVrirsprdai 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 391 -----------------SVAyydqEHQVLHMDKTLFDEISdtyPEMTNTRIRNILAAFlftGEDV--YKKISDLSGGERG 451
Cdd:COG3845 79 algigmvhqhfmlvpnlTVA----ENIVLGLEPTKGGRLD---RKAARARIRELSERY---GLDVdpDAKVEDLSVGEQQ 148
|
170 180
....*....|....*....|.
gi 496028547 452 RVSLVKLMLSKANFLLLDEPT 472
Cdd:COG3845 149 RVEILKALYRGARILILDEPT 169
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
2-236 |
1.64e-16 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 79.26 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSN-EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL-------AKDAKLGYLR-Q 72
Cdd:TIGR02315 1 MLEVENLSKVYPNGkQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLegtditkLRGKKLRKLRrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 73 INNVDSTLSIIDELyTVIEPILdmekrilkMQNEMRHLTGEKLEKLYSSytalthnyelmdgyAAKSKVVGILKGLGFEE 152
Cdd:TIGR02315 81 IGMIFQHYNLIERL-TVLENVL--------HGRLGYKPTWRSLLGRFSE--------------EDKERALSALERVGLAD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 153 ADFDRkINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYN---GAVVIVS-HDRYFLDKIVSKV 228
Cdd:TIGR02315 138 KAYQR-ADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINkedGITVIINlHQVDLAKKYADRI 216
|
....*...
gi 496028547 229 IDIENGNV 236
Cdd:TIGR02315 217 VGLKAGEI 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
328-487 |
1.80e-16 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 78.56 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFY----DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGeviygsNVSVAYYDQEHQVLH 403
Cdd:cd03266 2 ITADALTKRFRDVKKTVqavdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG------FATVDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 404 MDKTL--FDEISDTYPEMT-------------------NTRIrNILAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSK 462
Cdd:cd03266 76 ARRRLgfVSDSTGLYDRLTarenleyfaglyglkgdelTARL-EELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180
....*....|....*....|....*
gi 496028547 463 ANFLLLDEPTNHLDIVSKDVLENAL 487
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFI 179
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-216 |
2.00e-16 |
|
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: 77.08 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAkdaklGYLRQINNVdstlsi 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-----GKEVSFASP------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 idelytviepildmekrilkmqNEMRHLtgekleklyssytalthnyelmdgyaakskvvGIlkglgfeeadfdRKINTL 162
Cdd:cd03216 70 ----------------------RDARRA--------------------------------GI------------AMVYQL 83
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 163 SGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNG-AVVIVSH 216
Cdd:cd03216 84 SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIrrLRAQGvAVIFISH 140
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
345-520 |
2.16e-16 |
|
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: 80.93 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNV---------------SVAYYDQEHQV---LHMDK 406
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrRIGYVFQEARLfphLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 407 TLFDEISDTYPEMTNTRIRNILAaFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKD----V 482
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERVIE-LLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYeilpY 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 496028547 483 LENALNSFPGTVCYVSHDRYFINKTATRILDLTENRLL 520
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
328-517 |
2.55e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.36 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDR-----KKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVSvayYDQEHQV 401
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlIDGKDVT---KLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 402 LHMDKTLF-DEISDTYPEMT---NTRI-------RNILAAFLFTGEDVYK----------------KISDLSGGERGRVS 454
Cdd:COG1101 79 AKYIGRVFqDPMMGTAPSMTieeNLALayrrgkrRGLRRGLTKKRRELFRellatlglglenrldtKVGLLSGGQRQALS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 455 LvkLM--LSKANFLLLDEPTNHLDivskdvlenalnsfPgtvcyvshdryfinKTATRILDLTEN 517
Cdd:COG1101 159 L--LMatLTKPKLLLLDEHTAALD--------------P--------------KTAALVLELTEK 193
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-229 |
2.62e-16 |
|
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: 78.99 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 25 INEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDaKLGYLRQINNVDSTLSIIDELYTVIEpildmekrilkmq 104
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYIKADYEGTVRDLLSSITK------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 105 nemrhltgekleklyssyTALTHNYELMDgyaakskvvgILKGLGFEEAdFDRKINTLSGGQKTRVFLAKLLLEEPDIIL 184
Cdd:cd03237 88 ------------------DFYTHPYFKTE----------IAKPLQIEQI-LDREVPELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496028547 185 LDEPTNHLD----LRSIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVI 229
Cdd:cd03237 139 LDEPSAYLDveqrLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-238 |
2.63e-16 |
|
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: 77.35 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNE--IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAkdaklgylrqinnvdstl 80
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 siidelytviepildmEKRILKMQNEMRHLTGEKLEKLYSSYTALTHNyelmdgyaakskvVGIlkglgfeeadfdrkin 160
Cdd:cd03247 63 ----------------GVPVSDLEKALSSLISVLNQRPYLFDTTLRNN-------------LGR---------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 161 TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSiewlESYLLNY------NGAVVIVSHDRYFLDKiVSKVIDIENG 234
Cdd:cd03247 98 RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT----ERQLLSLifevlkDKTLIWITHHLTGIEH-MDKILFLENG 172
|
....
gi 496028547 235 NVQM 238
Cdd:cd03247 173 KIIM 176
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
328-500 |
2.72e-16 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 78.32 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFdRKKLFY---DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQEHQVLHM 404
Cdd:cd03263 1 LQIRNLTKTY-KKGTKPavdDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 405 ---DKTLFDEISDT-----------YPEMTNTRIRNILAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDE 470
Cdd:cd03263 80 cpqFDALFDELTVRehlrfyarlkgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190
....*....|....*....|....*....|..
gi 496028547 471 PTNHLDIVSKDVLENALNSFPG--TVCYVSHD 500
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-189 |
3.38e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 78.93 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-KD---------AKLGYL 70
Cdd:COG0411 3 PLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgRDitglpphriARLGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 71 R--QINNVDSTLsiidelyTVIEPILdmekriLKMQNEMRHLTGEKLEKLYSSYTALThnyelmdgyAAKSKVVGILKGL 148
Cdd:COG0411 83 RtfQNPRLFPEL-------TVLENVL------VAAHARLGRGLLAALLRLPRARREER---------EARERAEELLERV 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496028547 149 GFEEaDFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPT 189
Cdd:COG0411 141 GLAD-RADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPA 180
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-237 |
3.46e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.86 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDaklgYLRQINNVDSTLSI 82
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQ----TINLVRDKDGQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 IDElytviepildMEKRILKMQNEM--RHLTgeklekLYSSYTALTHNYEL------MDGYAAKSKVVGILKGLGFEEAD 154
Cdd:PRK10619 82 ADK----------NQLRLLRTRLTMvfQHFN------LWSHMTVLENVMEApiqvlgLSKQEARERAVKYLAKVGIDERA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 155 FDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD---LRSIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDI 231
Cdd:PRK10619 146 QGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFL 225
|
....*.
gi 496028547 232 ENGNVQ 237
Cdd:PRK10619 226 HQGKIE 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-236 |
3.85e-16 |
|
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: 82.19 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNE--IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL----AKDAKLGYLR-QINNV--D 77
Cdd:COG2274 478 NVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidLRQIDPASLRrQIGVVlqD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 78 STL---SIIDELyTVIEPILDMEkRILKmqnemrhltgekleklyssytalthnyelmdgyAAKskVVGILkglGFEEAD 154
Cdd:COG2274 558 VFLfsgTIRENI-TLGDPDATDE-EIIE---------------------------------AAR--LAGLH---DFIEAL 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 155 ---FDRKI----NTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSiewlESYLLNY------NGAVVIVSHDRYFL 221
Cdd:COG2274 598 pmgYDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAET----EAIILENlrrllkGRTVIIIAHRLSTI 673
|
250
....*....|....*
gi 496028547 222 dKIVSKVIDIENGNV 236
Cdd:COG2274 674 -RLADRIIVLDKGRI 687
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-217 |
4.18e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 78.59 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSF----GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL------AKDAKLGYL 70
Cdd:COG1116 6 PALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 71 RQinnvDSTLsiidelY---TVIEpildmekrilkmqN-----EMRHLTGEKLEKLYSSYTALthnyelmdgyaakskvV 142
Cdd:COG1116 86 FQ----EPAL------LpwlTVLD-------------NvalglELRGVPKAERRERARELLEL----------------V 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 143 GiLKGlgFEeadfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD--LRSI--EWLESYLLNYNGAVVIVSHD 217
Cdd:COG1116 127 G-LAG--FE----DAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDalTRERlqDELLRLWQETGKTVLFVTHD 198
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
273-517 |
4.72e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.39 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 273 AVITKLKQFNRekSIKRAESRQKQLEKIERVDAPQTYTENMRLSLDiakesgkdvlsvhnlsksfDRKKLFYDINFEIKR 352
Cdd:COG4178 330 ATVDRLAGFEE--ALEAADALPEAASRIETSEDGALALEDLTLRTP-------------------DGRPLLEDLSLSLKP 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 353 GERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQehqvlhmdK------TLFDEIsdTYP----EMTNT 422
Cdd:COG4178 389 GERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQ--------RpylplgTLREAL--LYPataeAFSDA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 423 RIRNILAAF--------LFTGEDvYKKIsdLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENAL-NSFPG- 492
Cdd:COG4178 459 ELREALEAVglghlaerLDEEAD-WDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLrEELPGt 535
|
250 260
....*....|....*....|....*....
gi 496028547 493 TVCYVSH----DRYFinktaTRILDLTEN 517
Cdd:COG4178 536 TVISVGHrstlAAFH-----DRVLELTGD 559
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
328-515 |
5.37e-16 |
|
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: 76.76 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQEHQVL----H 403
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLlylgH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 404 MD--KTLFDEISDT---YPEMTNTRIRNILAAFLFTG-EDVykKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDI 477
Cdd:cd03231 81 APgiKTTLSVLENLrfwHADHSDEQVEEALARVGLNGfEDR--PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496028547 478 VSKDVLENALNSFP---GTVCYVSHDRYFINKTATRILDLT 515
Cdd:cd03231 159 AGVARFAEAMAGHCargGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-236 |
6.36e-16 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 75.72 E-value: 6.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNE--IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqINNVDstL 80
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR------------LDGAD--I 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 SIIDElytviepildmekrilkmqNEMRHLTGekleklyssytALTHNYELMDGYAAKskvvgilkglgfeeadfdrkiN 160
Cdd:cd03246 67 SQWDP-------------------NELGDHVG-----------YLPQDDELFSGSIAE---------------------N 95
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 161 TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGA---VVIVSHdRYFLDKIVSKVIDIENGNV 236
Cdd:cd03246 96 ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAgatRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
330-511 |
6.65e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 79.74 E-value: 6.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 330 VHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS--------VAYYDQeHQ 400
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrFHGTDVSrlhardrkVGFVFQ-HY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 401 VL--HMdkTLFDEIS---DTYPEmtntRIRNILAAflftgedVYKKI-----------------SDLSGGERGRVSLVKL 458
Cdd:PRK10851 84 ALfrHM--TVFDNIAfglTVLPR----RERPNAAA-------IKAKVtqllemvqlahladrypAQLSGGQKQRVALARA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 459 MLSKANFLLLDEPTNHLDI-VSKDV---LENALNSFPGTVCYVSHDRYFINKTATRI 511
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAqVRKELrrwLRQLHEELKFTSVFVTHDQEEAMEVADRV 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
328-472 |
6.86e-16 |
|
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: 77.09 E-value: 6.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVS-----------VAYY 395
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdGRDITglppheraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 396 DQEHQVlhmdktlfdeisdtYPEMTntrIR-NI-LAAFLFTGEDVYKKI------------------SDLSGGER----- 450
Cdd:cd03224 81 PEGRRI--------------FPELT---VEeNLlLGAYARRRAKRKARLervyelfprlkerrkqlaGTLSGGEQqmlai 143
|
170 180
....*....|....*....|..
gi 496028547 451 GRVslvkLMlSKANFLLLDEPT 472
Cdd:cd03224 144 ARA----LM-SRPKLLLLDEPS 160
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-477 |
7.00e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 7.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL----------AKDAKLG-YL 70
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIggnpcarltpAKAHQLGiYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 71 rqinnVDSTLSIIDELyTVIEPILdmeKRILKMQNEMRHLTgEKLEKLYSSYTaLTHNYELMDgyAAKSKVVGILKGlgf 150
Cdd:PRK15439 91 -----VPQEPLLFPNL-SVKENIL---FGLPKRQASMQKMK-QLLAALGCQLD-LDSSAGSLE--VADRQIVEILRG--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 151 eeadfdrkintlsggqktrvflaklLLEEPDIILLDEPTNHLDLRSIEWLESY---LLNYNGAVVIVSHDRYFLDKIVSK 227
Cdd:PRK15439 155 -------------------------LMRDSRILILDEPTASLTPAETERLFSRireLLAQGVGIVFISHKLPEIRQLADR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 228 VIDIENGNVqmylgnytdfsnkkqmLLDAKMKEYlnqqqeirHQEAVITKLKQFNREKSIKRAESRQKQLEKIERVDAPq 307
Cdd:PRK15439 210 ISVMRDGTI----------------ALSGKTADL--------STDDIIQAITPAAREKSLSASQKLWLELPGNRRQQAA- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 308 tytenmrlsldiakesGKDVLSVHNLSksfdrKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYG 387
Cdd:PRK15439 265 ----------------GAPVLTVEDLT-----GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLN 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 388 ----SNVSVA--------YYDQEHQV--LHMDKTL-FDEISDTYPEMT----NTRIRNILAAFL------FTGEDvyKKI 442
Cdd:PRK15439 324 gkeiNALSTAqrlarglvYLPEDRQSsgLYLDAPLaWNVCALTHNRRGfwikPARENAVLERYRralnikFNHAE--QAA 401
|
490 500 510
....*....|....*....|....*....|....*
gi 496028547 443 SDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDI 477
Cdd:PRK15439 402 RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-263 |
7.06e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 77.75 E-value: 7.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA----------KDAKLGYL 70
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAgnhfdfsktpSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 71 RQinNVdstlSIIDELY------TVIEPILDMEKRILKMQNEmrhltgekleklyssytalthnyelmdgyAAKSKVVGI 144
Cdd:PRK11124 81 RR--NV----GMVFQQYnlwphlTVQQNLIEAPCRVLGLSKD-----------------------------QALARAEKL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 145 LKGLGFeeADF-DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD------LRSI--EWLESYLLNyngavVIVS 215
Cdd:PRK11124 126 LERLRL--KPYaDRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqIVSIirELAETGITQ-----VIVT 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 496028547 216 HDRYFLDKIVSKVIDIENGNVqMYLGNYTDFSNKKQmlldAKMKEYLN 263
Cdd:PRK11124 199 HEVEVARKTASRVVYMENGHI-VEQGDASCFTQPQT----EAFKNYLS 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-193 |
8.79e-16 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 77.34 E-value: 8.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL------AKDAKLGYLR---- 71
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVdgedltDSKKDINKLRrkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 72 ----QINnvdstlsiideLY---TVIEPIldME--KRILKM-QNEMRHLTGEKLEKlyssytalthnyelmdgyaakskv 141
Cdd:COG1126 81 mvfqQFN-----------LFphlTVLENV--TLapIKVKKMsKAEAEERAMELLER------------------------ 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496028547 142 VGIlkglgfeeADF-DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:COG1126 124 VGL--------ADKaDAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
328-476 |
8.91e-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: 78.99 E-value: 8.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYG----SNVS------------ 391
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvTGLPpekrnvgmvfqd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 392 ------------VAYYdqehqvLHMDKTLFDEISDtypemtntRIRNILA-----AFlftgEDvyKKISDLSGGERGRV- 453
Cdd:COG3842 86 yalfphltvaenVAFG------LRMRGVPKAEIRA--------RVAELLElvgleGL----AD--RYPHQLSGGQQQRVa 145
|
170 180
....*....|....*....|....*....
gi 496028547 454 ---SLV---KLmlskanfLLLDEPTNHLD 476
Cdd:COG3842 146 larALApepRV-------LLLDEPLSALD 167
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-217 |
9.60e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.43 E-value: 9.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MIlNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVT-------------LAKdaKL 67
Cdd:COG4604 1 MI-EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLvdgldvattpsreLAK--RL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 68 GYLRQINNVDSTLsiidelyTViepildmekRIL-----------KMQNEMRHLTGEKLEKLyssytalthnyELMDgya 136
Cdd:COG4604 78 AILRQENHINSRL-------TV---------RELvafgrfpyskgRLTAEDREIIDEAIAYL-----------DLED--- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 137 akskvvgiLKglgfeeadfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLR-SIEW---LESYLLNYNGAVV 212
Cdd:COG4604 128 --------LA---------DRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKhSVQMmklLRRLADELGKTVV 190
|
....*
gi 496028547 213 IVSHD 217
Cdd:COG4604 191 IVLHD 195
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
17-238 |
1.00e-15 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 80.58 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 17 IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLakdaklgylrqiNNVDstLSIIDElytviepildm 96
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL------------GGVD--LRDLDE----------- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 97 ekrilkmqNEMRHLTGEKLEKLYSSYTALTHNYELMDGYAAKSKVVGILK--GLGFEEADFDRKINT--------LSGGQ 166
Cdd:COG4987 405 --------DDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALErvGLGDWLAALPDGLDTwlgeggrrLSGGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496028547 167 KTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNY--NGAVVIVSHDRYFLDKiVSKVIDIENGNVQM 238
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAGLER-MDRILVLEDGRIVE 549
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
331-527 |
1.00e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.78 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 331 HNLSKSFD-RKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNV----------SVAYYDQE 398
Cdd:PRK13657 338 DDVSFSYDnSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIlIDGTDIrtvtraslrrNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 399 hqVLHMDKTLFDEISDTYPEMTNTRIRNILAA-----FLFTGEDVYKKI-----SDLSGGERGRVSLVKLMLSKANFLLL 468
Cdd:PRK13657 418 --AGLFNRSIEDNIRVGRPDATDEEMRAAAERaqahdFIERKPDGYDTVvgergRQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 469 DEPTNHLDIVSKDVLENALNSfpgtvcyVSHDR-YFI-------NKTATRILDLTENRLLNyIGNYD 527
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDE-------LMKGRtTFIiahrlstVRNADRILVFDNGRVVE-SGSFD 554
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-234 |
1.38e-15 |
|
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: 74.73 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSN--EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL----AKDAKLGYLRQinnvdsTL 80
Cdd:cd03228 5 NVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdgvdLRDLDLESLRK------NI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 SIIDElytviEPILdmekrilkmqnemrhltgekleklyssytalthnyelmdgyaakskvvgilkglgfeeadFDRKI- 159
Cdd:cd03228 79 AYVPQ-----DPFL------------------------------------------------------------FSGTIr 93
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 160 -NTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNG--AVVIVSHdRYFLDKIVSKVIDIENG 234
Cdd:cd03228 94 eNILSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVLDDG 170
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-237 |
1.64e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 76.33 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGsnEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqINNVDstlsi 82
Cdd:COG3840 2 LRLDDLTYRYG--DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIL------------WNGQD----- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 idelYTVIEPildmEKRILKM----QNEMRHLT-----------GEKLeklyssyTAlthnyelmdgyAAKSKVVGILKG 147
Cdd:COG3840 63 ----LTALPP----AERPVSMlfqeNNLFPHLTvaqniglglrpGLKL-------TA-----------EQRAQVEQALER 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 148 LGFEEADfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD--LRS--IEWLESYLLNYNGAVVIVSHDryfLD- 222
Cdd:COG3840 117 VGLAGLL-DRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpaLRQemLDLVDELCRERGLTVLMVTHD---PEd 192
|
250
....*....|....*..
gi 496028547 223 --KIVSKVIDIENGNVQ 237
Cdd:COG3840 193 aaRIADRVLLVADGRIA 209
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
327-511 |
1.91e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 78.34 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVS-VAYYDQEHQVL-- 402
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLdGVDLShVPPYQRPINMMfq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 403 ------HM------------DKTLFDEISDTYPEMTntrirnilaAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKAN 464
Cdd:PRK11607 99 syalfpHMtveqniafglkqDKLPKAEIASRVNEML---------GLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496028547 465 FLLLDEPTNHLDIVSKDVLE----NALNSFPGTVCYVSHDRYFINKTATRI 511
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDRMQlevvDILERVGVTCVMVTHDQEEAMTMAGRI 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-237 |
2.24e-15 |
|
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: 75.84 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-KDAKLGYL--RQINNVD 77
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgEDATDVPVqeRNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 78 STLSIIDELyTVIEPI---LDMEKRILKM-QNEMRhltgEKLEKLYssytalthnyelmdgyaaksKVVGiLKGLGfeea 153
Cdd:cd03296 81 QHYALFRHM-TVFDNVafgLRVKPRSERPpEAEIR----AKVHELL--------------------KLVQ-LDWLA---- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 154 dfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD------LRSieWLESYLLNYNGAVVIVSHDRYFLDKIVSK 227
Cdd:cd03296 131 --DRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDakvrkeLRR--WLRRLHDELHVTTVFVTHDQEEALEVADR 206
|
250
....*....|
gi 496028547 228 VIDIENGNVQ 237
Cdd:cd03296 207 VVVMNKGRIE 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-236 |
2.80e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 76.25 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVtLAKDAKLGYLRQinnvDSTLsi 82
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEARE----DTRL-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 idelytviepildmekrilkMQNEMRHLTGEKLeklyssytalTHNYELMDGYAAKSKVVGILKGLGFEeadfDRKIN-- 160
Cdd:PRK11247 86 --------------------MFQDARLLPWKKV----------IDNVGLGLKGQWRDAALQALAAVGLA----DRANEwp 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 161 -TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD-LRSIEW---LESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGN 235
Cdd:PRK11247 132 aALSGGQKQRVALARALIHRPGLLLLDEPLGALDaLTRIEMqdlIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
.
gi 496028547 236 V 236
Cdd:PRK11247 212 I 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-387 |
3.60e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGS---NeiiKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA---------KDA-KL 67
Cdd:COG3845 4 PALELRGITKRFGGvvaN---DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvrirspRDAiAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 68 GylrqINNVDSTLSIIDELyTVIEPILdmekrilkmqnemrhLTGEKLEKLyssytalthnyeLMDGYAAKSKVVGILKG 147
Cdd:COG3845 81 G----IGMVHQHFMLVPNL-TVAENIV---------------LGLEPTKGG------------RLDRKAARARIRELSER 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 148 LGFeEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD-------LRSIEWLESyllnyNG-AVVIVSHdry 219
Cdd:COG3845 129 YGL-DVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTpqeadelFEILRRLAA-----EGkSIIFITH--- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 220 fldkivskvidiengnvqmylgnytdfsnkkqmlldaKMKeylnqqqEIRhqeAV---ITKLKQFNREKSIKRAESRQKQ 296
Cdd:COG3845 200 -------------------------------------KLR-------EVM---AIadrVTVLRRGKVVGTVDTAETSEEE 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 297 L-------EKIERVDAPqtytenmrlsldiAKESGKDVLSVHNLS-KSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTT 368
Cdd:COG3845 233 LaelmvgrEVLLRVEKA-------------PAEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSE 299
|
410
....*....|....*....
gi 496028547 369 LLKIINGILEPDTGEVIYG 387
Cdd:COG3845 300 LAEALAGLRPPASGSIRLD 318
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
328-502 |
3.72e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.82 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSN------------------ 389
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrlallp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 390 --------VSV----AY--------------YDQEHQVLHMDKTLFDEISDtypemtntrirnilaaflftgedvyKKIS 443
Cdd:PRK11231 83 qhhltpegITVrelvAYgrspwlslwgrlsaEDNARVNQAMEQTRINHLAD-------------------------RRLT 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 444 DLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIvSKDV----LENALNSFPGTVCYVSHD-----RY 502
Cdd:PRK11231 138 DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI-NHQVelmrLMRELNTQGKTVVTVLHDlnqasRY 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-237 |
3.82e-15 |
|
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: 74.64 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 32 AIVGVNGAGKTTLLKILTGEEQADGGSVTL---------------AKDAKLGYLRQINNVDSTLSIIDELYTVIEPILDM 96
Cdd:cd03297 27 GIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdsrkkinlpPQQRKIGLVFQQYALFPHLNVRENLAFGLKRKRNR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 97 EKRILkmQNEMRHLTGekLEKLyssytalthnyelmdgyaakskvvgilkglgfeeadFDRKINTLSGGQKTRVFLAKLL 176
Cdd:cd03297 107 EDRIS--VDELLDLLG--LDHL------------------------------------LNRYPAQLSGGEKQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 177 LEEPDIILLDEPTNHLD--LRSI--EWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNVQ 237
Cdd:cd03297 147 AAQPELLLLDEPFSALDraLRLQllPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
332-533 |
3.93e-15 |
|
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: 74.95 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 332 NLSKSFDRKKL-FYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVS----------VAYYDQEH 399
Cdd:cd03254 7 NVNFSYDEKKPvLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdGIDIRdisrkslrsmIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 400 QVLhmDKTLFDEISDTYPEMTNTRIRNILAA-----FLFTGEDVYKKI-----SDLSGGERGRVSLVKLMLSKANFLLLD 469
Cdd:cd03254 87 FLF--SGTIMENIRLGRPNATDEEVIEAAKEagahdFIMKLPNGYDTVlgengGNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 470 EPTNHLDIVSKDVLENALNS-FPGTVCYVSHDRYFINKTATRILDLTENRLLNYiGNYDYYIEKR 533
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKlMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEE-GTHDELLAKK 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
328-391 |
4.00e-15 |
|
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: 74.88 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFY----------------------DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVI 385
Cdd:cd03220 1 IELENVSKSYPTYKGGSsslkklgilgrkgevgefwalkDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
....*.
gi 496028547 386 YGSNVS 391
Cdd:cd03220 81 VRGRVS 86
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-216 |
4.12e-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: 74.32 E-value: 4.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDA----KLGYLRQInnvds 78
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPlaeqRDEPHENI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 79 tlsiideLYtviepildmekrilkmqneMRHLTGEK-----LEKLysSYTALTHNYELMDGYAAKSKVvgilkGL-GFEe 152
Cdd:TIGR01189 76 -------LY-------------------LGHLPGLKpelsaLENL--HFWAAIHGGAQRTIEDALAAV-----GLtGFE- 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 153 adfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL---LNYNGAVVIVSH 216
Cdd:TIGR01189 122 ---DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLrahLARGGIVLLTTH 185
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
328-505 |
4.28e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 74.10 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGI--LEPDTGEVIYgsnvsvayydQEHQVLHMD 405
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILF----------KGEDITDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 406 KT------LFdeISDTYP-EMTNTRIRNILaAFLFTGedvykkisdLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIV 478
Cdd:cd03217 71 PEerarlgIF--LAFQYPpEIPGVKNADFL-RYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190
....*....|....*....|....*....|
gi 496028547 479 SKDVLENALNSF--PGT-VCYVSHDRYFIN 505
Cdd:cd03217 139 ALRLVAEVINKLreEGKsVLIITHYQRLLD 168
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-239 |
4.49e-15 |
|
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: 74.62 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKIL-------TGEEQADGGSVTLAKDAKLGYLRQINN 75
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMIlgiilpdSGEVLFDGKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 76 VDSTLSIIDEL-YtvIEPILDMEKRilkmqnEMRHLTGEKLEKLyssytalthnyELMDgYAakskvvgilkglgfeead 154
Cdd:cd03269 81 LYPKMKVIDQLvY--LAQLKGLKKE------EARRRIDEWLERL-----------ELSE-YA------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 155 fDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGA---VVIVSHDRYFLDKIVSKVIDI 231
Cdd:cd03269 123 -NKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgktVILSTHQMELVEELCDRVLLL 201
|
....*...
gi 496028547 232 ENGNVQMY 239
Cdd:cd03269 202 NKGRAVLY 209
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-225 |
5.89e-15 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 75.09 E-value: 5.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSF-GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL-------AKDAKL----- 67
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVdgqdvtaLRGRALrrlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 68 --GYLRQINNvdstlsIIDELyTVIEPILdmekrilkmqnemrhlTGeKLEKLySSYTALTHNY---ELMDGYAAKSKVv 142
Cdd:COG3638 81 riGMIFQQFN------LVPRL-SVLTNVL----------------AG-RLGRT-STWRSLLGLFppeDRERALEALERV- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 143 gilkGLgfeeADF-DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYN---GAVVIVS-HD 217
Cdd:COG3638 135 ----GL----ADKaYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAredGITVVVNlHQ 206
|
250
....*....|...
gi 496028547 218 -----RYFlDKIV 225
Cdd:COG3638 207 vdlarRYA-DRII 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
328-500 |
5.95e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 74.58 E-value: 5.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS--VAYYDQEHQVL-- 402
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlLDGKDITnlPPHKRPVNTVFqn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 403 -----HMdkTLFDEIS------DTYPEMTNTRIRNILaAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEP 471
Cdd:cd03300 81 yalfpHL--TVFENIAfglrlkKLPKAEIKERVAEAL-DLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190
....*....|....*....|....*....|...
gi 496028547 472 TNHLDI-VSKDV---LENALNSFPGTVCYVSHD 500
Cdd:cd03300 158 LGALDLkLRKDMqleLKRLQKELGITFVFVTHD 190
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-216 |
7.33e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.64 E-value: 7.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAkdaklGYLRQINNV----DSTLSI 82
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID-----GQEMRFASTtaalAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 I-DELYTVIEpildmekrilkmqnemrhLTgeKLEKLYssYTALTHNYELMDGYAAKSKVVGILKGLGfEEADFDRKINT 161
Cdd:PRK11288 84 IyQELHLVPE------------------MT--VAENLY--LGQLPHKGGIVNRRLLNYEAREQLEHLG-VDIDPDTPLKY 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 162 LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNGAVVI-VSH 216
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIreLRAEGRVILyVSH 198
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
340-512 |
7.43e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.47 E-value: 7.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 340 KKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYG---------------SNVSVAYYDQEHQVLhm 404
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvditdkkvklsdirKKVGLVFQYPEYQLF-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 405 DKTLFDEI---------SDtypEMTNTRIRNILAAFLFTGEDvYKKIS--DLSGGERGRVSLVKLMLSKANFLLLDEPTN 473
Cdd:PRK13637 98 EETIEKDIafgpinlglSE---EEIENRVKRAMNIVGLDYED-YKDKSpfELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496028547 474 HLDIVSKDVLENALNS----FPGTVCYVSHDRYFINKTATRIL 512
Cdd:PRK13637 174 GLDPKGRDEILNKIKElhkeYNMTIILVSHSMEDVAKLADRII 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
33-216 |
7.71e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.68 E-value: 7.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 33 IVGVNGAGKTTLLKILTGEEQADGGSVTLaKDAKLGYLRqinnvDSTLSiiDELYtviepildmekrilkmqneMRHLTG 112
Cdd:PRK13538 32 IEGPNGAGKTSLLRILAGLARPDAGEVLW-QGEPIRRQR-----DEYHQ--DLLY-------------------LGHQPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 113 EK-----LEKLySSYTALTHNYELMDGYAAKSKVvgilkGL-GFEEAdfdrKINTLSGGQKTRVFLAKLLLEEPDIILLD 186
Cdd:PRK13538 85 IKteltaLENL-RFYQRLHGPGDDEALWEALAQV-----GLaGFEDV----PVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190
....*....|....*....|....*....|...
gi 496028547 187 EPTNHLDLRSIEWLESYL---LNYNGAVVIVSH 216
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLaqhAEQGGMVILTTH 187
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-234 |
7.89e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.61 E-value: 7.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKD----------AKLGYLR 71
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 72 QINNVDSTlsiidelYTVIEPILdmekrilkmqnemrhltgeklekLYSSYTALThnyelmdGYAAKSKVVGILKgLGFE 151
Cdd:PRK13537 87 QFDNLDPD-------FTVRENLL-----------------------VFGRYFGLS-------AAAARALVPPLLE-FAKL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 152 EADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD--LRSIEW--LESyLLNYNGAVVIVSHDRYFLDKIVSK 227
Cdd:PRK13537 129 ENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDpqARHLMWerLRS-LLARGKTILLTTHFMEEAERLCDR 207
|
....*..
gi 496028547 228 VIDIENG 234
Cdd:PRK13537 208 LCVIEEG 214
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
345-488 |
8.30e-15 |
|
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: 74.19 E-value: 8.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS----------VAYYDQEhqVLHMDKTLFDEIS 413
Cdd:cd03251 20 DISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIlIDGHDVRdytlaslrrqIGLVSQD--VFLFNDTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 414 DTYPEMTNTRIRNILAA-----FLFTGEDVYKKI-----SDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVL 483
Cdd:cd03251 98 YGRPGATREEVEEAARAanaheFIMELPEGYDTVigergVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLV 177
|
....*
gi 496028547 484 ENALN 488
Cdd:cd03251 178 QAALE 182
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-236 |
8.95e-15 |
|
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: 73.68 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 29 EKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqINNVDstlsiidelYTVIEPILDMEKRILKMQNEMR 108
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNLIAGFETPQSGRVL------------INGVD---------VTAAPPADRPVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 109 HLTGEKLEKLyssytALTHNYELMDgyAAKSKVVGILKGLGFEEADfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEP 188
Cdd:cd03298 84 HLTVEQNVGL-----GLSPGLKLTA--EDRQAIEVALARVGLAGLE-KRLPGELSGGERQRVALARVLVRDKPVLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496028547 189 TNHLD--LRS-IEWLESYLLNYNG-AVVIVSHDRYFLDKIVSKVIDIENGNV 236
Cdd:cd03298 156 FAALDpaLRAeMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-225 |
1.06e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.42 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDA-------KLGylRQI 73
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvealsarAAS--RRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 74 NNV--DSTLSIIDELYTVIEpildmekrilkmqneM-RHLTGEKLEKLYSSYTALTHnyELMDGYAAkskvvgilkglgf 150
Cdd:PRK09536 80 ASVpqDTSLSFEFDVRQVVE---------------MgRTPHRSRFDTWTETDRAAVE--RAMERTGV------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 151 eeADF-DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDL-RSIEWLESY--LLNYNGAVVIVSHD-----RYfL 221
Cdd:PRK09536 130 --AQFaDRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDInHQVRTLELVrrLVDDGKTAVAAIHDldlaaRY-C 206
|
....
gi 496028547 222 DKIV 225
Cdd:PRK09536 207 DELV 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
317-476 |
1.12e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.14 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 317 LDIAKESGKDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVSVAYY 395
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLdGQDITHVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 396 DQEH------------------QV---LHMDKTLFDEIsdtypemtNTRIRNILAafLFTGEDV-YKKISDLSGGERGRV 453
Cdd:PRK09452 84 ENRHvntvfqsyalfphmtvfeNVafgLRMQKTPAAEI--------TPRVMEALR--MVQLEEFaQRKPHQLSGGQQQRV 153
|
170 180
....*....|....*....|...
gi 496028547 454 SLVKLMLSKANFLLLDEPTNHLD 476
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALD 176
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-188 |
1.13e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.91 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEkaaIVGV---NGAGKTTLLKILTGEEQADGGSVTLA----------KDAKL 67
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGE---IVGLlgpNGAGKTTTFYMIVGLVKPDSGRIFLDgedithlpmhKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 68 G--YLRQinnvdsTLSIIDELyTVIEPILdmekRILKMQNEMRHLTGEKLEklyssytalthnyELMDgyaakskvvgil 145
Cdd:COG1137 79 GigYLPQ------EASIFRKL-TVEDNIL----AVLELRKLSKKEREERLE-------------ELLE------------ 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496028547 146 kglgfeeaDF------DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEP 188
Cdd:COG1137 123 --------EFgithlrKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-236 |
1.17e-14 |
|
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: 77.15 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNE--IIK---SATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVtlakdaklgYLRqinnv 76
Cdd:TIGR03269 279 IIKVRNVSKRYISVDrgVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV---------NVR----- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 77 dstlsiidelytVIEPILDMEKRILKMQNEMRHLTGekleKLYSSYTALTH-----------NYELMDGYAaKSKVVGIL 145
Cdd:TIGR03269 345 ------------VGDEWVDMTKPGPDGRGRAKRYIG----ILHQEYDLYPHrtvldnlteaiGLELPDELA-RMKAVITL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 146 KGLGFEEAD----FDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLN----YNGAVVIVSHD 217
Cdd:TIGR03269 408 KMVGFDEEKaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKareeMEQTFIIVSHD 487
|
250
....*....|....*....
gi 496028547 218 RYFLDKIVSKVIDIENGNV 236
Cdd:TIGR03269 488 MDFVLDVCDRAALMRDGKI 506
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
330-512 |
1.21e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.02 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 330 VHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGS---NVSVAYYDQEHQVLHM-- 404
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitiDTARSLSQQKGLIRQLrq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 405 -------------DKTLFDEISD-------TYPEMTNTRIRNILAAFLFTG-EDVYKKisDLSGGERGRVSLVKLMLSKA 463
Cdd:PRK11264 86 hvgfvfqnfnlfpHRTVLENIIEgpvivkgEPKEEATARARELLAKVGLAGkETSYPR--RLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 464 NFLLLDEPTNHLDivsKDVLENALNSFPG------TVCYVSHDRYFINKTATRIL 512
Cdd:PRK11264 164 EVILFDEPTSALD---PELVGEVLNTIRQlaqekrTMVIVTHEMSFARDVADRAI 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
327-471 |
1.36e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.52 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS-----------VAY 394
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIfLDGEDIThlpmhkrarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 395 YDQEHQV---LhmdkTLFD------EISdtypEMTNTRIRNILAAFL--FTGEDVYKKISD-LSGGERGRVSLVKLMLSK 462
Cdd:COG1137 83 LPQEASIfrkL----TVEDnilavlELR----KLSKKEREERLEELLeeFGITHLRKSKAYsLSGGERRRVEIARALATN 154
|
....*....
gi 496028547 463 ANFLLLDEP 471
Cdd:COG1137 155 PKFILLDEP 163
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-216 |
1.37e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.98 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDA--------KLGYLRQ 72
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDiddpdvaeACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 73 INNVDSTLSIIDelytviepILDMEKRILKmqnemrhltgekleklyssytalTHNYELMDGYAAkskvVGiLKGLgfee 152
Cdd:PRK13539 81 RNAMKPALTVAE--------NLEFWAAFLG-----------------------GEELDIAAALEA----VG-LAPL---- 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 153 adFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL---LNYNGAVVIVSH 216
Cdd:PRK13539 121 --AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIrahLAQGGIVIAATH 185
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-188 |
1.39e-14 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 73.35 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA----------KDAKLG--YL 70
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqditklpmhKRARLGigYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 71 RQINNVDSTLSIIDELYTVIEPILDMEKRILKMQNEMrhltgekLEKLyssytALTHnyelmdgyaakskvvgILKGLGF 150
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEEL-------LEEF-----HITH----------------LRKSKAS 132
|
170 180 190
....*....|....*....|....*....|....*...
gi 496028547 151 eeadfdrkinTLSGGQKTRVFLAKLLLEEPDIILLDEP 188
Cdd:cd03218 133 ----------SLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
328-477 |
1.89e-14 |
|
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: 73.70 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSnVSVAYYDQEHQVLHMdkT 407
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAG-VDLHGLSRRARARRV--A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 408 LFDEISDTYPemtNTRIRNILA------AFLFTGE--------DVY-----------KKISDLSGGERGRVSLVKLMLSK 462
Cdd:TIGR03873 79 LVEQDSDTAV---PLTVRDVVAlgriphRSLWAGDsphdaavvDRAlartelshladRDMSTLSGGERQRVHVARALAQE 155
|
170
....*....|....*
gi 496028547 463 ANFLLLDEPTNHLDI 477
Cdd:TIGR03873 156 PKLLLLDEPTNHLDV 170
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
328-561 |
1.94e-14 |
|
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: 76.38 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGI--LEPDTGEVIY-----------------GS 388
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 389 NVSV---AYYDQEHQVLHMDKTLFDEISDTYPEM---------TNTRIRNILAAFL---FTGEDVYKK------------ 441
Cdd:TIGR03269 81 PCPVcggTLEPEEVDFWNLSDKLRRRIRKRIAIMlqrtfalygDDTVLDNVLEALEeigYEGKEAVGRavdliemvqlsh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 442 -----ISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENAL----NSFPGTVCYVSHDRYFINKTATRIL 512
Cdd:TIGR03269 161 rithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeavKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 496028547 513 dLTENRLLNYIGNYDYYIEK-REAVEEAANLSNIEQAQKGIDVSESKQEW 561
Cdd:TIGR03269 241 -WLENGEIKEEGTPDEVVAVfMEGVSEVEKECEVEVGEPIIKVRNVSKRY 289
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
13-236 |
2.13e-14 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 76.34 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 13 GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKD-----------AKLGYLRQinnvDSTL- 80
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrRQIAWVPQ----NPYLf 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 --SIIDelytviepildmekrILKMQNemRHLTGEKLEKLyssytalthnyelmdgyAAKSKVVGILKGLgfeEADFDRK 158
Cdd:COG4988 424 agTIRE---------------NLRLGR--PDASDEELEAA-----------------LEAAGLDEFVAAL---PDGLDTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 159 IN----TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNY--NGAVVIVSHDRYFLdKIVSKVIDIE 232
Cdd:COG4988 467 LGeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALL-AQADRILVLD 545
|
....
gi 496028547 233 NGNV 236
Cdd:COG4988 546 DGRI 549
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-217 |
2.67e-14 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 72.85 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNE----IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA--------KDAKLGY 69
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAgqdlfaldEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 70 LRQinnvdsTLSIIDelytviepildmekrilkmQNEMrhltgeklekLYSSYTALtHN----YELMDGYAAKSKVVGIL 145
Cdd:COG4181 88 RAR------HVGFVF-------------------QSFQ----------LLPTLTAL-ENvmlpLELAGRRDARARARALL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 146 K--GLGfeeADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS----IEWLESylLN--YNGAVVIVSHD 217
Cdd:COG4181 132 ErvGLG---HRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFE--LNreRGTTLVLVTHD 206
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-239 |
2.90e-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: 72.57 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 17 IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqinnVDSTLSIIDELYTVIEPildm 96
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT---------------VRGRVSSLLGLGGGFNP---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 97 ekrilkmqnemrHLTGEklEKLYssYTALTHNyelMDGYAAKSKVVGIlkgLGFEE--ADFDRKINTLSGGQKTRVFLAK 174
Cdd:cd03220 98 ------------ELTGR--ENIY--LNGRLLG---LSRKEIDEKIDEI---IEFSElgDFIDLPVKTYSSGMKARLAFAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 175 LLLEEPDIILLDEPT----NHLDLRSIEWLESyLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNVQMY 239
Cdd:cd03220 156 ATALEPDILLIDEVLavgdAAFQEKCQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
2-234 |
4.79e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.80 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSF---------GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSV--------TLAKD 64
Cdd:PRK10419 3 LLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplaKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 65 AKLGYLRQINNV--DStLSIIDELYTViepildmeKRILKmqNEMRHLTGekleklyssytalthnyelMDGYAAKSKVV 142
Cdd:PRK10419 83 QRKAFRRDIQMVfqDS-ISAVNPRKTV--------REIIR--EPLRHLLS-------------------LDKAERLARAS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 143 GILKGLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDL----RSIEWLESYLLNYNGAVVIVSHDR 218
Cdd:PRK10419 133 EMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDL 212
|
250
....*....|....*.
gi 496028547 219 YFLDKIVSKVIDIENG 234
Cdd:PRK10419 213 RLVERFCQRVMVMDNG 228
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
346-520 |
5.73e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 5.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 346 INFEIKRGERVAIIGDNGTGKTTLLKIINGILePDTGEVIY-GSNVSV----------AYYDQEHQ------VLHM---- 404
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFaGQPLEAwsaaelarhrAYLSQQQTppfampVFQYltlh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 405 --DKTLFDEISDTYPEmtntrirniLAAFLFTGEDVYKKISDLSGGERGRVSLVKLML-------SKANFLLLDEPTNHL 475
Cdd:PRK03695 94 qpDKTRTEAVASALNE---------VAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496028547 476 DIVSKDVLENALNSFP---GTVCYVSHDryfINKT---ATRILDLTENRLL 520
Cdd:PRK03695 165 DVAQQAALDRLLSELCqqgIAVVMSSHD---LNHTlrhADRVWLLKQGKLL 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
328-476 |
5.82e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 71.36 E-value: 5.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPD---TGEVIYGsNVSVAYYDQEHQ---V 401
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLN-GRRLTALPAEQRrigI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 402 LHMDKTLFDEIS-------DTYPEMT-NTRIRNILAAfL-------FTGEDVykkiSDLSGGERGRVSLVKLMLSKANFL 466
Cdd:COG4136 81 LFQDDLLFPHLSvgenlafALPPTIGrAQRRARVEQA-LeeaglagFADRDP----ATLSGGQRARVALLRALLAEPRAL 155
|
170
....*....|
gi 496028547 467 LLDEPTNHLD 476
Cdd:COG4136 156 LLDEPFSKLD 165
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-228 |
6.07e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 72.07 E-value: 6.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLaKDAKLGYLR--QINNVD- 77
Cdd:COG4674 9 PILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLF-GGTDLTGLDehEIARLGi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 78 ----STLSIIDELyTVIEpildmekrilkmqNEMRHLTGEKleklySSYTALTHNyelMDGyAAKSKVVGILK--GLgfe 151
Cdd:COG4674 88 grkfQKPTVFEEL-TVFE-------------NLELALKGDR-----GVFASLFAR---LTA-EERDRIEEVLEtiGL--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 152 EADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEP----TNHLDLRSIEWLESylLNYNGAVVIVSHDRYFLDKIVSK 227
Cdd:COG4674 142 TDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPvagmTDAETERTAELLKS--LAGKHSVVVVEHDMEFVRQIARK 219
|
.
gi 496028547 228 V 228
Cdd:COG4674 220 V 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-236 |
7.07e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 74.76 E-value: 7.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNE----IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKdaklgylRQINNVD 77
Cdd:PRK10535 4 LLELKDIRRSYPSGEeqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAG-------QDVATLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 78 StlsiiDELytviePILDMEKR--ILKMQNEMRHLTGEkleklyssytaltHNYELMDGYAAKSK------VVGILKGLG 149
Cdd:PRK10535 77 A-----DAL-----AQLRREHFgfIFQRYHLLSHLTAA-------------QNVEVPAVYAGLERkqrllrAQELLQRLG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 150 FEEAdFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNG-AVVIVSHDRYFLDKiVS 226
Cdd:PRK10535 134 LEDR-VEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILhqLRDRGhTVIIVTHDPQVAAQ-AE 211
|
250
....*....|
gi 496028547 227 KVIDIENGNV 236
Cdd:PRK10535 212 RVIEIRDGEI 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
316-476 |
7.17e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.14 E-value: 7.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 316 SLDIAKESGkDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILE--PDTGEViygsNVSVA 393
Cdd:COG2401 20 VLDLSERVA-IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCV----DVPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 394 YYDQEhqvlhmdKTLFDEISDTYPEMTNTRIRNI--LA-AFLFtgedvYKKISDLSGGERGRVSLVKLMLSKANFLLLDE 470
Cdd:COG2401 95 QFGRE-------ASLIDAIGRKGDFKDAVELLNAvgLSdAVLW-----LRRFKELSTGQKFRFRLALLLAERPKLLVIDE 162
|
....*.
gi 496028547 471 PTNHLD 476
Cdd:COG2401 163 FCSHLD 168
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
327-507 |
7.59e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.75 E-value: 7.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVS---VAYYDQEHQVL 402
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKkdlCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 403 HMDK-----TLFDE-ISDTYPEMTNTRIRNILAAFLFtGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLD 476
Cdd:PRK13540 81 HRSGinpylTLRENcLYDIHFSPGAVGITELCRLFSL-EHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180 190
....*....|....*....|....*....|....
gi 496028547 477 IVSKDVLENALNSFP---GTVCYVSHDRYFINKT 507
Cdd:PRK13540 160 ELSLLTIITKIQEHRakgGAVLLTSHQDLPLNKA 193
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
328-386 |
8.25e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.88 E-value: 8.25e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY 386
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHY 65
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-234 |
8.98e-14 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 70.93 E-value: 8.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSF-----GSNEI--IKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGS---------VTLAKDA 65
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilvrhdggwVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 66 K----------LGY----LRQINNVdSTLSIidelytVIEPILDMekrilkmqnemrhltGEKLEklyssytalthnyel 131
Cdd:COG4778 84 PreilalrrrtIGYvsqfLRVIPRV-SALDV------VAEPLLER---------------GVDRE--------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 132 mdgyAAKSKVVGILKGLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS----IEWLESYLLny 207
Cdd:COG4778 127 ----EARARARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKA-- 200
|
250 260
....*....|....*....|....*...
gi 496028547 208 NGAVVI-VSHDRYFLDKIVSKVIDIENG 234
Cdd:COG4778 201 RGTAIIgIFHDEEVREAVADRVVDVTPF 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-215 |
9.88e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.06 E-value: 9.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL-------AKDAKLGYLrqin 74
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdgepldpEDRRRIGYL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 75 nvdstlsiIDE--LY---TVIEPILDMEKrilkmqnemrhLTGekleklyssytalthnyelMDGYAAKSKVVGILKGLG 149
Cdd:COG4152 77 --------PEErgLYpkmKVGEQLVYLAR-----------LKG-------------------LSKAEAKRRADEWLERLG 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 150 FEEADfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNY--NGAVVIVS 215
Cdd:COG4152 119 LGDRA-NKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGTTVIFS 185
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-236 |
1.02e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 71.32 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqinnvdstlsiidel 86
Cdd:PRK11264 8 NLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIR-------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 87 ytVIEPILDMEKRILKMQNEMRHLTgEKLEKLYSSYTALTHNYELMDGYAAKSKVVGILK--------------GLGFEE 152
Cdd:PRK11264 62 --VGDITIDTARSLSQQKGLIRQLR-QHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKeeatararellakvGLAGKE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 153 ADFDRKintLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSI-EWLESY--LLNYNGAVVIVSHDRYFLDKIVSKVI 229
Cdd:PRK11264 139 TSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVgEVLNTIrqLAQEKRTMVIVTHEMSFARDVADRAI 215
|
....*..
gi 496028547 230 DIENGNV 236
Cdd:PRK11264 216 FMDQGRI 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
338-499 |
1.03e-13 |
|
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: 71.11 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 338 DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYG---SNVSVAYYDQEHQVLHMDKTLFDeis 413
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlIDGqdiREVTLDSLRRAIGVVPQDTVLFN--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 414 DTYpeMTNTRIRNILAaflfTGEDVYK-----KISD-------------------LSGGERGRVSLVKLMLSKANFLLLD 469
Cdd:cd03253 89 DTI--GYNIRYGRPDA----TDEEVIEaakaaQIHDkimrfpdgydtivgerglkLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190
....*....|....*....|....*....|..
gi 496028547 470 EPTNHLDIVSKDVLENALNSFPG--TVCYVSH 499
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSKgrTTIVIAH 194
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
346-500 |
1.06e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 70.94 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 346 INFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGsNVSVAYYD----------QEHqvlhmdkTLFdeisdt 415
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN-GQDLTALPpaerpvsmlfQEN-------NLF------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 416 yPEMT---N----------------TRIRNILAAFLFTG-EDvyKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHL 475
Cdd:COG3840 84 -PHLTvaqNiglglrpglkltaeqrAQVEQALERVGLAGlLD--RLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180
....*....|....*....|....*....
gi 496028547 476 DIVSKD---VLENALNSFPG-TVCYVSHD 500
Cdd:COG3840 161 DPALRQemlDLVDELCRERGlTVLMVTHD 189
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-193 |
1.11e-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: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGsvtlakdaklgylrqinnvdsTLSIIDEL 86
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSG---------------------RIYIGGRD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 87 YTVIEPildmEKRILKM--QNEmrhltgekleKLYSSYTA---LTHNYEL--MDGYAAKSKVVGILKGLGFEEAdFDRKI 159
Cdd:cd03301 64 VTDLPP----KDRDIAMvfQNY----------ALYPHMTVydnIAFGLKLrkVPKDEIDERVREVAELLQIEHL-LDRKP 128
|
170 180 190
....*....|....*....|....*....|....
gi 496028547 160 NTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:cd03301 129 KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
346-520 |
1.18e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.02 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 346 INFEIKRGERVAIIGDNGTGKTTLLKIINGILePDTGEVIYG----SNVSV-------AYYDQeHQV------------L 402
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNgrplSDWSAaelarhrAYLSQ-QQSppfampvfqylaL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 403 HMDKTLFDEISDTYPEMtntrirniLAAFLFTGEDVYKKISDLSGGERGRVSLVKLML---SKAN----FLLLDEPTNHL 475
Cdd:COG4138 93 HQPAGASSEAVEQLLAQ--------LAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwPTINpegqLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496028547 476 DIVSKDVLENALNSFP---GTVCYVSHDryfINKT---ATRILDLTENRLL 520
Cdd:COG4138 165 DVAQQAALDRLLRELCqqgITVVMSSHD---LNHTlrhADRVWLLKQGKLV 212
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
322-500 |
1.19e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.72 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 322 ESGKDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVSVAYYDQEHQ 400
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIPAMSRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 401 V------------LHMDKTLFDEISdtYPEMTNTRIRNIL--AAFLFTGEDV------YKKISDLSGGERGRVSLVKLML 460
Cdd:PRK11831 82 VrkrmsmlfqsgaLFTDMNVFDNVA--YPLREHTQLPAPLlhSTVMMKLEAVglrgaaKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496028547 461 SKANFLLLDEPTNHLDIVSKDVLE---NALNSFPGTVC-YVSHD 500
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVkliSELNSALGVTCvVVSHD 203
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-240 |
1.21e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.00 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFG----SNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKdaklgylRQINNVD 77
Cdd:PRK11629 5 LLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNG-------QPMSKLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 78 STLSIidelytviepilDMEKRILKMQNEMRHLTGEkleklyssYTALTH-NYELMDGYA----AKSKVVGILKGLGFEE 152
Cdd:PRK11629 78 SAAKA------------ELRNQKLGFIYQFHHLLPD--------FTALENvAMPLLIGKKkpaeINSRALEMLAAVGLEH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 153 ADFDRKiNTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYN----GAVVIVSHDRYfLDKIVSKV 228
Cdd:PRK11629 138 RANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHDLQ-LAKRMSRQ 215
|
250
....*....|..
gi 496028547 229 IDIENGNVQMYL 240
Cdd:PRK11629 216 LEMRDGRLTAEL 227
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-216 |
1.24e-13 |
|
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: 70.77 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA----------KDAKLG--Y 69
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgqdithlpmhERARLGigY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 70 LRQINNVDSTLSIIDELYTVIEPILDMEKrilkmqNEMRHLTGEKLEKLyssytALTHnyelmdgyaakskvvgILKGLG 149
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIRKDLDR------AEREERLEALLEEF-----QISH----------------LRDNKA 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 150 FeeadfdrkinTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD---LRSIEWLESYLLNYNGAVVIVSH 216
Cdd:TIGR04406 134 M----------SLSGGERRRVEIARALATNPKFILLDEPFAGVDpiaVGDIKKIIKHLKERGIGVLITDH 193
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-217 |
1.26e-13 |
|
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: 70.67 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTG-----EEQADGGSVTLAKDaklgylrqinnvd 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGK------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 78 stlsiidELYTVIEPILDMEKRI---------LKM--QNEMRH---LTGEKLEklyssytalthnyELMDGYAAKSkvvg 143
Cdd:cd03260 68 -------DIYDLDVDVLELRRRVgmvfqkpnpFPGsiYDNVAYglrLHGIKLK-------------EELDERVEEA---- 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 144 iLKGLG-FEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNG--AVVIVSHD 217
Cdd:cd03260 124 -LRKAAlWDEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
273-487 |
1.39e-13 |
|
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: 74.56 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 273 AVITKLKQFNREKSIKRAESRQKQLEkIERVDAPQTYTENMRLSLDIAKE--------SGKDVLSVHNLSKSFdrKKLFY 344
Cdd:TIGR01271 367 GAITKIQDFLCKEEYKTLEYNLTTTE-VEMVNVTASWDEGIGELFEKIKQnnkarkqpNGDDGLFFSNFSLYV--TPVLK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSvaYYDQEHQVlhMDKTLFDEI--SDTYPEMtnt 422
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIS--FSPQTSWI--MPGTIKDNIifGLSYDEY--- 516
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 423 RIRNILAAFLFTgEDVYK-----KIS------DLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVS-KDVLENAL 487
Cdd:TIGR01271 517 RYTSVIKACQLE-EDIALfpekdKTVlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTeKEIFESCL 592
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-484 |
1.54e-13 |
|
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: 73.57 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSN----EIIKSATFLINEHEKAAIVGVNGAGKT----TLLKILTGEEQADGGSVTLAKDAKLGY---- 69
Cdd:COG4172 6 LLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLsere 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 70 LRQI--NNVdstlSII--------DELYTViepildmEKRIlkmqnemrhltGEKLEklyssytalTHnyELMDGYAAKS 139
Cdd:COG4172 86 LRRIrgNRI----AMIfqepmtslNPLHTI-------GKQI-----------AEVLR---------LH--RGLSGAAARA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 140 KVVGILKGLGFEEADfdRKINT----LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDL---RSIewLEsyLLN-----Y 207
Cdd:COG4172 133 RALELLERVGIPDPE--RRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvqAQI--LD--LLKdlqreL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 208 NGAVVIVSHDryfLDkIVSKVID----------IENGNVQMYLGN----YTdfsnkkQMLLDAKMKeylnqqqeirhqea 273
Cdd:COG4172 207 GMALLLITHD---LG-VVRRFADrvavmrqgeiVEQGPTAELFAApqhpYT------RKLLAAEPR-------------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 274 vitklkqfnreksikraesrqkqlekieRVDAPqtytenmrlsldiAKESGKDVLSVHNLSKSFDRKK-LFY-------- 344
Cdd:COG4172 263 ----------------------------GDPRP-------------VPPDAPPLLEARDLKVWFPIKRgLFRrtvghvka 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 --DINFEIKRGERVAIIGDNGTGKTTLLKIINGiLEPDTGEVIY-GSNVSVAyydQEHQVLHMDKTL---FdeiSDTY-- 416
Cdd:COG4172 302 vdGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFdGQDLDGL---SRRALRPLRRRMqvvF---QDPFgs 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 417 --PEMTntrIRNILA---AFLF---TGEDVYKKISDL------------------SGGERGRVSLVKLMLSKANFLLLDE 470
Cdd:COG4172 375 lsPRMT---VGQIIAeglRVHGpglSAAERRARVAEAleevgldpaarhryphefSGGQRQRIAIARALILEPKLLVLDE 451
|
570
....*....|....*
gi 496028547 471 PTNHLDI-VSKDVLE 484
Cdd:COG4172 452 PTSALDVsVQAQILD 466
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-225 |
1.57e-13 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 73.47 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSF-GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVtlakdaklgylrQINNVdsTLS 81
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI------------AVNGV--PLA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 82 IIDELytviepilDMEKRILKM-QNEmrhltgekleklYSSYTALTHNYELMDGYAAKSKVVGILKGLGFEE--ADFDRK 158
Cdd:TIGR02857 388 DADAD--------SWRDQIAWVpQHP------------FLFAGTIAENIRLARPDASDAEIREALERAGLDEfvAALPQG 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 159 INT--------LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNY--NGAVVIVSHDR---YFLDKIV 225
Cdd:TIGR02857 448 LDTpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLalaALADRIV 527
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-217 |
1.64e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 73.55 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 13 GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLakdaklgylrqiNNVDSTLSIIDELytviep 92
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTL------------DGVPVSSLDQDEV------ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 93 ildmeKRILKMQNEMRHLTGekleklyssyTALTHNYELMDGYAAKSKVVGILKGLGFEE--ADFDRKINT--------L 162
Cdd:TIGR02868 408 -----RRRVSVCAQDAHLFD----------TTVRENLRLARPDATDEELWAALERVGLADwlRALPDGLDTvlgeggarL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 163 SGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNG--AVVIVSHD 217
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSgrTVVLITHH 529
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-217 |
1.89e-13 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 70.44 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIiKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLakdaklgylrqiNNVDST------- 79
Cdd:cd03299 5 NLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL------------NGKDITnlppekr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 80 -LSIIDELYTVIePILDMEKRIlkmQNEMRHLTGEKLEKlyssytalthnyelmdgyaaKSKVVGILKGLGFEEAdFDRK 158
Cdd:cd03299 72 dISYVPQNYALF-PHMTVYKNI---AYGLKKRKVDKKEI--------------------ERKVLEIAEMLGIDHL-LNRK 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 159 INTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLL----NYNGAVVIVSHD 217
Cdd:cd03299 127 PETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKkirkEFGVTVLHVTHD 189
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-219 |
1.96e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 70.81 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLK----ILT---------GEEQADGGSVTLAKdaKL 67
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKcfarLLTpqsgtvflgDKPISMLSSRQLAR--RL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 68 GYLRQINnvdstlsIIDELYTVIE-------PILDMEKRilkMQNEMRHLTGEKLEKlyssytalTHNYELMDgyaaksk 140
Cdd:PRK11231 79 ALLPQHH-------LTPEGITVRElvaygrsPWLSLWGR---LSAEDNARVNQAMEQ--------TRINHLAD------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 141 vvgilkglgfeeadfdRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDL-RSIEwLESYL--LNYNG-AVVIVSH 216
Cdd:PRK11231 134 ----------------RRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDInHQVE-LMRLMreLNTQGkTVVTVLH 196
|
....*...
gi 496028547 217 D-----RY 219
Cdd:PRK11231 197 DlnqasRY 204
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
325-501 |
2.85e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 71.67 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 325 KDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNV---SVAYYD---- 396
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfIDGEDVthrSIQQRDicmv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 397 -QEHQVL-HMdkTLFDEISdtY--------PEMTNTRIRNILAAFLFTG-EDVYkkISDLSGGERGRVSLVKLMLSKANF 465
Cdd:PRK11432 84 fQSYALFpHM--SLGENVG--YglkmlgvpKEERKQRVKEALELVDLAGfEDRY--VDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496028547 466 LLLDEPTNHLDI----VSKDVLENALNSFPGTVCYVSHDR 501
Cdd:PRK11432 158 LLFDEPLSNLDAnlrrSMREKIRELQQQFNITSLYVTHDQ 197
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-476 |
2.99e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 72.35 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 23 FLINEHEKAAIVGVNGAGKTTL-------LKILTGEEQADGGSVTLAKDAKLGYLR----QINNVDsTLSII--DELYTV 89
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALaralageLPLLSGERQSQFSHITRLSFEQLQKLVsdewQRNNTD-MLSPGedDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 90 IEPIldmekrilkmQNEmrhltgekleklyssytalTHNYELMDGYAAKskvVGILKGLgfeeadfDRKINTLSGGQKTR 169
Cdd:PRK10938 103 AEII----------QDE-------------------VKDPARCEQLAQQ---FGITALL-------DRRFKYLSTGETRK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 170 VFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNGAVVIVshdryfldkIVSKVIDIengnvqmylgnyTDFS 247
Cdd:PRK10938 144 TLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLasLHQSGITLVL---------VLNRFDEI------------PDFV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 248 NKKQMLLDAKMKEyLNQQQEIRhQEAVITKLkqfnreksikrAESrqkqlEKIERVDAPQTYTENMRLSLDiakeSGKDV 327
Cdd:PRK10938 203 QFAGVLADCTLAE-TGEREEIL-QQALVAQL-----------AHS-----EQLEGVQLPEPDEPSARHALP----ANEPR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIING----------IL---EPDTGEVIYGSNVSVAY 394
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndlTLfgrRRGSGETIWDIKKHIGY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 395 YDQEhqvLHMDktlfdeisdtYpeMTNTRIRN-ILAAFlFTGEDVYKKISD--------------------------LSG 447
Cdd:PRK10938 341 VSSS---LHLD----------Y--RVSTSVRNvILSGF-FDSIGIYQAVSDrqqklaqqwldilgidkrtadapfhsLSW 404
|
490 500
....*....|....*....|....*....
gi 496028547 448 GERGRVSLVKLMLSKANFLLLDEPTNHLD 476
Cdd:PRK10938 405 GQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
334-476 |
3.07e-13 |
|
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: 68.83 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 334 SKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPD---TGEVIYGSNVsvayYDQEHQVLHMDkTLFD 410
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP----YKEFAEKYPGE-IIYV 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 411 EISDTY-PEMTntrIRNIL-AAFLFTGEDVYKKISdlsGGERGRVSLVKLMLSKANFLLLDEPTNHLD 476
Cdd:cd03233 89 SEEDVHfPTLT---VRETLdFALRCKGNEFVRGIS---GGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-218 |
3.51e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.40 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL-AKDAKL--GYLRQINNVDS 78
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLdGVDLSHvpPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 79 TLSIIdelytviePILDMEKRI---LKM----QNEMRHLTGEKLeklyssytALTHnyelMDGYAAkskvvgilkglgfe 151
Cdd:PRK11607 99 SYALF--------PHMTVEQNIafgLKQdklpKAEIASRVNEML--------GLVH----MQEFAK-------------- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 152 eadfdRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD--LRSIEWLESY-LLNYNGAV-VIVSHDR 218
Cdd:PRK11607 145 -----RKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkLRDRMQLEVVdILERVGVTcVMVTHDQ 210
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
328-520 |
3.84e-13 |
|
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: 72.44 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSF---DRKKLfYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVS----------VA 393
Cdd:TIGR02203 331 VEFRNVTFRYpgrDRPAL-DSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLdGHDLAdytlaslrrqVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 394 YYDQehQVLHMDKTLFDEIS----DTYPEmtnTRIRNILAAF--------LFTGED--VYKKISDLSGGERGRVSLVKLM 459
Cdd:TIGR02203 410 LVSQ--DVVLFNDTIANNIAygrtEQADR---AEIERALAAAyaqdfvdkLPLGLDtpIGENGVLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 460 LSKANFLLLDEPTNHLDIVSKDVLENALNSF-PG-TVCYVSHDRYFINKtATRILDLTENRLL 520
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLmQGrTTLVIAHRLSTIEK-ADRIVVMDDGRIV 546
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-236 |
6.59e-13 |
|
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: 68.76 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSN----EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqINNVDstlsi 82
Cdd:cd03258 6 NVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVL------------VDGTD----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 idelytviepILDMEKRILKmqnEMRHLTGEKLE--KLYSSYTALtHNYEL------MDGYAAKSKVVGILKGLGFEEAD 154
Cdd:cd03258 69 ----------LTLLSGKELR---KARRRIGMIFQhfNLLSSRTVF-ENVALpleiagVPKAEIEERVLELLELVGLEDKA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 155 fDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNG----AVVIVSHDRYFLDKIVSKVID 230
Cdd:cd03258 135 -DAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelglTIVLITHEMEVVKRICDRVAV 213
|
....*.
gi 496028547 231 IENGNV 236
Cdd:cd03258 214 MEKGEV 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-195 |
8.21e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 70.36 E-value: 8.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAkDAKLGYL----RQINNVD 77
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-GQDITHVpaenRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 78 STLSIIDELyTVIEPI---LDMEKrilkmqnemrhltgekleklyssytalTHNYELmdgyaaKSKVVGILKGLGFEEAD 154
Cdd:PRK09452 93 QSYALFPHM-TVFENVafgLRMQK---------------------------TPAAEI------TPRVMEALRMVQLEEFA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496028547 155 fDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD--LR 195
Cdd:PRK09452 139 -QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDykLR 180
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
7-217 |
8.40e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 8.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYLRQINNVDSTLSIIDEL 86
Cdd:PRK09544 9 NVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 87 YTVIEP------ILDMEKRIlkmqnEMRHLTGEKLEKlyssytalthnyelmdgyaakskvvgilkglgfeeadfdrkin 160
Cdd:PRK09544 89 FLRLRPgtkkedILPALKRV-----QAGHLIDAPMQK------------------------------------------- 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496028547 161 tLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS-------IEWLESYLlnyNGAVVIVSHD 217
Cdd:PRK09544 121 -LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGqvalydlIDQLRREL---DCAVLMVSHD 180
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
333-519 |
8.87e-13 |
|
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: 67.90 E-value: 8.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 333 LSKSFDR-KKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSnVSVAYYDQEHQVLHMdktLFDE 411
Cdd:cd03298 3 LDKIRFSyGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-VDVTAAPPADRPVSM---LFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 412 iSDTYPEMT-------------------NTRIRNILAAFLFTGEDVyKKISDLSGGERGRVSLVKLMLSKANFLLLDEPT 472
Cdd:cd03298 79 -NNLFAHLTveqnvglglspglkltaedRQAIEVALARVGLAGLEK-RLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496028547 473 NHLDIVSKDVLENALNSFPG----TVCYVSHDRYFINKTATRILDLTENRL 519
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAetkmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
340-476 |
9.19e-13 |
|
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: 68.07 E-value: 9.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 340 KKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPD---TGEVIY-GSNVS-------VAYYDQEHQVLhmdKTL 408
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFnGQPRKpdqfqkcVAYVRQDDILL---PGL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 409 FDEISDTY------PEMTNTRIRNILAAFLFTGE----DV-YKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLD 476
Cdd:cd03234 97 TVRETLTYtailrlPRKSSDAIRKKRVEDVLLRDlaltRIgGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
345-476 |
9.19e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.11 E-value: 9.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGS---------------NVSVAYYDQEHQVLhmDKTLF 409
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrkglmklreSVGMVFQDPDNQLF--SASVY 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 410 DEISDTYPEM------TNTRIRNILAAflfTGED--VYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLD 476
Cdd:PRK13636 102 QDVSFGAVNLklpedeVRKRVDNALKR---TGIEhlKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
25-236 |
1.00e-12 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 68.68 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 25 INEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKD--AKLGYlRQINNVDSTLSII-DELYTVIEPildmekril 101
Cdd:TIGR02769 34 IEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlYQLDR-KQRRAFRRDVQLVfQDSPSAVNP--------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 102 kmQNEMRHLTGEKLEklyssytalthNYELMDGYAAKSKVVGILKGLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPD 181
Cdd:TIGR02769 104 --RMTVRQIIGEPLR-----------HLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 182 IILLDEPTNHLDL----RSIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNV 236
Cdd:TIGR02769 171 LIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-195 |
1.04e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 69.72 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqINNVDstlsiIDEL 86
Cdd:COG3839 8 NVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIL------------IGGRD-----VTDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 87 ytviEPildmEKRILKM--QNE--MRHLT-------GEKLEKlyssytalthnyelMDGYAAKSKVVGILKGLGFEEAdF 155
Cdd:COG3839 71 ----PP----KDRNIAMvfQSYalYPHMTvyeniafPLKLRK--------------VPKAEIDRRVREAAELLGLEDL-L 127
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496028547 156 DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD--LR 195
Cdd:COG3839 128 DRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDakLR 169
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
327-514 |
1.14e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.57 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS-------VAYYDQ- 397
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqIDGKTATrgdrsrfMAYLGHl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 398 --------EHQVLHMDKTLFDEISDTYPEmtntrirNILAAFLFTG-EDVYkkISDLSGGERGRVSLVKLMLSKANFLLL 468
Cdd:PRK13543 91 pglkadlsTLENLHFLCGLHGRRAKQMPG-------SALAIVGLAGyEDTL--VRQLSAGQKKRLALARLWLSPAPLWLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496028547 469 DEPTNHLDIVSKDVLENALNSF---PGTVCYVSHDRYFINKTATRILDL 514
Cdd:PRK13543 162 DEPYANLDLEGITLVNRMISAHlrgGGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
327-500 |
1.20e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.35 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKK-----------LFY----------DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEvi 385
Cdd:COG4586 1 IIEVENLSKTYRVYEkepglkgalkgLFRreyreveavdDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 386 ygsnVSVAYYD-----------------QEHQvLHMDKTL---FDEISDTYpEMTNTRIRNILAAF--LFTGEDVYKK-I 442
Cdd:COG4586 79 ----VRVLGYVpfkrrkefarrigvvfgQRSQ-LWWDLPAidsFRLLKAIY-RIPDAEYKKRLDELveLLDLGELLDTpV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496028547 443 SDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENAL----NSFPGTVCYVSHD 500
Cdd:COG4586 153 RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLkeynRERGTTILLTSHD 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
345-500 |
1.35e-12 |
|
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: 67.49 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY--------GSNVSVAYydQEHQVLHMdKTLFDEIS--- 413
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILegkqitepGPDRMVVF--QNYSLLPW-LTVRENIAlav 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 414 -DTYPEMTNTRIRNILA---AFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENAL-- 487
Cdd:TIGR01184 80 dRVLPDLSKSERRAIVEehiALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmq 159
|
170
....*....|....*
gi 496028547 488 --NSFPGTVCYVSHD 500
Cdd:TIGR01184 160 iwEEHRVTVLMVTHD 174
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
332-500 |
1.44e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.67 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 332 NLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYG---------SNVSVAYYDQEHQVL 402
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGekrmndvppAERGVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 403 -HMdkTLFDEIS------DTYPEMTNTRIRNIlAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHL 475
Cdd:PRK11000 88 pHL--SVAENMSfglklaGAKKEEINQRVNQV-AEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190
....*....|....*....|....*....|....
gi 496028547 476 DI---------VSKdvLENALNSfpgTVCYVSHD 500
Cdd:PRK11000 165 DAalrvqmrieISR--LHKRLGR---TMIYVTHD 193
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-241 |
2.20e-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: 66.04 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 16 EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTG--EEQADGGSVTlakdaklgylrqINNVDSTLSIIdelytviepi 93
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVL------------INGRPLDKRSF---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 94 ldmeKRILK--MQNEMrhltgeklekLYSSYTAlthnYELMDgYAAKskvvgiLKGLgfeeadfdrkintlSGGQKTRVF 171
Cdd:cd03213 81 ----RKIIGyvPQDDI----------LHPTLTV----RETLM-FAAK------LRGL--------------SGGERKRVS 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496028547 172 LAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNGAVVIVS-HD-RYFLDKIVSKVIDIENGNVqMYLG 241
Cdd:cd03213 122 IALELVSNPSLLFLDEPTSGLDSSSALQVMSLLrrLADTGRTIICSiHQpSSEIFELFDKLLLLSQGRV-IYFG 194
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
327-499 |
2.40e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.47 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDT--GEVIYGSNVSVAYYDQEHQ---- 400
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTEragi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 401 -VLHMDKTLFDEIS-----------------DTYPEMTNtRIRNILAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSK 462
Cdd:TIGR02633 81 vIIHQELTLVPELSvaeniflgneitlpggrMAYNAMYL-RAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496028547 463 ANFLLLDEPTNHLDIVSKDVLENALNSFP--GTVC-YVSH 499
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKahGVACvYISH 199
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
330-500 |
2.43e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.19 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 330 VHNLSKSFDRK-----KLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYgsnvsvAYYDQEHQvlhm 404
Cdd:PRK13651 5 VKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW------IFKDEKNK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 405 DKTLFDEISDTYPEMTNTRIRNILAA----------FLF-----------------------TGEDVYKKIS-------- 443
Cdd:PRK13651 75 KKTKEKEKVLEKLVIQKTRFKKIKKIkeirrrvgvvFQFaeyqlfeqtiekdiifgpvsmgvSKEEAKKRAAkyielvgl 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 444 ----------DLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIV-SKDVLE--NALNSFPGTVCYVSHD 500
Cdd:PRK13651 155 desylqrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEifDNLNKQGKTIILVTHD 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-236 |
2.51e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.04 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVtlakdaklgylrqinnvdstlsIIDEL 86
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDL----------------------IVDGL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 87 yTVIEPILDmekrilkmQNEMRHLTGEKLEK--LYSSYTALTHnyeLMDG---------YAAKSKVVGILKGLGFEEAdF 155
Cdd:PRK09493 64 -KVNDPKVD--------ERLIRQEAGMVFQQfyLFPHLTALEN---VMFGplrvrgaskEEAEKQARELLAKVGLAER-A 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 156 DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD--LRSiEWLESY--LLNYNGAVVIVSHDRYFLDKIVSKVIDI 231
Cdd:PRK09493 131 HHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDpeLRH-EVLKVMqdLAEEGMTMVIVTHEIGFAEKVASRLIFI 209
|
....*
gi 496028547 232 ENGNV 236
Cdd:PRK09493 210 DKGRI 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
330-500 |
2.52e-12 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 66.62 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 330 VHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGE-VIYGSNV---------SVAYYDQeh 399
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVvreprevrrRIGIVFQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 400 qvlhmDKTLFDEISDT-----------YP-EMTNTRIRNILaAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLL 467
Cdd:cd03265 81 -----DLSVDDELTGWenlyiharlygVPgAERRERIDELL-DFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 496028547 468 LDEPTNHLDIVSK----DVLENALNSFPGTVCYVSHD 500
Cdd:cd03265 155 LDEPTIGLDPQTRahvwEYIEKLKEEFGMTILLTTHY 191
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
327-476 |
2.70e-12 |
|
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: 66.84 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSF-DRKKLFY---DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVS---------- 391
Cdd:cd03258 1 MIELKNVSKVFgDTGGKVTalkDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDLTllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 392 ---VAYYDQEHQVLHmDKTLFDEISdtYP-EMTNT-------RIRNILAaflFTG----EDVYkkISDLSGGERGRVSLV 456
Cdd:cd03258 81 rrrIGMIFQHFNLLS-SRTVFENVA--LPlEIAGVpkaeieeRVLELLE---LVGledkADAY--PAQLSGGQKQRVGIA 152
|
170 180
....*....|....*....|
gi 496028547 457 KLMLSKANFLLLDEPTNHLD 476
Cdd:cd03258 153 RALANNPKVLLCDEATSALD 172
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
328-519 |
2.72e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 67.37 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDT-----------GEVIYGSNVSVAYYD 396
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrvegrveffNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 397 QEHQVLHMDKTLFD-----------EISDTYPEMtntRIRNILAAFLFTGE-------DVYKKISDLSGGERGRVSLVKL 458
Cdd:PRK14258 88 RQVSMVHPKPNLFPmsvydnvaygvKIVGWRPKL---EIDDIVESALKDADlwdeikhKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 459 MLSKANFLLLDEPTNHLDIVSKDVLENALNSFP----GTVCYVSHDRYFInktaTRILDLT------ENRL 519
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNLHQV----SRLSDFTaffkgnENRI 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-216 |
2.90e-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: 65.98 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDA----------KLGYLRQ 72
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPldfqrdsiarGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 73 INNVDSTLSIIDELyTVIEPILDMEkrilkmqnemrhltgekleklySSYTALTHnyelmdgyaakskvVGiLKGLGfee 152
Cdd:cd03231 81 APGIKTTLSVLENL-RFWHADHSDE----------------------QVEEALAR--------------VG-LNGFE--- 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 153 adfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNY---NGAVVIVSH 216
Cdd:cd03231 120 ---DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
327-520 |
2.95e-12 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 67.14 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSF---------DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVSVAYYD 396
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFrGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 397 QEHQVLHMDKTLF-DEISDTYPEMT--------------------NTRIRNILAAFLFTGEDVYKKISDLSGGERGRVSL 455
Cdd:TIGR02769 82 QRRAFRRDVQLVFqDSPSAVNPRMTvrqiigeplrhltsldeseqKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 456 VKLMLSKANFLLLDEPTNHLDIVSKDV---LENALNSFPGTVC-YVSHDRYFINKTATRILDLTENRLL 520
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVileLLRKLQQAFGTAYlFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
345-487 |
3.09e-12 |
|
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: 67.57 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSvaYYDQEHQVlhMDKTLFDEI--SDTYPEMtnt 422
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIS--FSSQFSWI--MPGTIKENIifGVSYDEY--- 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 423 RIRNILAAFLFTgEDVYKKIS-----------DLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVS-KDVLENAL 487
Cdd:cd03291 128 RYKSVVKACQLE-EDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTeKEIFESCV 203
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
328-489 |
3.37e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.49 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLS-KSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILePDTGEV-IYGSNVS----------VAYY 395
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLkINGIELReldpeswrkhLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 396 DQEHQVLHmdKTLFDEISDTYPEMTNTRIRNILA-AFLftGEDVYK-------KISD----LSGGERGRVSLVKLMLSKA 463
Cdd:PRK11174 429 GQNPQLPH--GTLRDNVLLGNPDASDEQLQQALEnAWV--SEFLPLlpqgldtPIGDqaagLSVGQAQRLALARALLQPC 504
|
170 180
....*....|....*....|....*.
gi 496028547 464 NFLLLDEPTNHLDIVSKDVLENALNS 489
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLVMQALNA 530
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
346-542 |
3.67e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.07 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 346 INFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYG------------SNVSVAYYDQEHQVLHMdkTLFDEI 412
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGrevnaenekwvrSKVGLVFQDPDDQVFSS--TVWDDV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 413 S------DTYPEMTNTRIRNILAAFLFtgEDVYKKIS-DLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLEN 485
Cdd:PRK13647 102 AfgpvnmGLDKDEVERRVEEALKAVRM--WDFRDKPPyHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 486 ALNSFPG---TVCYVSHDRYFINKTATRILDLTENRLLNYIGNydyYIEKREAVEEAANL 542
Cdd:PRK13647 180 ILDRLHNqgkTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK---SLLTDEDIVEQAGL 236
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-234 |
3.99e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 66.63 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTG--EEQADGGSVTLakdaklgylrqiNNVDstl 80
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILL------------DGED--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 siidelytviepILDM--EKRILK-----MQNEMRhLTGEKLEK-LYSSYTAltHNYELMDGYAAKSKVVGILKGLGFEE 152
Cdd:COG0396 66 ------------ILELspDERARAgiflaFQYPVE-IPGVSVSNfLRTALNA--RRGEELSAREFLKLLKEKMKELGLDE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 153 ADFDRKIN-TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESY---LLNYNGAVVIVSHDRYFLDKIV-SK 227
Cdd:COG0396 131 DFLDRYVNeGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGvnkLRSPDRGILIITHYQRILDYIKpDF 210
|
....*..
gi 496028547 228 VIDIENG 234
Cdd:COG0396 211 VHVLVDG 217
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
325-476 |
4.09e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 67.35 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 325 KDVLSVHNLSKSFDRKKLfYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQ------- 397
Cdd:PRK13634 6 QKVEHRYQYKTPFERRAL-YDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkplr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 398 ----------EHQvlhmdktLFDE--------------ISDtypEMTNTRIRNILAAFLFTGEDVYKKISDLSGGERGRV 453
Cdd:PRK13634 85 kkvgivfqfpEHQ-------LFEEtvekdicfgpmnfgVSE---EDAKQKAREMIELVGLPEELLARSPFELSGGQMRRV 154
|
170 180
....*....|....*....|...
gi 496028547 454 SLVKLMLSKANFLLLDEPTNHLD 476
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-259 |
5.63e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.03 E-value: 5.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSN-----EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVT-LAKDAKlgylrqin 74
Cdd:PRK13651 1 MQIKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwIFKDEK-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 75 nvDSTLSIIDELYTVIEPILDMEKRILKMQNEMRHLTGEKLEklYSSYTALTHNYEL----------MDGYAAKSKVVGI 144
Cdd:PRK13651 73 --NKKKTKEKEKVLEKLVIQKTRFKKIKKIKEIRRRVGVVFQ--FAEYQLFEQTIEKdiifgpvsmgVSKEEAKKRAAKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 145 LKGLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLR-SIEWLES-YLLNYNG-AVVIVSHDryfL 221
Cdd:PRK13651 149 IELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIfDNLNKQGkTIILVTHD---L 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 496028547 222 DKIV---SKVIDIENGNVqMYLGNYTDFSNKKQMLLDAKMK 259
Cdd:PRK13651 226 DNVLewtKRTIFFKDGKI-IKDGDTYDILSDNKFLIENNME 265
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
7-236 |
6.84e-12 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 67.44 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIikSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAkdaklGYLRQinnvDSTLSIIdel 86
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLN-----GRTLF----DSRKGIF--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 87 ytviepiLDMEKR-ILKMQNEMRhltgekLEKLYSSYTALTHNYELMDGYAAKSKVVGILKGLGFEEAdFDRKINTLSGG 165
Cdd:TIGR02142 70 -------LPPEKRrIGYVFQEAR------LFPHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHL-LGRLPGRLSGG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 166 QKTRVFLAKLLLEEPDIILLDEPTNHLDLRS----IEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNV 236
Cdd:TIGR02142 136 EKQRVAIGRALLSSPRLLLMDEPLAALDDPRkyeiLPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
327-484 |
7.76e-12 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 66.62 E-value: 7.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFY----DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEP---DTGEVIY-GSNVsVAYYDQE 398
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVkavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFdGEDL-LKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 399 hqvlhMDKTLFDEIS----DTY----PEMTntrIRNILAAFL-----FTGEDVYKK---------ISD-----------L 445
Cdd:COG0444 80 -----LRKIRGREIQmifqDPMtslnPVMT---VGDQIAEPLrihggLSKAEARERaiellervgLPDperrldrypheL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496028547 446 SGGERGRVSLVKLMLSKANFLLLDEPTNHLDiVS--KDVLE 484
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALD-VTiqAQILN 191
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-195 |
8.00e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 67.05 E-value: 8.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQA-------DGGSVTLakdaklgylRQINNVDst 79
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPtegqifiDGEDVTH---------RSIQQRD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 80 LSIIDELYTVIePILDMEKRI---LKMQN----EMRHLTGEKLEklyssytalthnyeLMDgyaakskvvgiLKGlgFEe 152
Cdd:PRK11432 80 ICMVFQSYALF-PHMSLGENVgygLKMLGvpkeERKQRVKEALE--------------LVD-----------LAG--FE- 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496028547 153 adfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD--LR 195
Cdd:PRK11432 131 ---DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDanLR 172
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
2-236 |
8.33e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 66.25 E-value: 8.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSF-GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVtLAKDAKLGYLRQ-INNVDST 79
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEV-LIKGEPIKYDKKsLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 80 LSII-----DELY--TVIEpilDMEKRILKMQnemrhLTGEKLEKlyssytalthnyelmdgyaaksKVVGILKGLGFEe 152
Cdd:PRK13639 80 VGIVfqnpdDQLFapTVEE---DVAFGPLNLG-----LSKEEVEK----------------------RVKEALKAVGME- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 153 aDFDRKI-NTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNGAVVIVS-HDRYFLDKIVSKV 228
Cdd:PRK13639 129 -GFENKPpHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLydLNKEGITIIIStHDVDLVPVYADKV 207
|
....*...
gi 496028547 229 IDIENGNV 236
Cdd:PRK13639 208 YVMSDGKI 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
327-476 |
8.36e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.75 E-value: 8.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVSVAYYDQEHQV---- 401
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIsLCGEPVPSRARHARQRVgvvp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 402 ----LHMDKTLFDE--ISDTYPEMTNTRIRNILAAFLFTGEDVYK---KISDLSGGERGRVSLVKLMLSKANFLLLDEPT 472
Cdd:PRK13537 87 qfdnLDPDFTVRENllVFGRYFGLSAAAARALVPPLLEFAKLENKadaKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
....
gi 496028547 473 NHLD 476
Cdd:PRK13537 167 TGLD 170
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-189 |
9.28e-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: 65.15 E-value: 9.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-KD-----------AKLGYL 70
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgRDitglppherarAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 71 RQINNVDSTLSIIDELytviepildmekrILKMQNEMRHLTGEKLEKLYSSYTALthnYELMdgyaakskvvgilkglgf 150
Cdd:cd03224 81 PEGRRIFPELTVEENL-------------LLGAYARRRAKRKARLERVYELFPRL---KERR------------------ 126
|
170 180 190
....*....|....*....|....*....|....*....
gi 496028547 151 eeadfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPT 189
Cdd:cd03224 127 -----KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-193 |
9.38e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.78 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL----------AKDAKLGYL 70
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvpararLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 71 RQINNVDSTlsiidelYTVIEPILdMEKRILKMQNEmrhltgeKLEKLYSSytalthnyeLMDGYAAKSKVvgilkglgf 150
Cdd:PRK13536 120 PQFDNLDLE-------FTVRENLL-VFGRYFGMSTR-------EIEAVIPS---------LLEFARLESKA--------- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496028547 151 eeadfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:PRK13536 167 -----DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-231 |
1.03e-11 |
|
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: 64.47 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEE--QADGGSVTLAKDaklgylrqinnvdstl 80
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 SIIDelytviepiLDMEKRILK-----MQNEMRhLTGEKLeklyssytalthnyelmdgyaakskvvgilkglgfeeADF 155
Cdd:cd03217 65 DITD---------LPPEERARLgiflaFQYPPE-IPGVKN-------------------------------------ADF 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 156 DRKIN-TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLE---SYLLNYNGAVVIVSHDRYFLDKIVSKVIDI 231
Cdd:cd03217 98 LRYVNeGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAeviNKLREEGKSVLIITHYQRLLDYIKPDRVHV 177
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-193 |
1.27e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEE--QADGGSVTLakdaklgylrQINNVDS 78
Cdd:COG2401 29 IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV----------PDNQFGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 79 TLSIIDELYtviepildmekrilkmqnemrhLTGEKLEklyssytalthnyelmdgyaakskVVGILKGLGFEEA-DFDR 157
Cdd:COG2401 99 EASLIDAIG----------------------RKGDFKD------------------------AVELLNAVGLSDAvLWLR 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 496028547 158 KINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:COG2401 133 RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
328-499 |
1.30e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSnVSVAYYDQE--------- 398
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG-QEMRFASTTaalaagvai 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 399 -HQVLHMdktlfdeisdtYPEMT----------------------NTRIRNILAAFlftGEDV--YKKISDLSGGERGRV 453
Cdd:PRK11288 84 iYQELHL-----------VPEMTvaenlylgqlphkggivnrrllNYEAREQLEHL---GVDIdpDTPLKYLSIGQRQMV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496028547 454 SLVKLMLSKANFLLLDEPTNHLDIVSKDVLE---NALNSFPGTVCYVSH 499
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFrviRELRAEGRVILYVSH 198
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
327-479 |
1.35e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.91 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGE-VIYGSNVS-----------VAY 394
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiIIDDEDISllplhararrgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 395 YDQEHQVLHMdKTLFDEI-------SDTYPEMTNTRIRNILAAFLFTG-EDVYKKisDLSGGERGRVSLVKLMLSKANFL 466
Cdd:PRK10895 83 LPQEASIFRR-LSVYDNLmavlqirDDLSAEQREDRANELMEEFHIEHlRDSMGQ--SLSGGERRRVEIARALAANPKFI 159
|
170
....*....|...
gi 496028547 467 LLDEPTNHLDIVS 479
Cdd:PRK10895 160 LLDEPFAGVDPIS 172
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
350-477 |
1.39e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.53 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 350 IKRGERVAIIGDNGTGKTTLLKIINGILEPDTG---------EVI---------------YGSNVSVA----YYDQEHQV 401
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeepswdEVLkrfrgtelqnyfkklYNGEIKVVhkpqYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 402 L---------HMDKT-LFDEISDTypemtnTRIRNILAaflftgedvyKKISDLSGGERGRVSLVKLMLSKANFLLLDEP 471
Cdd:PRK13409 176 FkgkvrellkKVDERgKLDEVVER------LGLENILD----------RDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
....*.
gi 496028547 472 TNHLDI 477
Cdd:PRK13409 240 TSYLDI 245
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-236 |
1.57e-11 |
|
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: 67.46 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSN-EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA----KDAKLGYLRQ-INNV 76
Cdd:TIGR01193 474 IVINDVSYSYGYGsNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNgfslKDIDRHTLRQfINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 77 DSTLSIIDElyTVIEPILdmekrilkMQNEmRHLTGEKLEKLYSSYTALTHNYELMDGYAAKSKVVGilkglgfeeadfd 156
Cdd:TIGR01193 554 PQEPYIFSG--SILENLL--------LGAK-ENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEG------------- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 157 rkiNTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNV 236
Cdd:TIGR01193 610 ---SSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
327-487 |
1.62e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.03 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILepdTGEVIYGSNVSV-------------- 392
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI---TGDKSAGSHIELlgrtvqregrlard 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 393 --------AYYDQEHQVLH----MDKTLFDEISDT------YPEMTNTRIRNILAAFLFTG--EDVYKKISDLSGGERGR 452
Cdd:PRK09984 81 irksrantGYIFQQFNLVNrlsvLENVLIGALGSTpfwrtcFSWFTREQKQRALQALTRVGmvHFAHQRVSTLSGGQQQR 160
|
170 180 190
....*....|....*....|....*....|....*
gi 496028547 453 VSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENAL 487
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTL 195
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
345-519 |
1.89e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 64.03 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYydqEHQVLH-------MDKTLF-----DEI 412
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY---EHKYLHskvslvgQEPVLFarslqDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 413 SDTYPEMTNTRIR----------NILAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDV 482
Cdd:cd03248 109 AYGLQSCSFECVKeaaqkahahsFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQ 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 496028547 483 LENALNSFPG--TVCYVSHDRYFINKtATRILDLTENRL 519
Cdd:cd03248 189 VQQALYDWPErrTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
328-487 |
2.22e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 64.72 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGsNVSVAYYDQEHQVLHMDKT 407
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLD-GKPVEGPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 408 LFD------------EISDTYPEMTNTRIRNILAAFLFTGEDvYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHL 475
Cdd:PRK11248 81 LLPwrnvqdnvafglQLAGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170
....*....|..
gi 496028547 476 DIVSKDVLENAL 487
Cdd:PRK11248 160 DAFTREQMQTLL 171
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-236 |
2.30e-11 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 63.73 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 25 INEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLG---------YLRQINNVDSTLSIIDELYTVIEPILD 95
Cdd:TIGR01277 21 VADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGlapyqrpvsMLFQENNLFAHLTVRQNIGLGLHPGLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 96 mekrilkmqnemrhLTGEKLEKLYSsytalthnyelmdgyAAKSkvVGIlkglgfeeADF-DRKINTLSGGQKTRVFLAK 174
Cdd:TIGR01277 101 --------------LNAEQQEKVVD---------------AAQQ--VGI--------ADYlDRLPEQLSGGQRQRVALAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496028547 175 LLLEEPDIILLDEPTNHLD--LRS--IEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNV 236
Cdd:TIGR01277 142 CLVRPNPILLLDEPFSALDplLREemLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
328-479 |
3.08e-11 |
|
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: 63.20 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSF--DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS-VAYYDQEHQ--V 401
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIeIDGIDIStIPLEDLRSSltI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 402 LHMDKTLFDeisdtypemtnTRIRNILAAF-LFTGEDVYKKIS------DLSGGERGRVSLVKLMLSKANFLLLDEPTNH 474
Cdd:cd03369 87 IPQDPTLFS-----------GTIRSNLDPFdEYSDEEIYGALRvsegglNLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
....*
gi 496028547 475 LDIVS 479
Cdd:cd03369 156 IDYAT 160
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
317-574 |
3.34e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 317 LDIAKESGKDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVSVAYY 395
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeIGGNPCARLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 396 DQEHQ----VLHMDKTLFDEISD--------TYPEMTNTRIRNILAAfLFTGEDVYKKISDLSGGERGRVSLVKLMLSKA 463
Cdd:PRK15439 81 AKAHQlgiyLVPQEPLLFPNLSVkenilfglPKRQASMQKMKQLLAA-LGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 464 NFLLLDEPTNHLDIVSKDVLENALNSFPGT---VCYVSHDRYFINKTATRILDLTenrllnyignyDYYI---EKREAVE 537
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLAQgvgIVFISHKLPEIRQLADRISVMR-----------DGTIalsGKTADLS 228
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 496028547 538 EAANLSNIEQAQKGIDVSESKQEWMD---NKTAQAQKKKI 574
Cdd:PRK15439 229 TDDIIQAITPAAREKSLSASQKLWLElpgNRRQQAAGAPV 268
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-196 |
3.55e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 18 IKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA--------KDAKLGYLRQINNVDSTLSIIdelytv 89
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILgqptrqalQKNLVAYVPQSEEVDWSFPVL------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 90 IEPILdmekrilkMQNEMRHLTGEKLEKlyssytalTHNYELMDGYAAKskvVGILkglgfeeaDF-DRKINTLSGGQKT 168
Cdd:PRK15056 97 VEDVV--------MMGRYGHMGWLRRAK--------KRDRQIVTAALAR---VDMV--------EFrHRQIGELSGGQKK 149
|
170 180
....*....|....*....|....*...
gi 496028547 169 RVFLAKLLLEEPDIILLDEPTNHLDLRS 196
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-217 |
3.89e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.76 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKD------------AKLGY 69
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 70 LRQINNVDSTLSIIDELYTVIEpildMEKRILKMQNEMRhlTGEKLEKLYSSYtalthnyelmdgyaakskvvgILKGLG 149
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQ----IRDDLSAEQREDR--ANELMEEFHIEH---------------------LRDSMG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 150 feeadfdrkiNTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS---IEWLESYLLNYNGAVVIVSHD 217
Cdd:PRK10895 136 ----------QSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISvidIKRIIEHLRDSGLGVLITDHN 196
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
332-520 |
4.41e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.85 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 332 NLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQEHQ----VLHMDKT 407
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVArrigLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 408 LFDEIS-------DTYPEMT-NTRIRN-----ILAAFLFTG--EDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPT 472
Cdd:PRK10253 92 TPGDITvqelvarGRYPHQPlFTRWRKedeeaVTKAMQATGitHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496028547 473 NHLDIVSK-DVLE--NALNSFPG-TVCYVSHDRYFINKTATRILDLTENRLL 520
Cdd:PRK10253 172 TWLDISHQiDLLEllSELNREKGyTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-216 |
4.85e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.39 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKIL------------TGEEQADGGSV------TLAKD 64
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlielypearvSGEVYLDGQDIfkmdviELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 65 AKLGYlrQINNVDSTLSIIDELytVIEPILDmekRILKMQNEMRHLTGEKLEKLyssytalthnyELMDgyAAKSKVvgi 144
Cdd:PRK14247 84 VQMVF--QIPNPIPNLSIFENV--ALGLKLN---RLVKSKKELQERVRWALEKA-----------QLWD--EVKDRL--- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496028547 145 lkglgfeeadfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNG--AVVIVSH 216
Cdd:PRK14247 141 -----------DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
328-500 |
5.33e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.54 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSN-VSVAYYD-----QEHQV 401
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTApLAEAREDtrlmfQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 402 LHMdKTLFDEISDTYPEMTNTRIRNILAAFlftgedvykKISD--------LSGGERGRVSLVKLMLSKANFLLLDEPTN 473
Cdd:PRK11247 93 LPW-KKVIDNVGLGLKGQWRDAALQALAAV---------GLADranewpaaLSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190
....*....|....*....|....*....|.
gi 496028547 474 HLD----IVSKDVLENALNSFPGTVCYVSHD 500
Cdd:PRK11247 163 ALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-490 |
5.82e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVT-LAKDAKLGYLRQ-----INN 75
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGPKSsqeagIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 76 VDSTLSIIDELyTVIEPI-LDMEKRilkmqnemRHLTGEKLEKLYSSYTALthnyelmdgyaakskvvgiLKGLGFEEAD 154
Cdd:PRK10762 84 IHQELNLIPQL-TIAENIfLGREFV--------NRFGRIDWKKMYAEADKL-------------------LARLNLRFSS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 155 fDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESY---LLNYNGAVVIVSHdryfldkivskvidi 231
Cdd:PRK10762 136 -DKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVireLKSQGRGIVYISH--------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 232 engnvqmylgnytdfsnkkqmlldaKMKEYLnqqqEIRHQeavITKLK--QFNREKSIkrAESRQKQLekIERVDAPQTY 309
Cdd:PRK10762 200 -------------------------RLKEIF----EICDD---VTVFRdgQFIAEREV--ADLTEDSL--IEMMVGRKLE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 310 TENMRlsldIAKESGKDVLSVHNLSKSFDRkklfyDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGS 388
Cdd:PRK10762 244 DQYPR----LDKAPGEVRLKVDNLSGPGVN-----DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVtLDGH 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 389 NVS-----------VAYYDQEHQ----VL------HMDKTLFDEISDTYPEMTNTRIRNILAAF--LFT----GEDvyKK 441
Cdd:PRK10762 315 EVVtrspqdglangIVYISEDRKrdglVLgmsvkeNMSLTALRYFSRAGGSLKHADEQQAVSDFirLFNiktpSME--QA 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 496028547 442 ISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENALNSF 490
Cdd:PRK10762 393 IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF 441
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-233 |
6.44e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 62.11 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGeeqadggsvTLAKDAKLGYLRQINNVDstlsiIDEL 86
Cdd:COG4136 6 NLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAG---------TLSPAFSASGEVLLNGRR-----LTAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 87 ytviePIldmEKR---ILkMQNEM--RHLT-GEKLekLYssytALTHNyelMDGYAAKSKVVGILKGLGFeeADF-DRKI 159
Cdd:COG4136 72 -----PA---EQRrigIL-FQDDLlfPHLSvGENL--AF----ALPPT---IGRAQRRARVEQALEEAGL--AGFaDRDP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 160 NTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD--LRS--IEWLESYLLNYNGAVVIVSHDRyflDKI--VSKVIDIEN 233
Cdd:COG4136 132 ATLSGGQRARVALLRALLAEPRALLLDEPFSKLDaaLRAqfREFVFEQIRQRGIPALLVTHDE---EDApaAGRVLDLGN 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-236 |
6.99e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.22 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 15 NEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKdaklgylRQINNvdstlsiidelytviepil 94
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMG-------REVNA------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 95 dmekrilKMQNEMRHLTG----EKLEKLYSSyTALTH------NYELmDGYAAKSKVVGILKGLGFEeaDF-DRKINTLS 163
Cdd:PRK13647 72 -------ENEKWVRSKVGlvfqDPDDQVFSS-TVWDDvafgpvNMGL-DKDEVERRVEEALKAVRMW--DFrDKPPYHLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496028547 164 GGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNGAVVIVS-HDRYFLDKIVSKVIDIENGNV 236
Cdd:PRK13647 141 YGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILdrLHNQGKTVIVAtHDVDLAAEWADQVIVLKEGRV 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
341-520 |
7.34e-11 |
|
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: 65.15 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 341 KLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYG----SNVSVAYYDQEHQVLHMDKTLFD-EISDT 415
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNgfslKDIDRHTLRQFINYLPQEPYIFSgSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 416 Y--PEMTNTRIRNILAAFLFT-------------GEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLD-IVS 479
Cdd:TIGR01193 568 LllGAKENVSQDEIWAACEIAeikddienmplgyQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDtITE 647
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496028547 480 KDVLENALNSFPGTVCYVSHdRYFINKTATRILDLTENRLL 520
Cdd:TIGR01193 648 KKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKII 687
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-225 |
7.94e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 64.28 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSvtlakdaklgylrqinnvdstLSIIDEL 86
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD---------------------LFIGEKR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 87 YTVIEPildmEKRILKMqnemrhltgeklekLYSSYtALTHNYELMDGYAAKSKVVGILKglgfEEAD------------ 154
Cdd:PRK11000 67 MNDVPP----AERGVGM--------------VFQSY-ALYPHLSVAENMSFGLKLAGAKK----EEINqrvnqvaevlql 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 155 ---FDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD--LR-----SIEWLESYLlnyNGAVVIVSHDRY----F 220
Cdd:PRK11000 124 ahlLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaaLRvqmriEISRLHKRL---GRTMIYVTHDQVeamtL 200
|
....*
gi 496028547 221 LDKIV 225
Cdd:PRK11000 201 ADKIV 205
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
327-522 |
9.69e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 62.90 E-value: 9.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFD-RKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVSVAyydQEHQVLHM 404
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlIRGEPITKE---NIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 405 DKTLF----DEISDTYPEM------------TNTRIRNILAAFLFTG-EDVYKKIS-DLSGGERGRVSLVKLMLSKANFL 466
Cdd:PRK13652 80 VGLVFqnpdDQIFSPTVEQdiafgpinlgldEETVAHRVSSALHMLGlEELRDRVPhHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 467 LLDEPTNHLDIVSKDVLENALNSFPG----TVCYVSHDRYFINKTATRILDLTENRLLNY 522
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-195 |
9.78e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.29 E-value: 9.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 22 TFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLakdaklgylrqiNNVDSTLSIIDelytviepildmeKRIL 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL------------NGQDHTTTPPS-------------RRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 102 KM----QNEMRHLTGEKleklyssYTALTHNYELMDGYAAKSKVVGILKGLGFEEAdFDRKINTLSGGQKTRVFLAKLLL 177
Cdd:PRK10771 74 SMlfqeNNLFSHLTVAQ-------NIGLGLNPGLKLNAAQREKLHAIARQMGIEDL-LARLPGQLSGGQRQRVALARCLV 145
|
170 180
....*....|....*....|
gi 496028547 178 EEPDIILLDEPTNHLD--LR 195
Cdd:PRK10771 146 REQPILLLDEPFSALDpaLR 165
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
332-476 |
1.11e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 63.31 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 332 NLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS------------VAYYDQE 398
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPararlararigvVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 399 HQVLHMDKTLFdeISDTYPEMTNTRIRNILAAFLFTGEDVYK---KISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHL 475
Cdd:PRK13536 126 DLEFTVRENLL--VFGRYFGMSTREIEAVIPSLLEFARLESKadaRVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
.
gi 496028547 476 D 476
Cdd:PRK13536 204 D 204
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
328-512 |
1.15e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 62.34 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINgILE-PDTGEV-IYGSNVSVAYYDQEHQVLHMD 405
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLN-LLEmPRSGTLnIAGNHFDFSKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 406 KT---LFDEIsDTYPEMtnTRIRNILAA---FLFTGEDVYKKISD------------------LSGGERGRVSLVKLMLS 461
Cdd:PRK11124 82 RNvgmVFQQY-NLWPHL--TVQQNLIEApcrVLGLSKDQALARAEkllerlrlkpyadrfplhLSGGQQQRVAIARALMM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 462 KANFLLLDEPTNHLD------IVS--KDVLENALnsfpgTVCYVSHDRYFINKTATRIL 512
Cdd:PRK11124 159 EPQVLLFDEPTAALDpeitaqIVSiiRELAETGI-----TQVIVTHEVEVARKTASRVV 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-250 |
1.26e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.34 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQAD----------GGSVT----LAKD--- 64
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksagshiellGRTVQregrLARDirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 65 --AKLGYLRQINNVDSTLSIIDELytviepILDMEKRILKMQNEMRHLTGEKLEKlysSYTALTHnyelmdgyaakskvV 142
Cdd:PRK09984 84 srANTGYIFQQFNLVNRLSVLENV------LIGALGSTPFWRTCFSWFTREQKQR---ALQALTR--------------V 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 143 GIlkglgfeeADF-DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYN---GAVVIVS-HD 217
Cdd:PRK09984 141 GM--------VHFaHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqndGITVVVTlHQ 212
|
250 260 270
....*....|....*....|....*....|...
gi 496028547 218 RYFLDKIVSKVIDIENGNVqMYLGNYTDFSNKK 250
Cdd:PRK09984 213 VDYALRYCERIVALRQGHV-FYDGSSQQFDNER 244
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-218 |
1.32e-10 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 63.28 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 33 IVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKL---GYLRQINNVDSTLSIIdelytviePILDMEKRI---LKMQNE 106
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTnvpPHLRHINMVFQSYALF--------PHMTVEENVafgLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 107 MRHltgekleklyssytalthnyelmdgyAAKSKVVGILKGLGFEEADfDRKINTLSGGQKTRVFLAKLLLEEPDIILLD 186
Cdd:TIGR01187 73 PRA--------------------------EIKPRVLEALRLVQLEEFA-DRKPHQLSGGQQQRVALARALVFKPKILLLD 125
|
170 180 190
....*....|....*....|....*....|....*.
gi 496028547 187 EPTNHLD--LRSIEWLESYLLNYNGAV--VIVSHDR 218
Cdd:TIGR01187 126 EPLSALDkkLRDQMQLELKTIQEQLGItfVFVTHDQ 161
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-216 |
1.35e-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: 61.72 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 17 IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLakDAKLGYLRQINNVDSTLSIIDElytviEPILdm 96
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL--DGKPISQYEHKYLHSKVSLVGQ-----EPVL-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 97 EKRILKmQNEMRHLTGEKLEKLYssytalthnyELMDGYAAKSKVVGILKGLgfeEADFDRKINTLSGGQKTRVFLAKLL 176
Cdd:cd03248 100 FARSLQ-DNIAYGLQSCSFECVK----------EAAQKAHAHSFISELASGY---DTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496028547 177 LEEPDIILLDEPTNHLDLRSIEWLES--YLLNYNGAVVIVSH 216
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQalYDWPERRTVLVIAH 207
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-260 |
1.39e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.10 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTgeeqadggsvtlakdaKLGYLrqINNVDSTLS 81
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN----------------RMNDL--NPEVTITGS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 82 IIDELYTVIEP---ILDMEKRI---LKMQNEMRHLTGEKLekLYSSYTALTHNYELMDGYAAKSkvvgiLKGLGFEEADF 155
Cdd:PRK14239 67 IVYNGHNIYSPrtdTVDLRKEIgmvFQQPNPFPMSIYENV--VYGLRLKGIKDKQVLDEAVEKS-----LKGASIWDEVK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 156 DRKINT---LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNG--AVVIVSHDRYFLDKIVSKVID 230
Cdd:PRK14239 140 DRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSMQQASRISDRTGF 219
|
250 260 270
....*....|....*....|....*....|
gi 496028547 231 IENGNVqmylgnyTDFSNKKQMLLDAKMKE 260
Cdd:PRK14239 220 FLDGDL-------IEYNDTKQMFMNPKHKE 242
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
328-520 |
1.52e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 64.36 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSF----DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS------VAYYD 396
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYrVAGQDVAtldadaLAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 397 QEH-----QVLHMDKTLFD----EISDTYP--EMTNTRIRNI-LAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKAN 464
Cdd:PRK10535 85 REHfgfifQRYHLLSHLTAaqnvEVPAVYAglERKQRLLRAQeLLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 465 FLLLDEPTNHLDIVS-KDVLE--NALNSFPGTVCYVSHDRYfINKTATRILDLTENRLL 520
Cdd:PRK10535 165 VILADEPTGALDSHSgEEVMAilHQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIV 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
327-499 |
1.53e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDT--GEVIYGSNVSVAYY--DQEHQ-- 400
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNirDTERAgi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 401 -VLHMDKTLFDEISDT----------------YPEMTnTRIRNILAAfLFTGEDVYKKISDLSGGERGRVSLVKLMLSKA 463
Cdd:PRK13549 85 aIIHQELALVKELSVLeniflgneitpggimdYDAMY-LRAQKLLAQ-LKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 496028547 464 NFLLLDEPTNHLDIVSKDVLENALNSFP--GTVC-YVSH 499
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKahGIACiYISH 201
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
328-519 |
1.58e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.01 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSF---------DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVS------ 391
Cdd:PRK10419 4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWrGEPLAklnraq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 392 VAYYDQEHQVLHMD--------KTLFDEISDTYPEMTN-------TRIRNILAAFLFTGEDVYKKISDLSGGERGRVSLV 456
Cdd:PRK10419 84 RKAFRRDIQMVFQDsisavnprKTVREIIREPLRHLLSldkaerlARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 457 KLMLSKANFLLLDEPTNHLDIVSK----DVLEnALNSFPGTVC-YVSHDRYFINKTATRILDLTENRL 519
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQagviRLLK-KLQQQFGTAClFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
349-511 |
1.64e-10 |
|
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: 60.28 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 349 EIKRGERVAIIGDNGTGKTTLLKIINGILEPdTGEVIYGSNVSVAYYDQehqvlhmdktlfdeisdtypemtntrirnil 428
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIP-NGDNDEWDGITPVYKPQ------------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 429 aaflftgedvykKIsDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENALNSF----PGTVCYVSHDRYFI 504
Cdd:cd03222 69 ------------YI-DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVL 135
|
....*..
gi 496028547 505 NKTATRI 511
Cdd:cd03222 136 DYLSDRI 142
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-484 |
1.67e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 15 NEIIKSATFLINEHEKAAIVGVNGAGKT-TLLKIL-----------TGEEQADGGSVTLAKDAKLGYLRQinnvDSTLSI 82
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvypSGDIRFHGESLLHASEQTLRGVRG----NKIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 IDELYTVIEPILDMEKR---ILKMQNEMRHltgekleklyssytalthnyelmdgYAAKSKVVGILKGLGFEEA-----D 154
Cdd:PRK15134 98 FQEPMVSLNPLHTLEKQlyeVLSLHRGMRR-------------------------EAARGEILNCLDRVGIRQAakrltD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 155 FDRKintLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLrSIEWLESYLLN-----YNGAVVIVSHDRYFLDKIVSKVI 229
Cdd:PRK15134 153 YPHQ---LSGGERQRVMIAMALLTRPELLIADEPTTALDV-SVQAQILQLLRelqqeLNMGLLFITHNLSIVRKLADRVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 230 DIENGN-VQmylgnytdfSNKKQMLLDAKMKEYLNQqqeirhqeavitklkQFNREKSiKRAESRQKQLEKIERVdapqt 308
Cdd:PRK15134 229 VMQNGRcVE---------QNRAATLFSAPTHPYTQK---------------LLNSEPS-GDPVPLPEPASPLLDV----- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 309 ytENMRLSLDIAKESGKDVLSVHNLSKSfdrkklfydINFEIKRGERVAIIGDNGTGKTT----LLKIINGilepdTGEV 384
Cdd:PRK15134 279 --EQLQVAFPIRKGILKRTVDHNVVVKN---------ISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 385 IYG----------------SNVSVAYYDQEHQV---LHMDKTLFDEISDTYPEMTNT-RIRNILAAFLFTGEDV---YKK 441
Cdd:PRK15134 343 WFDgqplhnlnrrqllpvrHRIQVVFQDPNSSLnprLNVLQIIEEGLRVHQPTLSAAqREQQVIAVMEEVGLDPetrHRY 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 496028547 442 ISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLD-IVSKDVLE 484
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDkTVQAQILA 466
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-193 |
1.83e-10 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 61.74 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA------KDAKLGYL-----R 71
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGgeeirlKPDRDGELvpadrR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 72 QINNVDSTLSIIDELY------TVIEPILDMEKRILKM-----QNEMRHLtgekLEKlyssytalthnyelmdgyaaksk 140
Cdd:COG4598 89 QLQRIRTRLGMVFQSFnlwshmTVLENVIEAPVHVLGRpkaeaIERAEAL----LAK----------------------- 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496028547 141 vVGIlkglgfeeADF-DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:COG4598 142 -VGL--------ADKrDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-189 |
2.10e-10 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 61.00 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-KD-----------AKLGYL 70
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDgEDitklppherarAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 71 RQINNVDSTLSIIDELYTVIEPILDMEKRILkmqnemrhltgeklEKLYSSYTALThnyELMDgyaakskvvgilkglgf 150
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKIP--------------DEIYELFPVLK---EMLG----------------- 126
|
170 180 190
....*....|....*....|....*....|....*....
gi 496028547 151 eeadfdRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPT 189
Cdd:TIGR03410 127 ------RRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
328-476 |
2.17e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 61.80 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFD----RKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGsNVSVAYYDQEHQVLH 403
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLD-GVPVTGPGADRGVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 404 MDKTLF---DEISDT--------YPEMTNTRI-RNILAafLFTGEDVYKK-ISDLSGGERGRVSLVKLMLSKANFLLLDE 470
Cdd:COG4525 83 QKDALLpwlNVLDNVafglrlrgVPKAERRARaEELLA--LVGLADFARRrIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
....*.
gi 496028547 471 PTNHLD 476
Cdd:COG4525 161 PFGALD 166
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
351-477 |
2.18e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.65 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 351 KRGERVAIIGDNGTGKTTLLKIINGIL---------EPDTGEVI---------------YGSNVSVA----YYDQEHQVL 402
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELkpnlgdydeEPSWDEVLkrfrgtelqdyfkklANGEIKVAhkpqYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 403 H------MDKTlfDE--ISDTYPEMTNtrIRNILAaflftgedvyKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNH 474
Cdd:COG1245 177 KgtvrelLEKV--DErgKLDELAEKLG--LENILD----------RDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
...
gi 496028547 475 LDI 477
Cdd:COG1245 243 LDI 245
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-236 |
2.20e-10 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 60.88 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 22 TFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-------KDAKLGYLRQ-INNVDSTLSIIDELyTVIEPI 93
Cdd:cd03292 21 NISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvsdlRGRAIPYLRRkIGVVFQDFRLLPDR-NVYENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 94 -LDMEkrilkmqnemrhLTGEKleklyssytalthnyelmdGYAAKSKVVGILKGLGFEEadfdrKINT----LSGGQKT 168
Cdd:cd03292 100 aFALE------------VTGVP-------------------PREIRKRVPAALELVGLSH-----KHRAlpaeLSGGEQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 169 RVFLAKLLLEEPDIILLDEPTNHLD----LRSIEWLESylLNYNGAVVIVS-HDRYFLDKIVSKVIDIENGNV 236
Cdd:cd03292 144 RVAIARAIVNSPTILIADEPTGNLDpdttWEIMNLLKK--INKAGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
347-476 |
2.21e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.14 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 347 NFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSN----------VSVAYydQEHQV-------------L 402
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtLNGQDhtttppsrrpVSMLF--QENNLfshltvaqniglgL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 403 HMDKTLFDEISDTYPEMT-NTRIRNILAAFlftgedvykkISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLD 476
Cdd:PRK10771 97 NPGLKLNAAQREKLHAIArQMGIEDLLARL----------PGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
9-234 |
3.26e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 60.18 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 9 SKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKdaKLGYLRQ---INNVdstlsiide 85
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQepwIQNG--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 86 lyTVIEPILdmekrilkMQNEMRHltgEKLEKLYSSyTALTHNYELMDGyaakskvvGILKGLGfeeadfDRKINtLSGG 165
Cdd:cd03250 81 --TIRENIL--------FGKPFDE---ERYEKVIKA-CALEPDLEILPD--------GDLTEIG------EKGIN-LSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 166 QKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWL-ESYL---LNYNGAVVIVSHDRYFLDKiVSKVIDIENG 234
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCIlglLLNNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
325-500 |
3.70e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.56 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 325 KDVLSVHNLSKSFDRKK----LFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVSvaYYDQEH 399
Cdd:PRK10584 4 ENIVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVsLVGQPLH--QMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 400 QVLHMDKTL---FDE--ISDTYPEMTNTRIRNIL-----------AAFLFT----GEDVYKKISDLSGGERGRVSLVKLM 459
Cdd:PRK10584 82 RAKLRAKHVgfvFQSfmLIPTLNALENVELPALLrgessrqsrngAKALLEqlglGKRLDHLPAQLSGGEQQRVALARAF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496028547 460 LSKANFLLLDEPTNHLDIVSKDVLENALNS----FPGTVCYVSHD 500
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSlnreHGTTLILVTHD 206
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
137-238 |
4.72e-10 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 60.93 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 137 AKSKVVGILKGLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS----IEWLESYLLNYNGAVV 212
Cdd:TIGR04521 118 AEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGrkeiLDLFKRLHKEKGLTVI 197
|
90 100
....*....|....*....|....*.
gi 496028547 213 IVSHDRYFLDKIVSKVIDIENGNVQM 238
Cdd:TIGR04521 198 LVTHSMEDVAEYADRVIVMHKGKIVL 223
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
346-470 |
5.03e-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: 62.51 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 346 INFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVI-------------YGSNVSVAYYDQeHqvlhmdktLFDEI 412
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILldgqpvtadnreaYRQLFSAVFSDF-H--------LFDRL 421
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 413 SDTYPEMTNTRIRNILAAFlftgeDVYKKIS---------DLSGGERGRVSLVKLMLSKANFLLLDE 470
Cdd:COG4615 422 LGLDGEADPARARELLERL-----ELDHKVSvedgrfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
325-515 |
5.73e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.17 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 325 KDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIIN--GILEPD---TGEVIY-GSNVSVAYYD-- 396
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYnGHNIYSPRTDtv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 397 ----------QEHQVLHM----------------DKTLFDEISDtypemtntriRNILAAFLFtgEDVYKKISD----LS 446
Cdd:PRK14239 83 dlrkeigmvfQQPNPFPMsiyenvvyglrlkgikDKQVLDEAVE----------KSLKGASIW--DEVKDRLHDsalgLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 447 GGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENALNSFPG--TVCYVSHDRyfinKTATRILDLT 515
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSM----QQASRISDRT 217
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-217 |
6.09e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.39 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA----------KDAKLGYLR 71
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRgqhieglpghQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 72 QINNVdstlSIIDELyTVIEpildmekRILKMQNemRHLTGEKLEKLYSSYTALTHNYELMDGYAAKSKVVGILkglgfe 151
Cdd:PRK11300 85 TFQHV----RLFREM-TVIE-------NLLVAQH--QQLKTGLFSGLLKTPAFRRAESEALDRAATWLERVGLL------ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 152 eaDF-DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLN----YNGAVVIVSHD 217
Cdd:PRK11300 145 --EHaNRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAElrneHNVTVLLIEHD 213
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
327-485 |
6.14e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 59.11 E-value: 6.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFyDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYG----SNVSVAY--YDQEHQ 400
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKncniNNIAKPYctYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 401 VLHMDKTLFDEISdTYPEMTNTRIRNILAAFLFTGEDVY-KKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVS 479
Cdd:PRK13541 80 GLKLEMTVFENLK-FWSEIYNSAETLYAAIHYFKLHDLLdEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
....*.
gi 496028547 480 KDVLEN 485
Cdd:PRK13541 159 RDLLNN 164
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-216 |
6.48e-10 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 59.55 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNE-IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL----AKDAKLGYLR-QINNV--DS 78
Cdd:cd03254 7 NVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdgidIRDISRKSLRsMIGVVlqDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 79 TL---SIIDELyTVIEPILDMEKRILKMQNEMRHLTGEKLEKLYssYTALTHNYelmdgyaakskvvgilkglgfeeadf 155
Cdd:cd03254 87 FLfsgTIMENI-RLGRPNATDEEVIEAAKEAGAHDFIMKLPNGY--DTVLGENG-------------------------- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 156 drkiNTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNGAVVIVSH 216
Cdd:cd03254 138 ----GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALekLMKGRTSIIIAH 196
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
327-476 |
6.62e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.48 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSF-DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSN---------------V 390
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksllevrktV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 391 SVAYYDQEHQVLH---MDKTLFDEISDTYP-EMTNTRIRNILAAFLFTGEDvYKKISDLSGGERGRVSLVKLMLSKANFL 466
Cdd:PRK13639 81 GIVFQNPDDQLFAptvEEDVAFGPLNLGLSkEEVEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170
....*....|
gi 496028547 467 LLDEPTNHLD 476
Cdd:PRK13639 160 VLDEPTSGLD 169
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-236 |
6.94e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.04 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 32 AIVGVNGAGKTTLLKILTGEEQADGGSVTLAkdaklgylrqinnvDSTLSiidelytviepilDMEKRIlkmqnemrHLT 111
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLN--------------GRVLF-------------DAEKGI--------CLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 112 GEKLE--------KLYSSYTALTHnyeLMDGYAAKS-----KVVGILkGLgfeEADFDRKINTLSGGQKTRVFLAKLLLE 178
Cdd:PRK11144 73 PEKRRigyvfqdaRLFPHYKVRGN---LRYGMAKSMvaqfdKIVALL-GI---EPLLDRYPGSLSGGEKQRVAIGRALLT 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 179 EPDIILLDEPTNHLDL-RSIEwlesyLLNY--------NGAVVIVSHDryfLDKIV---SKVIDIENGNV 236
Cdd:PRK11144 146 APELLLMDEPLASLDLpRKRE-----LLPYlerlareiNIPILYVSHS---LDEILrlaDRVVVLEQGKV 207
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
341-476 |
7.14e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 341 KLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGsNVSVAYYDQEHQVLHMDK-----------TLF 409
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG-DIVVSSTSKQKEIKPVRKkvgvvfqfpesQLF 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 410 DE--ISDTY--PE---MTNTRIRNILAAFL----FTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLD 476
Cdd:PRK13643 99 EEtvLKDVAfgPQnfgIPKEKAEKIAAEKLemvgLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
320-538 |
7.56e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.06 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 320 AKESGKDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEpdtgevIYGSNVSVayydqEH 399
Cdd:PRK14246 3 AGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIE------IYDSKIKV-----DG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 400 QVLHMDKTLF--DEIS------------DTYPEMT----------------NTRIRNILAAFLFT---GEDVYKKI---- 442
Cdd:PRK14246 72 KVLYFGKDIFqiDAIKlrkevgmvfqqpNPFPHLSiydniayplkshgikeKREIKKIVEECLRKvglWKEVYDRLnspa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 443 SDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENALNSFPG--TVCYVSHDRYFINKTATRILDLTENRLL 520
Cdd:PRK14246 152 SQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
250
....*....|....*...
gi 496028547 521 NYIGNYDYYIEKREAVEE 538
Cdd:PRK14246 232 EWGSSNEIFTSPKNELTE 249
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
322-476 |
7.70e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 7.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 322 ESGKDVLSVHNLSKSFDRK---KLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEP--DTGEVIYGsnvSVAYYD 396
Cdd:PLN03232 609 QPGAPAISIKNGYFSWDSKtskPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaeTSSVVIRG---SVAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 397 QEHQVLhmDKTLFDEI---SDTYPE-----MTNTRIRNILAafLFTGED---VYKKISDLSGGERGRVSLVKLMLSKANF 465
Cdd:PLN03232 686 QVSWIF--NATVRENIlfgSDFESErywraIDVTALQHDLD--LLPGRDlteIGERGVNISGGQKQRVSMARAVYSNSDI 761
|
170
....*....|.
gi 496028547 466 LLLDEPTNHLD 476
Cdd:PLN03232 762 YIFDDPLSALD 772
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
327-500 |
8.61e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.00 E-value: 8.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSF-DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSN--------------VS 391
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgirklVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 392 VAYYDQEHQVLhmDKTLFDEISDTyPE---MTNTRIRNIL-AAFLFTGEDVYKKIS--DLSGGERGRVSLVKLMLSKANF 465
Cdd:PRK13644 81 IVFQNPETQFV--GRTVEEDLAFG-PEnlcLPPIEIRKRVdRALAEIGLEKYRHRSpkTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 496028547 466 LLLDEPTNHLDIVS-KDVLENA--LNSFPGTVCYVSHD 500
Cdd:PRK13644 158 LIFDEVTSMLDPDSgIAVLERIkkLHEKGKTIVYITHN 195
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
328-522 |
9.27e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 59.64 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINgILE-PDTGEV-IYGSNVSVAYYDQEHQVLHMD 405
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLN-LLEtPDSGQLnIAGHQFDFSQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 406 KTL---FDEIsDTYPEMTntRIRNILAAFL----FTGEDVYKK---------ISD--------LSGGERGRVSLVKLMLS 461
Cdd:COG4161 82 QKVgmvFQQY-NLWPHLT--VMENLIEAPCkvlgLSKEQAREKamkllarlrLTDkadrfplhLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496028547 462 KANFLLLDEPTNHLDI-VSKDVLE--NALNSFPGTVCYVSHDRYFINKTATRILDLTENRLLNY 522
Cdd:COG4161 159 EPQVLLFDEPTAALDPeITAQVVEiiRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-215 |
9.70e-10 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 59.21 E-value: 9.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 17 IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADG---GSVTL---AKDAKL-----GYLRQINNVDSTLSIIDE 85
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFngqPRKPDQfqkcvAYVRQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 86 L-YTVIepildmekriLKMQNEMRhltgekleklyssytalthnyelmDGYAAKSKVVGILKGLGFEEADfDRKINTLSG 164
Cdd:cd03234 102 LtYTAI----------LRLPRKSS------------------------DAIRKKRVEDVLLRDLALTRIG-GNLVKGISG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496028547 165 GQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNY--NGAVVIVS 215
Cdd:cd03234 147 GERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLarRNRIVILT 199
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
351-477 |
1.00e-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: 59.69 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 351 KRGERVAIIGDNGTGKTTLLKIINGILEPDTGEviYGSN-----VSVAYYDQEHQVlHMDKTLFDEIS--------DTYP 417
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPpdwdeILDEFRGSELQN-YFTKLLEGDVKvivkpqyvDLIP 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496028547 418 EMTNTRIRNILAAFLFTG--EDVYKK----------ISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDI 477
Cdd:cd03236 101 KAVKGKVGELLKKKDERGklDELVDQlelrhvldrnIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-217 |
1.08e-09 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 59.24 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNE-IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-KDaklgyLRQINNVDSTLSIid 84
Cdd:cd03295 5 NVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDgED-----IREQDPVELRRKI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 85 eLYtVIEPIldmekrilkmqNEMRHLTGE-------KLEKlYSSYTALTHNYELmdgyaakskvvgiLKGLGFEEADF-D 156
Cdd:cd03295 78 -GY-VIQQI-----------GLFPHMTVEenialvpKLLK-WPKEKIRERADEL-------------LALVGLDPAEFaD 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 157 RKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGA----VVIVSHD 217
Cdd:cd03295 131 RYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgktIVFVTHD 195
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
337-476 |
1.27e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 59.76 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 337 FDRKKLFyDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGS-----------------NVSVAYYDQEH 399
Cdd:PRK13649 18 FEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknkdikqirkKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 400 QVLhmDKTLFDEIS------DTYPEMTNTRIRNILAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTN 473
Cdd:PRK13649 97 QLF--EETVLKDVAfgpqnfGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
...
gi 496028547 474 HLD 476
Cdd:PRK13649 175 GLD 177
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-236 |
1.32e-09 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 59.04 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 16 EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVT-----LAKDAKLGYLRQINNV--DSTL---SIIDE 85
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLvdghdLALADPAWLRRQVGVVlqENVLfnrSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 86 LyTVIEPILDMEKRIlkmqnemrhltgekleklYSSYTALTHNY--ELMDGYaakSKVVGiLKGLGfeeadfdrkintLS 163
Cdd:cd03252 96 I-ALADPGMSMERVI------------------EAAKLAGAHDFisELPEGY---DTIVG-EQGAG------------LS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 164 GGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNGAVVIVSHdRYFLDKIVSKVIDIENGNV 236
Cdd:cd03252 141 GGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMhdICAGRTVIIIAH-RLSTVKNADRIIVMEKGRI 214
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
325-476 |
1.36e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 59.36 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 325 KDVLSVHNLSKSFDRKKLFY---DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYG------SNVsvayY 395
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYtlnDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDgdllteENV----W 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 396 DQEHQV---------LHMDKTLFDEIS-------DTYPEMTNtRIRNILAaflFTGEDVYKK--ISDLSGGERGRVSLVK 457
Cdd:PRK13650 78 DIRHKIgmvfqnpdnQFVGATVEDDVAfglenkgIPHEEMKE-RVNEALE---LVGMQDFKErePARLSGGQKQRVAIAG 153
|
170
....*....|....*....
gi 496028547 458 LMLSKANFLLLDEPTNHLD 476
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLD 172
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
340-499 |
1.67e-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: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 340 KKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYgSNVSVAYYDqeHQVLH------------MDKT 407
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-DGVPLVQYD--HHYLHrqvalvgqepvlFSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 408 LFDEIS---DTYPEMTNTRIRNILAAFLFTGE-------DVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDI 477
Cdd:TIGR00958 571 VRENIAyglTDTPDEEIMAAAKAANAHDFIMEfpngydtEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180
....*....|....*....|..
gi 496028547 478 VSKDVLENALNSFPGTVCYVSH 499
Cdd:TIGR00958 651 ECEQLLQESRSRASRTVLLIAH 672
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-236 |
1.70e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.26 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 18 IKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAkdaklgylrqinnvDSTLSIidelytviEPILDME 97
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG--------------GMVLSE--------ETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 98 KRI-LKMQNEMRHLTGEKLEKlySSYTALTHN---YELMdgyaaKSKVVGILKGLGFEeaDF-DRKINTLSGGQKTRVFL 172
Cdd:PRK13635 81 RQVgMVFQNPDNQFVGATVQD--DVAFGLENIgvpREEM-----VERVDQALRQVGME--DFlNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 173 AKLLLEEPDIILLDEPTNHLDLRS-IEWLES-YLLNYNGAVVIVS--HDryfLDKIVS--KVIDIENGNV 236
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGrREVLETvRQLKEQKGITVLSitHD---LDEAAQadRVIVMNKGEI 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-239 |
1.77e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.55 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 17 IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqinnVDSTLSIIDELYTVIEPildm 96
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE---------------VNGRVSALLELGAGFHP---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 97 ekrilkmqnemrHLTGEklEKLYssYTALTHNyelMDGYAAKSKVVGILK--GLGfeeaDF-DRKINTLSGGQKTRVFLA 173
Cdd:COG1134 102 ------------ELTGR--ENIY--LNGRLLG---LSRKEIDEKFDEIVEfaELG----DFiDQPVKTYSSGMRARLAFA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 174 KLLLEEPDIILLDEPTNHLDL----RSIEWLESyLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNVQMY 239
Cdd:COG1134 159 VATAVDPDILLVDEVLAVGDAafqkKCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
345-476 |
1.98e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.61 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEvIYGSNVSVAYYDQEH---------QVLHM-DKTLFDEISD 414
Cdd:PRK11160 358 GLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGE-ILLNGQPIADYSEAAlrqaisvvsQRVHLfSATLRDNLLL 436
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 415 TYPEMTNTRIRNILA----AFLFTGE---DVYkkISD----LSGGERGRVSLVKLMLSKANFLLLDEPTNHLD 476
Cdd:PRK11160 437 AAPNASDEALIEVLQqvglEKLLEDDkglNAW--LGEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
32-237 |
1.99e-09 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 59.73 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 32 AIVGVNGAGKTTLLKILTGEEQADGGSVTLA-----KDAK----------LGYLRQinnvDSTLsiiDELYTVIEPILDM 96
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqDSARgiflpphrrrIGYVFQ----EARL---FPHLSVRGNLLYG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 97 EKRilkmqnemrhltgekleklyssyTALTHNYELMDGyaakskVVGILkGLGfeeADFDRKINTLSGGQKTRVFLAKLL 176
Cdd:COG4148 102 RKR-----------------------APRAERRISFDE------VVELL-GIG---HLLDRRPATLSGGERQRVAIGRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 177 LEEPDIILLDEPTNHLDLRS----IEWLESYLLNYNGAVVIVSHDryfLDKIV---SKVIDIENGNVQ 237
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLARkaeiLPYLERLRDELDIPILYVSHS---LDEVArlaDHVVLLEQGRVV 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
313-500 |
2.00e-09 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 59.73 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 313 MRLSLDIAKESGkdvlsvhnlskSFDrkkLfyDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNV-- 390
Cdd:COG4148 1 MMLEVDFRLRRG-----------GFT---L--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlq 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 391 -------------SVAYYDQEHQVL-HM-----------------DKTLFDEISDTypemtnTRIRNILAaflftgedvy 439
Cdd:COG4148 65 dsargiflpphrrRIGYVFQEARLFpHLsvrgnllygrkrapraeRRISFDEVVEL------LGIGHLLD---------- 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 440 KKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSK----DVLENALNSFPGTVCYVSHD 500
Cdd:COG4148 129 RRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKaeilPYLERLRDELDIPILYVSHS 193
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-193 |
2.13e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 58.85 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 6 TNISKSFGSNE--IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVtlakdaklgylrQINNVDSTLSII 83
Cdd:PRK13632 11 ENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI------------KIDGITISKENL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 84 DELYTVIEPILdmekrilkmQN------------------EMRHLTGEKLEKLYSSYtalthnyelmdgyaakSKVVGIL 145
Cdd:PRK13632 79 KEIRKKIGIIF---------QNpdnqfigatveddiafglENKKVPPKKMKDIIDDL----------------AKKVGME 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496028547 146 KGLgfeeadfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:PRK13632 134 DYL-------DKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
17-239 |
2.28e-09 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 60.05 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 17 IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSV-------------TLAKdaKLGYLRQinNVdstlsii 83
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVrldgadlkqwdreTFGK--HIGYLPQ--DV------- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 84 dELY--TVIEPILDMEkrilkmqnemRHLTGEKLeklyssYTA--LTHNYELM----DGYAAKSKVVGIlkglgfeeadf 155
Cdd:TIGR01842 402 -ELFpgTVAENIARFG----------ENADPEKI------IEAakLAGVHELIlrlpDGYDTVIGPGGA----------- 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 156 drkinTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYN---GAVVIVSHdRYFLDKIVSKVIDIE 232
Cdd:TIGR01842 454 -----TLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITH-RPSLLGCVDKILVLQ 527
|
....*..
gi 496028547 233 NGNVQMY 239
Cdd:TIGR01842 528 DGRIARF 534
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
325-472 |
2.42e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.35 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 325 KDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYydQEHQVLHM 404
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW--QTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 405 DKTLFDEISDTYPEMT-----------------NTRIRNILAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLL 467
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTveenlamggffaerdqfQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
....*
gi 496028547 468 LDEPT 472
Cdd:PRK11614 161 LDEPS 165
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
328-511 |
2.48e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.18 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEViygsNVSVAYYDQ-EHQ------ 400
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI----TINNINYNKlDHKlaaqlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 401 --VLHMDKTLFDEISDT--------------------YPEMtntRIR-NILAAFLFTGEDVYKKISDLSGGERGRVSLVK 457
Cdd:PRK09700 82 igIIYQELSVIDELTVLenlyigrhltkkvcgvniidWREM---RVRaAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496028547 458 LMLSKANFLLLDEPTNHLDIVSKDVL---ENALNSFPGTVCYVSH---------DRYFINKTATRI 511
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHklaeirricDRYTVMKDGSSV 224
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-219 |
3.09e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKIL-------TGEEQADGGSVTLAKDAK-LGYLRQI 73
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLagllhveSGQIQIDGKTATRGDRSRfMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 74 NNVDSTLSIIDELYTVIEpildmekrilkmqnemrhLTGEKLEKLYSSytALThnyelmdgyaakskVVGILkglGFEea 153
Cdd:PRK13543 91 PGLKADLSTLENLHFLCG------------------LHGRRAKQMPGS--ALA--------------IVGLA---GYE-- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 154 dfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL---LNYNGAVVIVSHDRY 219
Cdd:PRK13543 132 --DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMIsahLRGGGAALVTTHGAY 198
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-196 |
3.56e-09 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 57.63 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 15 NEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL----AKDAKLGYLR-QINNVDSTLSIIDElyTV 89
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdVRDYTLASLRrQIGLVSQDVFLFND--TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 90 IEPIldmekRILKmqnemRHLTGEKLEKlySSYTALTHNY--ELMDGYAAkskVVGilkglgfeeadfDRKINtLSGGQK 167
Cdd:cd03251 93 AENI-----AYGR-----PGATREEVEE--AARAANAHEFimELPEGYDT---VIG------------ERGVK-LSGGQR 144
|
170 180
....*....|....*....|....*....
gi 496028547 168 TRVFLAKLLLEEPDIILLDEPTNHLDLRS 196
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTES 173
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-222 |
3.58e-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: 57.76 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 33 IVGVNGAGKTTLLKILTGEEQADggsvtlakdakLGYLRQINNVDSTLSII--DELYTVIEPILDME-KRILKMQ----- 104
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPN-----------LGKFDDPPDWDEILDEFrgSELQNYFTKLLEGDvKVIVKPQyvdli 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 105 -NEMRHLTGEKLEKlyssytalTHNYELMDGYAAKSKVVGILkglgfeeadfDRKINTLSGGQKTRVFLAKLLLEEPDII 183
Cdd:cd03236 100 pKAVKGKVGELLKK--------KDERGKLDELVDQLELRHVL----------DRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496028547 184 LLDEPTNHLDLR---SIEWLESYLLNYNGAVVIVSHDRYFLD 222
Cdd:cd03236 162 FFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLD 203
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-241 |
3.69e-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: 58.53 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSA----TFLINEHEKAAIVGVNGAGKTTLLKILTG---EEQADGGSVTLakdaklgylrqiN 74
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAvdgvSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILF------------D 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 75 NVDstlsiidelytviepILDMEKRilkmqnEMRHLTGEKLeklyS-----SYTAL---------------THNyeLMDG 134
Cdd:COG0444 69 GED---------------LLKLSEK------ELRKIRGREI----QmifqdPMTSLnpvmtvgdqiaeplrIHG--GLSK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 135 YAAKSKVVGILK--GLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLrSIEW--LEsyLLN---- 206
Cdd:COG0444 122 AEARERAIELLErvGLPDPERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTALDV-TIQAqiLN--LLKdlqr 198
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 496028547 207 -YNGAVVIVSHD----RYFLDKIVskVidiengnvqMYLG 241
Cdd:COG0444 199 eLGLAILFITHDlgvvAEIADRVA--V---------MYAG 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-217 |
4.25e-09 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 57.48 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 18 IKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKdaklgylRQINNVDSTLSIIDELYTVIePILDME 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-------KQITEPGPDRMVVFQNYSLL-PWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 98 KRI-LKMQNEMRHLTGEKLEKLYSSYTALthnyelmdgyaakskvvgilkgLGFEEADfDRKINTLSGGQKTRVFLAKLL 176
Cdd:TIGR01184 73 ENIaLAVDRVLPDLSKSERRAIVEEHIAL----------------------VGLTEAA-DKRPGQLSGGMKQRVAIARAL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496028547 177 LEEPDIILLDEPTNHLDLRSIEWLESYLLN----YNGAVVIVSHD 217
Cdd:TIGR01184 130 SIRPKVLLLDEPFGALDALTRGNLQEELMQiweeHRVTVLMVTHD 174
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
327-391 |
4.68e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 57.69 E-value: 4.68e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 327 VLSVHNLSKSFDRKKLFY--DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS 391
Cdd:PRK13632 7 MIKVENVSFSYPNSENNAlkNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkIDGITIS 74
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-255 |
4.77e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.17 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 22 TFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-----KDAKlGYLRQINNV---------DstLSIIDELy 87
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgyvpfKRRK-EFARRIGVVfgqrsqlwwD--LPAIDSF- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 88 tviepildmekRILKmqnemrhltgekleKLYS-SYTALTHNYELMdgyaakskvVGILkGLGfeeaDF-DRKINTLSGG 165
Cdd:COG4586 118 -----------RLLK--------------AIYRiPDAEYKKRLDEL---------VELL-DLG----ELlDTPVRQLSLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 166 QKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYN---GAVVIV-SHDryfLDKIV---SKVIDIENGNVqM 238
Cdd:COG4586 159 QRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNrerGTTILLtSHD---MDDIEalcDRVIVIDHGRI-I 234
|
250 260
....*....|....*....|.
gi 496028547 239 YLGNYTD----FSNKKQMLLD 255
Cdd:COG4586 235 YDGSLEElkerFGPYKTIVLE 255
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-239 |
6.63e-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: 58.61 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 17 IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL--------AKDA---KLGYLRQinNVdstlsiidE 85
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdgadlsqwDREElgrHIGYLPQ--DV--------E 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 86 LY--TVIEPI-----LDMEK------------RILKmqnemrhltgekleklyssytalthnyeLMDGYaakskvvgilk 146
Cdd:COG4618 417 LFdgTIAENIarfgdADPEKvvaaaklagvheMILR----------------------------LPDGY----------- 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 147 glgfeeadfDRKI----NTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD-------LRSIEwlesYLLNYNGAVVIVS 215
Cdd:COG4618 458 ---------DTRIgeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAIR----ALKARGATVVVIT 524
|
250 260
....*....|....*....|....
gi 496028547 216 HDRYFLdKIVSKVIDIENGNVQMY 239
Cdd:COG4618 525 HRPSLL-AAVDKLLVLRDGRVQAF 547
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
345-499 |
7.15e-09 |
|
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: 56.35 E-value: 7.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYG-------------SNVSV------------------- 392
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDgvdiskiglhdlrSRISIipqdpvlfsgtirsnldpf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 393 -AYYDQE-HQVLhmDKTLFDEISDTYPEMTNTRIRNilaaflftGEdvykkiSDLSGGERGRVSLVKLMLSKANFLLLDE 470
Cdd:cd03244 102 gEYSDEElWQAL--ERVGLKEFVESLPGGLDTVVEE--------GG------ENLSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190
....*....|....*....|....*....|.
gi 496028547 471 PTNHLDIVSKDVLENALNS-FPG-TVCYVSH 499
Cdd:cd03244 166 ATASVDPETDALIQKTIREaFKDcTVLTIAH 196
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
328-476 |
7.90e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.78 E-value: 7.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKK-----LfYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVSvAYYDQE--- 398
Cdd:COG1135 2 IELENLSKTFPTKGgpvtaL-DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVdGVDLT-ALSERElra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 399 --HQV--------LHMDKTLFD------EISDTYPEMTNTRIRNILAaflFTG----EDVYkkISDLSGGERGRVS---- 454
Cdd:COG1135 80 arRKIgmifqhfnLLSSRTVAEnvalplEIAGVPKAEIRKRVAELLE---LVGlsdkADAY--PSQLSGGQKQRVGiara 154
|
170 180
....*....|....*....|..
gi 496028547 455 LVklmlSKANFLLLDEPTNHLD 476
Cdd:COG1135 155 LA----NNPKVLLCDEATSALD 172
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
340-476 |
9.80e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 9.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 340 KKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIygSNVSVAYYDQehQVLHMDKTL------FDEiS 413
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--AERSIAYVPQ--QAWIMNATVrgnilfFDE-E 747
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 414 DTYPEMTNTRIRNILA--AFLFTG--EDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLD 476
Cdd:PTZ00243 748 DAARLADAVRVSQLEAdlAQLGGGleTEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-216 |
9.98e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.87 E-value: 9.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 32 AIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDA----------KLGYLRQINNVDSTLSIIDELYtviepildmekril 101
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltnisdvhqNMGYCPQFDAIDDLLTGREHLY-------------- 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 102 kMQNEMRHLTGEKLEKLyssytaltHNYElmdgyaakskvvgiLKGLGFEEADfDRKINTLSGGQKTRVFLAKLLLEEPD 181
Cdd:TIGR01257 2035 -LYARLRGVPAEEIEKV--------ANWS--------------IQSLGLSLYA-DRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190
....*....|....*....|....*....|....*...
gi 496028547 182 IILLDEPTNHLDLRSIEWLESYLLNY---NGAVVIVSH 216
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSIireGRAVVLTSH 2128
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
346-519 |
1.05e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.06 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 346 INFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVSVA---YYDQEHQVLHMDKTLFDEISDTYPEMTN 421
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGKPVTAEqpeDYRKLFSAVFTDFHLFDQLLGPEGKPAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 422 TRIRNILAAFLFTGEDVY---KKISD--LSGGERGRVSLVKLMLSKANFLLLDE------PtnHLDIVSKDVLENALNSF 490
Cdd:PRK10522 422 PALVEKWLERLKMAHKLEledGRISNlkLSKGQKKRLALLLALAEERDILLLDEwaadqdP--HFRREFYQVLLPLLQEM 499
|
170 180 190
....*....|....*....|....*....|
gi 496028547 491 PGTVCYVSH-DRYFINktATRILDLTENRL 519
Cdd:PRK10522 500 GKTIFAISHdDHYFIH--ADRLLEMRNGQL 527
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
327-385 |
1.20e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.34 E-value: 1.20e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 327 VLSVHNLSKSFD-RKKLFY--------DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVI 385
Cdd:PRK15112 4 LLEVRNLSKTFRyRTGWFRrqtveavkPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL 71
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
345-384 |
1.22e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 56.56 E-value: 1.22e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV 384
Cdd:PRK13635 25 DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI 64
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
323-392 |
1.40e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 56.20 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 323 SGKDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGI--LEPD---TGEV------IYGSNVS 391
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEIlldgedIYDPDVD 86
|
.
gi 496028547 392 V 392
Cdd:COG1117 87 V 87
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-216 |
1.48e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.00 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTgeeqadggsvtlakdaKLGYLRQINNVDSTLSIIDE- 85
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFN----------------RLLELNEEARVEGEVRLFGRn 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 86 LYTV-IEPIlDMEKRI---LKMQNEMRHLT-------GEKLEKLYSSYTALTHNYElmdgYAAKskvvgilKGLGFEEAD 154
Cdd:PRK14267 73 IYSPdVDPI-EVRREVgmvFQYPNPFPHLTiydnvaiGVKLNGLVKSKKELDERVE----WALK-------KAALWDEVK 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 155 fDR---KINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNGAVVIVSH 216
Cdd:PRK14267 141 -DRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLfeLKKEYTIVLVTH 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
328-476 |
1.51e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.13 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQEHQVLHMDK- 406
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 407 ---------TLFDEISDTYPEMT--------------------NTRIRNILAAFLFTGEDVYKKISDLSGGERGRVSLVK 457
Cdd:PRK10619 86 qlrllrtrlTMVFQHFNLWSHMTvlenvmeapiqvlglskqeaRERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIAR 165
|
170
....*....|....*....
gi 496028547 458 LMLSKANFLLLDEPTNHLD 476
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALD 184
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-193 |
1.53e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 56.02 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSN----EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-------------- 62
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDgvpvtgpgadrgvv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 63 --KDAKLGYLRQINNVDSTLsiidelytviepildmekRILKMQNEMRHLTGEKLEKLyssytalthnyelmdgyaaksk 140
Cdd:COG4525 82 fqKDALLPWLNVLDNVAFGL------------------RLRGVPKAERRARAEELLAL---------------------- 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496028547 141 vVGiLKGLGfeeadfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:COG4525 122 -VG-LADFA------RRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2-217 |
1.70e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.09 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLakDAKLGYLRqinnvdstls 81
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHY--RMRDGQLR---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 82 iidELYTVIEPildmEKRILkMQNEMRHLTGEKLEKLYSSYTALTHNYE-LMdgyAAKSKVVGILKG-----LGFEEADF 155
Cdd:PRK11701 74 ---DLYALSEA----ERRRL-LRTEWGFVHQHPRDGLRMQVSAGGNIGErLM---AVGARHYGDIRAtagdwLERVEIDA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 156 DRkIN----TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDL----RSIEWLESYLLNYNGAVVIVSHD 217
Cdd:PRK11701 143 AR-IDdlptTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVsvqaRLLDLLRGLVRELGLAVVIVTHD 211
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
325-476 |
1.91e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.17 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 325 KDVLsVHNLSKSFDRKKLFY-----DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQEH 399
Cdd:PRK13645 5 KDII-LDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 400 QVlhmdKTLFDEISDT--YPE---MTNTRIRNILAAFLFTGED---VYKKIS------------------DLSGGERGRV 453
Cdd:PRK13645 84 EV----KRLRKEIGLVfqFPEyqlFQETIEKDIAFGPVNLGENkqeAYKKVPellklvqlpedyvkrspfELSGGQKRRV 159
|
170 180
....*....|....*....|...
gi 496028547 454 SLVKLMLSKANFLLLDEPTNHLD 476
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLD 182
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
321-487 |
2.01e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.65 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 321 KESGKDVLSVHNLSKSFDRKK--LFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSnvsVAYYDQ 397
Cdd:TIGR00957 630 KPGEGNSITVHNATFTWARDLppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVhMKGS---VAYVPQ 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 398 ehQVLHMDKTLFDEISDTYPeMTNTRIRNILAA--------FLFTGE--DVYKKISDLSGGERGRVSLVKLMLSKANFLL 467
Cdd:TIGR00957 707 --QAWIQNDSLRENILFGKA-LNEKYYQQVLEAcallpdleILPSGDrtEIGEKGVNLSGGQKQRVSLARAVYSNADIYL 783
|
170 180
....*....|....*....|.
gi 496028547 468 LDEPTNHLDI-VSKDVLENAL 487
Cdd:TIGR00957 784 FDDPLSAVDAhVGKHIFEHVI 804
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
341-488 |
2.12e-08 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 55.24 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 341 KLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS----------VAYYDQEHQVlhMDKTLF 409
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlLDGVDIRdlnlrwlrsqIGLVSQEPVL--FDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 410 DEIS--DTYPEMTnTRIRNILAA----FLFTGEDVY-----KKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIV 478
Cdd:cd03249 95 ENIRygKPDATDE-EVEEAAKKAnihdFIMSLPDGYdtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170
....*....|
gi 496028547 479 SKDVLENALN 488
Cdd:cd03249 174 SEKLVQEALD 183
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-217 |
2.12e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.17 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNE----IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLakdakLGylrqinnvd 77
Cdd:PRK10584 6 IVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL-----VG--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 78 STLSIIDElytviepildmEKRI-LKMQNemrhlTGEKLEK--LYSSYTALtHNYEL------MDGYAAKSKVVGILKGL 148
Cdd:PRK10584 72 QPLHQMDE-----------EARAkLRAKH-----VGFVFQSfmLIPTLNAL-ENVELpallrgESSRQSRNGAKALLEQL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 149 GFEEAdFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYN----GAVVIVSHD 217
Cdd:PRK10584 135 GLGKR-LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNrehgTTLILVTHD 206
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
327-476 |
2.29e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.78 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYG---------------SNVS 391
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgkpldyskrgllalrQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 392 VAYYDQEHQVLHMDktlFDeiSDTYPEMTNTRI------RNILAAFLFTGEDVYKK--ISDLSGGERGRVSLVKLMLSKA 463
Cdd:PRK13638 81 TVFQDPEQQIFYTD---ID--SDIAFSLRNLGVpeaeitRRVDEALTLVDAQHFRHqpIQCLSHGQKKRVAIAGALVLQA 155
|
170
....*....|...
gi 496028547 464 NFLLLDEPTNHLD 476
Cdd:PRK13638 156 RYLLLDEPTAGLD 168
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
2-217 |
2.32e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.48 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA----------------KDA 65
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegpgaergvvfqNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 66 KLGYLRQINNVDSTLsiidELYTViepilDMEKRilkmqnemRHLTGEKLEKLyssytalthnyelmdgyaakskvvgil 145
Cdd:PRK11248 81 LLPWRNVQDNVAFGL----QLAGV-----EKMQR--------LEIAHQMLKKV--------------------------- 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496028547 146 kglGFEEADfDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNY----NGAVVIVSHD 217
Cdd:PRK11248 117 ---GLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLwqetGKQVLLITHD 188
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-236 |
2.44e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.02 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSF-----------GSNEIIKSATFLINEHEKAAIVGVNGAGKTT----LLKILT--GEEQADGGSV-TLA 62
Cdd:PRK15134 274 PLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIWFDGQPLhNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 63 KDAKLGYLRQINNVdstlsiIDELYTVIEPILDMEKRILK-MQNEMRHLTGEKLEKlyssytalthnyelmdgyaaksKV 141
Cdd:PRK15134 354 RRQLLPVRHRIQVV------FQDPNSSLNPRLNVLQIIEEgLRVHQPTLSAAQREQ----------------------QV 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 142 VGILKGLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDlRSIE-----WLESYLLNYNGAVVIVSH 216
Cdd:PRK15134 406 IAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQaqilaLLKSLQQKHQLAYLFISH 484
|
250 260
....*....|....*....|
gi 496028547 217 DRYFLDKIVSKVIDIENGNV 236
Cdd:PRK15134 485 DLHVVRALCHQVIVLRQGEV 504
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-262 |
2.45e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.43 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGgsvTLAKDAKLGYLRQinnvdstlsi 82
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELES---EVRVEGRVEFFNQ---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 idELYtviepildmEKRI----LKMQNEMRHLTGEKLEklYSSYTALTHNYELMdGYAAKSKVVGILKGlGFEEADFDRK 158
Cdd:PRK14258 75 --NIY---------ERRVnlnrLRRQVSMVHPKPNLFP--MSVYDNVAYGVKIV-GWRPKLEIDDIVES-ALKDADLWDE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 159 INT--------LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD----LRSIEWLESYLLNYNGAVVIVSHDRYFLDKIvS 226
Cdd:PRK14258 140 IKHkihksaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLRSELTMVIVSHNLHQVSRL-S 218
|
250 260 270
....*....|....*....|....*....|....*....
gi 496028547 227 KVIDIENGNvQMYLGNYTDFSNKKQML---LDAKMKEYL 262
Cdd:PRK14258 219 DFTAFFKGN-ENRIGQLVEFGLTKKIFnspHDSRTREYV 256
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
15-237 |
2.70e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.51 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 15 NEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVtlakdaklgylrqinnvdstlsIIDELYTVIEPIL 94
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI----------------------IIDGDLLTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 95 DMEKRI-LKMQNEMRHLTGEKLEklysSYTALTHNYELMDGYAAKSKVVGILKGLGFEeaDF-DRKINTLSGGQKTRVFL 172
Cdd:PRK13650 78 DIRHKIgMVFQNPDNQFVGATVE----DDVAFGLENKGIPHEEMKERVNEALELVGMQ--DFkEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 173 AKLLLEEPDIILLDEPTNHLD----LRSIEWLESYLLNYNGAVVIVSHDryfLDKIV--SKVIDIENGNVQ 237
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD---LDEVAlsDRVLVMKNGQVE 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-193 |
3.33e-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: 54.54 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 14 SNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL----AKDAKLGYLR-QINNV--DSTL------ 80
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdIREVTLDSLRrAIGVVpqDTVLfndtig 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 --------SIIDElyTVIEP--ILDMEKRILKMQnemrhltgekleklyssytalthnyelmDGYAAkskVVGiLKGLgf 150
Cdd:cd03253 93 ynirygrpDATDE--EVIEAakAAQIHDKIMRFP----------------------------DGYDT---IVG-ERGL-- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496028547 151 eeadfdrkinTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:cd03253 137 ----------KLSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
352-504 |
3.55e-08 |
|
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: 52.76 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 352 RGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYgsnvsvayydqehqvlhmdktlfdeisdtypemTNTRIRNILAAF 431
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------IDGEDILEEVLD 47
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 432 LFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENALNSFPGTVCYVSHDRYFI 504
Cdd:smart00382 48 QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
137-250 |
3.60e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.22 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 137 AKSKVVGILKGLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGA---VVI 213
Cdd:PRK13641 121 AKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVIL 200
|
90 100 110
....*....|....*....|....*....|....*..
gi 496028547 214 VSHDRYFLDKIVSKVIDIENGNVQMYLGNYTDFSNKK 250
Cdd:PRK13641 201 VTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-225 |
4.55e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQadggsvtlakdaklgylrqinnvdstls 81
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPA---------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 82 iidelYTVIE-PILDMEKRILKMQNEMRHLTGEKLEKLYSSYTALTHNYE-LMDGYAAKSKVVG---------------I 144
Cdd:CHL00131 59 -----YKILEgDILFKGESILDLEPEERAHLGIFLAFQYPIEIPGVSNADfLRLAYNSKRKFQGlpeldplefleiineK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 145 LKGLGFEEADFDRKINT-LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD---LRSIEWLESYLLNYNGAVVIVSHDRYF 220
Cdd:CHL00131 134 LKLVGMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDidaLKIIAEGINKLMTSENSIILITHYQRL 213
|
....*
gi 496028547 221 LDKIV 225
Cdd:CHL00131 214 LDYIK 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
345-477 |
4.59e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.89 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS-------VAYYDQEHQVLHMDKTLFDEI--SD 414
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsILGQPTRqalqknlVAYVPQSEEVDWSFPVLVEDVvmMG 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 415 TYPEMTNTRI-----RNILAAFLF---TGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDI 477
Cdd:PRK15056 105 RYGHMGWLRRakkrdRQIVTAALArvdMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
345-500 |
5.16e-08 |
|
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: 55.91 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGsNVSVAYYDQEHQVLHM-----DKTLFD-EISDtype 418
Cdd:COG4618 350 GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD-GADLSQWDREELGRHIgylpqDVELFDgTIAE---- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 419 mtntrirNIlAAFL-FTGEDVYK--------------------KISD----LSGGERGRVSLVKLMLSKANFLLLDEPTN 473
Cdd:COG4618 425 -------NI-ARFGdADPEKVVAaaklagvhemilrlpdgydtRIGEggarLSGGQRQRIGLARALYGDPRLVVLDEPNS 496
|
170 180 190
....*....|....*....|....*....|
gi 496028547 474 HLDIVSKDVLENALNSF---PGTVCYVSHD 500
Cdd:COG4618 497 NLDDEGEAALAAAIRALkarGATVVVITHR 526
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
345-476 |
5.86e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 54.71 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYG--------------SNVSVAYYDQEHQ----VLHMDK 406
Cdd:PRK13633 28 DVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDgldtsdeenlwdirNKAGMVFQNPDNQivatIVEEDV 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496028547 407 TLFDEISDTYPEMTNTRIRNILAAflfTGEDVYKKISD--LSGGERGRVSLVKLMLSKANFLLLDEPTNHLD 476
Cdd:PRK13633 108 AFGPENLGIPPEEIRERVDESLKK---VGMYEYRRHAPhlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
345-500 |
6.61e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 54.42 E-value: 6.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPD--------------TGEVIYG--SNVSVAYYDQEHQVLhmDKTL 408
Cdd:PRK13640 25 DISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpnskitvdgitlTAKTVWDirEKVGIVFQNPDNQFV--GATV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 409 FDEIS-------DTYPEMTnTRIRNILAAFLFTgEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLD----- 476
Cdd:PRK13640 103 GDDVAfglenraVPRPEMI-KIVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDpagke 180
|
170 180
....*....|....*....|....*...
gi 496028547 477 ----IVSKDVLENALnsfpgTVCYVSHD 500
Cdd:PRK13640 181 qilkLIRKLKKKNNL-----TVISITHD 203
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-196 |
6.77e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 55.56 E-value: 6.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 11 SF---GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA----KDAKLGYLRqinnvdSTLSII 83
Cdd:COG1132 346 SFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDgvdiRDLTLESLR------RQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 84 DE---LY--TVIEPIL------DME--KRILKMqnemrhltgekleklyssytALTHNY--ELMDGYAAkskVVGilkgl 148
Cdd:COG1132 420 PQdtfLFsgTIRENIRygrpdaTDEevEEAAKA--------------------AQAHEFieALPDGYDT---VVG----- 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496028547 149 gfEEAdfdrkiNTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS 196
Cdd:COG1132 472 --ERG------VNLSGGQRQRIAIARALLKDPPILILDEATSALDTET 511
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-238 |
6.96e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 54.28 E-value: 6.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 18 IKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqINNVDSTLSIIDelytviepILDME 97
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKII------------IDGVDITDKKVK--------LSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 98 KRI-LKMQNEMRHLTGEKLEKlysSYTALTHNYELMDGyAAKSKVVGILKGLGFEEADF-DRKINTLSGGQKTRVFLAKL 175
Cdd:PRK13637 83 KKVgLVFQYPEYQLFEETIEK---DIAFGPINLGLSEE-EIENRVKRAMNIVGLDYEDYkDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 176 LLEEPDIILLDEPTNHLD-------LRSIEWLESyllNYNGAVVIVSHDRYFLDKIVSKVIDIENGNVQM 238
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDpkgrdeiLNKIKELHK---EYNMTIILVSHSMEDVAKLADRIIVMNKGKCEL 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
310-487 |
7.09e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.90 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 310 TENMRLSLDIAKESGKDVLSVHNLSKSFDRK---KLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEP--DTGEV 384
Cdd:PLN03130 597 AEERVLLPNPPLEPGLPAISIKNGYFSWDSKaerPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrsDASVV 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 385 IYGsnvSVAYYDQEHQVLHM---DKTLFDeiSDTYPEMTNTRIRniLAAF-----LFTGED---VYKKISDLSGGERGRV 453
Cdd:PLN03130 677 IRG---TVAYVPQVSWIFNAtvrDNILFG--SPFDPERYERAID--VTALqhdldLLPGGDlteIGERGVNISGGQKQRV 749
|
170 180 190
....*....|....*....|....*....|....*
gi 496028547 454 SLVKLMLSKANFLLLDEPTNHLDI-VSKDVLENAL 487
Cdd:PLN03130 750 SMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCI 784
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
10-238 |
8.50e-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: 8.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 10 KSFGSNEIIksaTFlinEHEKAAIVGVNGAGKTTLLK----ILTGEeqADGGSVTLAKDAKLgylrqINNVDSTLSI--- 82
Cdd:cd03240 10 RSFHERSEI---EF---FSPLTLIVGQNGAGKTTIIEalkyALTGE--LPPNSKGGAHDPKL-----IREGEVRAQVkla 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 ----IDELYTVIEPILDMEKRILKMQNEMRHLtgekleklyssytalthnyeLMDGyaakskvvgilkglgfeeadfdrk 158
Cdd:cd03240 77 fenaNGKKYTITRSLAILENVIFCHQGESNWP--------------------LLDM------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 159 INTLSGGQKT------RVFLAKLLLEEPDIILLDEPTNHLDLRSIEW-----LESYLLNYNGAVVIVSHDRYFLDKIvSK 227
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDAA-DH 191
|
250
....*....|.
gi 496028547 228 VIDIENGNVQM 238
Cdd:cd03240 192 IYRVEKDGRQK 202
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
2-189 |
1.08e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.34 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL-AKDAKLGYLRQInnVDSTL 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFdGKDITDWQTAKI--MREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 SIIDELYTVIEPILDMEKRILKMQNEMRHLTGEKLEKLYSSYTALthnyelmdgyaakskvvgilkglgfeeadFDRKIN 160
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRL-----------------------------HERRIQ 133
|
170 180 190
....*....|....*....|....*....|..
gi 496028547 161 ---TLSGGQKTRVFLAKLLLEEPDIILLDEPT 189
Cdd:PRK11614 134 ragTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
331-476 |
1.24e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 54.04 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 331 HNLSKSFD-RKKLFY---DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQE-------- 398
Cdd:PRK11153 5 KNISKVFPqGGRTIHalnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarrqi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 399 -----HQVLHMDKTLFD------EISDTYPEMTNTRIRNILAAF-LFTGEDVYKkiSDLSGGERGRVSLVKLMLSKANFL 466
Cdd:PRK11153 85 gmifqHFNLLSSRTVFDnvalplELAGTPKAEIKARVTELLELVgLSDKADRYP--AQLSGGQKQRVAIARALASNPKVL 162
|
170
....*....|
gi 496028547 467 LLDEPTNHLD 476
Cdd:PRK11153 163 LCDEATSALD 172
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
340-522 |
1.33e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 53.68 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 340 KKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVSVAYYDQEHQVLHMDKTLFDEisdtYPE 418
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItIAGYHITPETGNKNLKKLRKKVSLVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 419 ---MTNTRIRNILAA---FLFTGEDV-------YKKIS-----------DLSGGERGRVSLVKLMLSKANFLLLDEPTNH 474
Cdd:PRK13641 96 aqlFENTVLKDVEFGpknFGFSEDEAkekalkwLKKVGlsedliskspfELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496028547 475 LDIVSKDVLENALNSFPG---TVCYVSHDRYFINKTATRILDLTENRLLNY 522
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKLIKH 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-216 |
1.37e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.73 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 14 SNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLakDAKlgYLRQINNVdstlsiidELYTVI--- 90
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL--DGV--PLVQYDHH--------YLHRQValv 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 91 --EPILdmekrilkMQNEMRHLTG------EKLEKLYSSYTALTHNY--ELMDGYaakskvvgilkglgfeEADFDRKIN 160
Cdd:TIGR00958 561 gqEPVL--------FSGSVRENIAygltdtPDEEIMAAAKAANAHDFimEFPNGY----------------DTEVGEKGS 616
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496028547 161 TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGAVVIVSH 216
Cdd:TIGR00958 617 QLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-196 |
1.58e-07 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 52.41 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSN--EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL----AKDAKLGYLRqinnvdSTL 80
Cdd:cd03369 11 NLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdgidISTIPLEDLR------SSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 SIIDElytviEPILdmekrilkmqnemrhLTGekleklyssytALTHNYELMDGYAAKSkvvgILKGLGFEEADfdrkiN 160
Cdd:cd03369 85 TIIPQ-----DPTL---------------FSG-----------TIRSNLDPFDEYSDEE----IYGALRVSEGG-----L 124
|
170 180 190
....*....|....*....|....*....|....*.
gi 496028547 161 TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS 196
Cdd:cd03369 125 NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
2-236 |
2.07e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.88 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSF-GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKdaklgylrqinnvdstl 80
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 siidelytviEPILDMEKRilkmqnEMRHLTGEKLEKLYSSYTALTHNYEL--------MDGYAAKSKVVGILKGLGFEE 152
Cdd:PRK13652 66 ----------EPITKENIR------EVRKFVGLVFQNPDDQIFSPTVEQDIafgpinlgLDEETVAHRVSSALHMLGLEE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 153 AdFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS----IEWLESYLLNYNGAVVIVSHDRYFLDKIVSKV 228
Cdd:PRK13652 130 L-RDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGvkelIDFLNDLPETYGMTVIFSTHQLDLVPEMADYI 208
|
....*...
gi 496028547 229 IDIENGNV 236
Cdd:PRK13652 209 YVMDKGRI 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
345-575 |
2.68e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.47 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGsNVSVAYYDQEHQVLHMDKTL-----FDE---ISDTY 416
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHKTKDKYIRPVRKRIgmvfqFPEsqlFEDTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 417 -------PEMTNTRIRNI-------LAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDV 482
Cdd:PRK13646 104 ereiifgPKNFKMNLDEVknyahrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 483 LENALNSFP----GTVCYVSHDRYFINKTATRILDLTENRLLNYIGNYDYYIEKREAVEEAANLSNIEQAQKGIdvsESK 558
Cdd:PRK13646 184 VMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADWHIGLPEIVQLQYDF---EQK 260
|
250
....*....|....*..
gi 496028547 559 QEWMDNKTAQAQKKKIK 575
Cdd:PRK13646 261 YQTKLKDIALTEEEFVS 277
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-480 |
2.74e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.68 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTG---EEQADG-----GSVTLAKDAKLGYLRQI 73
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvypHGTWDGeiywsGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 74 NNVDSTLSIIDELyTVIEPILdmekrilkMQNEmrhltgekleklyssytaLTHNYELMDGYAAKSKVVGILKGLGFEEA 153
Cdd:TIGR02633 81 VIIHQELTLVPEL-SVAENIF--------LGNE------------------ITLPGGRMAYNAMYLRAKNLLRELQLDAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 154 DFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESY---LLNYNGAVVIVSHDRYFLDKIVSKVID 230
Cdd:TIGR02633 134 NVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIirdLKAHGVACVYISHKLNEVKAVCDTICV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 231 IENGNvqmYLGNyTDFSNkkqmlldakMKEylnqqqeirhqEAVITKLkqFNREKSikraesrqkqlekiervdapqtyt 310
Cdd:TIGR02633 214 IRDGQ---HVAT-KDMST---------MSE-----------DDIITMM--VGREIT------------------------ 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 311 enmRLSLDIAKESGKDVLSVHNLSkSFD----RKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILE-------- 378
Cdd:TIGR02633 244 ---SLYPHEPHEIGDVILEARNLT-CWDvinpHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgkfegnvf 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 379 --------------------------------PDTGeviYGSNVSVAYYDQEHQVLHMDKTlfDEISDTYPEMTNTRIRN 426
Cdd:TIGR02633 320 ingkpvdirnpaqairagiamvpedrkrhgivPILG---VGKNITLSVLKSFCFKMRIDAA--AELQIIGSAIQRLKVKT 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 496028547 427 iLAAFLftgedvykKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSK 480
Cdd:TIGR02633 395 -ASPFL--------PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAK 439
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3-201 |
2.80e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.30 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYLRQinNVDSTLSI 82
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK--EVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 IDELYTVIEPILDMEkriLKMQNEMRHltgeklEKLYSSYTAlthnyELMDGYAAKSKVVGILKGLgfeeadfDRKINTL 162
Cdd:PRK10253 86 LAQNATTPGDITVQE---LVARGRYPH------QPLFTRWRK-----EDEEAVTKAMQATGITHLA-------DQSVDTL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496028547 163 SGGQKTRVFLAKLLLEEPDIILLDEPTNHLDL-RSIEWLE 201
Cdd:PRK10253 145 SGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIsHQIDLLE 184
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
323-476 |
2.83e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.93 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 323 SGKDVLSVHNLSKSFDRK-----KLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQ 397
Cdd:PRK13631 17 SDDIILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 398 EHQVL-HMDKTL--FDEISDT------YPE---MTNTRIRNI----------------LAAFLFTG---EDVYKKIS--D 444
Cdd:PRK13631 97 HELITnPYSKKIknFKELRRRvsmvfqFPEyqlFKDTIEKDImfgpvalgvkkseakkLAKFYLNKmglDDSYLERSpfG 176
|
170 180 190
....*....|....*....|....*....|..
gi 496028547 445 LSGGERGRVSLVKLMLSKANFLLLDEPTNHLD 476
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
156-222 |
2.96e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.78 E-value: 2.96e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496028547 156 DRKINTLSGGQKTRVFLAKLLLEEPD--IILLDEPTNHLDLRSIEWLESY---LLNYNGAVVIVSHDRYFLD 222
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVikgLIDLGNTVILIEHNLDVLS 153
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-193 |
3.10e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 52.77 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSN----EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqINNVD-STLS 81
Cdd:COG1135 6 NLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVL------------VDGVDlTALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 82 iidelytviepildmEKRILKMQ----------NemrhltgeklekLYSSYTALtHNYEL------MDGYAAKSKVVGIL 145
Cdd:COG1135 74 ---------------ERELRAARrkigmifqhfN------------LLSSRTVA-ENVALpleiagVPKAEIRKRVAELL 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496028547 146 K--GLGfEEADfdRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:COG1135 126 ElvGLS-DKAD--AYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-255 |
3.13e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.97 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLakDAKLGYL-RQINNVDStL 80
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKV--DGKVLYFgKDIFQIDA-I 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 SIIDELYTVIEpildmekrilkMQNEMRHLTgeklekLYSSYTALTHNYELMDGYAAKSKVVGILKGLGFEEADFDR--- 157
Cdd:PRK14246 87 KLRKEVGMVFQ-----------QPNPFPHLS------IYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRlns 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 158 KINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNGAVVIVSHDRYFLDKIVSKVIDIENGN 235
Cdd:PRK14246 150 PASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLIteLKNEIAIVIVSHNPQQVARVADYVAFLYNGE 229
|
250 260
....*....|....*....|
gi 496028547 236 VQMYLGNYTDFSNKKQMLLD 255
Cdd:PRK14246 230 LVEWGSSNEIFTSPKNELTE 249
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-193 |
3.16e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 53.51 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 16 EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQAD---GGSVTL---AKDAKL-----GYLRQinnvdstlsiiD 84
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLngmPIDAKEmraisAYVQQ-----------D 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 85 ELY----TVIEPILDMEKriLKMQnemRHLTG-EKLEKLYSSYTALThnyeLMDgyAAKSK--VVGILKGLgfeeadfdr 157
Cdd:TIGR00955 108 DLFiptlTVREHLMFQAH--LRMP---RRVTKkEKRERVDEVLQALG----LRK--CANTRigVPGRVKGL--------- 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 496028547 158 kintlSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:TIGR00955 168 -----SGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-236 |
3.71e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.41 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 8 ISKSF-GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-------KDAKLGYLR-QINNV-- 76
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghditrlKNREVPFLRrQIGMIfq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 77 DSTLSIIDELY-TVIEPILdmekrilkmqnemrhLTGEKLEKLYSSYTALTHNYELMDgyaaKSKVVGIlkglgfeeadf 155
Cdd:PRK10908 87 DHHLLMDRTVYdNVAIPLI---------------IAGASGDDIRRRVSAALDKVGLLD----KAKNFPI----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 156 drkinTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNG---AVVIVSHDRYFLDKIVSKVIDIE 232
Cdd:PRK10908 137 -----QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLS 211
|
....
gi 496028547 233 NGNV 236
Cdd:PRK10908 212 DGHL 215
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
32-241 |
4.65e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 52.27 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 32 AIVGVNGAGKTTLLKILT-------GEEQADGGSVTLAKDAKLGYLRQinnvdsTLSII-DELYTVIEPildmekrilkm 103
Cdd:PRK11308 45 AVVGESGCGKSTLARLLTmietptgGELYYQGQDLLKADPEAQKLLRQ------KIQIVfQNPYGSLNP----------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 104 qnemRHLTGEKLEKLYSSYTALThnyelmdgyAA--KSKVVGILKGLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPD 181
Cdd:PRK11308 108 ----RKKVGQILEEPLLINTSLS---------AAerREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 182 IILLDEPTNHLDLrSIewlESYLLN--------YNGAVVIVSHDryfldkiVSKVIDIENGNVQMYLG 241
Cdd:PRK11308 175 VVVADEPVSALDV-SV---QAQVLNlmmdlqqeLGLSYVFISHD-------LSVVEHIADEVMVMYLG 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
161-233 |
5.17e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 49.84 E-value: 5.17e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 161 TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNYNGAVVIVSHdRYFLDKIVSKVIDIEN 233
Cdd:cd03223 91 VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-218 |
5.62e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 50.87 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLG-----YLRQINn 75
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlkpeiYRQQVS- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 76 vdstlsiidelYTVIEPILdmekrilkmqnemrhlTGEkleklySSYTALTHNYELMDGYAAKSKVVGILKGLGFEEADF 155
Cdd:PRK10247 85 -----------YCAQTPTL----------------FGD------TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTIL 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 156 DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD---LRSI-EWLESYLLNYNGAVVIVSHDR 218
Cdd:PRK10247 132 TKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDesnKHNVnEIIHRYVREQNIAVLWVTHDK 198
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-193 |
6.26e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 51.24 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGS---NE--IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA----------KDAK 66
Cdd:COG1101 1 MLELKNLSKTFNPgtvNEkrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDgkdvtklpeyKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 67 L-GYLRQinnvD------STLSiidelytvIEPILDM-----EKRILKM--QNEMRHLTGEKLEKLyssytalthnyelm 132
Cdd:COG1101 81 YiGRVFQ----DpmmgtaPSMT--------IEENLALayrrgKRRGLRRglTKKRRELFRELLATL-------------- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496028547 133 dgyaakskvvgilkGLGFEeadfDR---KINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:COG1101 135 --------------GLGLE----NRldtKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
132-236 |
6.98e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 51.32 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 132 MDGYAAKSKVVGILKGLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS----IEWLESYLLNY 207
Cdd:PRK13646 116 MNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSkrqvMRLLKSLQTDE 195
|
90 100
....*....|....*....|....*....
gi 496028547 208 NGAVVIVSHDRYFLDKIVSKVIDIENGNV 236
Cdd:PRK13646 196 NKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
8-217 |
8.38e-07 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 50.72 E-value: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 8 ISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVtlakdaklgylrqinnvdstlsIIDEly 87
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKV----------------------LIDG-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 88 tviEPILDMEKRilkmqnEMRHLTGEKLEKLYSSYTALTHNYELmDGYAAKSKVVGILK--------------GLgfeEA 153
Cdd:cd03294 86 ---QDIAAMSRK------ELRELRRKKISMVFQSFALLPHRTVL-ENVAFGLEVQGVPRaereeraaealelvGL---EG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 154 DFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD-LRSIEwLESYLL----NYNGAVVIVSHD 217
Cdd:cd03294 153 WEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDpLIRRE-MQDELLrlqaELQKTIVFITHD 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
151-216 |
8.49e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.12 E-value: 8.49e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 151 EEADFDRkinTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLN--YNGAVVIVSH 216
Cdd:COG4178 478 EEADWDQ---VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH 542
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
329-508 |
9.15e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.94 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 329 SVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQ--EHQVLHMDK 406
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 407 TLfdeisdtyPEMTNTRIRNILA--------AF-LFTGED----------------VYKKISDLSGGERGRVSLVKLMLS 461
Cdd:PRK10575 93 QL--------PAAEGMTVRELVAigrypwhgALgRFGAADrekveeaislvglkplAHRLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496028547 462 KANFLLLDEPTNHLDIVSK-DVLE--NALNSFPG-TVCYVSHDryfINKTA 508
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQvDVLAlvHRLSQERGlTVIAVLHD---INMAA 212
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
592-635 |
1.04e-06 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 46.31 E-value: 1.04e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 496028547 592 LQTVDEEFANPKNSSNVGKLMELQKQKEALEERLDKLMADWEEL 635
Cdd:pfam16326 24 IAELEAQLADPELYSDYEKLQELSAELEELEAELEELYERWEEL 67
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-250 |
1.11e-06 |
|
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: 52.22 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 17 IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGE-EQADGgsvTLAKDAKLGYLRQI---------NNVDSTLSIIDEL 86
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGElEPSEG---KIKHSGRISFSPQTswimpgtikDNIIFGLSYDEYR 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 87 YTVIEPILDMEKRILKMQNEmrhltgekleklyssytaltHNYELMDGyaakskvvGIlkglgfeeadfdrkinTLSGGQ 166
Cdd:TIGR01271 518 YTSVIKACQLEEDIALFPEK--------------------DKTVLGEG--------GI----------------TLSGGQ 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 167 KTRVFLAKLLLEEPDIILLDEPTNHLD-LRSIEWLESYL--LNYNGAVVIVSHDRYFLDKiVSKVIDIENGNVQMYlGNY 243
Cdd:TIGR01271 554 RARISLARAVYKDADLYLLDSPFTHLDvVTEKEIFESCLckLMSNKTRILVTSKLEHLKK-ADKILLLHEGVCYFY-GTF 631
|
....*..
gi 496028547 244 TDFSNKK 250
Cdd:TIGR01271 632 SELQAKR 638
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-250 |
1.25e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.78 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 18 IKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYLRQINNVDSTLSIIDELYTVIEPILDME 97
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 98 KRILKMQNEMRHLtGEKLEKLYSSYTALTHNYELMDGYAAKSKvvgilkglgFEeadfdrkintLSGGQKTRVFLAKLLL 177
Cdd:PRK13645 107 TIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLPEDYVKRSP---------FE----------LSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 178 EEPDIILLDEPTNHLDLRSIEWLESYLL----NYNGAVVIVSHDRYFLDKIVSKVIDIENGNVQMYLGNYTDFSNKK 250
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFErlnkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE 243
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
327-500 |
1.37e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.48 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDIN---FEIKRGERVAIIGDNGTGKTTLLKIINGILE------PDTGEVIYGSNV------- 390
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEefegkvKIDGELLTAENVwnlrrki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 391 SVAYYDQEHQVLHM---DKTLFDEISDTYP--EMTNTRIRNILAAFLFTGEDvyKKISDLSGGERGRVSLVKLMLSKANF 465
Cdd:PRK13642 84 GMVFQNPDNQFVGAtveDDVAFGMENQGIPreEMIKRVDEALLAVNMLDFKT--REPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 496028547 466 LLLDEPTNHLDIVSKD----VLENALNSFPGTVCYVSHD 500
Cdd:PRK13642 162 IILDESTSMLDPTGRQeimrVIHEIKEKYQLTVLSITHD 200
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-196 |
1.42e-06 |
|
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: 51.26 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSFGSNEI--IKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL----AKDAKLGYLR-QINNVDST 79
Cdd:TIGR02203 335 NVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLdghdLADYTLASLRrQVALVSQD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 80 LSIIDElyTVIEPIldmekrilkMQNEMRHLTGEKLEKLyssytalthnyeLMDGYAaKSKVVGILKGLGFEEADfdrKI 159
Cdd:TIGR02203 415 VVLFND--TIANNI---------AYGRTEQADRAEIERA------------LAAAYA-QDFVDKLPLGLDTPIGE---NG 467
|
170 180 190
....*....|....*....|....*....|....*..
gi 496028547 160 NTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS 196
Cdd:TIGR02203 468 VLLSGGQRQRLAIARALLKDAPILILDEATSALDNES 504
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-235 |
1.55e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 51.36 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 17 IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKdaklgylRQINNVD-STLSiidELYTVIEpild 95
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG-------QPIADYSeAALR---QAISVVS---- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 96 meKRIlkmqnemrHLtgekleklYSsyTALTHNYELMDGYAAKSKVVGILKGLGFEE-ADFDRKINT--------LSGGQ 166
Cdd:PRK11160 421 --QRV--------HL--------FS--ATLRDNLLLAAPNASDEALIEVLQQVGLEKlLEDDKGLNAwlgeggrqLSGGE 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 167 KTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNY--NGAVVIVSHDRYFL---DKIVskVID----IENGN 235
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHRLTGLeqfDRIC--VMDngqiIEQGT 556
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
135-249 |
1.62e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 50.62 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 135 YAAKSKVVGILKGLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLN---YNGAV 211
Cdd:PRK13631 150 SEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDakaNNKTV 229
|
90 100 110
....*....|....*....|....*....|....*...
gi 496028547 212 VIVSHDRYFLDKIVSKVIDIENGNVQMYLGNYTDFSNK 249
Cdd:PRK13631 230 FVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-255 |
1.65e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.13 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNE--IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAklgylrqINNVDST 79
Cdd:PRK13648 7 IIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQA-------ITDDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 80 lsiidelytviepilDMEKRI-LKMQNEMRHLTGEKLEklYSSYTALTHN---YELMdgyaaKSKVVGILKGLG-FEEAD 154
Cdd:PRK13648 80 ---------------KLRKHIgIVFQNPDNQFVGSIVK--YDVAFGLENHavpYDEM-----HRRVSEALKQVDmLERAD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 155 FDRkiNTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNGAVVIVS--HDryfLDKIV--SKV 228
Cdd:PRK13648 138 YEP--NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVrkVKSEHNITIISitHD---LSEAMeaDHV 212
|
250 260
....*....|....*....|....*...
gi 496028547 229 IDIENGNV-QMylGNYTDFSNKKQMLLD 255
Cdd:PRK13648 213 IVMNKGTVyKE--GTPTEIFDHAEELTR 238
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
137-195 |
2.21e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 49.63 E-value: 2.21e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 137 AKSKVVGILKGLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLR 195
Cdd:PRK13634 121 AKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-189 |
2.22e-06 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 49.21 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA-KD---------AKLG-- 68
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgEDitglpphriARLGig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 69 YLRQINNVDSTLsiidelyTVIEPiLDMEKRILKMQNEMRhltgEKLEKLYSSYTALthnYELMDGYAAkskvvgilkgl 148
Cdd:COG0410 82 YVPEGRRIFPSL-------TVEEN-LLLGAYARRDRAEVR----ADLERVYELFPRL---KERRRQRAG----------- 135
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496028547 149 gfeeadfdrkinTLSGGQKTRVFLAKLLLEEPDIILLDEPT 189
Cdd:COG0410 136 ------------TLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
328-487 |
2.25e-06 |
|
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: 51.06 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSF--DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDtGEV----IYGSNVSVAYYDQEHQV 401
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIqidgVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 402 LHMDKTLFDEIS----DTYPEMTNTRI---------RNILAAF-------LFTGEDVykkisdLSGGERGRVSLVKLMLS 461
Cdd:TIGR01271 1297 IPQKVFIFSGTFrknlDPYEQWSDEEIwkvaeevglKSVIEQFpdkldfvLVDGGYV------LSNGHKQLMCLARSILS 1370
|
170 180
....*....|....*....|....*.
gi 496028547 462 KANFLLLDEPTNHLDIVSKDVLENAL 487
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVTLQIIRKTL 1396
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-196 |
2.42e-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: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 15 NEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL----AKDAKLGYLR-QINNV--DSTL---SIID 84
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdgvdIRDLNLRWLRsQIGLVsqEPVLfdgTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 85 EL-YTVIEPILDMEKRILKMqnemrhltgekleklyssytALTHNY--ELMDGYaakSKVVGiLKGLgfeeadfdrkinT 161
Cdd:cd03249 96 NIrYGKPDATDEEVEEAAKK--------------------ANIHDFimSLPDGY---DTLVG-ERGS------------Q 139
|
170 180 190
....*....|....*....|....*....|....*
gi 496028547 162 LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS 196
Cdd:cd03249 140 LSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
345-499 |
2.46e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 48.87 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNV---------------SVAYYDQEHQVLhmDKTLF 409
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNesepsfeatrsrnrySVAYAAQKPWLL--NATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 410 DEISDTYPeMTNTRIRNILAA--------FLFTGE--DVYKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVS 479
Cdd:cd03290 97 ENITFGSP-FNKQRYKAVTDAcslqpdidLLPFGDqtEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180
....*....|....*....|....*
gi 496028547 480 KDVLENA-----LNSFPGTVCYVSH 499
Cdd:cd03290 176 SDHLMQEgilkfLQDDKRTLVLVTH 200
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
14-225 |
3.05e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.05 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 14 SNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKdaklgylRQINNvdstLSIIDELytviepi 93
Cdd:PRK15439 275 TGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG-------KEINA----LSTAQRL------- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 94 ldmeKRILKMQNEMRHLTGEKLEK-LYSSYTALTHNyeLMDGYAAKSKVVGILKG----LGFEEADFDRKINTLSGGQKT 168
Cdd:PRK15439 337 ----ARGLVYLPEDRQSSGLYLDApLAWNVCALTHN--RRGFWIKPARENAVLERyrraLNIKFNHAEQAARTLSGGNQQ 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 169 RVFLAKLLLEEPDIILLDEPTNHLDL--RS-IEWLESYLLNYNGAVVIVSHDryfLDKIV 225
Cdd:PRK15439 411 KVLIAKCLEASPQLLIVDEPTRGVDVsaRNdIYQLIRSIAAQNVAVLFISSD---LEEIE 467
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
345-500 |
3.16e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 50.03 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVSVAYYDQEHQVLHMDKTLFDEISDTYPEMT--- 420
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTvld 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 421 NT-------------RIRNILAAFLFTGEDVYKK--ISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLEN 485
Cdd:PRK10070 126 NTafgmelaginaeeRREKALDALRQVGLENYAHsyPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
|
170
....*....|....*....
gi 496028547 486 ALNSFPG----TVCYVSHD 500
Cdd:PRK10070 206 ELVKLQAkhqrTIVFISHD 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
332-492 |
3.25e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 332 NLSKSFDRKK---LFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYG-----SNVSVAYYDQEHQVLH 403
Cdd:PTZ00265 387 NVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlKDINLKWWRSKIGVVS 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 404 MDKTLF------------------DEISDTYPEMTNTRIRN--------------------------------------- 426
Cdd:PTZ00265 467 QDPLLFsnsiknnikyslyslkdlEALSNYYNEDGNDSQENknkrnscrakcagdlndmsnttdsneliemrknyqtikd 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 427 ----------ILAAFLFTGEDVYKKI-----SDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENALNSFP 491
Cdd:PTZ00265 547 sevvdvskkvLIHDFVSALPDKYETLvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLK 626
|
.
gi 496028547 492 G 492
Cdd:PTZ00265 627 G 627
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
315-488 |
3.29e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 50.02 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 315 LSLDIAKESGKDV-------LSVHNLSKSFDRKKL--FYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVI 385
Cdd:PRK11176 322 LDLEQEKDEGKRVierakgdIEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 386 Y-GSNV----------SVAYYDQehQVLHMDKTLFDEIS----DTYpemtnTRIRNILAAFLFTGEDVYKKISD------ 444
Cdd:PRK11176 402 LdGHDLrdytlaslrnQVALVSQ--NVHLFNDTIANNIAyartEQY-----SREQIEEAARMAYAMDFINKMDNgldtvi 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496028547 445 ------LSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENALN 488
Cdd:PRK11176 475 gengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALD 524
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
325-523 |
3.74e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.87 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 325 KDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIING-----ILEpdtGEVIYgSNVSVAYYDQEH 399
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykILE---GDILF-KGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 400 Q-----------------VLHMD--------KTLFDEISDTYP----EMTNTRIRNILAAFLFTGEDVYKkisDLSGGER 450
Cdd:CHL00131 81 RahlgiflafqypieipgVSNADflrlaynsKRKFQGLPELDPleflEIINEKLKLVGMDPSFLSRNVNE---GFSGGEK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 451 GRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENALNSfpgtvcyvshdryFINKTATRILDLTENRLLNYI 523
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINK-------------LMTSENSIILITHYQRLLDYI 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
32-216 |
3.93e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 48.96 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 32 AIVGVNGAGKTTLLKILTGEEQADGGSVTLAkDAKLGYLRQINNVDSTLSIIDELYTVIEPILdMEKRILK---MQNEMR 108
Cdd:PRK13643 36 ALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG-DIVVSSTSKQKEIKPVRKKVGVVFQFPESQL-FEETVLKdvaFGPQNF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 109 HLTGEKLEKLYssytalthnyelmdgyAAKSKVVGILKGLgFEEADFDrkintLSGGQKTRVFLAKLLLEEPDIILLDEP 188
Cdd:PRK13643 114 GIPKEKAEKIA----------------AEKLEMVGLADEF-WEKSPFE-----LSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190
....*....|....*....|....*....|.
gi 496028547 189 TNHLDLRS-IEWLESY--LLNYNGAVVIVSH 216
Cdd:PRK13643 172 TAGLDPKArIEMMQLFesIHQSGQTVVLVTH 202
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-194 |
4.06e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 48.63 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSN---------EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVtLAKDAKLGYLR 71
Cdd:PRK15112 3 TLLEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL-LIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 72 QINNVDSTLSIIDELYTVIEPildmekrilkmqnemRHLTGEKLEklyssyTALTHNYELmDGYAAKSKVVGILKGLGFE 151
Cdd:PRK15112 82 YSYRSQRIRMIFQDPSTSLNP---------------RQRISQILD------FPLRLNTDL-EPEQREKQIIETLRQVGLL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496028547 152 EADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDL 194
Cdd:PRK15112 140 PDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
332-487 |
4.28e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.68 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 332 NLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDT-----GEV-IYGSNVsvayYDQEHQVLHMD 405
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVrLFGRNI----YSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 406 KT--LFDEISDTYPEMT---NTRIRNILAAFLFTGEDVYKKI---------------------SDLSGGERGRVSLVKLM 459
Cdd:PRK14267 85 REvgMVFQYPNPFPHLTiydNVAIGVKLNGLVKSKKELDERVewalkkaalwdevkdrlndypSNLSGGQRQRLVIARAL 164
|
170 180
....*....|....*....|....*...
gi 496028547 460 LSKANFLLLDEPTNHLDIVSKDVLENAL 487
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELL 192
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
157-217 |
4.64e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.39 E-value: 4.64e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496028547 157 RKINTLSGGQKTRVFLAKLLLE-EPDI------ILLDEPTNHLDLRSIEWLESyLLN----YNGAVVIVSHD 217
Cdd:PRK03695 122 RSVNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLDVAQQAALDR-LLSelcqQGIAVVMSSHD 192
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
357-499 |
4.70e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.10 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 357 AIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNV---------------SVAYYDQEHQ--------------VLHMDKT 407
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrRIGYVFQDARlfphykvrgnlrygMAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 408 LFDEIS---------DTYPemtntrirnilaaflftgedvykkiSDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIV 478
Cdd:PRK11144 108 QFDKIVallgiepllDRYP-------------------------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180
....*....|....*....|....*
gi 496028547 479 SKDVLENALNSFPGTV----CYVSH 499
Cdd:PRK11144 163 RKRELLPYLERLAREInipiLYVSH 187
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
328-514 |
4.96e-06 |
|
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: 47.32 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSksfdrkklfyDINFEIKRGERVAIIGDNGTGKTTLLkiiNGILEpDTGEVIYGSNVSVAYYDqehqvlhmdKT 407
Cdd:cd03238 6 ANVHNLQ----------NLDVSIPLNVLVVVTGVSGSGKSTLV---NEGLY-ASGKARLISFLPKFSRN---------KL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 408 LF-DEISdtypemtntRIRNILAAFLFTGedvyKKISDLSGGERGRVSLVKLMLS--KANFLLLDEPTNHLDIVSKDVLE 484
Cdd:cd03238 63 IFiDQLQ---------FLIDVGLGYLTLG----QKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQLL 129
|
170 180 190
....*....|....*....|....*....|...
gi 496028547 485 NALNSF---PGTVCYVSHDRYFInKTATRILDL 514
Cdd:cd03238 130 EVIKGLidlGNTVILIEHNLDVL-SSADWIIDF 161
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-236 |
4.97e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 49.26 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 18 IKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqINNVDstlsiidelytvIEPILDME 97
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL------------IDGVD------------IAKISDAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 98 krilkmqneMRHLTGEKLEKLYSSYTALTHnYELMDGYAAKSKVVGILKGLGFEEA-DFDRKI----------NTLSGGQ 166
Cdd:PRK10070 100 ---------LREVRRKKIAMVFQSFALMPH-MTVLDNTAFGMELAGINAEERREKAlDALRQVglenyahsypDELSGGM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496028547 167 KTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLL----NYNGAVVIVSHDRYFLDKIVSKVIDIENGNV 236
Cdd:PRK10070 170 RQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVklqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
327-520 |
5.33e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-GSNVSVAYYDQEHQ----V 401
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlGKEVTFNGPKSSQEagigI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 402 LHMDKTLFDEISDTYP-----EMTNT--RIR--------NILAAFLFTGEDVYKKISDLSGGERGRVSLVKLMLSKANFL 466
Cdd:PRK10762 84 IHQELNLIPQLTIAENiflgrEFVNRfgRIDwkkmyaeaDKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 467 LLDEPTNHLDIVSKDVLENALNSFPGTVC---YVSH----------------DRYFINKTAtrILDLTENRLL 520
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKSQGRgivYISHrlkeifeicddvtvfrDGQFIAERE--VADLTEDSLI 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
325-512 |
5.70e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.47 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 325 KDVLSVHNLSKSFDRKKLFYD----INFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEViygSNVSVAYYDQEHQ 400
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQQKIAavrnLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLV---QCDKMLLRRRSRQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 401 VLHMdktlfDEISDTypEMTNTRIRNILAAF---------LFT-GEDVYKKIS--------------------------- 443
Cdd:PRK10261 87 VIEL-----SEQSAA--QMRHVRGADMAMIFqepmtslnpVFTvGEQIAESIRlhqgasreeamveakrmldqvripeaq 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 444 --------DLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSK-------DVLENALNSfpgTVCYVSHDRYFINKTA 508
Cdd:PRK10261 160 tilsryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSM---GVIFITHDMGVVAEIA 236
|
....
gi 496028547 509 TRIL 512
Cdd:PRK10261 237 DRVL 240
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
16-259 |
5.87e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 48.31 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 16 EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVtLAKDAKLGYLRqinnvdstlsiidelytviepild 95
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSR------------------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 96 meKRILKMQNEMRHLTGEKLEKLYS-------SYTALthNYELMDGYAAKsKVVGILKGLGFEEADfDRKINTLSGGQKT 168
Cdd:PRK13636 75 --KGLMKLRESVGMVFQDPDNQLFSasvyqdvSFGAV--NLKLPEDEVRK-RVDNALKRTGIEHLK-DKPTHCLSFGQKK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 169 RVFLAKLLLEEPDIILLDEPTNHLDLRSI----EWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNVqMYLGNYT 244
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDPMGVseimKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV-ILQGNPK 227
|
250
....*....|....*
gi 496028547 245 DFSNKKQMLLDAKMK 259
Cdd:PRK13636 228 EVFAEKEMLRKVNLR 242
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
332-386 |
6.54e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 6.54e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 332 NLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY 386
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF 57
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-242 |
6.66e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.55 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 18 IKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVT-LAKDAKLGYLRQINNVDSTLSIIDElytviEPILDM 96
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLGMKDDEWRAVRSDIQMIFQ-----DPLASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 97 EKRIlkmqnEMRHLTGEKLEKLYSSYTALthnyELMDGYAAKSKVVGILKGLgfeeadFDRKINTLSGGQKTRVFLAKLL 176
Cdd:PRK15079 112 NPRM-----TIGEIIAEPLRTYHPKLSRQ----EVKDRVKAMMLKVGLLPNL------INRYPHEFSGGQCQRIGIARAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 177 LEEPDIILLDEPTNHLDLrSIE-----WLESYLLNYNGAVVIVSHDRYFLDKIVSKVIdiengnvQMYLGN 242
Cdd:PRK15079 177 ILEPKLIICDEPVSALDV-SIQaqvvnLLQQLQREMGLSLIFIAHDLAVVKHISDRVL-------VMYLGH 239
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-480 |
6.71e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 6 TNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgYLRQINNVDSTLSIIDE 85
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIL--------FQGKEIDFKSSKEALEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 86 LYTVIEPILDMEKRILKMQNemrhltgekleklyssytALTHNYELMDGYAAKSKVVGILKGLgFEEADFD----RKINT 161
Cdd:PRK10982 74 GISMVHQELNLVLQRSVMDN------------------MWLGRYPTKGMFVDQDKMYRDTKAI-FDELDIDidprAKVAT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 162 LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSiewlesyllnyngavviVSHdryfLDKIVSKVIDIENGNVqmYLG 241
Cdd:PRK10982 135 LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE-----------------VNH----LFTIIRKLKERGCGIV--YIS 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 242 NytdfsnkkqmlldaKMKEYLNQQQEI---RHQEAVIT-KLKQFNREKSIKRAESRQKQLEKIERVDAPqtytenmrlsl 317
Cdd:PRK10982 192 H--------------KMEEIFQLCDEItilRDGQWIATqPLAGLTMDKIIAMMVGRSLTQRFPDKENKP----------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 318 diakesGKDVLSVHNLSKSfdRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVI-YGSNVSvayyd 396
Cdd:PRK10982 247 ------GEVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITlHGKKIN----- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 397 qehqvlhmDKTLFDEISDTYPEMTNTRIRNILAAFL-------FTGEDVYK----------------------------- 440
Cdd:PRK10982 314 --------NHNANEAINHGFALVTEERRSTGIYAYLdigfnslISNIRNYKnkvglldnsrmksdtqwvidsmrvktpgh 385
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 496028547 441 --KISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSK 480
Cdd:PRK10982 386 rtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAK 427
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
345-481 |
7.27e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVS---------VAYYDQ------E---HQ--VLH 403
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwLFGQPVDagdiatrrrVGYMSQafslygEltvRQnlELH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 404 MDktLFDEISDTYPEmtntRIRNILAAF-LftgEDVYKKISD-LSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKD 481
Cdd:NF033858 364 AR--LFHLPAAEIAA----RVAEMLERFdL---ADVADALPDsLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARD 434
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
341-499 |
8.94e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.98 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 341 KLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGiLEPDTGEVIYGSNVSVAYYDQehQVLHMD-KTLFDEI--SDTYP 417
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGE-LWPVYGGRLTKPAKGKLFYVP--QRPYMTlGTLRDQIiyPDSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 418 EMTNTRIR---------NILAAFLFTGEDVYKKISD----LSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLE 484
Cdd:TIGR00954 543 DMKRRGLSdkdleqildNVQLTHILEREGGWSAVQDwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMY 622
|
170
....*....|....*
gi 496028547 485 NALNSFPGTVCYVSH 499
Cdd:TIGR00954 623 RLCREFGITLFSVSH 637
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-408 |
9.06e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 130 ELMDGYAAKskvVGILKGLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDII--LLDEPTNHLDLRSIEWLESY---L 204
Cdd:PRK00635 448 EVLQGLKSR---LSILIDLGLPYLTPERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVikkL 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 205 LNYNGAVVIVSHDryflDKIVS---KVIDIENGnVQMYLGnytdfsnkkQMLLDAKMKEYLNQQQEIRHQeavitKLKQf 281
Cdd:PRK00635 525 RDQGNTVLLVEHD----EQMISladRIIDIGPG-AGIFGG---------EVLFNGSPREFLAKSDSLTAK-----YLRQ- 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 282 nrEKSIKRAESRQKQLEkiervdapqtytenmRLSLDIAkesgkdvlSVHNLSksfdrkklfyDINFEIKRGERVAIIGD 361
Cdd:PRK00635 585 --ELTIPIPEKRTNSLG---------------TLTLSKA--------TKHNLK----------DLTISLPLGRLTVVTGV 629
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 496028547 362 NGTGKTTLlkiINGILEPDTGEVIYGSNVSVAYYDQE--HQVLHMDKTL 408
Cdd:PRK00635 630 SGSGKSSL---INDTLVPAVEEFIEQGFCSNLSIQWGaiSRLVHITRDL 675
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
330-480 |
9.84e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 49.24 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 330 VHNLSKSFDR--KKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSVAYYDQEHQVLHM--- 404
Cdd:TIGR01257 931 VKNLVKIFEPsgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMcpq 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 405 DKTLFDEISDT-----YPEMTNTRIRNILAAFLFTGEDV------YKKISDLSGGERGRVSLVKLMLSKANFLLLDEPTN 473
Cdd:TIGR01257 1011 HNILFHHLTVAehilfYAQLKGRSWEEAQLEMEAMLEDTglhhkrNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
....*..
gi 496028547 474 HLDIVSK 480
Cdd:TIGR01257 1091 GVDPYSR 1097
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
145-193 |
1.02e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.82 E-value: 1.02e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 496028547 145 LKGLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:PRK13649 129 LALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
2-223 |
1.16e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.48 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSV-----TLAKDaKLGYLRQINNV 76
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlferqSIKKD-LCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 77 DSTlsiidelyTVIEPILDMEKRILKmqnemrhltgekleKLYSSYTALthnyelmdgyaAKSKVVGILKglgfEEADFD 156
Cdd:PRK13540 80 GHR--------SGINPYLTLRENCLY--------------DIHFSPGAV-----------GITELCRLFS----LEHLID 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 157 RKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLNY---NGAVVIVSHDRYFLDK 223
Cdd:PRK13540 123 YPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHrakGGAVLLTSHQDLPLNK 192
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
323-386 |
1.24e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 47.29 E-value: 1.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496028547 323 SGKDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY 386
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILL 64
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-241 |
1.43e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 29 EKAAIVGVNGAGKTT----LLKIL---TGEEQADGGSVTLAKDAKLGYLRQinnvdSTLSIIDELYTVIEPildmekril 101
Cdd:PRK10261 351 ETLSLVGESGSGKSTtgraLLRLVesqGGEIIFNGQRIDTLSPGKLQALRR-----DIQFIFQDPYASLDP--------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 102 kmqnemRHLTGekleklYSSYTAL-THNyeLMDGYAAKSKVVGILKGLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEP 180
Cdd:PRK10261 417 ------RQTVG------DSIMEPLrVHG--LLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNP 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 181 DIILLDEPTNHLDLRSIEWLESYLLN----YNGAVVIVSHDRYFLDKIVSKVidiengnVQMYLG 241
Cdd:PRK10261 483 KVIIADEAVSALDVSIRGQIINLLLDlqrdFGIAYLFISHDMAVVERISHRV-------AVMYLG 540
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-216 |
1.68e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 16 EIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTL-----AKDAKLGYLRQINNVDS------TLSIID 84
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndshnLKDINLKWWRSKIGVVSqdpllfSNSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 85 ELYTVIEPILDME-------------KRILKMQNEMRHLTGEKLEKLYSSYTA-----LTHNYELMDgyaaKSKVVGILK 146
Cdd:PTZ00265 479 NIKYSLYSLKDLEalsnyynedgndsQENKNKRNSCRAKCAGDLNDMSNTTDSnelieMRKNYQTIK----DSEVVDVSK 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 147 GL---GFEEADFDR-------KINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSiEWLESYLL-----NYNGAV 211
Cdd:PTZ00265 555 KVlihDFVSALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-EYLVQKTInnlkgNENRIT 633
|
....*
gi 496028547 212 VIVSH 216
Cdd:PTZ00265 634 IIIAH 638
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
32-196 |
1.82e-05 |
|
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: 45.70 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 32 AIVGVNGAGKTTLLKILTGEEQAD--GGSVTLA-KDAKLGYLRQINNVDStLSIIDELYTVIEPIldmekrilkmqnemr 108
Cdd:cd03232 37 ALMGESGAGKTTLLDVLAGRKTAGviTGEILINgRPLDKNFQRSTGYVEQ-QDVHSPNLTVREAL--------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 109 hltgeklekLYSSYtalthnyelmdgyaakskvvgiLKGLGFEeadfdrkintlsggQKTRVFLAKLLLEEPDIILLDEP 188
Cdd:cd03232 101 ---------RFSAL----------------------LRGLSVE--------------QRKRLTIGVELAAKPSILFLDEP 135
|
....*...
gi 496028547 189 TNHLDLRS 196
Cdd:cd03232 136 TSGLDSQA 143
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-217 |
1.86e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.01 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 3 LNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGsVTLAKDAKLGYLRQINNVDstlsi 82
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGGRSIFNYRD----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 idelytviepILDMEKRILKMQNEMRHLTGEKLEKLYSSYTAlthnYELMDGYAAKSKVVGILKGLGFEEADFDRKINT- 161
Cdd:PRK14271 96 ----------VLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRA----HKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSp 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 162 --LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNGAVVIVSHD 217
Cdd:PRK14271 162 frLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIrsLADRLTVIIVTHN 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
162-216 |
1.88e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 46.57 E-value: 1.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 162 LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS---IEWL-----ESYllnyngAVVIVSH 216
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStakIEELilelkKDY------TIVIVTH 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
161-206 |
2.36e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 2.36e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 496028547 161 TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLN 206
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1403
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
328-481 |
2.58e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 46.53 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLsksfdrkKLFYDINFEIKRGERV-AIIGDNGTGKTTLLKIINGILEPDTGEV--IYGSNVSV------------ 392
Cdd:COG3950 6 LTIENF-------RGFEDLEIDFDNPPRLtVLVGENGSGKTTLLEAIALALSGLLSRLddVKFRKLLIrngefgdsakli 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 393 AYYDQEHQVLHMDKTLFDEISDTYPEMTN---------TRIRNILAAFLFTGEDVYKKISDLSGGERGRV-SLVKLMLSK 462
Cdd:COG3950 79 LYYGTSRLLLDGPLKKLERLKEEYFSRLDgydslldedSNLREFLEWLREYLEDLENKLSDELDEKLEAVrEALNKLLPD 158
|
170
....*....|....*....
gi 496028547 463 ANFLLLDEPTNHLDIVSKD 481
Cdd:COG3950 159 FKDIRIDRDPGRLVILDKN 177
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-195 |
2.58e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.76 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSF-GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGsvtlakdaklgylrqinnvdsTLSIIDE 85
Cdd:PRK11650 8 AVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSG---------------------EIWIGGR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 86 LYTVIEPildmEKRILKM--QNemrhltgekleklYSSYTALThNYELMdGYAAK-------------SKVVGILKGLGF 150
Cdd:PRK11650 67 VVNELEP----ADRDIAMvfQN-------------YALYPHMS-VRENM-AYGLKirgmpkaeieervAEAARILELEPL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496028547 151 eeadFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD--LR 195
Cdd:PRK11650 128 ----LDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDakLR 170
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
327-477 |
2.79e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.36 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPD--------TGEVIYGSNvSVAYYDQE 398
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGE-PLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 399 H-----QVL-HMDKTLF----DEIS--DTYPEM-----TNTRIRNIL-AAFLFTGED--VYKKISDLSGGERGRVSLVKL 458
Cdd:PRK13547 80 RlarlrAVLpQAAQPAFafsaREIVllGRYPHArragaLTHRDGEIAwQALALAGATalVGRDVTTLSGGELARVQFARV 159
|
170 180
....*....|....*....|....*...
gi 496028547 459 M---------LSKANFLLLDEPTNHLDI 477
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-480 |
4.23e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.46 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKIL---------TGEEQADGGSVTlAKDAKLGYLRQ 72
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvyphgtyEGEIIFEGEELQ-ASNIRDTERAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 73 INNVDSTLSIIDELyTVIEPILdmekrilkMQNEMRHltgekleklyssytalthnYELMDGYAAKSKVVGILKGLGFeE 152
Cdd:PRK13549 84 IAIIHQELALVKEL-SVLENIF--------LGNEITP-------------------GGIMDYDAMYLRAQKLLAQLKL-D 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 153 ADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESY---LLNYNGAVVIVSHDryfLDKI--VSK 227
Cdd:PRK13549 135 INPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIirdLKAHGIACIYISHK---LNEVkaISD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 228 VIDIengnvqmylgnytdfsnkkqmlldakmkeylnqqqeIRHQEAVIT-KLKQFNREKSIKRAESRqkqlekiervdap 306
Cdd:PRK13549 212 TICV------------------------------------IRDGRHIGTrPAAGMTEDDIITMMVGR------------- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 307 qtytENMRLSLDIAKESGKDVLSVHNLSkSFD----RKKLFYDINFEIKRGERVAIIGDNGTGKTTLLK----------- 371
Cdd:PRK13549 243 ----ELTALYPREPHTIGEVILEVRNLT-AWDpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQclfgaypgrwe 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 372 ------------------IINGI-----------LEPDTGeviYGSNVSVAYYDQEHQVLHMDKTLfdEISDTYPEMTNT 422
Cdd:PRK13549 318 geifidgkpvkirnpqqaIAQGIamvpedrkrdgIVPVMG---VGKNITLAALDRFTGGSRIDDAA--ELKTILESIQRL 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 423 RIRnILAAFLftgedvykKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSK 480
Cdd:PRK13549 393 KVK-TASPEL--------AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAK 441
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
162-285 |
4.38e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 45.56 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 162 LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD---LRSIEWLESYLLNYNGAVVI-VSHDryfLDKIV--SKVIDIENGN 235
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDpagKEQILKLIRKLKKKNNLTVIsITHD---IDEANmaDQVLVLDDGK 220
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 236 VqMYLGNYTDFSNKKQMLLDA--------KMKEYLNQQ-----QEIRHQEAVITKLKQFNREK 285
Cdd:PRK13640 221 L-LAQGSPVEIFSKVEMLKEIgldipfvyKLKNKLKEKgisvpQEINTEEKLVQYLCQLNSKM 282
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
334-476 |
4.51e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.41 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 334 SKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPD--TGEVIYGsnvsvayyDQEHQVLHMDKTLFDE 411
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILAN--------NRKPTKQILKRTGFVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 412 ISDT-YPEMTN----------------TRIRNILAAFLFTGEDVYKK----------ISDLSGGERGRVSLVKLMLSKAN 464
Cdd:PLN03211 147 QDDIlYPHLTVretlvfcsllrlpkslTKQEKILVAESVISELGLTKcentiignsfIRGISGGERKRVSIAHEMLINPS 226
|
170
....*....|..
gi 496028547 465 FLLLDEPTNHLD 476
Cdd:PLN03211 227 LLILDEPTSGLD 238
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-241 |
4.55e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 45.88 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 22 TFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAkdaklGylrqinnvdstlsiidelytviEPILDMEKRIL 101
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD-----G----------------------QDITGLSGREL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 102 K-----MQneM---------------RHLTGEKLEklyssytalthNYELMDGYAAKSKVVGILKGLGFEEADFDRKINT 161
Cdd:COG4608 91 RplrrrMQ--MvfqdpyaslnprmtvGDIIAEPLR-----------IHGLASKAERRERVAELLELVGLRPEHADRYPHE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 162 LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLrSIewlESYLLN--------YNGAVVIVSHD----RYFLDKIVskVi 229
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDV-SI---QAQVLNlledlqdeLGLTYLFISHDlsvvRHISDRVA--V- 230
|
250
....*....|..
gi 496028547 230 diengnvqMYLG 241
Cdd:COG4608 231 --------MYLG 234
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
33-220 |
5.21e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 46.33 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 33 IVGVNGAGKTTLLKILTGEEQADGGSVTL----AKDAKLGYLRQInnvdstLSII-------DELYTVIEPILDmekril 101
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLdgqpVTADNREAYRQL------FSAVfsdfhlfDRLLGLDGEADP------ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 102 kmqNEMRHLtgekLEKLyssytALTHnyelmdgyaaksKVvgilkglGFEeadfDRKINT--LSGGQKTRVFLAKLLLEE 179
Cdd:COG4615 431 ---ARAREL----LERL-----ELDH------------KV-------SVE----DGRFSTtdLSQGQRKRLALLVALLED 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 180 PDIILLDE------PT------NHL--DLRSiewlesyllnyNG-AVVIVSHD-RYF 220
Cdd:COG4615 476 RPILVFDEwaadqdPEfrrvfyTELlpELKA-----------RGkTVIAISHDdRYF 521
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
338-476 |
5.33e-05 |
|
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: 44.54 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 338 DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLL------KIINGIlepdTGEV-IYGS------NVSVAYYdqEHQVLHM 404
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLdvlagrKTAGVI----TGEIlINGRpldknfQRSTGYV--EQQDVHS 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496028547 405 dktlfdeisdtyPEMTntrirnILAAFLFTGedvykKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLD 476
Cdd:cd03232 92 ------------PNLT------VREALRFSA-----LLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
345-476 |
5.67e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 45.13 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIY-----------------------------GSNVS--VA 393
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYnnqaitddnfeklrkhigivfqnpdnqfvGSIVKydVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 394 YYDQEHQVLH--MDKTLFDEISDTypEMTNTRIRNILAaflftgedvykkisdLSGGERGRVSLVKLMLSKANFLLLDEP 471
Cdd:PRK13648 107 FGLENHAVPYdeMHRRVSEALKQV--DMLERADYEPNA---------------LSGGQKQRVAIAGVLALNPSVIILDEA 169
|
....*
gi 496028547 472 TNHLD 476
Cdd:PRK13648 170 TSMLD 174
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-215 |
5.79e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.41 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 6 TNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVT-LAKDAKLGylRQINNVDSTLSIID 84
Cdd:PLN03211 72 SDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTiLANNRKPT--KQILKRTGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 85 ELY---TVIEPILDMEkrILKMQNEMrhltgEKLEKLYSSYTALThnyELmdgyaAKSKVVGILKGLGFeeadfdrkINT 161
Cdd:PLN03211 150 ILYphlTVRETLVFCS--LLRLPKSL-----TKQEKILVAESVIS---EL-----GLTKCENTIIGNSF--------IRG 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496028547 162 LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNGAVVIVS 215
Cdd:PLN03211 207 ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLgsLAQKGKTIVTS 262
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
156-217 |
6.97e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.67 E-value: 6.97e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 156 DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDL--RSiewlESYLLNYN----G-AVVIVSHD 217
Cdd:PRK11288 391 EQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVgaKH----EIYNVIYElaaqGvAVLFVSSD 455
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
327-376 |
7.71e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 7.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGI 376
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV 50
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
162-238 |
8.14e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 45.08 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 162 LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD-------LRSIEWLESyllNYNGAVVIVSHdryFLDKIVS--KVIDIE 232
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrrevVNTIKELNK---KYGITIILITH---YMEEAVEadRIIVMD 218
|
....*.
gi 496028547 233 NGNVQM 238
Cdd:PRK13633 219 SGKVVM 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
161-217 |
1.01e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.39 E-value: 1.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 161 TLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD----LRSIEWLESYLLNYngAVVIVSHD 217
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDpistLRIEELMHELKEQY--TIIIVTHN 209
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
325-484 |
1.05e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 44.52 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 325 KDVLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSnvsvAYYDQEhQVLHM 404
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGE----VYLDGQ-DIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 405 DKTLFD-------EISDTYPEMT---------------------NTRIRNIL-AAFLFtgEDVYKKI----SDLSGGERG 451
Cdd:PRK14247 76 DVIELRrrvqmvfQIPNPIPNLSifenvalglklnrlvkskkelQERVRWALeKAQLW--DEVKDRLdapaGKLSGGQQQ 153
|
170 180 190
....*....|....*....|....*....|...
gi 496028547 452 RVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLE 484
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIE 186
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
162-217 |
1.08e-04 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 43.57 E-value: 1.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496028547 162 LSGG--QKtrVFLAKLLLEEPDIILLDEPTNHLDLRSIEwlESY-----LLNYNGAVVIVSHD 217
Cdd:cd03215 105 LSGGnqQK--VVLARWLARDPRVLILDEPTRGVDVGAKA--EIYrlireLADAGKAVLLISSE 163
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
357-506 |
1.10e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.75 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 357 AIIGDNGTGKTTLLKIINGILepdTGEVIYGSNVSVAYYD--QEHQVLHMDKTLFDEISDTypEMTNTRIRNILAAFLFT 434
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYAL---TGELPPNSKGGAHDPKliREGEVRAQVKLAFENANGK--KYTITRSLAILENVIFC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 435 -GEDVYKKISD----LSGGERG------RVSLVKLMLSKANFLLLDEPTNHLD-----IVSKDVLENALNSFPGTVCYVS 498
Cdd:cd03240 101 hQGESNWPLLDmrgrCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeenieESLAEIIEERKSQKNFQLIVIT 180
|
....*...
gi 496028547 499 HDRYFINK 506
Cdd:cd03240 181 HDEELVDA 188
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
1-222 |
1.23e-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: 44.30 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLAKDAKLGYLRQINNVDSTL 80
Cdd:pfam13304 76 LDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 81 SIIDELYTVIEPILDMEKRiLKMQNEMRHLTgEKLEKLYSSYTALTHNYELMDGYAAKSKVVGILKGLGFEEADFDRKIN 160
Cdd:pfam13304 156 LLDEGLLLEDWAVLDLAAD-LALFPDLKELL-QRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELP 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 161 --TLSGGQKTRVFLAKLLLE---EPDIILLDEPTNHLD---LRSI-EWLEsYLLNYNGAVVIVSHDRYFLD 222
Cdd:pfam13304 234 afELSDGTKRLLALLAALLSalpKGGLLLIDEPESGLHpklLRRLlELLK-ELSRNGAQLILTTHSPLLLD 303
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-196 |
1.31e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 44.84 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 22 TFLINEHEKAAIVGVNGAGKTTLLKILtgeeqadggsvtlakdakLGYLR-----QINNVDstLSIIDELY--------- 87
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNAL------------------LGFLPyqgslKINGIE--LRELDPESwrkhlswvg 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 88 --------TVIEPILdmekrilkMQNEmrHLTGEKLEKLyssytalthnyeLMDGYAAKSkVVGILKGLGFEEADfdRKI 159
Cdd:PRK11174 430 qnpqlphgTLRDNVL--------LGNP--DASDEQLQQA------------LENAWVSEF-LPLLPQGLDTPIGD--QAA 484
|
170 180 190
....*....|....*....|....*....|....*..
gi 496028547 160 nTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS 196
Cdd:PRK11174 485 -GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
328-522 |
1.45e-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: 44.07 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSF--DRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSN---VSVAYYDQEHQVL 402
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSwnsVPLQKWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 403 HMDKTLFD----EISDTYPEMTNTRI---------RNILAAF-------LFTGEDVykkisdLSGGERGRVSLVKLMLSK 462
Cdd:cd03289 83 PQKVFIFSgtfrKNLDPYGKWSDEEIwkvaeevglKSVIEQFpgqldfvLVDGGCV------LSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 463 ANFLLLDEPTNHLDIVSKDVLENAL-NSFPGTVCYVSHDRYFINKTATRILDLTENRLLNY 522
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLkQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQY 217
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
148-240 |
1.97e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 148 LGFEEADFDRKINTLSGGQKTRVFLAKLLL---EEPDIILLDEPTNHLDLRSIEWLESYL--LNYNG-AVVIVSHDRYFL 221
Cdd:PRK00635 796 LGLDYLPLGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLqsLTHQGhTVVIIEHNMHVV 875
|
90 100
....*....|....*....|.
gi 496028547 222 dKIVSKVIDI--ENGNVQMYL 240
Cdd:PRK00635 876 -KVADYVLELgpEGGNLGGYL 895
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
328-477 |
2.81e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.93 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDR----KKLFYDINFEIKRGERVAIIGDNGTGKT-TLLKIINGILEPD----TGEVIY------------ 386
Cdd:PRK15134 6 LAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFhgesllhaseqt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 387 -----GSNVSVAYydQEHQV----LH-MDKTLFdEISDTYPEMTNTRIR-NILAAFLFTG-EDVYKKISD----LSGGER 450
Cdd:PRK15134 86 lrgvrGNKIAMIF--QEPMVslnpLHtLEKQLY-EVLSLHRGMRREAARgEILNCLDRVGiRQAAKRLTDyphqLSGGER 162
|
170 180
....*....|....*....|....*..
gi 496028547 451 GRVSLVKLMLSKANFLLLDEPTNHLDI 477
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDV 189
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-236 |
3.20e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 18 IKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLakdaklgYLRQINNVDSTLSIIDELYTVIEPildme 97
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITL-------HGKKINNHNANEAINHGFALVTEE----- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 98 krilkmqnemRHLTG--EKLEKLYSSYTALTHNYE----LMDGYAAKSKVVGILKGLGFEEADFDRKINTLSGGQKTRVF 171
Cdd:PRK10982 332 ----------RRSTGiyAYLDIGFNSLISNIRNYKnkvgLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVI 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 172 LAKLLLEEPDIILLDEPTNHLDLRS---IEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNV 236
Cdd:PRK10982 402 IGRWLLTQPEILMLDEPTRGIDVGAkfeIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-193 |
5.14e-04 |
|
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: 41.86 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 1 MILNATNISKSFGSNE----IIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADG---GSVTL----AKDAKLGY 69
Cdd:cd03233 2 STLSWRNISFTTGKGRskipILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYngipYKEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 70 LRQInnvdstlsiideLYTVIEpildmekrilkmQNEMRHLTGEkleklyssytalthnyELMDgYAAKskvvgiLKGlg 149
Cdd:cd03233 82 PGEI------------IYVSEE------------DVHFPTLTVR----------------ETLD-FALR------CKG-- 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496028547 150 feeADFDRKIntlSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:cd03233 113 ---NEFVRGI---SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
298-487 |
5.29e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.17 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 298 EKI-ERVDAP-QTYTENMRlsldiAKESGKdvLSVHNLSKSFDRKKL-FYDINFEIKRGERVAIIGDNGTGKTTLLKIIN 374
Cdd:PRK10790 316 ERVfELMDGPrQQYGNDDR-----PLQSGR--IDIDNVSFAYRDDNLvLQNINLSVPSRGFVALVGHTGSGKSTLASLLM 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 375 GILEPDTGEvIYGSNVSVAYYdqEHQVLH------------MDKTLFD------EISD-----------------TYPEM 419
Cdd:PRK10790 389 GYYPLTEGE-IRLDGRPLSSL--SHSVLRqgvamvqqdpvvLADTFLAnvtlgrDISEeqvwqaletvqlaelarSLPDG 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496028547 420 TNTRIrnilaaflftGEdvykKISDLSGGERGRVSLVKLMLSKANFLLLDEPTNHLDIVSKDVLENAL 487
Cdd:PRK10790 466 LYTPL----------GE----QGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL 519
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-194 |
6.17e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 42.15 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 15 NEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlaKDAKLGYLRQInnvdstlsiidelyTVIEPIL 94
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--HSGRISFSSQF--------------SWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 95 DMEKRILKMQ-NEMRHLTGEKLEKLYSSYTAlthnyelmdgYAAKSKVVGILKGLgfeeadfdrkinTLSGGQKTRVFLA 173
Cdd:cd03291 114 IKENIIFGVSyDEYRYKSVVKACQLEEDITK----------FPEKDNTVLGEGGI------------TLSGGQRARISLA 171
|
170 180
....*....|....*....|.
gi 496028547 174 KLLLEEPDIILLDEPTNHLDL 194
Cdd:cd03291 172 RAVYKDADLYLLDSPFGYLDV 192
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-242 |
6.58e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 42.50 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIK---SATFLINEHEKAAIVGVNGAGKTTLLKILTGE-EQADGGSVTLAKdaklgylRQINNVD 77
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFING-------KPVDIRN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 78 STLSIIDELYTVIEpilDMEKR-ILKMQNEMRHLTGEKLEklysSYTALTHnyelMDGYAAKSKVVGILKGLGFEEADFD 156
Cdd:TIGR02633 330 PAQAIRAGIAMVPE---DRKRHgIVPILGVGKNITLSVLK----SFCFKMR----IDAAAELQIIGSAIQRLKVKTASPF 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 157 RKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS---IEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIEN 233
Cdd:TIGR02633 399 LPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGE 478
|
....*....
gi 496028547 234 GNVQMYLGN 242
Cdd:TIGR02633 479 GKLKGDFVN 487
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-193 |
7.99e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 11 SFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEE-QADGGSVTLakdakLGYLRQINnvdstlsiidelytv 89
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpQGYSNDLTL-----FGRRRGSG--------------- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 90 iEPILDMEKRILKMQNEMrHLTgekleklYS-SYTALThnyELMDGY------------AAKSKVVGILKGLGFEEADFD 156
Cdd:PRK10938 329 -ETIWDIKKHIGYVSSSL-HLD-------YRvSTSVRN---VILSGFfdsigiyqavsdRQQKLAQQWLDILGIDKRTAD 396
|
170 180 190
....*....|....*....|....*....|....*..
gi 496028547 157 RKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:PRK10938 397 APFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
321-392 |
8.20e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 8.20e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496028547 321 KESGKDVLSVHNLSKSFdrkKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEVIYGSNVSV 392
Cdd:PRK13546 21 KERMKDALIPKHKNKTF---FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSV 89
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
345-393 |
8.40e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.57 E-value: 8.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 496028547 345 DINFEIKRGERVAIIGDNGTGKTTLLKIINGILEPDTGEV-IYGSNVSVA 393
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVdIKGSAALIA 91
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-50 |
9.43e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 9.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTG 50
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
163-241 |
9.46e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 41.63 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 163 SGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLrSIEWLESYLLN-----YNGAVVIVSHDRYFLDKIVSKVIdiengnvQ 237
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAQIMTLLNelkreFNTAIIMITHDLGVVAGICDKVL-------V 234
|
....
gi 496028547 238 MYLG 241
Cdd:PRK09473 235 MYAG 238
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
327-386 |
1.34e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.93 E-value: 1.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496028547 327 VLSVHNLSKSFDRKKLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGI--LEPDTGEVIY 386
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEF 62
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
157-194 |
1.80e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 40.54 E-value: 1.80e-03
10 20 30
....*....|....*....|....*....|....*...
gi 496028547 157 RKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDL 194
Cdd:PRK10575 143 RLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
148-235 |
1.89e-03 |
|
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: 39.28 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 148 LGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD---------LRSIEWLESYLLNYNGAVVIVSHDR 218
Cdd:smart00382 47 DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLTVILTTNDE 126
|
90 100
....*....|....*....|..
gi 496028547 219 YFLDK-----IVSKVIDIENGN 235
Cdd:smart00382 127 KDLGPallrrRFDRRIVLLLIL 148
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
162-196 |
2.12e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 40.96 E-value: 2.12e-03
10 20 30
....*....|....*....|....*....|....*
gi 496028547 162 LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS 196
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-193 |
2.45e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 41.10 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSF-GSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKIL-------TGEEQADG---GSVTLAkdaklGYLRQINN 75
Cdd:PRK13657 339 DVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILIDGtdiRTVTRA-----SLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 76 V--DSTL---SIIDELytviepildmekRILK---MQNEMRhltgEKLEKlyssytALTHNYEL--MDGYAAkskVVGil 145
Cdd:PRK13657 414 VfqDAGLfnrSIEDNI------------RVGRpdaTDEEMR----AAAER------AQAHDFIErkPDGYDT---VVG-- 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496028547 146 kglgfeeadfDRKiNTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:PRK13657 467 ----------ERG-RQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
162-232 |
2.60e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.48 E-value: 2.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 162 LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLR----SIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIE 232
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
156-221 |
2.74e-03 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 39.62 E-value: 2.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 156 DRKINtLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLES-----YLLNYNGAVVIVSHDRYFL 221
Cdd:cd03290 136 ERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegilkFLQDDKRTLVLVTHKLQYL 205
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
162-301 |
2.79e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 40.22 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 162 LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLLN-YNGAVVIVSHDRYFLDKIVSKVIDIENGNVQMYl 240
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQaFADCTVILSEHRIEAMLECQRFLVIEENKVRQY- 217
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496028547 241 gnytdfsNKKQMLLDAKMkeylNQQQEIRHQEavitKLKQFNREKSIKRAESRQKQLEKIE 301
Cdd:cd03289 218 -------DSIQKLLNEKS----HFKQAISPSD----RLKLFPRRNSSKSKRKPRPQIQALQ 263
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
156-193 |
2.90e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 2.90e-03
10 20 30
....*....|....*....|....*....|....*...
gi 496028547 156 DRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
32-217 |
2.95e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 32 AIVGVNGAGKTTLLK----ILTGE--EQADGGSVTLAKDAKLGYlrqinnVDSTLSIIDELYTVIEPILDMEKRILKMQN 105
Cdd:COG0419 27 LIVGPNGAGKSTILEairyALYGKarSRSKLRSDLINVGSEEAS------VELEFEHGGKRYRIERRQGEFAEFLEAKPS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 106 E----MRHLTG-EKLEKLYSSYTALTHnyELMDGYAAKSKVVGILKGLGFEEADFDRkINTLSGGQKTRVFLAKLLLeep 180
Cdd:COG0419 101 ErkeaLKRLLGlEIYEELKERLKELEE--ALESALEELAELQKLKQEILAQLSGLDP-IETLSGGERLRLALADLLS--- 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 496028547 181 diILLDepTNHLDLRSIEWLESYLLNyngaVVIVSHD 217
Cdd:COG0419 175 --LILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
162-216 |
3.11e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 40.77 E-value: 3.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 496028547 162 LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYL--LNYNGAVVIVSH 216
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALdeLQKNRTSLVIAH 537
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
160-193 |
3.19e-03 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 40.47 E-value: 3.19e-03
10 20 30
....*....|....*....|....*....|....
gi 496028547 160 NTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD 193
Cdd:PRK10790 475 NNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
2-224 |
3.97e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.39 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 2 ILNATNISKSFGSNEIIKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEE--QADGGSVTLaKDAKLGYLRQINNVDST 79
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEF-KGKDLLELSPEDRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 80 LSIIDElYTVIEPILDMEKRILKMQNEMRHLTG-EKLEKlyssytalthnYELMDGYAAKSKVVGILKGLgfeeadFDRK 158
Cdd:PRK09580 80 IFMAFQ-YPVEIPGVSNQFFLQTALNAVRSYRGqEPLDR-----------FDFQDLMEEKIALLKMPEDL------LTRS 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 159 INT-LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLE---SYLLNYNGAVVIVSHDRYFLDKI 224
Cdd:PRK09580 142 VNVgFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAdgvNSLRDGKRSFIIVTHYQRILDYI 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
328-476 |
3.97e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 39.83 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 328 LSVHNLSKSFDRK-KLFYDINFEIKRGERVAIIGDNGTGKTTLLKIINGiLEPDT-GEVIYGSNVsvayydqehqVLHMd 405
Cdd:PRK11650 4 LKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG-LERITsGEIWIGGRV----------VNEL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 406 ktlfdEISDT-----------YPEMT-------------------NTRIRNIlAAFLFTGEDVYKKISDLSGGERGRVSL 455
Cdd:PRK11650 72 -----EPADRdiamvfqnyalYPHMSvrenmayglkirgmpkaeiEERVAEA-ARILELEPLLDRKPRELSGGQRQRVAM 145
|
170 180
....*....|....*....|.
gi 496028547 456 VKLMLSKANFLLLDEPTNHLD 476
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLD 166
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-197 |
4.46e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 39.78 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 7 NISKSF--GSNEII--KSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTlakdaklgylrqINNVDST-LS 81
Cdd:PRK11153 6 NISKVFpqGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVL------------VDGQDLTaLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 82 iidelytviepilDMEKRILKMQNEM--RHLTgeklekLYSSYT-----ALTHNYELMDGYAAKSKVVGILKGLGFEEAD 154
Cdd:PRK11153 74 -------------EKELRKARRQIGMifQHFN------LLSSRTvfdnvALPLELAGTPKAEIKARVTELLELVGLSDKA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496028547 155 fDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLD---LRSI 197
Cdd:PRK11153 135 -DRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDpatTRSI 179
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
142-231 |
4.47e-03 |
|
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: 39.16 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 142 VGILKGLGFEEADFDRKINTLSGGQKTRVFLAKLLLEEPDIIL--LDEPTNHL----DLRSIEWLESyLLNYNGAVVIVS 215
Cdd:cd03270 118 LGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLhprdNDRLIETLKR-LRDLGNTVLVVE 196
|
90
....*....|....*.
gi 496028547 216 HDRYFLdKIVSKVIDI 231
Cdd:cd03270 197 HDEDTI-RAADHVIDI 211
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
153-252 |
5.64e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 39.77 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 153 ADFDRKINTLSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDLRS---IEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVI 229
Cdd:PRK09700 401 HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAkaeIYKVMRQLADDGKVILMVSSELPEIITVCDRIA 480
|
90 100
....*....|....*....|...
gi 496028547 230 DIENGNVQMYLGNYTDFSNKKQM 252
Cdd:PRK09700 481 VFCEGRLTQILTNRDDMSEEEIM 503
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
162-236 |
6.63e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 38.91 E-value: 6.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496028547 162 LSGGQKTRVFLAKLLLEEPDIILLDEPTNHLDL----RSIEWLESYLLNYNGAVVIVSHDRYFLDKIVSKVIDIENGNV 236
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVvaqaRILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-226 |
9.14e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 38.85 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 18 IKSATFLINEHEKAAIVGVNGAGKTTLLKILTGEEQADGGSVTLA------------KDAKLGYL---RQINNVDSTLSI 82
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDgeditglsprerRRLGVAYIpedRLGRGLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496028547 83 IDELytviepILD------MEKRILKMQNEMRHLTGEkleklyssytalthnyeLMDGYAAKSkvvgilkglgfeeADFD 156
Cdd:COG3845 354 AENL------ILGryrrppFSRGGFLDRKAIRAFAEE-----------------LIEEFDVRT-------------PGPD 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496028547 157 RKINTLSGG--QKtrVFLAKLLLEEPDIILLDEPTNHLDLRSIEWLESYLL---NYNGAVVIVSHDryfLDKIVS 226
Cdd:COG3845 398 TPARSLSGGnqQK--VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLelrDAGAAVLLISED---LDEILA 467
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