|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-483 |
5.03e-138 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 409.45 E-value: 5.03e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 7 ISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQETEAYD------ 80
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDdltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 81 ---SGHPEPAE----------------------AALLEK------WNVPARA-----------------FSQLSGGEKLK 112
Cdd:COG0488 81 tvlDGDAELRAleaeleeleaklaepdedlerlAELQEEfealggWEAEARAeeilsglgfpeedldrpVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 113 ARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKLIEHKGNYSSYMEV 192
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 193 RKQRRLTQQREYENQQHMIRRIEAQMNELSAwskKAhaqstkiegfkeyhrvkakRTDAQIKSKQKRLEKeLEKAKAEPV 272
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRFRA---KA-------------------RKAKQAQSRIKALEK-LEREEPPRR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 273 EAeyEVRFSIEHRKKAGKRFLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWIS 351
Cdd:COG0488 298 DK--TVEIRFPPPERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDsGTVKLG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 352 PSANVGYLTQEVFDLPLDKTPEQLFYKETFEAR-GNVQSLMKHLGFTAAQWTEPIGKMSMGERVKCKLMAFILEEKDVLI 430
Cdd:COG0488 376 ETVKIGYFDQHQEELDPDKTVLDELRDGAPGGTeQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 494651374 431 LDEPTNHLDLPSREQLEDTLARYDGTLIIVSHDRYFVEKTTDIRLDISNGSVR 483
Cdd:COG0488 456 LDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-541 |
5.16e-65 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 222.90 E-value: 5.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQ------ETE 77
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQdpprnvEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 78 AYD---SGHPEPAE------------------------AALLEK------WNVPAR--------------AFSQLSGGEK 110
Cdd:PRK11147 83 VYDfvaEGIEEQAEylkryhdishlvetdpseknlnelAKLQEQldhhnlWQLENRinevlaqlgldpdaALSSLSGGWL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 111 LKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKLIEHKGNYSSYM 190
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 191 EvRKQRRLtqqreyenqqhmirRIEAQMNELsaWSKKAHAQSTKI-EGfkeyhrVKAKRTDAQiksKQKRLEKELEKAKA 269
Cdd:PRK11147 243 L-EKEEAL--------------RVEELQNAE--FDRKLAQEEVWIrQG------IKARRTRNE---GRVRALKALRRERS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 270 EPVEAEYEVRFSIEHRKKAGKRFLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSI 348
Cdd:PRK11147 297 ERREVMGTAKMQVEEASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADsGRI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 349 WISPSANVGYLTQEVFDLPLDKTPEQLFY--KETFEARG---NVQSLMKHLGFTAAQWTEPIGKMSMGERVKCKLMAFIL 423
Cdd:PRK11147 377 HCGTKLEVAYFDQHRAELDPEKTVMDNLAegKQEVMVNGrprHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 424 EEKDVLILDEPTNHLDLPSREQLEDTLARYDGTLIIVSHDRYFVEKT-TDIRLDISNGSV-------------RKQWKES 489
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTvTECWIFEGNGKIgryvggyhdarqqQAQYLAL 536
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 494651374 490 -PSVRDDAEELRLKLETERQEVLGKLSFmtpadKQYRELDQ---KFKELTEEIKKL 541
Cdd:PRK11147 537 kQPAVKKKEEAAAPKAETVKRSSKKLSY-----KLQRELEQlpqLLEDLEAEIEAL 587
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-467 |
3.05e-62 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 213.21 E-value: 3.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQ--------------------- 62
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSldpnerlgklrqdqfafeeft 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 63 -----MMQDVNIYMVEQETEAYDSgHPEPAE-----AALLEK-------WNVPARA-----------------FSQLSGG 108
Cdd:PRK15064 81 vldtvIMGHTELWEVKQERDRIYA-LPEMSEedgmkVADLEVkfaemdgYTAEARAgelllgvgipeeqhyglMSEVAPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 109 EKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKLIEHKGNYSS 188
Cdd:PRK15064 160 WKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 189 YMEVRKQRRltqqreyENQQHMIRRIEAQMNELSAWSKKAHAQSTKiegfkeyhrvkAKrtdaQIKSKQKRLEK-ELEKA 267
Cdd:PRK15064 240 YMTAATQAR-------ERLLADNAKKKAQIAELQSFVSRFSANASK-----------AK----QATSRAKQIDKiKLEEV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 268 KAEPVEAEYeVRFsiEHRKKAGKRFLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ-EKAQG 346
Cdd:PRK15064 298 KPSSRQNPF-IRF--EQDKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGElEPDSG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 347 SIWISPSANVGYLTQE-VFDLPLDKTpeqLF-----YKETFEARGNVQSLMKHLGFTAAQWTEPIGKMSMGERVKC---K 417
Cdd:PRK15064 375 TVKWSENANIGYYAQDhAYDFENDLT---LFdwmsqWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMlfgK 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 494651374 418 LMafiLEEKDVLILDEPTNHLDLPSREQLEDTLARYDGTLIIVSHDRYFV 467
Cdd:PRK15064 452 LM---MQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFV 498
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-472 |
5.65e-58 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 203.86 E-value: 5.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 19 LFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQETEAYDsghpEPA----------- 87
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALP----QPAleyvidgdrey 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 88 ---EAAL---------------------LEKWNVPARA--------FSQ---------LSGGEKLKARLAKGFSSSSSLL 126
Cdd:PRK10636 92 rqlEAQLhdanerndghaiatihgkldaIDAWTIRSRAasllhglgFSNeqlerpvsdFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 127 LLDEPTNHLDQHSLEILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKLIEHKGNYSSYMEVRKQRRLTQQREYEN 206
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQAMYES 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 207 QQHmirrieaqmnelsawsKKAHAQSTkiegfkeYHRVKAKRTDA-QIKSKQKRLEK-ELekakAEPVEAEYEVRFSIEH 284
Cdd:PRK10636 252 QQE----------------RVAHLQSY-------IDRFRAKATKAkQAQSRIKMLERmEL----IAPAHVDNPFHFSFRA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 285 RKKAGKRFLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ-EKAQGSIWISPSANVGYLTQEV 363
Cdd:PRK10636 305 PESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGElAPVSGEIGLAKGIKLGYFAQHQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 364 FD-LPLDKTPEQLFYKetFEARGNVQSLMKHL---GFTAAQWTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLD 439
Cdd:PRK10636 385 LEfLRADESPLQHLAR--LAPQELEQKLRDYLggfGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
490 500 510
....*....|....*....|....*....|...
gi 494651374 440 LPSREQLEDTLARYDGTLIIVSHDRYFVEKTTD 472
Cdd:PRK10636 463 LDMRQALTEALIDFEGALVVVSHDRHLLRSTTD 495
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-469 |
1.01e-55 |
|
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: 195.92 E-value: 1.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 18 PLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQETE-------------------- 77
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQldptktvrenveegvaeikd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 78 ---AYDS-----GHPEPAEAALLEK-------------WN------VPARAF---------SQLSGGEKLKARLAKGFSS 121
Cdd:TIGR03719 99 aldRFNEisakyAEPDADFDKLAAEqaelqeiidaadaWDldsqleIAMDALrcppwdadvTKLSGGERRRVALCRLLLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 122 SSSLLLLDEPTNHLDQHSLEILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKLIEHKGNYSSYMEvRKQRRLTQQ 201
Cdd:TIGR03719 179 KPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLE-QKQKRLEQE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 202 -REYENQQHMIRRieaqmnELsawskkahaqstkiegfkEYHRVKAKRTDAQIKSKQKRLEKELEKAKAEPVEAEyEVRf 280
Cdd:TIGR03719 258 eKEESARQKTLKR------EL------------------EWVRQSPKGRQAKSKARLARYEELLSQEFQKRNETA-EIY- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 281 sIEHRKKAGKRFLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWISPSANVGYL 359
Cdd:TIGR03719 312 -IPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPdSGTIEIGETVKLAYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQEVFDLPLDKTPEQ---------LFYKETFEARGNVQSlmkhLGFTAAQWTEPIGKMSMGERVKCKLMAFILEEKDVLI 430
Cdd:TIGR03719 391 DQSRDALDPNKTVWEeisggldiiKLGKREIPSRAYVGR----FNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
490 500 510
....*....|....*....|....*....|....*....
gi 494651374 431 LDEPTNHLDLPSREQLEDTLARYDGTLIIVSHDRYFVEK 469
Cdd:TIGR03719 467 LDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDR 505
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
295-514 |
2.79e-54 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 191.43 E-value: 2.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 295 VRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWISPSANVGYLTQEVF--------- 364
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPdSGEVSIPKGLRIGYLPQEPPldddltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 365 -----DLPLDKTPEQLFYKET------------------FEARG------NVQSLMKHLGFTAAQWTEPIGKMSMGERVK 415
Cdd:COG0488 81 tvldgDAELRALEAELEELEAklaepdedlerlaelqeeFEALGgweaeaRAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 416 CKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLARYDGTLIIVSHDRYFVEKTTDIRLDISNGSVR------KQWKES 489
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTlypgnySAYLEQ 240
|
250 260
....*....|....*....|....*
gi 494651374 490 psvRDDAEELRLKLETERQEVLGKL 514
Cdd:COG0488 241 ---RAERLEQEAAAYAKQQKKIAKE 262
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
293-480 |
6.89e-53 |
|
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: 6.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWISPSANVGYLTQevfdlpldkt 371
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPdEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 372 peqlfyketfeargnvqslmkhlgftaaqwtepigkMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLA 451
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180
....*....|....*....|....*....
gi 494651374 452 RYDGTLIIVSHDRYFVEKTTDIRLDISNG 480
Cdd:cd03221 115 EYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-466 |
2.44e-49 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 178.77 E-value: 2.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 18 PLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQE---------------------- 75
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEpqldpektvrenveegvaevka 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 76 --------TEAYdsGHPEPAEAALLEK-------------WNVPAR---------------AFSQLSGGEKLKARLAKGF 119
Cdd:PRK11819 101 aldrfneiYAAY--AEPDADFDALAAEqgelqeiidaadaWDLDSQleiamdalrcppwdaKVTKLSGGERRRVALCRLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 120 SSSSSLLLLDEPTNHLDQHSLEILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKLIEHKGNYSSYMEvRKQRRLT 199
Cdd:PRK11819 179 LEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLE-QKAKRLA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 200 QQreyenqqhmirrieaqmnelsawskkahaqstkiegfkeyhrvkaKRTDAqikSKQKRLEKELE-----------KAK 268
Cdd:PRK11819 258 QE---------------------------------------------EKQEA---ARQKALKRELEwvrqspkarqaKSK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 269 AEPveAEYEVRFSIEHRKKA-------------GKRFLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLL 335
Cdd:PRK11819 290 ARL--ARYEELLSEEYQKRNetneifippgprlGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 336 KVILGQEKA-QGSIWISPSANVGYLTQEVFDLPLDKTpeqlfykeTFEARGNVQSLMK-------------HLGFTAAQW 401
Cdd:PRK11819 368 KMITGQEQPdSGTIKIGETVKLAYVDQSRDALDPNKT--------VWEEISGGLDIIKvgnreipsrayvgRFNFKGGDQ 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494651374 402 TEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLARYDGTLIIVSHDRYF 466
Cdd:PRK11819 440 QKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWF 504
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-178 |
6.84e-45 |
|
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: 154.91 E-value: 6.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIymveqeteAYdsghp 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKI--------GY----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 85 epaeaallekwnvparaFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYKGTIIFVSHDRAFI 164
Cdd:cd03221 68 -----------------FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFL 130
|
170
....*....|....
gi 494651374 165 DAAATKIWAIEGKK 178
Cdd:cd03221 131 DQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-191 |
1.05e-42 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 159.85 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 2 KEMLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQETEAYDS 81
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 82 ----------GHPEPAEA---ALLEKWN-VPARAF---SQLSGGEKlkAR--LAKGFSSSSSLLLLDEPTNHLDQHSLEI 142
Cdd:COG0488 393 dktvldelrdGAPGGTEQevrGYLGRFLfSGDDAFkpvGVLSGGEK--ARlaLAKLLLSPPNVLLLDEPTNHLDIETLEA 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494651374 143 LLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKLIEHKGNYSSYME 191
Cdd:COG0488 471 LEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
100-482 |
1.13e-41 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 159.26 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 100 RAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKL 179
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 180 IEHKGNYSSYMEVRKQRRLTQQREYENqqhmirrieaqmNELSawskKAHAQStkiegFKEYHRVKAKRTdAQIKSKQKR 259
Cdd:PLN03073 420 VTYKGDYDTFERTREEQLKNQQKAFES------------NERS----RSHMQA-----FIDKFRYNAKRA-SLVQSRIKA 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 260 LEKeLEKAKAEPVEAEYEVRFSIEHrKKAGKRFLEVRDAAKSY-DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVI 338
Cdd:PLN03073 478 LDR-LGHVDAVVNDPDYKFEFPTPD-DRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLI 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 339 LGQ-EKAQGSIWISPSANVGYLTQEVFD-LPLDKTPeqLFYKETFEARGNVQSLMKHL---GFTAAQWTEPIGKMSMGER 413
Cdd:PLN03073 556 SGElQPSSGTVFRSAKVRMAVFSQHHVDgLDLSSNP--LLYMMRCFPGVPEQKLRAHLgsfGVTGNLALQPMYTLSGGQK 633
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494651374 414 VKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLARYDGTLIIVSHDRYFVEKTTDIRLDISNGSV 482
Cdd:PLN03073 634 SRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
293-476 |
6.70e-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: 127.60 E-value: 6.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI----------SPSANVGYLTQ 361
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPsAGEVLWngepirdareDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 362 EVfDLPLDKTP-EQL-FY---KETFEARGNVQSLMKHLGFTAAQWTePIGKMSMGERVKCKLMAFILEEKDVLILDEPTN 436
Cdd:COG4133 83 AD-GLKPELTVrENLrFWaalYGLRADREAIDEALEAVGLAGLADL-PVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494651374 437 HLDLPSREQLEDTLARY---DGTLIIVSHDRYFVEKTTDIRLD 476
Cdd:COG4133 161 ALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAARVLDLG 203
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
293-463 |
4.30e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.19 E-value: 4.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWI------SPSANVGYLTQ-EVF 364
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPpTSGTVRLfgkpprRARRRIGYVPQrAEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 365 D--LPLdkTPEQ-----------LFYKETFEARGNVQSLMKHLGfTAAQWTEPIGKMSMGE--RVkckLMAFIL-EEKDV 428
Cdd:COG1121 87 DwdFPI--TVRDvvlmgrygrrgLFRRPSRADREAVDEALERVG-LEDLADRPIGELSGGQqqRV---LLARALaQDPDL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 494651374 429 LILDEPTNHLDLPSREQLEDT---LARYDGTLIIVSHD 463
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELlreLRREGKTILVVTHD 198
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
293-482 |
4.47e-29 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 112.88 E-value: 4.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWI----------SPSANVGYLTQ 361
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDsGEIKVlgkdikkepeEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 362 EvFDLPLDKTPEQLFyketfeargnvqslmkhlgftaaqwtepigKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLP 441
Cdd:cd03230 81 E-PSLYENLTVRENL------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494651374 442 SREQLEDTLARY---DGTLIIVSHDRYFVEKTTDIRLDISNGSV 482
Cdd:cd03230 130 SRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
300-466 |
6.43e-29 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 120.61 E-value: 6.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 300 KSYDG-RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWISPSANVGYLTQE--------------- 362
Cdd:PRK11819 14 KVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEfEGEARPAPGIKVGYLPQEpqldpektvrenvee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 363 ----VFDLpLDK---------TPEQLFyKETFEARGNVQSLMKHLGFT--------AAQ------WTEPIGKMSMGERVK 415
Cdd:PRK11819 94 gvaeVKAA-LDRfneiyaayaEPDADF-DALAAEQGELQEIIDAADAWdldsqleiAMDalrcppWDAKVTKLSGGERRR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494651374 416 ---CKLMafiLEEKDVLILDEPTNHLDLPSREQLEDTLARYDGTLIIVSHDRYF 466
Cdd:PRK11819 172 valCRLL---LEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYF 222
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-190 |
1.57e-28 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 119.23 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNI-YMveqeteAYDSGH 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIgYY------AQDHAY 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 84 PEPAEAALLE---KWNVPA------RA------FSQ---------LSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHS 139
Cdd:PRK15064 394 DFENDLTLFDwmsQWRQEGddeqavRGtlgrllFSQddikksvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494651374 140 LEILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKLIEHKGNYSSYM 190
Cdd:PRK15064 474 IESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYL 524
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
300-509 |
2.15e-28 |
|
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: 118.88 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 300 KSYD-GRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWISPSANVGYLTQEVfdlPLDktPEQLFY 377
Cdd:TIGR03719 12 KVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDfNGEARPQPGIKVGYLPQEP---QLD--PTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 378 KETFEARGNVQSLMKHLGFTAAQWTEP---------------------------------------------IGKMSMGE 412
Cdd:TIGR03719 87 ENVEEGVAEIKDALDRFNEISAKYAEPdadfdklaaeqaelqeiidaadawdldsqleiamdalrcppwdadVTKLSGGE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 413 RVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLARYDGTLIIVSHDRYFVEKTTDIRLDISNGSvRKQWKESPSV 492
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGR-GIPWEGNYSS 245
|
250
....*....|....*..
gi 494651374 493 RDDAEELRLKLEtERQE 509
Cdd:TIGR03719 246 WLEQKQKRLEQE-EKEE 261
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
293-463 |
6.04e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 111.69 E-value: 6.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWI----------SPSANVGYLTQ 361
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTsGEVRVlgedvardpaEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 362 EvFDLPLDKTPEQL--FYKETF-----EARGNVQSLMKHLGFTAAQwTEPIGKMSMGERVKCKLMAFILEEKDVLILDEP 434
Cdd:COG1131 81 E-PALYPDLTVRENlrFFARLYglprkEARERIDELLELFGLTDAA-DRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 494651374 435 TNHLDLPSREQLED---TLARYDGTLIIVSHD 463
Cdd:COG1131 159 TSGLDPEARRELWEllrELAAEGKTVLLSTHY 190
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-196 |
6.97e-28 |
|
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: 117.34 E-value: 6.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQETEAYDSGH- 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKt 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 84 -----PEPAEAALLEKWNVPARAF---------------SQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEIL 143
Cdd:TIGR03719 403 vweeiSGGLDIIKLGKREIPSRAYvgrfnfkgsdqqkkvGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRAL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494651374 144 LNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKLIE-HKGNYSSYMEVRKQR 196
Cdd:TIGR03719 483 EEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEwFEGNFSEYEEDKKRR 536
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
294-480 |
8.55e-28 |
|
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: 108.87 E-value: 8.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 294 EVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWISPsanvgyltQEVFDLPLDKTP 372
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEILIDG--------KDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 373 EQLFYketfeargnvqslmkhlgftaaqwtepIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLAR 452
Cdd:cd00267 73 RRIGY---------------------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRE 125
|
170 180 190
....*....|....*....|....*....|.
gi 494651374 453 Y---DGTLIIVSHDRYFVEKTTDIRLDISNG 480
Cdd:cd00267 126 LaeeGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
308-436 |
3.10e-27 |
|
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: 106.96 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 308 FKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWI-----------SPSANVGYLTQEVFDLPLDKTPEQL 375
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLdgqdltdderkSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 376 FYKETFEARGN------VQSLMKHLGFTAAQ---WTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTN 436
Cdd:pfam00005 81 RLGLLLKGLSKrekdarAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
293-485 |
7.62e-27 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 108.79 E-value: 7.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWI----------SPSANVGYLTQ 361
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDsGSILIdgedvrkeprEARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 362 EvFDLPLDKTPEQ--LFYKETF-----EARGNVQSLMKHLGFTAAQwTEPIGKMSMGERVKCKLMAFILEEKDVLILDEP 434
Cdd:COG4555 82 E-RGLYDRLTVREniRYFAELYglfdeELKKRIEELIELLGLEEFL-DRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494651374 435 TNHLDLPSREQLEDTLARY---DGTLIIVSHDRYFVEKTTDIRLDISNGSVRKQ 485
Cdd:COG4555 160 TNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQ 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
293-472 |
1.71e-26 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 107.42 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSY-DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWI--------SPSA---NVGYL 359
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTsGEVLVdgkditkkNLRElrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQEvfdlpldktPE-QLF----YKE-TF----------EARGNVQSLMKHLGFtAAQWTEPIGKMSMGERvkcKLMAF-- 421
Cdd:COG1122 81 FQN---------PDdQLFaptvEEDvAFgpenlglpreEIRERVEEALELVGL-EHLADRPPHELSGGQK---QRVAIag 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494651374 422 ILE-EKDVLILDEPTNHLDLPSREQLEDTLARYDG---TLIIVSHDRYFVEKTTD 472
Cdd:COG1122 148 VLAmEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELAD 202
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
294-472 |
1.83e-26 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 106.85 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 294 EVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWISP------SANVGYLTQ--EV- 363
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKpTSGSIRVFGkplekeRKRIGYVPQrrSId 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 364 FDLPLdkTPEQL-----------FYKETFEARGNVQSLMKHLGFTAAqWTEPIGKMSMGERvKCKLMAFIL-EEKDVLIL 431
Cdd:cd03235 81 RDFPI--SVRDVvlmglyghkglFRRLSKADKAKVDEALERVGLSEL-ADRQIGELSGGQQ-QRVLLARALvQDPDLLLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494651374 432 DEPTNHLDLPSREQLEDTLARY--DG-TLIIVSHDRYFVEKTTD 472
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELrrEGmTILVVTHDLGLVLEYFD 200
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-472 |
2.14e-26 |
|
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: 112.69 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 1 MKEMLKISG--ISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLIcNQKAPSQGQIQ-----MMQDV------ 67
Cdd:COG1123 1 MTPLLEVRDlsVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAL-MGLLPHGGRISgevllDGRDLlelsea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 68 ----NIYMVEQE--------------TEAYDSGHPEPAEA-----ALLEKWNVPARAFS---QLSGGEKLKARLAKGFSS 121
Cdd:COG1123 80 lrgrRIGMVFQDpmtqlnpvtvgdqiAEALENLGLSRAEArarvlELLEAVGLERRLDRyphQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 122 SSSLLLLDEPTNHLD----QHSLEILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKLIEHkgnyssymevrkqrr 197
Cdd:COG1123 160 DPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVED--------------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 198 ltqqreyenqqhmirrieaqmnelsawskkahaqstkiegfkeyhrvkakRTDAQIKSKQKRLEKELEKAKAEPVEAEye 277
Cdd:COG1123 225 --------------------------------------------------GPPEEILAAPQALAAVPRLGAARGRAAP-- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 278 vrfsiehRKKAGKRFLEVRDAAKSYDGR-----TLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI- 350
Cdd:COG1123 253 -------AAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPtSGSILFd 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 351 -------SPSA------NVGYLTQE----------VFDLpLDKTPEQLFYKETFEARGNVQSLMKHLGFTAAQWTEPIGK 407
Cdd:COG1123 326 gkdltklSRRSlrelrrRVQMVFQDpysslnprmtVGDI-IAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHE 404
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494651374 408 MSMGE--RVkCKLMAFILeEKDVLILDEPTNHLDLPSREQ----LEDTLARYDGTLIIVSHDRYFVEKTTD 472
Cdd:COG1123 405 LSGGQrqRV-AIARALAL-EPKLLILDEPTSALDVSVQAQilnlLRDLQRELGLTYLFISHDLAVVRYIAD 473
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
292-462 |
2.24e-26 |
|
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: 107.86 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 292 FLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVI--------------LGQEKAQGSIW-ISPsaNV 356
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItgdlpptygndvrlFGERRGGEDVWeLRK--RI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 357 GYLTQEVF-DLPLDKTPEQ-----------LFYKETFEARGNVQSLMKHLGFTA-AQwtEPIGKMSMGERVKC----KLM 419
Cdd:COG1119 81 GLVSPALQlRFPRDETVLDvvlsgffdsigLYREPTDEQRERARELLELLGLAHlAD--RPFGTLSQGEQRRVliarALV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494651374 420 AfileEKDVLILDEPTNHLDLPSREQLEDTLARY--DG--TLIIVSH 462
Cdd:COG1119 159 K----DPELLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTH 201
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
293-463 |
3.48e-26 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 107.44 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWI--------SPSA---NVGYLT 360
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSsGEVLLdgrdlaslSRRElarRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 361 QE--------VFDL-PLDKTPEQ-LFYKETFEARGNVQSLMKHLGfTAAQWTEPIGKMSMGERVKCKL-MAfILEEKDVL 429
Cdd:COG1120 82 QEppapfgltVRELvALGRYPHLgLFGRPSAEDREAVEEALERTG-LEHLADRPVDELSGGERQRVLIaRA-LAQEPPLL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 494651374 430 ILDEPTNHLDLPSREQLEDT---LARYDG-TLIIVSHD 463
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELlrrLARERGrTVVMVLHD 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
294-463 |
6.96e-25 |
|
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: 101.36 E-value: 6.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 294 EVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWIspsanvgyltqevFDLPLDKTP 372
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSsGEILL-------------DGKDLASLS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 373 eqlfYKETFEARGNVQSLMKHLGFTA-AQwtEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLA 451
Cdd:cd03214 68 ----PKELARKIAYVPQALELLGLAHlAD--RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLR 141
|
170
....*....|....*.
gi 494651374 452 RY----DGTLIIVSHD 463
Cdd:cd03214 142 RLarerGKTVVMVLHD 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-180 |
7.31e-25 |
|
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: 101.36 E-value: 7.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 6 KISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMqdvniymvEQETEAYDsghpe 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD--------GKDLASLS----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 86 PAEAA--------LLEKWNVPA---RAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLD-QHSLEIL--LNQIKNYK 151
Cdd:cd03214 68 PKELArkiayvpqALELLGLAHladRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiAHQIELLelLRRLARER 147
|
170 180 190
....*....|....*....|....*....|...
gi 494651374 152 G-TIIFVSHDrafIDAA---ATKIWAIEGKKLI 180
Cdd:cd03214 148 GkTVVMVLHD---LNLAaryADRVILLKDGRIV 177
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
294-480 |
3.10e-24 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 100.62 E-value: 3.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 294 EVRDAAKSYDG--RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWISP-----------SANVGYL 359
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTsGEVLVDGkdltklslkelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQEvfdlpldktPE-QLFYKETF---------------EARGNVQSLMKHLGFtAAQWTEPIGKMSMGERVKCKLMAFIL 423
Cdd:cd03225 81 FQN---------PDdQFFGPTVEeevafglenlglpeeEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 424 EEKDVLILDEPTNHLDLPSREQLEDTLARY--DG-TLIIVSHDRYFVEKTTDIRLDISNG 480
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-284 |
3.00e-23 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 103.88 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 10 ISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQETEAYDsghPEP--- 86
Cdd:PRK11147 325 VNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELD---PEKtvm 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 87 ---AEAalleKWNV-------------------PARAFS---QLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLE 141
Cdd:PRK11147 402 dnlAEG----KQEVmvngrprhvlgylqdflfhPKRAMTpvkALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLE 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 142 ILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKLIehkGNY-SSYMEVRKQRrltqqreyENQQHMIRRIEAQMNE 220
Cdd:PRK11147 478 LLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKI---GRYvGGYHDARQQQ--------AQYLALKQPAVKKKEE 546
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494651374 221 LSAWSKKAHAQSTKIEGFKEyhrvkaKRTDAQIKSKQKRLEKELEKAKAEPVEAEYevrFSIEH 284
Cdd:PRK11147 547 AAAPKAETVKRSSKKLSYKL------QRELEQLPQLLEDLEAEIEALQAQVADADF---FSQPH 601
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-196 |
9.34e-23 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 101.73 E-value: 9.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 19 LFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQETEAYDSGH------PEPAEAALL 92
Cdd:PRK11819 339 LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKtvweeiSGGLDIIKV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 93 EKWNVPARAF---------------SQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYKGTIIFV 157
Cdd:PRK11819 419 GNREIPSRAYvgrfnfkggdqqkkvGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 494651374 158 SHDRAFIDAAATKIWAIEGKKLIE-HKGNYSSYMEVRKQR 196
Cdd:PRK11819 499 SHDRWFLDRIATHILAFEGDSQVEwFEGNFQEYEEDKKRR 538
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
302-482 |
1.82e-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: 95.40 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 302 YDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSI-----WISPSA---NVGYLTQEVFDlpldktp 372
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGlIKESSGSIllngkPIKAKErrkSIGYVMQDVDY------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 373 eQLFY-----------KETFEARGNVQSLMKHLGFTAAQWTEPIgKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLP 441
Cdd:cd03226 83 -QLFTdsvreelllglKELDAGNEQAETVLKDLDLYALKERHPL-SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494651374 442 SREQLED---TLARYDGTLIIVSHDRYFVEKTTDIRLDISNGSV 482
Cdd:cd03226 161 NMERVGElirELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
272-485 |
3.09e-22 |
|
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: 100.23 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 272 VEAEYEVRFSIEHRKKAGKRFLEVRDAAKSYDG--RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSI 348
Cdd:COG4987 313 LDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQsGSI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 349 WI-----------SPSANVGYLTQE--VFD------LPL---DKTPEQLfyketfeargnVQSLMK-HLGFTAAQWTE-- 403
Cdd:COG4987 393 TLggvdlrdldedDLRRRIAVVPQRphLFDttlrenLRLarpDATDEEL-----------WAALERvGLGDWLAALPDgl 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 404 --PIG----KMSMGE-------RVkcklmafILEEKDVLILDEPTNHLDLPSREQLEDTLARY--DGTLIIVSHDRYFVE 468
Cdd:COG4987 462 dtWLGeggrRLSGGErrrlalaRA-------LLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAGLE 534
|
250
....*....|....*..
gi 494651374 469 KtTDIRLDISNGSVRKQ 485
Cdd:COG4987 535 R-MDRILVLEDGRIVEQ 550
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-178 |
3.09e-22 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 93.08 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 6 KISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMmqdvniymveqeteaydsgHPE 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI-------------------DGK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 86 PAEAALLEKWNVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYKG---TIIFVSHDRA 162
Cdd:cd00267 62 DIAKLPLEELRRRIGYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPE 141
|
170
....*....|....*.
gi 494651374 163 FIDAAATKIWAIEGKK 178
Cdd:cd00267 142 LAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-180 |
2.36e-21 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 93.57 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDV----------NIYMV 72
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgRDLaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 73 EQETEA------YDS---G-HP-------------EPAEAALlEKWNVPA---RAFSQLSGGEKLKARLAKGFSSSSSLL 126
Cdd:COG1120 81 PQEPPApfgltvRELvalGrYPhlglfgrpsaedrEAVEEAL-ERTGLEHladRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494651374 127 LLDEPTNHLD-QHSLEIL--LNQIKNYKG-TIIFVSHDrafIDAAA---TKIWAIEGKKLI 180
Cdd:COG1120 160 LLDEPTSHLDlAHQLEVLelLRRLARERGrTVVMVLHD---LNLAAryaDRLVLLKDGRIV 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-183 |
7.51e-21 |
|
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: 91.84 E-value: 7.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDV---------NIYMVE 73
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgEDVrkeprearrQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 74 QETEAYD------------SGHPEPAEAA---------LLEKWNVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPT 132
Cdd:COG4555 81 DERGLYDrltvreniryfaELYGLFDEELkkrieelieLLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494651374 133 NHLDQHSLEILLNQIKNYKG---TIIFVSHDRAFIDAAATKIWAIEGKKLIEHK 183
Cdd:COG4555 161 NGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
301-463 |
7.76e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.37 E-value: 7.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 301 SYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWISPSANVGYLTQ--EVFD-LPLdkTPEQL- 375
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRpTSGTVRRAGGARVAYVPQrsEVPDsLPL--TVRDLv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 376 ----------FYKETFEARGNVQSLMKHLGFTAAQwTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQ 445
Cdd:NF040873 79 amgrwarrglWRRLTRDDRAAVDDALERVGLADLA-GRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180
....*....|....*....|.
gi 494651374 446 LEDTLARY--DG-TLIIVSHD 463
Cdd:NF040873 158 IIALLAEEhaRGaTVVVVTHD 178
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
293-462 |
9.74e-21 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 89.36 E-value: 9.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRT--LFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWI--------SPSA---NVGY 358
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTsGEILIdgvdlrdlDLESlrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 359 LTQEVFdlpldktpeqLFyKETFeaRGNVqslmkhlgftaaqwtepigkMSMGERvkcKLMAF---ILEEKDVLILDEPT 435
Cdd:cd03228 81 VPQDPF----------LF-SGTI--RENI--------------------LSGGQR---QRIAIaraLLRDPPILILDEAT 124
|
170 180
....*....|....*....|....*....
gi 494651374 436 NHLDLPSREQLEDTLARYDG--TLIIVSH 462
Cdd:cd03228 125 SALDPETEALILEALRALAKgkTVIVIAH 153
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
271-463 |
2.08e-20 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 94.90 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 271 PVEAEYEVRFsIEHRKKAGKrfLEVRDAAKSYDGRT--LFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GS 347
Cdd:COG2274 455 PPEREEGRSK-LSLPRLKGD--IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTsGR 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 348 IWI--------SPSA---NVGYLTQEVFdlpldktpeqLFYketfearGNVQS--LMKHLGFT------AAQWT---EPI 405
Cdd:COG2274 532 ILIdgidlrqiDPASlrrQIGVVLQDVF----------LFS-------GTIREniTLGDPDATdeeiieAARLAglhDFI 594
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494651374 406 GKMSMG------ER-------VKCKLM---AFILEEKdVLILDEPTNHLDLPSREQLEDTLARYDG--TLIIVSHD 463
Cdd:COG2274 595 EALPMGydtvvgEGgsnlsggQRQRLAiarALLRNPR-ILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHR 669
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-179 |
2.28e-20 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 89.49 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI----QMMQDVN-------IYMVE 73
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgKPLSAMPppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 74 QE------------TEAYDSGHPEPAEA---ALLEKWNVPA----RAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNH 134
Cdd:COG4619 81 QEpalwggtvrdnlPFPFQLRERKFDREralELLERLGLPPdildKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494651374 135 LDQHS----LEILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKL 179
Cdd:COG4619 161 LDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-169 |
6.93e-20 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 87.92 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQmmqdVNIYMVEQETEAYDS-- 81
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVL----WNGEPIRDAREDYRRrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 82 ---GH-------------------------PEPAEAALLEKWNVPARA---FSQLSGGEKLKARLAKGFSSSSSLLLLDE 130
Cdd:COG4133 78 aylGHadglkpeltvrenlrfwaalyglraDREAIDEALEAVGLAGLAdlpVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494651374 131 PTNHLDQHSLEILLNQIKNYK---GTIIFVSHDRAFIDAAAT 169
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAARV 199
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
293-472 |
1.33e-19 |
|
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: 86.47 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWISpsaNVGYLTQEVFDLPLDKT 371
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEPDSGSILID---GEDLTDLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 372 PEQLFyketfeargnvQS--LMKHLgfTAAQ-WTEPigkMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLED 448
Cdd:cd03229 78 IGMVF-----------QDfaLFPHL--TVLEnIALG---LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRA 141
|
170 180
....*....|....*....|....*...
gi 494651374 449 TL----ARYDGTLIIVSHDRYFVEKTTD 472
Cdd:cd03229 142 LLkslqAQLGITVVLVTHDLDEAARLAD 169
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
293-462 |
1.42e-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: 87.65 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDG--RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIW--------ISPS---ANVGY 358
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTsGSVLldgtdirqLDPAdlrRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 359 LTQEVFdlpldktpeqLFY----------------KETFEA--RGNVQSLM-KH-LGFtAAQWTEPIGKMSMGERVKCKL 418
Cdd:cd03245 83 VPQDVT----------LFYgtlrdnitlgapladdERILRAaeLAGVTDFVnKHpNGL-DLQIGERGRGLSGGQRQAVAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494651374 419 MAFILEEKDVLILDEPTNHLDLPSREQLEDTLARY--DGTLIIVSH 462
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITH 197
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
293-480 |
3.59e-19 |
|
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: 86.39 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDG----RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI--------SPSA----- 354
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVRVdgtdisklSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 355 --NVGYLTQE--------VFD---LPLdktpeQLFYKETFEARGNVQSLMKHLGFTAAQwTEPIGKMSMGE--RVkcklm 419
Cdd:cd03255 81 rrHIGFVFQSfnllpdltALEnveLPL-----LLAGVPKKERRERAEELLERVGLGDRL-NHYPSELSGGQqqRV----- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 420 AF---ILEEKDVLILDEPTNHLDLPSREQLEDTL---ARYDG-TLIIVSHDRYFVEKtTDIRLDISNG 480
Cdd:cd03255 150 AIaraLANDPKIILADEPTGNLDSETGKEVMELLrelNKEAGtTIVVVTHDPELAEY-ADRIIELRDG 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
309-480 |
3.87e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 86.62 E-value: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 309 KNVNFTVMHGEKIAITGPNGSGKTTLLK--------------------------------VILGQeKAQgSIWISPSANV 356
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKilsgllqptsgevrvaglvpwkrrkkflrrigVVFGQ-KTQ-LWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 357 GYLTQEVFDLPldktpeqlfykeTFEARGNVQSLMKHLGFTAAQWTePIGKMSMGERVKCKLMAFILEEKDVLILDEPTN 436
Cdd:cd03267 116 FYLLAAIYDLP------------PARFKKRLDELSELLDLEELLDT-PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494651374 437 HLDLPSREQLEDTLARY----DGTLIIVSHDRYFVEKTTDIRLDISNG 480
Cdd:cd03267 183 GLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
293-464 |
5.90e-19 |
|
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: 85.65 E-value: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWIS-------PSA--NVGYLTQE 362
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERpDSGEILIDgrdvtgvPPErrNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 363 --------VFD-----LPLDKTPEQlfyketfEARGNVQSLMKHLGFTaAQWTEPIGKMSMGERVKCKLMAFILEEKDVL 429
Cdd:cd03259 81 yalfphltVAEniafgLKLRGVPKA-------EIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 494651374 430 ILDEPTNHLDLPSREQLEDTLARY----DGTLIIVSHDR 464
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELqrelGITTIYVTHDQ 191
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
293-485 |
7.71e-19 |
|
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: 84.96 E-value: 7.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-------GSIW---ISPSANVG----- 357
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDsgeitfdGKSYqknIEALRRIGaliea 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 358 -----YLTQEvfdlpldktpEQLFYKETFEARGN--VQSLMKHLGFTAAQwTEPIGKMSMGERVKCKLMAFILEEKDVLI 430
Cdd:cd03268 81 pgfypNLTAR----------ENLRLLARLLGIRKkrIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494651374 431 LDEPTNHLD----LPSREQLEDtLARYDGTLIIVSHDRYFVEKTTDIRLDISNGSVRKQ 485
Cdd:cd03268 150 LDEPTNGLDpdgiKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
293-485 |
2.33e-18 |
|
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: 88.28 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSY-DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI-----------SPSANVGYL 359
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPySGSILIngvdlsdldpaSWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQE--VFDLPL---------DKTPEQLfyketfeargnVQSLMKH--LGFTAAQ---WTEPIG----KMSMGE--RVkck 417
Cdd:COG4988 417 PQNpyLFAGTIrenlrlgrpDASDEEL-----------EAALEAAglDEFVAALpdgLDTPLGeggrGLSGGQaqRL--- 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494651374 418 lmAF---ILEEKDVLILDEPTNHLDLPSREQLEDTLARY--DGTLIIVSHDRYFVEKtTDIRLDISNGSVRKQ 485
Cdd:COG4988 483 --ALaraLLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLAQ-ADRILVLDDGRIVEQ 552
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
293-463 |
3.42e-18 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 83.32 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSY--DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWIS----------PSANVGYL 359
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTsGTAYINgysirtdrkaARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQevFD-LPLDKTPEQL--FY-----KETFEARGNVQSLMKHLGFTaAQWTEPIGKMSMGErvKCKL---MAFILEEKdV 428
Cdd:cd03263 81 PQ--FDaLFDELTVREHlrFYarlkgLPKSEIKEEVELLLRVLGLT-DKANKRARTLSGGM--KRKLslaIALIGGPS-V 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 494651374 429 LILDEPTNHLDLPSREQLEDTLARYDG--TLIIVSHD 463
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
305-482 |
4.74e-18 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 87.53 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 305 RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQGSIWISPSA-NVGYLTQEVFDLPL---------DKTPEQ 374
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPALPQpaleyvidgDREYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 375 LFYK--------------------ETFEA---RGNVQSLMKHLGFTAAQWTEPIGKMSMGERVKCKLMAFILEEKDVLIL 431
Cdd:PRK10636 94 LEAQlhdanerndghaiatihgklDAIDAwtiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494651374 432 DEPTNHLDLPSREQLEDTLARYDGTLIIVSHDRYFVEKTTDIRLDISNGSV 482
Cdd:PRK10636 174 DEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSL 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
288-463 |
5.34e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.99 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 288 AGKRFLEVRDAAKSY----DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI------SPSANV 356
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPtSGEVLVdgkpvtGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 357 GYLTQE--------VFD-----LPLDKTPEQlfyketfEARGNVQSLMKHLGFTAAQWTEPiGKMSMGERVKCKLM-AFI 422
Cdd:COG1116 83 GVVFQEpallpwltVLDnvalgLELRGVPKA-------ERRERARELLELVGLAGFEDAYP-HQLSGGMRQRVAIArALA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494651374 423 LeEKDVLILDEPTNHLDLPSREQLEDTLAR----YDGTLIIVSHD 463
Cdd:COG1116 155 N-DPEVLLMDEPFGALDALTRERLQDELLRlwqeTGKTVLFVTHD 198
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
293-485 |
6.23e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 82.33 E-value: 6.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVIL-------GQEKAQGS-IWISPSANVGYLTQEVF 364
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILgiilpdsGEVLFDGKpLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 365 DLPLDKTPEQLFY--------KEtfEARGNVQSLMKHLGFTaAQWTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTN 436
Cdd:cd03269 81 LYPKMKVIDQLVYlaqlkglkKE--EARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494651374 437 HLDLPSREQLED---TLARYDGTLIIVSHDRYFVEKTTDIRLDISNGSVRKQ 485
Cdd:cd03269 158 GLDPVNVELLKDvirELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
293-464 |
8.48e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 84.81 E-value: 8.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSI---------WISPSA-NVGYLTQ 361
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPdSGRIvlngrdlftNLPPRErRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 362 E--------VFD-----LPLDKTPEQlfyketfEARGNVQSLMK--HLgftaaqwtEPIGK-----MSMGE--RVKcklM 419
Cdd:COG1118 83 HyalfphmtVAEniafgLRVRPPSKA-------EIRARVEELLElvQL--------EGLADrypsqLSGGQrqRVA---L 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494651374 420 AFILE-EKDVLILDEPTNHLDLPSREQLE----DTLARYDGTLIIVSHDR 464
Cdd:COG1118 145 ARALAvEPEVLLLDEPFGALDAKVRKELRrwlrRLHDELGGTTVFVTHDQ 194
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-171 |
1.68e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 82.06 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 1 MKEMLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM------QDVNI-YmVE 73
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFgkpprrARRRIgY-VP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 74 QeTEAYDSGHP--------------------------EPAEAAL-----LEKWNvpaRAFSQLSGGEKLKARLAKGFSSS 122
Cdd:COG1121 82 Q-RAEVDWDFPitvrdvvlmgrygrrglfrrpsradrEAVDEALervglEDLAD---RPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494651374 123 SSLLLLDEPTNHLDQHSLEI---LLNQIKNYKGTIIFVSHDRAFIDAAATKI 171
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEAlyeLLRELRREGKTILVVTHDLGAVREYFDRV 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
293-464 |
4.97e-17 |
|
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: 83.88 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRT-LFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ-EKAQGSIWI--------SPSA---NVGYL 359
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFvDPTEGSIAVngvpladaDADSwrdQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQEVFDLP-----------LDKTPEQLfyKETFEARGnVQSLMKHLGftaAQWTEPIGK----MSMGERVKCKLMAFILE 424
Cdd:TIGR02857 402 PQHPFLFAgtiaenirlarPDASDAEI--REALERAG-LDEFVAALP---QGLDTPIGEggagLSGGQAQRLALARAFLR 475
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494651374 425 EKDVLILDEPTNHLDLPSREQLEDTLARYDG--TLIIVSHDR 464
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL 517
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-160 |
5.31e-17 |
|
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: 79.88 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 6 KISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI------QMMQDVNIYMVEQETEAy 79
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrvfgkpLEKERKRIGYVPQRRSI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 80 DSGHP--------------------------EPAEAAL-----LEKWNvpaRAFSQLSGGEKLKARLAKGFSSSSSLLLL 128
Cdd:cd03235 80 DRDFPisvrdvvlmglyghkglfrrlskadkAKVDEALervglSELAD---RQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190
....*....|....*....|....*....|....*
gi 494651374 129 DEPTNHLDQHSLEI---LLNQIKNYKGTIIFVSHD 160
Cdd:cd03235 157 DEPFAGVDPKTQEDiyeLLRELRREGMTILVVTHD 191
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
293-472 |
6.41e-17 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 79.86 E-value: 6.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLF----KNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWISP--------------S 353
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKpTSGSIIFDGkdllklsrrlrkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 354 ANVGYLTQE---VFDlPLDKTPEQLfyKETFEARGNVQS----------LMKHLGFTAAQWTEPIGKMSMGE--RVkCKL 418
Cdd:cd03257 82 KEIQMVFQDpmsSLN-PRMTIGEQI--AEPLRIHGKLSKkearkeavllLLVGVGLPEEVLNRYPHELSGGQrqRV-AIA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 419 MAFILEEKdVLILDEPTNHLDLPSREQLEDTL----ARYDGTLIIVSHDRYFVEKTTD 472
Cdd:cd03257 158 RALALNPK-LLIADEPTSALDVSVQAQILDLLkklqEELGLTLLFITHDLGVVAKIAD 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
293-463 |
9.59e-17 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 79.44 E-value: 9.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGR----TLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWIS------PSANVGYLTQ 361
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTsGEVLVDgepvtgPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 362 E--------VFD---LPLD--KTPEQlfyketfEARGNVQSLMKHLGFTAAQWTEPiGKMS--MGERVkCKLMAFILeEK 426
Cdd:cd03293 81 QdallpwltVLDnvaLGLElqGVPKA-------EARERAEELLELVGLSGFENAYP-HQLSggMRQRV-ALARALAV-DP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 494651374 427 DVLILDEPTNHLDLPSREQLEDTLAR----YDGTLIIVSHD 463
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDiwreTGKTVLLVTHD 191
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-179 |
1.27e-16 |
|
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: 77.44 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMqdvNIYMVEQETEAydSGH- 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL---GKDIKKEPEEV--KRRi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 84 ---PEpaEAALLEKWNVpaRAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYK---GTIIFV 157
Cdd:cd03230 76 gylPE--EPSLYENLTV--RENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLS 151
|
170 180
....*....|....*....|..
gi 494651374 158 SHDRAFIDAAATKIWAIEGKKL 179
Cdd:cd03230 152 SHILEEAERLCDRVAILNNGRI 173
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
293-497 |
3.13e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 77.79 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSY-DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI--------SPSA------NV 356
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPtSGQVLVngqdlsrlKRREipylrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 357 GYLTQE--------VFD---LPLdktpeQLFYKETFEARGNVQSLMKHLGFTAAQWTEPIgKMSMGE--RVkcklmAF-- 421
Cdd:COG2884 82 GVVFQDfrllpdrtVYEnvaLPL-----RVTGKSRKEIRRRVREVLDLVGLSDKAKALPH-ELSGGEqqRV-----AIar 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 422 -ILEEKDVLILDEPTNHLDlP--SRE--QLEDTLARYDGTLIIVSHDRYFVEKTTDIRLDISNGSVrkqwkespsVRDDA 496
Cdd:COG2884 151 aLVNRPELLLADEPTGNLD-PetSWEimELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL---------VRDEA 220
|
.
gi 494651374 497 E 497
Cdd:COG2884 221 R 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-472 |
5.82e-16 |
|
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: 80.62 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLI--CNQKAPSQGQIqmmqdvnIY------------ 70
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRI-------IYhvalcekcgyve 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 71 ---------------MVEQETEAYDSGHPE-------------------------------------PAEAA------LL 92
Cdd:TIGR03269 74 rpskvgepcpvcggtLEPEEVDFWNLSDKLrrrirkriaimlqrtfalygddtvldnvlealeeigyEGKEAvgravdLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 93 EKWNVPARAF---SQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEI----LLNQIKNYKGTIIFVSHDRAFID 165
Cdd:TIGR03269 154 EMVQLSHRIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 166 AAATK-IWAIEGKkliehkgnyssymevrkqrrltqqreyenqqhmirrieaqmnelsawskkahaqstkiegfkeyhrV 244
Cdd:TIGR03269 234 DLSDKaIWLENGE------------------------------------------------------------------I 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 245 KAKRTDAQIKSKQKRLEKELEKAKaepveaEYEVRFSIEHRKKAGKRFLEV-RDAAKSYDgrtlfkNVNFTVMHGEKIAI 323
Cdd:TIGR03269 248 KEEGTPDEVVAVFMEGVSEVEKEC------EVEVGEPIIKVRNVSKRYISVdRGVVKAVD------NVSLEVKEGEIFGI 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 324 TGPNGSGKTTLLKVILG-QEKAQGSIWI------------------SPSANVGYLTQEVFDLP----LDKTPEQLFYKET 380
Cdd:TIGR03269 316 VGTSGAGKTTLSKIIAGvLEPTSGEVNVrvgdewvdmtkpgpdgrgRAKRYIGILHQEYDLYPhrtvLDNLTEAIGLELP 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 381 FE-ARGNVQSLMKHLGFTAAQWTEPIGK----MSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTL--AR- 452
Cdd:TIGR03269 396 DElARMKAVITLKMVGFDEEKAEEILDKypdeLSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkARe 475
|
570 580
....*....|....*....|.
gi 494651374 453 -YDGTLIIVSHDRYFVEKTTD 472
Cdd:TIGR03269 476 eMEQTFIIVSHDMDFVLDVCD 496
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
293-463 |
6.69e-16 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 77.16 E-value: 6.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWI--------SPSA------NVG 357
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIdgedisglSEAElyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 358 YLTQE--------VFD---LPLDktpEQLFYKETfEARGNVQSLMKHLGFTAAQWTEPiGKMS--MGERVkcklmAF--- 421
Cdd:cd03261 81 MLFQSgalfdsltVFEnvaFPLR---EHTRLSEE-EIREIVLEKLEAVGLRGAEDLYP-AELSggMKKRV-----ALara 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494651374 422 ILEEKDVLILDEPTNHLDLPSREQLEDTLAR----YDGTLIIVSHD 463
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSlkkeLGLTSIMVTHD 196
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
293-462 |
7.88e-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: 75.99 E-value: 7.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWISPSAnvgyltqevFDLPLDKT 371
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGlSPPLAGRVLLNGGP---------LDFQRDSI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 372 PEQLFY-------KETFEARGNVQsLMKHLGFTAAQWTE------------PIGKMSMGERVKCKLMAFILEEKDVLILD 432
Cdd:cd03231 72 ARGLLYlghapgiKTTLSVLENLR-FWHADHSDEQVEEAlarvglngfedrPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190
....*....|....*....|....*....|...
gi 494651374 433 EPTNHLDLPSREQLEDTLARY---DGTLIIVSH 462
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
293-485 |
1.00e-15 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 75.04 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDG--RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWISP----------SANVGYL 359
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPqQGEITLDGvpvsdlekalSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQEVFdlpldktpeqLFyketfeargnVQSLMKHLGftaaqwtepiGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLD 439
Cdd:cd03247 81 NQRPY----------LF----------DTTLRNNLG----------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494651374 440 LPSREQLEDTLARY--DGTLIIVSHDRYFVEKTTDIrLDISNGSVRKQ 485
Cdd:cd03247 131 PITERQLLSLIFEVlkDKTLIWITHHLTGIEHMDKI-LFLENGKIIMQ 177
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
293-462 |
1.30e-15 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 74.56 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDG--RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWI--------SPSA---NVGY 358
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGlLRPTSGRVRLdgadisqwDPNElgdHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 359 LTQEVfdlpldktpeQLFyketfeaRGNVqslmkhlgftaaqwTEPIgkMSMGERVKCKLMAFILEEKDVLILDEPTNHL 438
Cdd:cd03246 81 LPQDD----------ELF-------SGSI--------------AENI--LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180
....*....|....*....|....*..
gi 494651374 439 DLPSREQLEDTLAR---YDGTLIIVSH 462
Cdd:cd03246 128 DVEGERALNQAIAAlkaAGATRIVIAH 154
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
293-462 |
1.71e-15 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 74.00 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWISpsanvgylTQEV-FDLPLDk 370
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPdSGEILVD--------GKEVsFASPRD- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 371 tpeqlfyketfeargnvqslMKHLG-FTAAQwtepigkMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDT 449
Cdd:cd03216 72 --------------------ARRAGiAMVYQ-------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKV 124
|
170
....*....|....*.
gi 494651374 450 LARY--DG-TLIIVSH 462
Cdd:cd03216 125 IRRLraQGvAVIFISH 140
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
243-463 |
2.07e-15 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 78.94 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 243 RVKAKRTDAQIKSKQKRLEKELEKAKAEPVEAEYevrfsiehrkkagkrfLEVRDAAKSYDG-RTLFKNVNFTVMHGEKI 321
Cdd:TIGR02868 301 RAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPT----------------LELRDLSAGYPGaPPVLDGVSLDLPPGERV 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 322 AITGPNGSGKTTLLKVILG-QEKAQGSIWIS-----------PSANVGYLTQE--VFDLPL---------DKTPEQLFyk 378
Cdd:TIGR02868 365 AILGPSGSGKSTLLATLAGlLDPLQGEVTLDgvpvssldqdeVRRRVSVCAQDahLFDTTVrenlrlarpDATDEELW-- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 379 ETFEARGnvqsLMKHLGFTAAQWTEPIGKM----SMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQ-LEDTLARY 453
Cdd:TIGR02868 443 AALERVG----LADWLRALPDGLDTVLGEGgarlSGGERQRLALARALLADAPILLLDEPTEHLDAETADElLEDLLAAL 518
|
250
....*....|.
gi 494651374 454 DG-TLIIVSHD 463
Cdd:TIGR02868 519 SGrTVVLITHH 529
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
293-462 |
3.32e-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: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK---AQGSIWispsanvgYLTQEVFDLPLD 369
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyevTEGEIL--------FKGEDITDLPPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 370 ktpEQ------LFYKETFEARG-NVQSLMKHL--GFtaaqwtepigkmSMGERVKCKLMAFILEEKDVLILDEPTNHLDL 440
Cdd:cd03217 73 ---ERarlgifLAFQYPPEIPGvKNADFLRYVneGF------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180
....*....|....*....|....*
gi 494651374 441 PSREQLEDTLARY---DGTLIIVSH 462
Cdd:cd03217 138 DALRLVAEVINKLreeGKSVLIITH 162
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
293-463 |
3.93e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 74.69 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYD----GRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI--------SPSA----- 354
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVLIdgqdisslSERElarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 355 --NVGY----------LTqeVFD---LPL--DKTPEQlfyketfEARGNVQSLMKHLGFtAAQWTEPIGKMSMGE--RVk 415
Cdd:COG1136 85 rrHIGFvfqffnllpeLT--ALEnvaLPLllAGVSRK-------ERRERARELLERVGL-GDRLDHRPSQLSGGQqqRV- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494651374 416 cklmAF---ILEEKDVLILDEPTNHLDLPSREQLED---TLARYDG-TLIIVSHD 463
Cdd:COG1136 154 ----AIaraLVNRPKLILADEPTGNLDSKTGEEVLEllrELNRELGtTIVMVTHD 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
300-486 |
4.52e-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: 74.25 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 300 KSYDGRTLfkNVNFTVmHGEKIAITGPNGSGKTTLLKVILGQEKA-------QGSIWISPSAN---------VGYLTQE- 362
Cdd:cd03297 8 KRLPDFTL--KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPdggtivlNGTVLFDSRKKinlppqqrkIGLVFQQy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 363 ------------VFDLPLDKTPEQLFYKETFEARGNVQSLMKhlgftaaqwtEPIGKMSMGERVKCKLMAFILEEKDVLI 430
Cdd:cd03297 85 alfphlnvrenlAFGLKRKRNREDRISVDELLDLLGLDHLLN----------RYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 431 LDEPTNHLDLPSREQ----LEDTLARYDGTLIIVSHDRYFVEKTTDIRLDISNGSVRKQW 486
Cdd:cd03297 155 LDEPFSALDRALRLQllpeLKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
293-463 |
5.50e-15 |
|
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: 74.63 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWI--------SPSA------NVG 357
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDsGEILVdgqditglSEKElyelrrRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 358 YLTQE--------VFD---LPLD---KTPEQlfyketfEARGNVQSLMKHLGFTAAqwtepIGKM----S--MGERVkck 417
Cdd:COG1127 86 MLFQGgalfdsltVFEnvaFPLRehtDLSEA-------EIRELVLEKLELVGLPGA-----ADKMpselSggMRKRV--- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494651374 418 lmAF----ILEEKdVLILDEPTNHLDlP--SR---EQLEDTLARYDGTLIIVSHD 463
Cdd:COG1127 151 --ALaralALDPE-ILLYDEPTAGLD-PitSAvidELIRELRDELGLTSVVVTHD 201
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
301-482 |
6.32e-15 |
|
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: 73.35 E-value: 6.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 301 SYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ---EKAQGSIWI--------SPSANVGYLTQEvfdlplD 369
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtgLGVSGEVLIngrpldkrSFRKIIGYVPQD------D 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 370 KTPEQLFYKETfeargnvqslmkhLGFTAAqwtepIGKMSMGER----VKCKLmafiLEEKDVLILDEPTNHLDLPSREQ 445
Cdd:cd03213 92 ILHPTLTVRET-------------LMFAAK-----LRGLSGGERkrvsIALEL----VSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 494651374 446 LEDTLARY--DGTLIIVS-HD-RYFVEKTTDIRLDISNGSV 482
Cdd:cd03213 150 VMSLLRRLadTGRTIICSiHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-175 |
6.91e-15 |
|
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: 73.66 E-value: 6.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 11 SYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM-MQDVN----------IYMVEQETEA- 78
Cdd:cd03225 8 SYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLTklslkelrrkVGLVFQNPDDq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 79 ------YD--------SGHPEP-----AEAAL-------LEKWNVparafSQLSGGEKLKARLAkG----------Fsss 122
Cdd:cd03225 88 ffgptvEEevafglenLGLPEEeieerVEEALelvglegLRDRSP-----FTLSGGQKQRVAIA-GvlamdpdillL--- 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494651374 123 ssllllDEPTNHLDQHSLEILLNQIKNYKG---TIIFVSHDRAFIDAAATKIWAIE 175
Cdd:cd03225 159 ------DEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLE 208
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
293-463 |
7.57e-15 |
|
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: 74.01 E-value: 7.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGR----TLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWISP--------------- 352
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPtSGTVRLAGqdlfaldedararlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 353 SANVGYLTQEvFDL------------PLdktpeqlfyketfEARGnvqslMKHLGFTAAQWTEPIG----------KMSM 410
Cdd:COG4181 89 ARHVGFVFQS-FQLlptltalenvmlPL-------------ELAG-----RRDARARARALLERVGlghrldhypaQLSG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494651374 411 GE--RVkcklM---AFILEEKdVLILDEPTNHLDLPSREQLEDTL----ARYDGTLIIVSHD 463
Cdd:COG4181 150 GEqqRV----AlarAFATEPA-ILFADEPTGNLDAATGEQIIDLLfelnRERGTTLVLVTHD 206
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
293-461 |
7.57e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.15 E-value: 7.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI-------SPSANVGYLTQE-- 362
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPdSGEVLWdgepldpEDRRRIGYLPEErg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 363 ------VFdlpldktpEQLFYketF---------EARGNVQSLMKHLGFtAAQWTEPIGKMSMGERVKCKLMAFILEEKD 427
Cdd:COG4152 82 lypkmkVG--------EQLVY---LarlkglskaEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 494651374 428 VLILDEPTNHLDLPSREQLEDTLARY--DGTLIIVS 461
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELaaKGTTVIFS 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
309-463 |
9.55e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.12 E-value: 9.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 309 KNVNFTVMHGEKIAITGPNGSGKTTLLKVILGqekaqgsIwISPSA-NV---GYLTQE-----------VF--------D 365
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTG-------I-LVPTSgEVrvlGYVPFKrrkefarrigvVFgqrsqlwwD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 366 LPLdktpeqlfyKETF------------EARGNVQSLMKHLGFtAAQWTEPIGKMSMGERVKCKLMAFILEEKDVLILDE 433
Cdd:COG4586 111 LPA---------IDSFrllkaiyripdaEYKKRLDELVELLDL-GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDE 180
|
170 180 190
....*....|....*....|....*....|....
gi 494651374 434 PTNHLDLPSREQLEDTL----ARYDGTLIIVSHD 463
Cdd:COG4586 181 PTIGLDVVSKEAIREFLkeynRERGTTILLTSHD 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-181 |
1.16e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 73.16 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYE-INSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDV-------------N 68
Cdd:COG2884 1 MIRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgQDLsrlkrreipylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 69 IYMVEQE-------TeAYD--------SGHPePAEA-----ALLEKWNVPARAFS---QLSGGEKLK---AR-------- 114
Cdd:COG2884 81 IGVVFQDfrllpdrT-VYEnvalplrvTGKS-RKEIrrrvrEVLDLVGLSDKAKAlphELSGGEQQRvaiARalvnrpel 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494651374 115 -LAkgfsssssllllDEPTNHLD-QHSLEI--LLNQIkNYKG-TIIFVSHDRAFIDAAATKIWAIEGKKLIE 181
Cdd:COG2884 159 lLA------------DEPTGNLDpETSWEImeLLEEI-NRRGtTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
303-479 |
2.27e-14 |
|
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: 71.03 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 303 DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWISPSANVGYLTQEVFdLPLDKTPEQLFYKetf 381
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGlWPWGSGRIGMPEGEDLLFLPQRPY-LPLGTLREQLIYP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 382 eargnvqslmkhlgftaaqWTEpigKMSMGERvkcKLMAF---ILEEKDVLILDEPTNHLDLPSREQLEDTLARYDGTLI 458
Cdd:cd03223 88 -------------------WDD---VLSGGEQ---QRLAFarlLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVI 142
|
170 180
....*....|....*....|.
gi 494651374 459 IVSHdRYFVEKTTDIRLDISN 479
Cdd:cd03223 143 SVGH-RPSLWKFHDRVLDLDG 162
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-179 |
2.29e-14 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 72.06 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 15 NSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDVN-------------IYMVEQETE--- 77
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgQDVSdlrgraipylrrkIGVVFQDFRllp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 78 ---AYD--------SGHPePAE-----AALLEKWNVP--ARAF-SQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLD-Q 137
Cdd:cd03292 92 drnVYEnvafalevTGVP-PREirkrvPAALELVGLShkHRALpAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDpD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494651374 138 HSLEI--LLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKL 179
Cdd:cd03292 171 TTWEImnLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
293-469 |
2.32e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.07 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWIS----PS------ANVGYLTQ 361
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGlTHPDAGSISLCgepvPSrarharQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 362 evFDlPLDktPEqlfyketFEARGNVQSLMKHLGFTAAQWTE-----------------PIGKMSMGERVKCKLMAFILE 424
Cdd:PRK13537 88 --FD-NLD--PD-------FTVRENLLVFGRYFGLSAAAARAlvppllefaklenkadaKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494651374 425 EKDVLILDEPTNHLDLPSR----EQLEDTLARyDGTLIIVSHdryFVEK 469
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARhlmwERLRSLLAR-GKTILLTTH---FMEE 200
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
292-464 |
2.42e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 74.36 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 292 FLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI--------SPSA-NVGYLTQ 361
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPdSGRILLdgrdvtglPPEKrNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 362 E--------VFD-----LPLDKTPEQlfyketfEARGNVQSLMKHLGFTA------AQwtepigkMSMGE--RVkcklmA 420
Cdd:COG3842 85 DyalfphltVAEnvafgLRMRGVPKA-------EIRARVAELLELVGLEGladrypHQ-------LSGGQqqRV-----A 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494651374 421 F---ILEEKDVLILDEPTNHLDLPSREQLEDTLARY----DGTLIIVSHDR 464
Cdd:COG3842 146 LaraLAPEPRVLLLDEPLSALDAKLREEMREELRRLqrelGITFIYVTHDQ 196
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
5-160 |
3.01e-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: 72.92 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDVN----------IYMVE 73
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAgVDLHglsrrararrVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 74 QETE----------------------AYDSGHPEPAEAALL---EKWNVPARAFSQLSGGEKLKARLAKGFSSSSSLLLL 128
Cdd:TIGR03873 82 QDSDtavpltvrdvvalgriphrslwAGDSPHDAAVVDRALartELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 494651374 129 DEPTNHLD---QHSLEILLNQIKNYKGTIIFVSHD 160
Cdd:TIGR03873 162 DEPTNHLDvraQLETLALVRELAATGVTVVAALHD 196
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-160 |
5.17e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.11 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 3 EMLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQ-------------------- 62
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngrpladwspaelarrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 63 MMQDVNI---YMVEQETE--AYDSGHPEPAEAALLEKW----NVPA---RAFSQLSGGEKLKARLAKGFSSSSSLLLL-- 128
Cdd:PRK13548 81 LPQHSSLsfpFTVEEVVAmgRAPHGLSRAEDDALVAAAlaqvDLAHlagRDYPQLSGGEQQRVQLARVLAQLWEPDGPpr 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 494651374 129 ----DEPTNHLD----QHSLEILLNQIKNYKGTIIFVSHD 160
Cdd:PRK13548 161 wlllDEPTSALDlahqHHVLRLARQLAHERGLAVIVVLHD 200
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-180 |
6.37e-14 |
|
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: 70.75 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 7 ISGISYEINSVP-LFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM-----------------MQDVN 68
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLngkpikakerrksigyvMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 69 --IYMVEQETEAY----DSGHPEPAEAALLEKWNVPARA----FSqLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQH 138
Cdd:cd03226 82 yqLFTDSVREELLlglkELDAGNEQAETVLKDLDLYALKerhpLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494651374 139 SLEI---LLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKLI 180
Cdd:cd03226 161 NMERvgeLIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
293-462 |
9.35e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.29 E-value: 9.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWISPSanvgyltqevfDLPLDKT 371
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGlLPPAAGTIKLDGG-----------DIDDPDV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 372 PEQLFY-------KETFEARGNVQSLMKHLGFTAAQWTE-------------PIGKMSMGERVKCKLMAFILEEKDVLIL 431
Cdd:PRK13539 72 AEACHYlghrnamKPALTVAENLEFWAAFLGGEELDIAAaleavglaplahlPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 494651374 432 DEPTNHLDLPSREQLEDTLARY---DGTLIIVSH 462
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRAHlaqGGIVIAATH 185
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
293-463 |
9.69e-14 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 70.83 E-value: 9.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWIS---------PSANVGYLTQE 362
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdSGTILFGgedatdvpvQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 363 --------VFD---LPLDKTPEQLFYKETfEARGNVQSLMKHLGFTAAQWTEPiGKMSMGERVKCKLMAFILEEKDVLIL 431
Cdd:cd03296 83 yalfrhmtVFDnvaFGLRVKPRSERPPEA-EIRAKVHELLKLVQLDWLADRYP-AQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 494651374 432 DEPTNHLDLPSREQLEDTLAR-YDG---TLIIVSHD 463
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRlHDElhvTTVFVTHD 196
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-191 |
1.12e-13 |
|
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: 73.71 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 11 SYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM----MQDVNIY-------MVEQETEA- 78
Cdd:COG2274 482 RYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidLRQIDPAslrrqigVVLQDVFLf 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 79 YDS-------GHPEPAEAALLEKwnvpARAF---------------------SQLSGGEKLK---AR-LAKG-----Fss 121
Cdd:COG2274 562 SGTirenitlGDPDATDEEIIEA----ARLAglhdfiealpmgydtvvgeggSNLSGGQRQRlaiARaLLRNpriliL-- 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494651374 122 sssllllDEPTNHLDQHSLEILLNQIKNYKG--TIIFVSHDRAFIdAAATKIWAIEGKKLIEHkGNYSSYME 191
Cdd:COG2274 636 -------DEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTI-RLADRIIVLDKGRIVED-GTHEELLA 698
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
293-472 |
1.12e-13 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 70.25 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWI------SPSANVGYLTQEV-- 363
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDsGTIIIdglkltDDKKNINELRQKVgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 364 ----FDLPLDKT--------PEQLFYKETFEARGNVQSLMKHLGFtAAQWTEPIGKMSMGE--RVK-CKLMAFileEKDV 428
Cdd:cd03262 81 vfqqFNLFPHLTvlenitlaPIKVKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQqqRVAiARALAM---NPKV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494651374 429 LILDEPTNHLDLPSREQLEDT---LARYDGTLIIVSHDRYFVEKTTD 472
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVmkdLAEEGMTMVVVTHEMGFAREVAD 203
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-175 |
1.16e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 70.54 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 1 MKEMLKISGIS-----YEINSV--PLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVN----- 68
Cdd:COG4778 1 MTTLLEVENLSktftlHLQGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGwvdla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 69 ------IYMVEQETEAYDS----------------------GHPEpAEA-----ALLEKWNVPARAFS----QLSGGEKL 111
Cdd:COG4778 81 qaspreILALRRRTIGYVSqflrviprvsaldvvaepllerGVDR-EEArararELLARLNLPERLWDlppaTFSGGEQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494651374 112 KARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYK--GT-IIFVSHDRAFIDAAATKIWAIE 175
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKarGTaIIGIFHDEEVREAVADRVVDVT 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
293-463 |
1.39e-13 |
|
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: 70.54 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIW--------ISPSANVGY----- 358
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPtSGSVLfdgeditgLPPHEIARLgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 359 --LTQEVFDLP-LD--KTPEQLFYKETF----------EARGNVQSLMKHLGFtAAQWTEPIGKMSMGERvkcKL----M 419
Cdd:cd03219 81 fqIPRLFPELTvLEnvMVAAQARTGSGLllararreerEARERAEELLERVGL-ADLADRPAGELSYGQQ---RRleiaR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494651374 420 AFILEEKdVLILDEPTNHLDLPSREQLED---TLARYDGTLIIVSHD 463
Cdd:cd03219 157 ALATDPK-LLLLDEPAAGLNPEETEELAElirELRERGITVLLVEHD 202
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
293-484 |
1.39e-13 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 70.09 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWISP----------SANVGYLTQ 361
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPtSGRATVAGhdvvreprevRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 362 evfDLPLDktpEQLFYKETF------------EARGNVQSLMKHLGFTAAQwTEPIGKMSMGERVKCKLMAFILEEKDVL 429
Cdd:cd03265 81 ---DLSVD---DELTGWENLyiharlygvpgaERRERIDELLDFVGLLEAA-DRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494651374 430 ILDEPTNHLDLPSREQL----EDTLARYDGTLIIVSHDRYFVEKTTDIRLDISNGSVRK 484
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVweyiEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIA 212
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-275 |
1.50e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 73.28 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNI-YMVEQETE---AY 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLgYFAQHQLEflrAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 80 DS--GH-----PEPAEAALLE----------KWNVPARAFSqlsGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEI 142
Cdd:PRK10636 392 ESplQHlarlaPQELEQKLRDylggfgfqgdKVTEETRRFS---GGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 143 LLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKLIEHKGNYSSYmevrkQRRLTQQREYENQQhmirriEAQMNELS 222
Cdd:PRK10636 469 LTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY-----QQWLSDVQKQENQT------DEAPKENN 537
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 494651374 223 AWSKKAHaqstkiegfKEYHRVKAK-RTDAQIKSKQ-KRLEKELEKAKAEPVEAE 275
Cdd:PRK10636 538 ANSAQAR---------KDQKRREAElRTQTQPLRKEiARLEKEMEKLNAQLAQAE 583
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-159 |
1.54e-13 |
|
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: 68.61 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIqmmqdvniyMVEQETEAYDSghp 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI---------LVDGKEVSFAS--- 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 85 ePAEAallekWNVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYKG---TIIFVSH 159
Cdd:cd03216 69 -PRDA-----RRAGIAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
293-463 |
1.63e-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: 69.59 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI--------SPSA-NVGYLTQE 362
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPtSGRIYIggrdvtdlPPKDrDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 363 --------VFD-----LPLDKTPeqlfyKETFEARgnVQSLMKHLGFTAAQWTEPiGKMSMGERVKCKLMAFILEEKDVL 429
Cdd:cd03301 81 yalyphmtVYDniafgLKLRKVP-----KDEIDER--VREVAELLQIEHLLDRKP-KQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 494651374 430 ILDEPTNHLD----LPSREQLEDTLARYDGTLIIVSHD 463
Cdd:cd03301 153 LMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-181 |
1.65e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 70.07 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 1 MKEMLKISGISYEI----NSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDV-------- 67
Cdd:COG1136 1 MSPLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgQDIsslserel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 68 ------NIYMVEQ------ETEAYD--------SGHP--EPAEAA--LLEKWNVPARAF---SQLSGGEKLK---AR--- 114
Cdd:COG1136 81 arlrrrHIGFVFQffnllpELTALEnvalplllAGVSrkERRERAreLLERVGLGDRLDhrpSQLSGGQQQRvaiARalv 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494651374 115 ------LAkgfsssssllllDEPTNHLDQHS----LEILLNQIKNYKGTIIFVSHDRAfIDAAATKIWAIEGKKLIE 181
Cdd:COG1136 161 nrpkliLA------------DEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLRDGRIVS 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
293-462 |
1.76e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 72.89 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDG-RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ-EKAQGSIWI--------SPSA---NVGYL 359
Cdd:COG1132 340 IEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFyDPTSGRILIdgvdirdlTLESlrrQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQEVFdlpldktpeqLFyKETfeARGNVqsLMKHLGFTAAQWTE--------------------PIG----KMSMGERvk 415
Cdd:COG1132 420 PQDTF----------LF-SGT--IRENI--RYGRPDATDEEVEEaakaaqahefiealpdgydtVVGergvNLSGGQR-- 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494651374 416 cKLMAF---ILEEKDVLILDEPTNHLDLPSREQLEDTLARY--DGTLIIVSH 462
Cdd:COG1132 483 -QRIAIaraLLKDPPILILDEATSALDTETEALIQEALERLmkGRTTIVIAH 533
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
260-481 |
2.01e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.92 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 260 LEKELEKAKAEPVEAEyevrfSIEHRKKAGkrfLEVRDAA-KSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVI 338
Cdd:COG4178 338 FEEALEAADALPEAAS-----RIETSEDGA---LALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 339 LG-QEKAQGSIWISPSANVGYLTQEVFdLPLDKTPEQLFYKETFEARG-----------NVQSLMKHLGfTAAQWTEpig 406
Cdd:COG4178 410 AGlWPYGSGRIARPAGARVLFLPQRPY-LPLGTLREALLYPATAEAFSdaelrealeavGLGHLAERLD-EEADWDQ--- 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 407 KMSMGE--RVkcklmAF---ILEEKDVLILDEPTNHLDLPSREQLEDTLAR--YDGTLIIVSH----DRYFvekttDIRL 475
Cdd:COG4178 485 VLSLGEqqRL-----AFarlLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGHrstlAAFH-----DRVL 554
|
....*.
gi 494651374 476 DISNGS 481
Cdd:COG4178 555 ELTGDG 560
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
293-468 |
2.08e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 70.15 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGrtlFK---NVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIW-------------IspsAN 355
Cdd:COG4674 11 LYVEDLTVSFDG---FKalnDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRpDSGSVLfggtdltgldeheI---AR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 356 VG----------YLTQEVFD-----LPLDKTP-EQLFYKETFEARGNVQSLMK------HLGFTAA-------QWTEpIG 406
Cdd:COG4674 85 LGigrkfqkptvFEELTVFEnlelaLKGDRGVfASLFARLTAEERDRIEEVLEtigltdKADRLAGllshgqkQWLE-IG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494651374 407 kMsmgervkckLMAfilEEKDVLILDEPTNHLDLPSREQ---LEDTLARyDGTLIIVSHDRYFVE 468
Cdd:COG4674 164 -M---------LLA---QDPKLLLLDEPVAGMTDAETERtaeLLKSLAG-KHSVVVVEHDMEFVR 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
293-463 |
2.25e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 71.64 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI--------SPSA-NVGYLTQE 362
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPtSGEILIggrdvtdlPPKDrNIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 363 --------VFD-----LPLDKTPeqlfyKETFEARgnVQSLMKHLGFT------AAQwtepigkMSMGER---------V 414
Cdd:COG3839 84 yalyphmtVYEniafpLKLRKVP-----KAEIDRR--VREAAELLGLEdlldrkPKQ-------LSGGQRqrvalgralV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494651374 415 KcklmafileEKDVLILDEPTNHLDLPSREQLEDTLARY----DGTLIIVSHD 463
Cdd:COG3839 150 R---------EPKVFLLDEPLSNLDAKLRVEMRAEIKRLhrrlGTTTIYVTHD 193
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
172-280 |
2.25e-13 |
|
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: 65.67 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 172 WAIEGKKLIEHKGNYSSYMEVRKQRRLTQQREYENQQHMIRRIEAQMNELSAWSKKAhaqstkiegfkeyhrvkakrtdA 251
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKA----------------------K 58
|
90 100
....*....|....*....|....*....
gi 494651374 252 QIKSKQKRLEKeLEKAKAePVEAEYEVRF 280
Cdd:pfam12848 59 QAQSRIKALEK-MERIEK-PERDKPKLRF 85
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
305-469 |
2.35e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.60 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 305 RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKaqgsiwispsanvGYLTQEVFDLPLDKTPEQLFYKETFEAR 384
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK-------------GTPVAGCVDVPDNQFGREASLIDAIGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 385 GNVQSLMKHLGF----TAAQWTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDlpsREQ-------LEDTLARY 453
Cdd:COG2401 110 GDFKDAVELLNAvglsDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD---RQTakrvarnLQKLARRA 186
|
170
....*....|....*.
gi 494651374 454 DGTLIIVSHdRYFVEK 469
Cdd:COG2401 187 GITLVVATH-HYDVID 201
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-180 |
2.38e-13 |
|
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: 69.67 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEI-NSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQ--------------------M 63
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdgkditkknlrelrrkvglV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 64 MQDVNIYM----VEQETeAY---DSGHPEP-----AEAAL----LEKWnvPARAFSQLSGGEKLKARLAkG--------- 118
Cdd:COG1122 81 FQNPDDQLfaptVEEDV-AFgpeNLGLPREeirerVEEALelvgLEHL--ADRPPHELSGGQKQRVAIA-Gvlamepevl 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494651374 119 -FsssssllllDEPTNHLDQHSLEILLNQIKNYKG---TIIFVSHDRAFIDAAATKIWAIEGKKLI 180
Cdd:COG1122 157 vL---------DEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
293-463 |
2.83e-13 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 69.57 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWIS--PSANVG------------ 357
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPtSGEILLDgkDITNLPphkrpvntvfqn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 358 -----YLTqeVFD-----LPLDKTPEQLFYKETFEARGNVQslMKHLGftaaqwTEPIGKMSMGERVKCKLMAFILEEKD 427
Cdd:cd03300 81 yalfpHLT--VFEniafgLRLKKLPKAEIKERVAEALDLVQ--LEGYA------NRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 494651374 428 VLILDEPTNHLDLPSRE--QLE-DTLARYDG-TLIIVSHD 463
Cdd:cd03300 151 VLLLDEPLGALDLKLRKdmQLElKRLQKELGiTFVFVTHD 190
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
286-464 |
2.92e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.40 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 286 KKAGKRFLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWI-------------- 350
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQpTAGQIMLdgvdlshvppyqrp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 351 -----SPSANVGYLTQE---VFDLPLDKTPeqlfyKETFEARGNVQSLMKHLGFTAAQwtEPiGKMSMGERVKCKLMAFI 422
Cdd:PRK11607 93 inmmfQSYALFPHMTVEqniAFGLKQDKLP-----KAEIASRVNEMLGLVHMQEFAKR--KP-HQLSGGQRQRVALARSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494651374 423 LEEKDVLILDEPTNHLD--LPSREQLE--DTLARYDGTLIIVSHDR 464
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQ 210
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
293-383 |
3.02e-13 |
|
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: 68.65 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDA-----AKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ-EKAQGSIWISPSanVGYLTQE---- 362
Cdd:cd03250 1 ISVEDAsftwdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGElEKLSGSVSVPGS--IAYVSQEpwiq 78
|
90 100
....*....|....*....|....*....
gi 494651374 363 --------VFDLPLDKTpeqlFYKETFEA 383
Cdd:cd03250 79 ngtireniLFGKPFDEE----RYEKVIKA 103
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-167 |
3.23e-13 |
|
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: 67.79 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 11 SYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI----QMMQDV-------NIYMVEQETEAY 79
Cdd:cd03228 9 SYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgVDLRDLdleslrkNIAYVPQDPFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 80 DsghpepaeAALLEkwNVparafsqLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYKG--TIIFV 157
Cdd:cd03228 89 S--------GTIRE--NI-------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVI 151
|
170
....*....|
gi 494651374 158 SHDRAFIDAA 167
Cdd:cd03228 152 AHRLSTIRDA 161
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-179 |
3.35e-13 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 67.63 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGIS--YEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM------------------- 63
Cdd:cd03246 1 LEVENVSfrYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqwdpnelgdhvgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 64 -MQDVNIYmveqeteaydSGhpepaeaALLEkwNVparafsqLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEI 142
Cdd:cd03246 81 lPQDDELF----------SG-------SIAE--NI-------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 494651374 143 LLNQIKNYK---GTIIFVSHDRAFIdAAATKIWAIEGKKL 179
Cdd:cd03246 135 LNQAIAALKaagATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
293-462 |
3.95e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 68.15 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-----------QEKAQGSIWISPSANVGYLTQ 361
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGllrpdsgevrwNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 362 EVFDLPLDKTPEQL-FYKETFE-ARGNVQSLMKHLGFTAAQWTePIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLD 439
Cdd:TIGR01189 81 LPGLKPELSALENLhFWAAIHGgAQRTIEDALAAVGLTGFEDL-PAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180
....*....|....*....|....*.
gi 494651374 440 LPSREQLEDTLARY---DGTLIIVSH 462
Cdd:TIGR01189 160 KAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
276-468 |
4.25e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.76 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 276 YEVRFSI--EHRKKAGKRFLEVRDAAKSYDGRTLfkNVNF-TVMHGEKIAITGPNGSGKTTLLKVILGQEKAQGSiWISP 352
Cdd:PRK13409 322 EPIEFEErpPRDESERETLVEYPDLTKKLGDFSL--EVEGgEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG-EVDP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 353 SANVGYLTQEV---FDLP----LDKTPEQL---FYKETFEARGNVQSLMKHlgftaaqwtePIGKMSMGERVKCKLMAFI 422
Cdd:PRK13409 399 ELKISYKPQYIkpdYDGTvedlLRSITDDLgssYYKSEIIKPLQLERLLDK----------NVKDLSGGELQRVAIAACL 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494651374 423 LEEKDVLILDEPTNHLDLPSREQLEDTLARY----DGTLIIVSHDRYFVE 468
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDVEQRLAVAKAIRRIaeerEATALVVDHDIYMID 518
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
290-461 |
5.07e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 68.55 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 290 KRFLEVRDAAKSYDGrtlfknVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI-------SPSA---NVGY 358
Cdd:cd03266 9 KRFRDVKKTVQAVDG------VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPdAGFATVdgfdvvkEPAEarrRLGF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 359 LTQEVFDLPLDKTPEQLFYKETF------EARGNVQSLMKHLGFtAAQWTEPIGKMSMGERVKCKLMAFILEEKDVLILD 432
Cdd:cd03266 83 VSDSTGLYDRLTARENLEYFAGLyglkgdELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190
....*....|....*....|....*....|.
gi 494651374 433 EPTNHLDLPSREQLEDTLARY--DGTLIIVS 461
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLraLGKCILFS 192
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
293-463 |
5.99e-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: 68.36 E-value: 5.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVI------LGQEKAQGSIWISPSaNVGYLTQEVFDL 366
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndlIPGAPDEGEVLLDGK-DIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 367 ------------PLDKT-------PEQLF-YKETFEARGNVQSLMKhlgfTAAQWTE-----PIGKMSMGERVKCKLMAF 421
Cdd:cd03260 80 rrrvgmvfqkpnPFPGSiydnvayGLRLHgIKLKEELDERVEEALR----KAALWDEvkdrlHALGLSGGQQQRLCLARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494651374 422 ILEEKDVLILDEPTNHLDLPSREQLEDTLARY--DGTLIIVSHD 463
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
292-483 |
6.26e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 70.64 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 292 FLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ-EKAQGSIWIS----PSANVGYLTQEVFDL 366
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTlTPTAGTVLVAgddvEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 367 PLD----------------KTPEQ-LFYKETFEARGNVQSLMKHLGfTAAQWTEPIGKMSMGERVKCKLMAFILEEKDVL 429
Cdd:PRK09536 83 PQDtslsfefdvrqvvemgRTPHRsRFDTWTETDRAAVERAMERTG-VAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494651374 430 ILDEPTNHLDLPSREQ---LEDTLARYDGTLIIVSHDRYFVEKTTDIRLDISNGSVR 483
Cdd:PRK09536 162 LLDEPTASLDINHQVRtleLVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVR 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
293-463 |
6.30e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 67.99 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTV---MHGekiaITGPNGSGKTTLLKVILG-QEKAQGSIWI---SPSAN-------VGY 358
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLgpgMYG----LLGPNGAGKTTLMRILATlTPPSSGTIRIdgqDVLKQpqklrrrIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 359 LTQEVFDLPLDKTPEQLFY--------KETFEARgnVQSLMKHLGFTAAQwTEPIGKMSMGERVKCKLMAFILEEKDVLI 430
Cdd:cd03264 77 LPQEFGVYPNFTVREFLDYiawlkgipSKEVKAR--VDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190
....*....|....*....|....*....|....*
gi 494651374 431 LDEPTNHLDLPSREQLEDTLARY--DGTLIIVSHD 463
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELgeDRIVILSTHI 188
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
289-461 |
6.31e-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: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 289 GKRFLEVRDAAKSydgRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ----EKAQGSIWISPSA--------NV 356
Cdd:cd03234 7 WDVGLKAKNWNKY---ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRveggGTTSGQILFNGQPrkpdqfqkCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 357 GYLTQEVFDLPLDKTPEQLFYKETFEARGN----------VQSLMKHLGFTaaqwtePIGKM-----SMGERVKCKLMAF 421
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLTYTAILRLPRKssdairkkrvEDVLLRDLALT------RIGGNlvkgiSGGERRRVSIAVQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494651374 422 ILEEKDVLILDEPTNHLDLPSREQLEDTLARY--DGTLIIVS 461
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVSTLSQLarRNRIVILT 199
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-160 |
6.74e-13 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 68.17 E-value: 6.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQ-------------------MMQ 65
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvardpaevrrrigyVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 66 DVNIYM---VEQETEAYDSGHPEPAEAA------LLEK---WNVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTN 133
Cdd:COG1131 81 EPALYPdltVRENLRFFARLYGLPRKEArerideLLELfglTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190
....*....|....*....|....*....|
gi 494651374 134 HLDQHSLEILLNQIKNYKG---TIIFVSHD 160
Cdd:COG1131 161 GLDPEARRELWELLRELAAegkTVLLSTHY 190
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-171 |
6.81e-13 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 67.21 E-value: 6.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQmMQDVNIYMVEQETEAydsghP 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL-IDGEDLTDLEDELPP-----L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 85 EPAEAALLEKWNVPAR-------AFSqLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLD---QHSLEILLNQIKNYKG-T 153
Cdd:cd03229 75 RRRIGMVFQDFALFPHltvleniALG-LSGGQQQRVALARALAMDPDVLLLDEPTSALDpitRREVRALLKSLQAQLGiT 153
|
170
....*....|....*...
gi 494651374 154 IIFVSHDRAFIDAAATKI 171
Cdd:cd03229 154 VVLVTHDLDEAARLADRV 171
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
301-472 |
7.10e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 7.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 301 SYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ-EKAQGSIWISPSANVGYLTQEvfdLPLDKT-PeqLFYK 378
Cdd:PRK09544 13 SFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLvAPDEGVIKRNGKLRIGYVPQK---LYLDTTlP--LTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 379 ETFEARGNVQS--LMKHLGFTAAQ--WTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLARYD 454
Cdd:PRK09544 88 RFLRLRPGTKKedILPALKRVQAGhlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLR 167
|
170 180
....*....|....*....|..
gi 494651374 455 GTL----IIVSHDRYFVEKTTD 472
Cdd:PRK09544 168 RELdcavLMVSHDLHLVMAKTD 189
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-168 |
1.27e-12 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 67.16 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDV--------NIYMVEQ- 74
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgRDVtgvpperrNIGMVFQd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 75 ----------ETEAY---DSGHPEP-------AEAALLEKWNVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNH 134
Cdd:cd03259 81 yalfphltvaENIAFglkLRGVPKAeirarvrELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 494651374 135 LDQHSLEILLNQIKNY----KGTIIFVSHDRAfiDAAA 168
Cdd:cd03259 161 LDAKLREELREELKELqrelGITTIYVTHDQE--EALA 196
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-167 |
1.47e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 66.49 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 15 NSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQETEAYDS------------- 81
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSlpltvrdlvamgr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 82 -------GHPEPAEAALLEKW-------NVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQI 147
Cdd:NF040873 83 warrglwRRLTRDDRAAVDDAlervglaDLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALL 162
|
170 180
....*....|....*....|...
gi 494651374 148 KNYKG---TIIFVSHDRAFIDAA 167
Cdd:NF040873 163 AEEHArgaTVVVVTHDLELVRRA 185
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
213-473 |
1.70e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 70.27 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 213 RIEAQMNELSAWSKKAHAQSTKIegFKEYHRVKAKRTDAQiKSKQKRLEKELEKAKAEPVEAEYEVrFSIEHRKKAGK-- 290
Cdd:PLN03073 99 RMSDGMDDSEVAKKKPEPDDGPL--LSERDLAKIERRKRK-EERQREVQYQAHVAEMEAAKAGMPG-VYVNHDGNGGGpa 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 291 -RFLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLK--------------------------------- 336
Cdd:PLN03073 175 iKDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipkncqilhveqevvgddttalqc 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 337 --------VILGQEKAQ-----------GSIWISPSANVGYLTQEVFDLPLDKTPEQLFYKETFEARGNVQSLMKHLGFT 397
Cdd:PLN03073 255 vlntdierTQLLEEEAQlvaqqrelefeTETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFT 334
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494651374 398 AAQWTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLARYDGTLIIVSHDRYFVEK-TTDI 473
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTvVTDI 411
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
293-462 |
1.88e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 69.67 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI--------SPS----ANVGYL 359
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPdSGEILIdgkpvrirSPRdaiaLGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQE--VFD---------LPLDKTPEQLFYKEtfEARGNVQSLMKHLGFtAAQWTEPIGKMSMGER-----VKCklmafIL 423
Cdd:COG3845 86 HQHfmLVPnltvaenivLGLEPTKGGRLDRK--AARARIRELSERYGL-DVDPDAKVEDLSVGEQqrveiLKA-----LY 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494651374 424 EEKDVLILDEPTNHLDLPSREQLEDTLARY--DG-TLIIVSH 462
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITH 199
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-201 |
2.16e-12 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 69.41 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGIS--YEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIqMMQDVNIY------------ 70
Cdd:COG4987 334 LELEDVSfrYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI-TLGGVDLRdldeddlrrria 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 71 MVEQETEAYDS--------GHPEPAEAAL--------LEKWnvpARAF------------SQLSGGEKlkARLAkgfsss 122
Cdd:COG4987 413 VVPQRPHLFDTtlrenlrlARPDATDEELwaalervgLGDW---LAALpdgldtwlgeggRRLSGGER--RRLAlarall 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 123 --ssllllDEPTNHLDQHSLEILLNQIKNY-KG-TIIFVSHDRAFIDaAATKIWAIEGKKLIEhKGNYSSYMEVRKQ-RR 197
Cdd:COG4987 488 rdapilllDEPTEGLDAATEQALLADLLEAlAGrTVLLITHRLAGLE-RMDRILVLEDGRIVE-QGTHEELLAQNGRyRQ 565
|
....
gi 494651374 198 LTQQ 201
Cdd:COG4987 566 LYQR 569
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
314-482 |
2.54e-12 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 66.36 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 314 TVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWI-------SPSAN--VGYLTQE--VF-------DLPLDKTPEq 374
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQsGRVLIngvdvtaAPPADrpVSMLFQEnnLFahltveqNVGLGLSPG- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 375 lfYKETFEARGNVQSLMKHLGFTAAQWTEPiGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLED---TLA 451
Cdd:cd03298 99 --LKLTAEDRQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDlvlDLH 175
|
170 180 190
....*....|....*....|....*....|..
gi 494651374 452 RYDG-TLIIVSHDRYFVEKTTDIRLDISNGSV 482
Cdd:cd03298 176 AETKmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-191 |
2.92e-12 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 69.02 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 10 ISYEiNSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQmmqdVNiymvEQETEAYDS-------- 81
Cdd:COG4988 344 FSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL----IN----GVDLSDLDPaswrrqia 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 82 -------------------GHPEPAEAAL---LEKwnVPARAF----------------SQLSGGEK----LkAR-LAKG 118
Cdd:COG4988 415 wvpqnpylfagtirenlrlGRPDASDEELeaaLEA--AGLDEFvaalpdgldtplgeggRGLSGGQAqrlaL-ARaLLRD 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 119 -----FsssssllllDEPTNHLDQHSLEILLNQIKNYKG--TIIFVSHDRAFIdAAATKIWAIEGKKLIEHkGNYSSYME 191
Cdd:COG4988 492 aplllL---------DEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALL-AQADRILVLDDGRIVEQ-GTHEELLA 560
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-181 |
3.53e-12 |
|
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: 65.03 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 11 SYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMmQDVNIYMVEQETEAYDSGHPEPA--- 87
Cdd:cd03247 9 SYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL-DGVPVSDLEKALSSLISVLNQRPylf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 88 EAALLEkwNVPARafsqLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLD----QHSLEILLNQIKNykGTIIFVSHDRAF 163
Cdd:cd03247 88 DTTLRN--NLGRR----FSGGERQRLALARILLQDAPIVLLDEPTVGLDpiteRQLLSLIFEVLKD--KTLIWITHHLTG 159
|
170
....*....|....*...
gi 494651374 164 IdAAATKIWAIEGKKLIE 181
Cdd:cd03247 160 I-EHMDKILFLENGKIIM 176
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
293-488 |
4.09e-12 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 66.10 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYD-GRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWI-----------SPSANVGYL 359
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRfYDVSSGSILIdgqdirevtldSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQevfDLPL--------------DKTPEQLfyketFEARGNVQSLMKHLGFTAAQWTEpIG----KMSMGERVKCKLMAF 421
Cdd:cd03253 81 PQ---DTVLfndtigynirygrpDATDEEV-----IEAAKAAQIHDKIMRFPDGYDTI-VGerglKLSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 422 ILEEKDVLILDEPTNHLDLPSREQLEDTLAR-----------------YDGTLIIVSHDRYFVEKTTDIRLDISNGSVRK 484
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDvskgrttiviahrlstiVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
....
gi 494651374 485 QWKE 488
Cdd:cd03253 232 MWKA 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
293-463 |
4.46e-12 |
|
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: 66.17 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSY-DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVI--LgQEKAQGSIWI--------SPSA---NVGY 358
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrL-IEPTSGEIFIdgedireqDPVElrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 359 LTQEVFDLP-------------LDKTPeqlfyKETFEARgnVQSLMKHLGFTAAQWTE--PiGKMSMGERVKCKLMAFIL 423
Cdd:cd03295 80 VIQQIGLFPhmtveenialvpkLLKWP-----KEKIRER--ADELLALVGLDPAEFADryP-HELSGGQQQRVGVARALA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494651374 424 EEKDVLILDEPTNHLDLPSREQLEDTLARYD----GTLIIVSHD 463
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQqelgKTIVFVTHD 195
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
293-463 |
6.30e-12 |
|
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: 65.99 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWISPS-----------ANVGYLT 360
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPdAGTVDLAGVdlhglsrraraRRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 361 QEVFDLP---------LDKTPEQ-LFYKETFEARGNVQSLMKHLGFTAAQwTEPIGKMSMGERVKCKLMAFILEEKDVLI 430
Cdd:TIGR03873 82 QDSDTAVpltvrdvvaLGRIPHRsLWAGDSPHDAAVVDRALARTELSHLA-DRDMSTLSGGERQRVHVARALAQEPKLLL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 494651374 431 LDEPTNHLDLpsREQLE-----DTLARYDGTLIIVSHD 463
Cdd:TIGR03873 161 LDEPTNHLDV--RAQLEtlalvRELAATGVTVVAALHD 196
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-181 |
7.31e-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: 65.30 E-value: 7.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYE----INSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDV----------- 67
Cdd:cd03258 1 MIELKNVSKVfgdtGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgTDLtllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 68 --NIYMVEQ-----------ETEAYdsghpePAEAALLEKWNVPARAF----------------SQLSGGEKLKARLAKG 118
Cdd:cd03258 81 rrRIGMIFQhfnllssrtvfENVAL------PLEIAGVPKAEIEERVLellelvgledkadaypAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494651374 119 FSSSSSLLLLDEPTNHLD---QHSLEILLNQIKNYKG-TIIFVSHDRAFIDAAATKIWAIEGKKLIE 181
Cdd:cd03258 155 LANNPKVLLCDEATSALDpetTQSILALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEKGEVVE 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
278-351 |
8.54e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.10 E-value: 8.54e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494651374 278 VRFSIEHRKKAGKRFLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWIS 351
Cdd:COG1134 12 KSYRLYHEPSRSLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPtSGRVEVN 86
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
278-483 |
1.07e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 64.48 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 278 VRFSIEHRKKAGKRFLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI--SPSA 354
Cdd:cd03220 8 KSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPdSGTVTVrgRVSS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 355 ----NVGyltqevFDlpldktPEqlfyketFEARGNVQSLMKHLGFTAAQW-----------------TEPIGKMSMGER 413
Cdd:cd03220 88 llglGGG------FN------PE-------LTGRENIYLNGRLLGLSRKEIdekideiiefselgdfiDLPVKTYSSGMK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494651374 414 VKcklMAF---ILEEKDVLILDEPT----NHLDLPSREQLEDTLARyDGTLIIVSHDRYFVEKTTDIRLDISNGSVR 483
Cdd:cd03220 149 AR---LAFaiaTALEPDILLIDEVLavgdAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-182 |
1.20e-11 |
|
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: 64.45 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEI----NSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQ------------------- 60
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSiifdgkdllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 61 ---IQM-MQD----VNIYMV--EQETEAY-----DSGHPEPAEAALLEKWNVP-----ARAF-SQLSGGEKLKARLAKGF 119
Cdd:cd03257 81 rkeIQMvFQDpmssLNPRMTigEQIAEPLrihgkLSKKEARKEAVLLLLVGVGlpeevLNRYpHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494651374 120 SSSSSLLLLDEPTNHLDQHS----LEILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKLIEH 182
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
293-463 |
1.21e-11 |
|
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: 65.06 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWI--------SPSA--------- 354
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTsGRILFdgrditglPPHRiarlgiart 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 355 --------------NV---------GYLTQEVFDLPLDKTPEQlfyketfEARGNVQSLMKHLGFtAAQWTEPIGKMSMG 411
Cdd:COG0411 85 fqnprlfpeltvleNVlvaaharlgRGLLAALLRLPRARREER-------EARERAEELLERVGL-ADRADEPAGNLSYG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 412 ERvkcKL----MAFILEEKdVLILDEPTNHLDLPSREQLEDT---LARYDG-TLIIVSHD 463
Cdd:COG0411 157 QQ---RRleiaRALATEPK-LLLLDEPAAGLNPEETEELAELirrLRDERGiTILLIEHD 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
293-482 |
1.25e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 64.35 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTL-FKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWIS-------PSANVGYLTQEV 363
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNgqdvsdlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 364 ------FDLPLDKT-------PEQLFYKETFEARGNVQSLMKHLGFTAAQWTEPIGkMSMGERVKCKLMAFILEEKDVLI 430
Cdd:cd03292 81 gvvfqdFRLLPDRNvyenvafALEVTGVPPREIRKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494651374 431 LDEPTNHLDLPSREQLEDTLARYD--GTLIIVS-HDRYFVEKTTDIRLDISNGSV 482
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINkaGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-179 |
1.50e-11 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 64.05 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYE----INSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDV------------ 67
Cdd:cd03255 1 IELKNLSKTygggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgTDIsklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 68 --NIYMVEQETE------AYD--------SGHP--EPAEAA--LLEKWNVPARAF---SQLSGGEKLKARLAKGFSSSSS 124
Cdd:cd03255 81 rrHIGFVFQSFNllpdltALEnvelplllAGVPkkERRERAeeLLERVGLGDRLNhypSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494651374 125 LLLLDEPTNHLDQHS----LEILLNQIKNYKGTIIFVSHDRaFIDAAATKIWAIEGKKL 179
Cdd:cd03255 161 IILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
292-462 |
1.83e-11 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 64.17 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 292 FLEVRDAAKSYD-GRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWI-----------SPSANVGY 358
Cdd:cd03254 2 EIEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfYDPQKGQILIdgidirdisrkSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 359 LTQEVFDLPlDKTPEQLFYKETFEARGNVQSLMKHLGFT----------AAQWTEPIGKMSMGERvkcKLMAF---ILEE 425
Cdd:cd03254 82 VLQDTFLFS-GTIMENIRLGRPNATDEEVIEAAKEAGAHdfimklpngyDTVLGENGGNLSQGER---QLLAIaraMLRD 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 494651374 426 KDVLILDEPTNHLDLPSREQLEDTLARY--DGTLIIVSH 462
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAH 196
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-160 |
2.15e-11 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 64.37 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQ--------------------M 63
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlngrplaawspwelarrravL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 64 MQDVNI---YMVEQ----ETEAYDSGHPEPAEAAL--LEK---WNVPARAFSQLSGGEKLK---AR-LAKGFSSSSSLLL 127
Cdd:COG4559 81 PQHSSLafpFTVEEvvalGRAPHGSSAAQDRQIVReaLALvglAHLAGRSYQTLSGGEQQRvqlARvLAQLWEPVDGGPR 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 494651374 128 L---DEPTNHLD---QHSLEILLNQIKNYKGTIIFVSHD 160
Cdd:COG4559 161 WlflDEPTSALDlahQHAVLRLARQLARRGGGVVAVLHD 199
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-138 |
3.37e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 65.25 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDV-----------NIYMV 72
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvealsaraasrRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 73 EQETE-AYD------------------SGHPEPAEAAL---LEKWNVPA---RAFSQLSGGEKLKARLAKGFSSSSSLLL 127
Cdd:PRK09536 83 PQDTSlSFEfdvrqvvemgrtphrsrfDTWTETDRAAVeraMERTGVAQfadRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170
....*....|.
gi 494651374 128 LDEPTNHLDQH 138
Cdd:PRK09536 163 LDEPTASLDIN 173
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
293-364 |
3.76e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.12 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWIS-------P-----SANVGYL 359
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGRIFLDgedithlPmhkraRLGIGYL 83
|
....*..
gi 494651374 360 TQE--VF 364
Cdd:COG1137 84 PQEasIF 90
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
293-350 |
3.82e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 63.64 E-value: 3.82e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWI 350
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEVRL 61
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
293-464 |
4.13e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.58 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWISpSANVGYLTQE--------- 362
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPdSGRIMLD-GQDITHVPAEnrhvntvfq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 363 ---------VFD-----LPLDKTPEQLFYKETFEARGNVQslMKHLGftaaqwTEPIGKMSMGERVKCKLMAFILEEKDV 428
Cdd:PRK09452 94 syalfphmtVFEnvafgLRMQKTPAAEITPRVMEALRMVQ--LEEFA------QRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 494651374 429 LILDEPTNHLDLPSREQLED---TLARYDG-TLIIVSHDR 464
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNelkALQRKLGiTFVFVTHDQ 205
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-189 |
4.42e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 65.65 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 19 LFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQE-TEAYD-------------SGHP 84
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHhVDGLDlssnpllymmrcfPGVP 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 85 EPAEAALLEKW----NVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYKGTIIFVSHD 160
Cdd:PLN03073 604 EQKLRAHLGSFgvtgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHD 683
|
170 180
....*....|....*....|....*....
gi 494651374 161 RAFIDAAATKIWAIEGKKLIEHKGNYSSY 189
Cdd:PLN03073 684 EHLISGSVDELWVVSEGKVTPFHGTFHDY 712
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-472 |
4.59e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 1 MKEMLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM------------MQDVN 68
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIggnpcarltpakAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 69 IYMVEQETEAYDS---------GHPEPAEA-----ALLEKWNV---PARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEP 131
Cdd:PRK15439 88 IYLVPQEPLLFPNlsvkenilfGLPKRQASmqkmkQLLAALGCqldLDSSAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 132 TNHLDQHSLEILLNQIKNY--KGT-IIFVSHdrafidaaatkiwaiegkKLIEhkgnyssymevrkqrrltqqreyenqq 208
Cdd:PRK15439 168 TASLTPAETERLFSRIRELlaQGVgIVFISH------------------KLPE--------------------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 209 hmIRRIEAQmneLSAWSKKAHAQSTKIEGFKEYHRVKA---KRTDAQIKSKQKrLEKELEKAKaepveaeyevrfsieHR 285
Cdd:PRK15439 203 --IRQLADR---ISVMRDGTIALSGKTADLSTDDIIQAitpAAREKSLSASQK-LWLELPGNR---------------RQ 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 286 KKAGKRFLEVRDAakSYDGrtlFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIW-----ISPSANVGYL 359
Cdd:PRK15439 262 QAAGAPVLTVEDL--TGEG---FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARgGRIMlngkeINALSTAQRL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQEVFDLPLDKTPEQLFyketFEA--RGNVQSLMKH---------------------LGFTAAQWTEPIGKMSMGERVKC 416
Cdd:PRK15439 337 ARGLVYLPEDRQSSGLY----LDAplAWNVCALTHNrrgfwikparenavleryrraLNIKFNHAEQAARTLSGGNQQKV 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 417 kLMAFILE-EKDVLILDEPTNHLDLPSRE---QLEDTLARYDGTLIIVSHDRYFVEKTTD 472
Cdd:PRK15439 413 -LIAKCLEaSPQLLIVDEPTRGVDVSARNdiyQLIRSIAAQNVAVLFISSDLEEIEQMAD 471
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-483 |
6.25e-11 |
|
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: 64.85 E-value: 6.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICN-------------QKAPSQGQ-IQMMQDVNI 69
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywSGSPLKASnIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 70 YMVEQETE-------------AYDSGHPEPAEA---------ALLEKWNVPA----RAFSQLSGGEKLKARLAKGFSSSS 123
Cdd:TIGR02633 81 VIIHQELTlvpelsvaeniflGNEITLPGGRMAynamylrakNLLRELQLDAdnvtRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 124 SLLLLDEPTNHLDQHSLEILLNQIKNYKG---TIIFVSHDRAFIDAAATKIWAIEGKkliEHKGnySSYMEVRKQRRLTQ 200
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDG---QHVA--TKDMSTMSEDDIIT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 201 Q---RE----YENQQHMIRRIEAQMNELSAWskkaHAQSTKIegfkeyhrvkaKRTDaqikskqkrlekelekakaepve 273
Cdd:TIGR02633 236 MmvgREitslYPHEPHEIGDVILEARNLTCW----DVINPHR-----------KRVD----------------------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 274 aeyevrfsiehrkkagkrflevrdaaksydgrtlfkNVNFTVMHGEKIAITGPNGSGKTTLLKVILG--QEKAQGSIWIS 351
Cdd:TIGR02633 278 ------------------------------------DVSFSLRRGEILGVAGLVGAGRTELVQALFGayPGKFEGNVFIN 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 352 ------------------------------PSANVGY------LTQEVFDLPLDKTPEQlfyketfearGNVQSLMKHLG 395
Cdd:TIGR02633 322 gkpvdirnpaqairagiamvpedrkrhgivPILGVGKnitlsvLKSFCFKMRIDAAAEL----------QIIGSAIQRLK 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 396 FTAAQWTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQ---LEDTLARYDGTLIIVSHDRYFVEKTTD 472
Cdd:TIGR02633 392 VKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEiykLINQLAQEGVAIIVVSSELAEVLGLSD 471
|
570
....*....|.
gi 494651374 473 IRLDISNGSVR 483
Cdd:TIGR02633 472 RVLVIGEGKLK 482
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
293-349 |
7.46e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 62.39 E-value: 7.46e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK---AQGSIW 349
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyevTSGSIL 60
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
293-434 |
1.01e-10 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 61.79 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI-------SP-----SANVGYL 359
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGKILLdgqditkLPmhkraRLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQE--VF-DLpldkTPEQ-------LFYKETFEARGNVQSLMKHLGFTAAQwTEPIGKMSMGERVKCKLMAFILEEKDVL 429
Cdd:cd03218 81 PQEasIFrKL----TVEEnilavleIRGLSKKEREEKLEELLEEFHITHLR-KSKASSLSGGERRRVEIARALATNPKFL 155
|
....*
gi 494651374 430 ILDEP 434
Cdd:cd03218 156 LLDEP 160
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
293-462 |
1.25e-10 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 61.48 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSY--DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWI-----------SPSANVGY 358
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRfYDVDSGRILIdghdvrdytlaSLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 359 LTQEVFdLPLDKTPEQLFYKETFEARGNVQSLMKhlgftAAQWTE-----------PIG----KMSMGERVKCKLMAFIL 423
Cdd:cd03251 81 VSQDVF-LFNDTVAENIAYGRPGATREEVEEAAR-----AANAHEfimelpegydtVIGergvKLSGGQRQRIAIARALL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 494651374 424 EEKDVLILDEPTNHLDLPSREQLEDTLARY--DGTLIIVSH 462
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAH 195
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
293-351 |
1.36e-10 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 61.82 E-value: 1.36e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494651374 293 LEVRDAAKSY-DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWIS 351
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlVEPTSGSVLID 61
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
292-340 |
2.12e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.20 E-value: 2.12e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 494651374 292 FLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG 340
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG 49
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-165 |
2.13e-10 |
|
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: 60.68 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI--------QM-MQDV--NIYMVEQET--------EAYDSGH 83
Cdd:cd03245 23 VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirQLdPADLrrNIGYVPQDVtlfygtlrDNITLGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 84 PEPAEAALLEKWNVP-ARAFSQ----------------LSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQ 146
Cdd:cd03245 103 PLADDERILRAAELAgVTDFVNkhpngldlqigergrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKER 182
|
170 180
....*....|....*....|.
gi 494651374 147 IKNYKG--TIIFVSHDRAFID 165
Cdd:cd03245 183 LRQLLGdkTLIIITHRPSLLD 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
275-467 |
2.42e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.88 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 275 EYEVRFSI-EHRK-KAGKRFLEVRDAAKSYDGRTLfkNVNF-TVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSiwI 350
Cdd:COG1245 322 DEPIEFEVhAPRReKEEETLVEYPDLTKSYGGFSL--EVEGgEIREGEVLGIVGPNGIGKTTFAKILAGVLKPdEGE--V 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 351 SPSANVGYLTQEVFDLpLDKTPEQLFYKETFEARGN--VQS-LMKHLGFtaaqwtEPI-----GKMSMGERVKCKLMAFI 422
Cdd:COG1245 398 DEDLKISYKPQYISPD-YDGTVEEFLRSANTDDFGSsyYKTeIIKPLGL------EKLldknvKDLSGGELQRVAIAACL 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494651374 423 LEEKDVLILDEPTNHLDLPSREQLEDTLARY----DGTLIIVSHDRYFV 467
Cdd:COG1245 471 SRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaenrGKTAMVVDHDIYLI 519
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
322-482 |
3.15e-10 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 59.93 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 322 AITGPNGSGKTTL---LKVILGQEKAQGSIW-------ISPSANVGYLTQEvFDLPLDKTpeqlfYKETFEARGNVQSLM 391
Cdd:cd03240 26 LIVGQNGAGKTTIieaLKYALTGELPPNSKGgahdpklIREGEVRAQVKLA-FENANGKK-----YTITRSLAILENVIF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 392 KHLGFTAAQWTEPIGKMSMGERVKCKL-------MAFILEeKDVLILDEPTNHLDLPSRE-QLEDTLARYDGT----LII 459
Cdd:cd03240 100 CHQGESNWPLLDMRGRCSGGEKVLASLiirlalaETFGSN-CGILALDEPTTNLDEENIEeSLAEIIEERKSQknfqLIV 178
|
170 180
....*....|....*....|....*.
gi 494651374 460 VSHDRYFVEKTTD---IRLDISNGSV 482
Cdd:cd03240 179 ITHDEELVDAADHiyrVEKDGRQKSR 204
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-182 |
3.32e-10 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 60.27 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLI-----CNQKAPSQGQIQMMqDVNIY--------- 70
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLD-GKDIYdldvdvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 71 -----MVEQETE----------AY--------DSGHPEPAEAALLEK---W-NVPARAF-SQLSGGEKLKARLAKGFSSS 122
Cdd:cd03260 80 rrrvgMVFQKPNpfpgsiydnvAYglrlhgikLKEELDERVEEALRKaalWdEVKDRLHaLGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494651374 123 SSLLLLDEPTNHLDQHS---LEILLNQIKNyKGTIIFVSHDRAFIDAAATKIWAIEGKKLIEH 182
Cdd:cd03260 160 PEVLLLDEPTSALDPIStakIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
312-462 |
3.63e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 60.37 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 312 NFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWI--------SPSAN-VGYLTQE--VFD---------LPLDK 370
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGfLTPASGSLTLngqdhtttPPSRRpVSMLFQEnnLFShltvaqnigLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 371 ----TPEQlfyKETFEARGNVQSLMKHLGFTAAQwtepigkMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQ- 445
Cdd:PRK10771 99 glklNAAQ---REKLHAIARQMGIEDLLARLPGQ-------LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEm 168
|
170 180
....*....|....*....|
gi 494651374 446 ---LEDTLARYDGTLIIVSH 462
Cdd:PRK10771 169 ltlVSQVCQERQLTLLMVSH 188
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
10-174 |
4.48e-10 |
|
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: 61.92 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 10 ISYEiNSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMmQDVNIYMVE----QETEAYDSGHP- 84
Cdd:TIGR02857 329 VAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV-NGVPLADADadswRDQIAWVPQHPf 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 85 -------------------------------EPAEAALLEKWNVPA-RAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPT 132
Cdd:TIGR02857 407 lfagtiaenirlarpdasdaeirealeraglDEFVAALPQGLDTPIgEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494651374 133 NHLDQHSLEILLNQIKNYKG--TIIFVSHDRAFIdAAATKIWAI 174
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQgrTVLLVTHRLALA-ALADRIVVL 529
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
302-463 |
4.67e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.39 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 302 YDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWISPSANVGYLTQEV----------FDLPLDK 370
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRlMTPAHGHVWLDGEHIQHYASKEVarrigllaqnATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 371 T----------PEQ-LFYKETFEARGNVQSLMKHLGFTAAQwTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLD 439
Cdd:PRK10253 97 TvqelvargryPHQpLFTRWRKEDEEAVTKAMQATGITHLA-DQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180
....*....|....*....|....*...
gi 494651374 440 LPSREQLEDTLA---RYDG-TLIIVSHD 463
Cdd:PRK10253 176 ISHQIDLLELLSelnREKGyTLAAVLHD 203
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-179 |
5.38e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 59.65 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 16 SVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDV------------NIYMVEQETEAYDSgh 83
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrkkflrriGVVFGQKTQLWWDL-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 84 pEPAEAALLEK--WNVPARAFS---------------------QLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSL 140
Cdd:cd03267 111 -PVIDSFYLLAaiYDLPPARFKkrldelselldleelldtpvrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494651374 141 EILLNQIKNY----KGTIIFVSHDRAFIDAAATKIWAI-EGKKL 179
Cdd:cd03267 190 ENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIdKGRLL 233
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-160 |
7.06e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.74 E-value: 7.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 1 MKEMLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQETEaYD 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY-LD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 81 SGHPEPAEAALLEKWNV------PARAFSQ-----------LSGGEKLKARLAKGFSSSSSLLLLDEPTNHLD---QHSL 140
Cdd:PRK09544 80 TTLPLTVNRFLRLRPGTkkedilPALKRVQaghlidapmqkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvngQVAL 159
|
170 180
....*....|....*....|.
gi 494651374 141 EILLNQIKNYKG-TIIFVSHD 160
Cdd:PRK09544 160 YDLIDQLRRELDcAVLMVSHD 180
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-180 |
7.17e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.47 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLIcnqkA---PSQGQIQMM-QDVNIY----------MVEQETEA--------Y- 79
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARM----AgllPGQGEILLNgRPLSDWsaaelarhraYLSQQQSPpfampvfqYl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 80 -----DSGHPEPAEAALLE---------KWNvpaRAFSQLSGGEKLKARLAKGF-------SSSSSLLLLDEPTNHLD-- 136
Cdd:COG4138 91 alhqpAGASSEAVEQLLAQlaealgledKLS---RPLTQLSGGEWQRVRLAAVLlqvwptiNPEGQLLLLDEPMNSLDva 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494651374 137 -QHSLEILLNQIKNYKGTIIFVSHD--RAFidAAATKIWAIEGKKLI 180
Cdd:COG4138 168 qQAALDRLLRELCQQGITVVMSSHDlnHTL--RHADRVWLLKQGKLV 212
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
311-463 |
7.65e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 7.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 311 VNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQGSI---------WISPSANV--GYLTQE---VFDLPL-------- 368
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIqfagqpleaWSAAELARhrAYLSQQqtpPFAMPVfqyltlhq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 369 -DKTPEQLFYKETFEARGNVQsLMKHLGftaaqwtEPIGKMSMGE--RVkcKLMAFILE-------EKDVLILDEPTNHL 438
Cdd:PRK03695 95 pDKTRTEAVASALNEVAEALG-LDDKLG-------RSVNQLSGGEwqRV--RLAAVVLQvwpdinpAGQLLLLDEPMNSL 164
|
170 180
....*....|....*....|....*...
gi 494651374 439 DLPSR---EQLEDTLARYDGTLIIVSHD 463
Cdd:PRK03695 165 DVAQQaalDRLLSELCQQGIAVVMSSHD 192
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
301-462 |
8.90e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.40 E-value: 8.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 301 SYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQGSIWI--------SPSA---NVGYLTQEvfdlPld 369
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKIngielrelDPESwrkHLSWVGQN----P-- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 370 ktpeQLFyKETFeaRGNV------------QSLMKHLG---FTAAQ---WTEPIGK----MSMGERVKCKLMAFILEEKD 427
Cdd:PRK11174 433 ----QLP-HGTL--RDNVllgnpdasdeqlQQALENAWvseFLPLLpqgLDTPIGDqaagLSVGQAQRLALARALLQPCQ 505
|
170 180 190
....*....|....*....|....*....|....*..
gi 494651374 428 VLILDEPTNHLDLPSREQLEDTLARY--DGTLIIVSH 462
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTH 542
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
293-482 |
1.01e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 59.43 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDG-RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWIS----PSAN-------VGYL 359
Cdd:PRK13652 4 IETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKpTSGSVLIRgepiTKENirevrkfVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQEVFDLPLDKTPEQLFY---------KETFEARgnVQSLMKHLGFTAAQWTEPiGKMSMGERVKCKLMAFILEEKDVLI 430
Cdd:PRK13652 84 FQNPDDQIFSPTVEQDIAfgpinlgldEETVAHR--VSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494651374 431 LDEPTNHLDLPSREQL----EDTLARYDGTLIIVSHDRYFVEKTTDIRLDISNGSV 482
Cdd:PRK13652 161 LDEPTAGLDPQGVKELidflNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
291-480 |
1.01e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 58.73 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 291 RFLEVrdaAKSY-DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWIS-------PSANVGYLTQ 361
Cdd:PRK10908 3 RFEHV---SKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERpSAGKIWFSghditrlKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 362 EV------FDLPLDKT-------PEQLFYKETFEARGNVQSLMKHLGFTAAQWTEPIgKMSMGERVKCKLMAFILEEKDV 428
Cdd:PRK10908 80 QIgmifqdHHLLMDRTvydnvaiPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494651374 429 LILDEPTNHLDLPSRE---QLEDTLARYDGTLIIVSHDRYFVEKTTDIRLDISNG 480
Cdd:PRK10908 159 LLADEPTGNLDDALSEgilRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
293-541 |
1.20e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.36 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSY-DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLL------------KV-ILGQEKAQGSI-WIspSANVG 357
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLlhlngiylpqrgRVkVMGREVNAENEkWV--RSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 358 YltqeVFDLPLDktpeQLFYKETFE--ARGNVqslmkHLGFTAAQWTEPIGK-----------------MSMGERVKCKL 418
Cdd:PRK13647 83 L----VFQDPDD----QVFSSTVWDdvAFGPV-----NMGLDKDEVERRVEEalkavrmwdfrdkppyhLSYGQKKRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 419 MAFILEEKDVLILDEPTNHLDLPSREQLEDTLARYDG---TLIIVSHDRYFVEKTTDIRLDISNGSVRKQWKESPSVRDD 495
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNqgkTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 494651374 496 ---AEELRLKLETERQEVLGKLSFMTpadkqyreLDQKFKELTEEIKKL 541
Cdd:PRK13647 230 iveQAGLRLPLVAQIFEDLPELGQSK--------LPLTVKEAVQIIRKL 270
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
293-452 |
1.23e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.94 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWIS------PSANVGYLTQEVFD 365
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGfVPYQHGSITLDgkpvegPGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 366 LPLDKTPE------QLFYKETFEARGNVQSLMKHLGFTAAQwTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLD 439
Cdd:PRK11248 82 LPWRNVQDnvafglQLAGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170
....*....|...
gi 494651374 440 LPSREQLEDTLAR 452
Cdd:PRK11248 161 AFTREQMQTLLLK 173
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
318-472 |
1.24e-09 |
|
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: 58.96 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 318 GEKIAITGPNGSGKTTLLKVILGQEKAQGSIWISPSANVGYLTQE--------VFDLPLDKTP---EQLFYKetfeargn 386
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYikadyegtVRDLLSSITKdfyTHPYFK-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 387 vQSLMKHLGFtaaqwtEPI-----GKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLARY----DGTL 457
Cdd:cd03237 97 -TEIAKPLQI------EQIldrevPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTA 169
|
170
....*....|....*
gi 494651374 458 IIVSHDRYFVEKTTD 472
Cdd:cd03237 170 FVVEHDIIMIDYLAD 184
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
293-463 |
1.41e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.78 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQgsiwispSANVGYLTQEVFDLPLDKTP 372
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPD-------AGEVHYRMRDGQLRDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 373 EQ----LFYKE--------------TFEARGNV-QSLM----KHLG---FTAAQWTEPI-----------GKMSMGERVK 415
Cdd:PRK11701 80 EAerrrLLRTEwgfvhqhprdglrmQVSAGGNIgERLMavgaRHYGdirATAGDWLERVeidaariddlpTTFSGGMQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494651374 416 CKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLARYDGTL----IIVSHD 463
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglavVIVTHD 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-182 |
1.59e-09 |
|
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: 60.30 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYE-----INSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI----------------- 61
Cdd:COG1123 260 LLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltklsrrslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 62 -----QM-MQDVN-----IYMVEQE-TEAYDSGHPEPAE------AALLEKWNVPARAFS----QLSGGEK--------- 110
Cdd:COG1123 340 lrrrvQMvFQDPYsslnpRMTVGDIiAEPLRLHGLLSRAerrervAELLERVGLPPDLADryphELSGGQRqrvaiaral 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494651374 111 -LKARL--AkgfsssssllllDEPTNHLDQHSLEILLNQIKNYK----GTIIFVSHDRAFIDAAATKIWAIEGKKLIEH 182
Cdd:COG1123 420 aLEPKLliL------------DEPTSALDVSVQAQILNLLRDLQrelgLTYLFISHDLAVVRYIADRVAVMYDGRIVED 486
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-133 |
1.62e-09 |
|
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: 56.50 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 20 FEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDV----------NIYMVEQETE----------- 77
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgQDLtdderkslrkEIGYVFQDPQlfprltvrenl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 78 ------AYDSGHPEPAEAALLEKW--------NVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTN 133
Cdd:pfam00005 81 rlglllKGLSKREKDARAEEALEKlglgdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
23-181 |
2.67e-09 |
|
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: 57.51 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDV-------------NIYMVEQETEAYDS------- 81
Cdd:cd03261 19 VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgEDIsglseaelyrlrrRMGMLFQSGALFDSltvfenv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 82 ----------GHPEPAEAAL--LEKWNVPARAF---SQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQ 146
Cdd:cd03261 99 afplrehtrlSEEEIREIVLekLEAVGLRGAEDlypAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDL 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 494651374 147 IKNYKG----TIIFVSHDRAFIDAAATKIWAIEGKKLIE 181
Cdd:cd03261 179 IRSLKKelglTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
293-485 |
4.14e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 57.45 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVI------------LGQEKAQGSIWISPSAN----- 355
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIDTARSLSQQKGlirql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 356 ---VGYLTQEvFDL-------------PL--DKTPeqlfyKETFEARGnvQSLMKHLGFTAAQWTEPiGKMSMGERVKCK 417
Cdd:PRK11264 84 rqhVGFVFQN-FNLfphrtvleniiegPVivKGEP-----KEEATARA--RELLAKVGLAGKETSYP-RRLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494651374 418 LMAFILEEKDVLILDEPTNHLDLPSREQLEDT---LARYDGTLIIVSHDRYFVEKTTDIRLDISNGSVRKQ 485
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTirqLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQ 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-62 |
4.37e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 57.01 E-value: 4.37e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQ 62
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
292-462 |
5.42e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.49 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 292 FLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI--------SP----SANVGY 358
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPdSGEILLdgepvrfrSPrdaqAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 359 LTQEVFDLP---------LDKTPEQLF---YKETFEArgnVQSLMKHLGFTAAQWTePIGKMSMGER-----VKcklmAF 421
Cdd:COG1129 84 IHQELNLVPnlsvaenifLGREPRRGGlidWRAMRRR---ARELLARLGLDIDPDT-PVGDLSVAQQqlveiAR----AL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494651374 422 ILEEKdVLILDEPTNHLDLPSREQLEDTLA--RYDGTLII-VSH 462
Cdd:COG1129 156 SRDAR-VLILDEPTASLTEREVERLFRIIRrlKAQGVAIIyISH 198
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-160 |
5.98e-09 |
|
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: 56.33 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISY----EINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDVN-----IYMVEQ 74
Cdd:cd03293 1 LEVRNVSKtyggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgEPVTgpgpdRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 75 ET----------------EAYDSGHPEPAEAA--LLEKwnVPARAF-----SQLSGGEKLKARLAKGFSSSSSLLLLDEP 131
Cdd:cd03293 81 QDallpwltvldnvalglELQGVPKAEARERAeeLLEL--VGLSGFenaypHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190
....*....|....*....|....*....|...
gi 494651374 132 TNHLDQHSLEI----LLNQIKNYKGTIIFVSHD 160
Cdd:cd03293 159 FSALDALTREQlqeeLLDIWRETGKTVLLVTHD 191
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-160 |
6.17e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 56.69 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLfeQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIqMMQDVNIY----------MVE 73
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRI-LWNGQDLTalppaerpvsMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 74 QETEAY--------------DSGHPEPAE----AALLEKWNVP---ARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPT 132
Cdd:COG3840 78 QENNLFphltvaqniglglrPGLKLTAEQraqvEQALERVGLAgllDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|..
gi 494651374 133 NHLD---QHSLEILLNQI-KNYKGTIIFVSHD 160
Cdd:COG3840 158 SALDpalRQEMLDLVDELcRERGLTVLMVTHD 189
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-161 |
8.43e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.73 E-value: 8.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQD----------------- 66
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlctyqkqlcfvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 67 ----VNIYMVEQETEAYD----SGHPEPAEAALLEKW----NVPArafSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNH 134
Cdd:PRK13540 81 hrsgINPYLTLRENCLYDihfsPGAVGITELCRLFSLehliDYPC---GLLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180 190
....*....|....*....|....*....|
gi 494651374 135 LDQHSLEILLNQIKNYK---GTIIFVSHDR 161
Cdd:PRK13540 158 LDELSLLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-174 |
8.57e-09 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 55.97 E-value: 8.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGIS--YEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQmmqdVN-IYMVEQETEAYDS 81
Cdd:cd03263 1 LQIRNLTktYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAY----INgYSIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 82 ---------------------------GHPE---PAEAA-------LLEKWNVPARafsQLSGGEKLKARLAKGFSSSSS 124
Cdd:cd03263 77 lgycpqfdalfdeltvrehlrfyarlkGLPKseiKEEVElllrvlgLTDKANKRAR---TLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494651374 125 LLLLDEPTNHLDQHSLEILLNQIKNYKG--TIIFVSHDRAFIDAAATKIwAI 174
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRI-AI 204
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
293-463 |
8.62e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 56.30 E-value: 8.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLfkNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWI--------SPSAN-VGYLTQE 362
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGfLPPDSGRILWngqdltalPPAERpVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 363 --------VFD---LPLDK----TPEQlfyKETFE---ARGNVQSLMKHLgftaaqwtePiGKMSMGERVKCKLMAFILE 424
Cdd:COG3840 80 nnlfphltVAQnigLGLRPglklTAEQ---RAQVEqalERVGLAGLLDRL---------P-GQLSGGQRQRVALARCLVR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494651374 425 EKDVLILDEPTNHLDlPS--RE--QLEDTLAR-YDGTLIIVSHD 463
Cdd:COG3840 147 KRPILLLDEPFSALD-PAlrQEmlDLVDELCReRGLTVLMVTHD 189
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
293-434 |
8.79e-09 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 56.13 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI-------SP-----SANVGYL 359
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPdAGKILIdgqdithLPmheraRLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQE--VF-DLPLDKTPE---QLFYKETFEARGN-VQSLMKHLGFTAAQwTEPIGKMSMGERVKCKLMAFILEEKDVLILD 432
Cdd:TIGR04406 82 PQEasIFrKLTVEENIMavlEIRKDLDRAEREErLEALLEEFQISHLR-DNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
..
gi 494651374 433 EP 434
Cdd:TIGR04406 161 EP 162
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
293-340 |
9.03e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.19 E-value: 9.03e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG 340
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
270-485 |
9.13e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.91 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 270 EPVEAEYEVRFSIEHRKKAGKRFLEVRDAAKSYDGRTL--FKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QG 346
Cdd:PRK11160 316 EITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPqQG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 347 SIWISPS-----------ANVGYLTQEVF--------DLPL---DKTPEQLfyKETFEARGnvqsLMKHL----GFTAaq 400
Cdd:PRK11160 396 EILLNGQpiadyseaalrQAISVVSQRVHlfsatlrdNLLLaapNASDEAL--IEVLQQVG----LEKLLeddkGLNA-- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 401 WTEPIGK-MSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLARY--DGTLIIVSHDRYFVEKTTDIRLdI 477
Cdd:PRK11160 468 WLGEGGRqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHRLTGLEQFDRICV-M 546
|
....*...
gi 494651374 478 SNGSVRKQ 485
Cdd:PRK11160 547 DNGQIIEQ 554
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
293-466 |
1.45e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 57.12 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSY---DGRTLFK--NVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWIS----PSANVG----- 357
Cdd:COG4615 328 LELRGVTYRYpgeDGDEGFTlgPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGlYRPESGEILLDgqpvTADNREayrql 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 358 --------YLTQEVFDLPLDKTPEQlfyketfeargnVQSLMKHLG-----------FTAAqwtepigKMSMGERvkcKL 418
Cdd:COG4615 408 fsavfsdfHLFDRLLGLDGEADPAR------------ARELLERLEldhkvsvedgrFSTT-------DLSQGQR---KR 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494651374 419 MAFI---LEEKDVLILDE------PT------NHLdLPS-REQledtlarydG-TLIIVSHD-RYF 466
Cdd:COG4615 466 LALLvalLEDRPILVFDEwaadqdPEfrrvfyTEL-LPElKAR---------GkTVIAISHDdRYF 521
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
293-462 |
1.46e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 56.76 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI----------SPSANVGYLTQ 361
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPdAGKITVlgvpvpararLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 362 evFDlPLDktPEqlfyketFEARGNVQSLMKHLGFTAAQWTE-----------------PIGKMSMGERVKCKLMAFILE 424
Cdd:PRK13536 122 --FD-NLD--LE-------FTVRENLLVFGRYFGMSTREIEAvipsllefarleskadaRVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494651374 425 EKDVLILDEPTNHLDLPSR----EQLEDTLARyDGTLIIVSH 462
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARhliwERLRSLLAR-GKTILLTTH 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
293-349 |
1.52e-08 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 55.37 E-value: 1.52e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIW 349
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPrSGSIR 61
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-166 |
1.59e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.35 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 9 GISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQ--KAPSQGQIQMMqDVNIYMVEQETEAYDSGHPEP 86
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDVP-DNQFGREASLIDAIGRKGDFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 87 AEAALL------EKWNVPARaFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLD----QHSLEILLNQIKNYKGTIIF 156
Cdd:COG2401 114 DAVELLnavglsDAVLWLRR-FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtaKRVARNLQKLARRAGITLVV 192
|
170
....*....|
gi 494651374 157 VSHDRAFIDA 166
Cdd:COG2401 193 ATHHYDVIDD 202
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
23-181 |
1.81e-08 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 55.14 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM---------------------MQDVNIY---------MV 72
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFdgeditglppheiarlgigrtFQIPRLFpeltvlenvMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 73 ---EQETEAYDSGHPEPAEAALLEK-------------WNVPArafSQLSGGEKLKARLAKGFSSSSSLLLLDEPT---N 133
Cdd:cd03219 99 aaqARTGSGLLLARARREEREARERaeellervgladlADRPA---GELSYGQQRRLEIARALATDPKLLLLDEPAaglN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494651374 134 HLDQHSLEILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAI-EGKKLIE 181
Cdd:cd03219 176 PEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLdQGRVIAE 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
294-463 |
2.01e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 55.47 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 294 EVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVI--LgQEKAQGSIWI-------SPSA----NVGYLT 360
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIsrL-LPPDSGEVLVdgldvatTPSRelakRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 361 QE-VFDLPLdkTPEQL--F----Y---KETFEARGNVQSLMKHLGFTAAQwTEPIGKMSMGERvkckLMAFI----LEEK 426
Cdd:COG4604 82 QEnHINSRL--TVRELvaFgrfpYskgRLTAEDREIIDEAIAYLDLEDLA-DRYLDELSGGQR----QRAFIamvlAQDT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494651374 427 DVLILDEPTNHLDLP-SRE------QLEDTLARydgTLIIVSHD 463
Cdd:COG4604 155 DYVLLDEPLNNLDMKhSVQmmkllrRLADELGK---TVVIVLHD 195
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
293-469 |
2.55e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 54.71 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQGSIWI-------SPSANVGYLTQE--- 362
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdglkvnDPKVDERLIRQEagm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 363 VFdlpldktpeQLFY----------------------KEtfEARGNVQSLMKHLGFTAAQWTEPiGKMSMGER------- 413
Cdd:PRK09493 82 VF---------QQFYlfphltalenvmfgplrvrgasKE--EAEKQARELLAKVGLAERAHHYP-SELSGGQQqrvaiar 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494651374 414 ---VKCKLMAFileekdvlilDEPTNHLDLPSRE---QLEDTLARYDGTLIIVSHDRYFVEK 469
Cdd:PRK09493 150 alaVKPKLMLF----------DEPTSALDPELRHevlKVMQDLAEEGMTMVIVTHEIGFAEK 201
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-160 |
2.72e-08 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 54.22 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 30 GDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI----QMMQDVNI------------YMVEQ----------ETEAYDSGH 83
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngTVLFDSRKkinlppqqrkigLVFQQyalfphlnvrENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 84 PEPAE-----AALLEKWNVPA---RAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHS---LEILLNQI-KNYK 151
Cdd:cd03297 103 KRNREdrisvDELLDLLGLDHllnRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqLLPELKQIkKNLN 182
|
....*....
gi 494651374 152 GTIIFVSHD 160
Cdd:cd03297 183 IPVIFVTHD 191
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
272-451 |
3.20e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.43 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 272 VEAEYEVRFsiEHRKKAG---KRFL----EVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA 344
Cdd:PLN03211 43 MDVCYRVKF--ENMKNKGsniKRILghkpKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 345 Q---GSIWIS---PSANV----GYLTQEVFDLP------------LDKTPEQLFYKETFEArgnVQSLMKHLGFTAAQWT 402
Cdd:PLN03211 121 NnftGTILANnrkPTKQIlkrtGFVTQDDILYPhltvretlvfcsLLRLPKSLTKQEKILV---AESVISELGLTKCENT 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494651374 403 ----EPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLA 451
Cdd:PLN03211 198 iignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLG 250
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
284-438 |
3.93e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 284 HRKKAGKRFLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWIS--PSANVG--- 357
Cdd:PRK15439 3 TSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGiVPPDSGTLEIGgnPCARLTpak 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 358 ------YLT-QEVFDLPLDKTPEQLFYK--ETFEARGNVQSLMKHLGfTAAQWTEPIGKMSMGERVKCKLMAFILEEKDV 428
Cdd:PRK15439 83 ahqlgiYLVpQEPLLFPNLSVKENILFGlpKRQASMQKMKQLLAALG-CQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170
....*....|
gi 494651374 429 LILDEPTNHL 438
Cdd:PRK15439 162 LILDEPTASL 171
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-190 |
4.32e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 55.99 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGIS--YEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI----------------QMM-- 64
Cdd:PRK11160 339 LTLNNVSftYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIllngqpiadyseaalrQAIsv 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 65 --QDVNIY---MVEQETEAYDSGHPEPAEAAL----LEKW---NVPARAF-----SQLSGGEKLKARLAKGFSSSSSLLL 127
Cdd:PRK11160 419 vsQRVHLFsatLRDNLLLAAPNASDEALIEVLqqvgLEKLledDKGLNAWlgeggRQLSGGEQRRLGIARALLHDAPLLL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494651374 128 LDEPTNHLD----QHSLEILLNQIKNyKgTIIFVSHdRAFIDAAATKIWAIEGKKLIEHkGNYSSYM 190
Cdd:PRK11160 499 LDEPTEGLDaeteRQILELLAEHAQN-K-TVLMITH-RLTGLEQFDRICVMDNGQIIEQ-GTHQELL 561
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
293-349 |
5.45e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.39 E-value: 5.45e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ-EKAQGSIW 349
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQiAPDHGEIL 65
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
287-464 |
5.87e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.56 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 287 KAGKRFLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVIlgqekaqgSIWISP-SANVGYLTQEVFD 365
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIV--------ASLISPtSGTLLFEGEDIST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 366 LPLDKTPEQLFY--------KET--------FEARgNVQSLMKHLGFTAAQW-------TEPIGKMSMGERVKCKLMAFI 422
Cdd:PRK10247 74 LKPEIYRQQVSYcaqtptlfGDTvydnlifpWQIR-NQQPDPAIFLDDLERFalpdtilTKNIAELSGGEKQRISLIRNL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494651374 423 LEEKDVLILDEPTNHLDLPSREQLEDTLARYDG----TLIIVSHDR 464
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVReqniAVLWVTHDK 198
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
293-485 |
6.27e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 55.19 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG---QEKAQGSI-----------WISPSANVG- 357
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqYEPTSGRIiyhvalcekcgYVERPSKVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 358 -------YLTQEVFDL-PLDKTPEQLFYKE-------TFEARG------NVQSLMKHLGFTAaqwTEPIGK--------- 407
Cdd:TIGR03269 81 pcpvcggTLEPEEVDFwNLSDKLRRRIRKRiaimlqrTFALYGddtvldNVLEALEEIGYEG---KEAVGRavdliemvq 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 408 -----------MSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPS----REQLEDTLARYDGTLIIVSHDRYFVEKTTD 472
Cdd:TIGR03269 158 lshrithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTaklvHNALEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250
....*....|...
gi 494651374 473 IRLDISNGSVRKQ 485
Cdd:TIGR03269 238 KAIWLENGEIKEE 250
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
306-485 |
6.38e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.63 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 306 TLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVI-------------LGQ------EKAQGSIwisPSANVGYLTQEVFDL 366
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILaglddgssgevslVGQplhqmdEEARAKL---RAKHVGFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 367 PLDKT------PEQLFYKETFEARGNVQSLMKHLGFTAAQWTEPiGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDL 440
Cdd:PRK10584 101 PTLNAlenvelPALLRGESSRQSRNGAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494651374 441 PSREQLEDTL----ARYDGTLIIVSHDRYFVEKtTDIRLDISNGSVRKQ 485
Cdd:PRK10584 180 QTGDKIADLLfslnREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
311-463 |
6.41e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 53.69 E-value: 6.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 311 VNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQGSIWIS-------PSANV----GYLTQE---VFDLP----Ldktp 372
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNgrplsdwSAAELarhrAYLSQQqspPFAMPvfqyL---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 373 eQLFYketfEARGNVQSLMKHLGFTAAQ------WTEPIGKMSMGE--RVkcKLMAFILE-------EKDVLILDEPTNH 437
Cdd:COG4138 91 -ALHQ----PAGASSEAVEQLLAQLAEAlgledkLSRPLTQLSGGEwqRV--RLAAVLLQvwptinpEGQLLLLDEPMNS 163
|
170 180
....*....|....*....|....*....
gi 494651374 438 LDLPSREQLEDTLARY---DGTLIIVSHD 463
Cdd:COG4138 164 LDVAQQAALDRLLRELcqqGITVVMSSHD 192
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-67 |
6.69e-08 |
|
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: 53.31 E-value: 6.69e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDV 67
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV 85
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
303-500 |
7.14e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 53.84 E-value: 7.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 303 DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLL------------KVIL------------GQEKAQGSIWISPSAN-VG 357
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLAlhlngllrpqkgKVLVsgidtgdfsklqGIRKLVGIVFQNPETQfVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 358 YLTQEvfDLPLDktPEQLFYKETfEARGNVQSLMKHLGFTAAQWTEPigKMSMGERVKCKLMAFILE-EKDVLILDEPTN 436
Cdd:PRK13644 93 RTVEE--DLAFG--PENLCLPPI-EIRKRVDRALAEIGLEKYRHRSP--KTLSGGQGQCVALAGILTmEPECLIFDEVTS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 437 HLDLPSREQ-LEDT--LARYDGTLIIVSH--------DRYFVEKTTDIRLD------ISNGSVRKQWKESPSVRDDAEEL 499
Cdd:PRK13644 166 MLDPDSGIAvLERIkkLHEKGKTIVYITHnleelhdaDRIIVMDRGKIVLEgepenvLSDVSLQTLGLTPPSLIELAENL 245
|
.
gi 494651374 500 R 500
Cdd:PRK13644 246 K 246
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-159 |
7.33e-08 |
|
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: 52.16 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 18 PLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQeteaydsgHPEPAEAALLEK--- 94
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQ--------RPYLPLGTLREQliy 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494651374 95 -WNvparafSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYKGTIIFVSH 159
Cdd:cd03223 87 pWD------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH 146
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-68 |
8.42e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.55 E-value: 8.42e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494651374 4 MLKISGIS---YE--INSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDVN 68
Cdd:COG1101 1 MLELKNLSktfNPgtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDgKDVT 71
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
293-348 |
8.43e-08 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 52.82 E-value: 8.43e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSI 348
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPrSGSI 57
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
293-487 |
8.54e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.11 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRT---LFKNVNFTVMHGEKIAITGPNGSGKTT---LLK-----------------------------V 337
Cdd:TIGR00958 479 IEFQDVSFSYPNRPdvpVLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQnlyqptggqvlldgvplvqydhhylhrqvA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 338 ILGQEKA--QGSIwispSANVGYltqevfdlPLDKTPEQlfyketfEARGNVQSLMKH---LGFTAAQWTEpIGK----M 408
Cdd:TIGR00958 559 LVGQEPVlfSGSV----RENIAY--------GLTDTPDE-------EIMAAAKAANAHdfiMEFPNGYDTE-VGEkgsqL 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494651374 409 SMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLARYDGTLIIVSHDRYFVEKTTDIrLDISNGSVRKQWK 487
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQI-LVLKKGSVVEMGT 696
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
317-476 |
9.15e-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: 51.61 E-value: 9.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 317 HGEKIAITGPNGSGKTTLLKVILGQEKAQGS--IWISPSANVGYLTQEVFDLPLDKTpeqlfyketfeargnvqslmkhl 394
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGgvIYIDGEDILEEVLDQLLLIIVGGK----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 395 gftaaqwtepiGKMSMGERVKCKLMAFILEEK-DVLILDEPTNHLDLPSREQLED---------TLARYDGTLIIVSHDR 464
Cdd:smart00382 58 -----------KASGSGELRLRLALALARKLKpDVLILDEITSLLDAEQEALLLLleelrllllLKSEKNLTVILTTNDE 126
|
170
....*....|...
gi 494651374 465 YFV-EKTTDIRLD 476
Cdd:smart00382 127 KDLgPALLRRRFD 139
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
293-464 |
9.56e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 54.32 E-value: 9.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKaQGSIWISPSA-----------NVGYLTQ 361
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEH-QTSGHIRFHGtdvsrlhardrKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 362 E--------VFD--------LPLDKTPeqlfykETFEARGNVQSL--MKHLGFTAAQWTepiGKMSMGERVKCKLMAFIL 423
Cdd:PRK10851 82 HyalfrhmtVFDniafgltvLPRRERP------NAAAIKAKVTQLleMVQLAHLADRYP---AQLSGGQKQRVALARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494651374 424 EEKDVLILDEPTNHLDLPSREQLEDTLARYDGTL----IIVSHDR 464
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkftsVFVTHDQ 197
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
290-463 |
1.12e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 53.48 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 290 KRFLEVRDAAKSYDG--RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGqekaqgsiWISPSANvgylTQEVFDLP 367
Cdd:PRK13635 3 EEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNG--------LLLPEAG----TITVGGMV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 368 LDKT---------------PEQLFYKET--------FEARG--------NVQSLMKHLGFTAAQWTEPiGKMSMGERVKC 416
Cdd:PRK13635 71 LSEEtvwdvrrqvgmvfqnPDNQFVGATvqddvafgLENIGvpreemveRVDQALRQVGMEDFLNREP-HRLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494651374 417 KLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLARY----DGTLIIVSHD 463
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkeqkGITVLSITHD 200
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
309-488 |
1.31e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.13 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 309 KNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI------SPSANVGYLTQE---VFDLPLDKTPEQLFYK 378
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPtSGKIIIdgvditDKKVKLSDIRKKvglVFQYPEYQLFEETIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 379 -----------ETFEARGNVQSLMKHLGFTAAQWTE--PIgKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSRE- 444
Cdd:PRK13637 104 diafgpinlglSEEEIENRVKRAMNIVGLDYEDYKDksPF-ELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDe 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494651374 445 ---QLEDTLARYDGTLIIVSH---------DRYFVEKTTDIRLDisnGSVRKQWKE 488
Cdd:PRK13637 183 ilnKIKELHKEYNMTIILVSHsmedvaklaDRIIVMNKGKCELQ---GTPREVFKE 235
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
304-449 |
1.44e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.94 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 304 GRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ-EKAQGSiwISPSANVGYLTQEVFDLPLDKTPEQLFYKETFE 382
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGElEPSEGK--IKHSGRISFSSQFSWIMPGTIKENIIFGVSYDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 383 ARgnVQSLMKhlgftAAQWTEPIGK---------------MSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLE 447
Cdd:cd03291 127 YR--YKSVVK-----ACQLEEDITKfpekdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIF 199
|
..
gi 494651374 448 DT 449
Cdd:cd03291 200 ES 201
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-180 |
1.55e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.63 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLIcnqkA---PSQGQIQMMQD------------VNIYMVEQETEAY-------- 79
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARM----AgllPGSGSIQFAGQpleawsaaelarHRAYLSQQQTPPFampvfqyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 80 -----DSGHPEPAEAAL------LEKWNVPARAFSQLSGGEKLKARLAKGFSSSSSLLLL-------DEPTNHLD---QH 138
Cdd:PRK03695 91 tlhqpDKTRTEAVASALnevaeaLGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDINPagqllllDEPMNSLDvaqQA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494651374 139 SLEILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKLI 180
Cdd:PRK03695 171 ALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-207 |
1.58e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 53.96 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 1 MKEMLKISGI--SYEI--NSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDVN------- 68
Cdd:PRK10535 1 MTALLELKDIrrSYPSgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAgQDVAtldadal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 69 ----------IYM---------VEQETEAydsghpePAEAALLEKWNVPARAF----------------SQLSGGEKLKA 113
Cdd:PRK10535 81 aqlrrehfgfIFQryhllshltAAQNVEV-------PAVYAGLERKQRLLRAQellqrlgledrveyqpSQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 114 RLAKGFSSSSSLLLLDEPTNHLDQHSLE---ILLNQIKNYKGTIIFVSHDRAfIDAAATKIWAIEGKKLIEHKGNYSSYM 190
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEevmAILHQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIVRNPPAQEKVN 232
|
250
....*....|....*..
gi 494651374 191 EVRKQRRLTQQREYENQ 207
Cdd:PRK10535 233 VAGGTEPVVNTASGWRQ 249
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-181 |
1.64e-07 |
|
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: 52.89 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 18 PLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDV-------------NIYMVEQEteAYDSGH 83
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgQDLyqldrkqrrafrrDVQLVFQD--SPSAVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 84 P---------EPAE--------------AALLEKWNVPA----RAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLD 136
Cdd:TIGR02769 103 PrmtvrqiigEPLRhltsldeseqkariAELLDMVGLRSedadKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494651374 137 QHSLEILLNQIKNYK---GT-IIFVSHDRAFIDAAATKIWAIEGKKLIE 181
Cdd:TIGR02769 183 MVLQAVILELLRKLQqafGTaYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
293-463 |
1.66e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 52.93 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSY-DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLL-------------------------KVILGQEKAQG 346
Cdd:PRK13636 6 LKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFqnlngilkpssgrilfdgkpidysrKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 347 SIWISP-----SANVgylTQEVFDLPLD-KTPEQlfyketfEARGNVQSLMKHLGFTAAQwTEPIGKMSMGERVKCKLMA 420
Cdd:PRK13636 86 MVFQDPdnqlfSASV---YQDVSFGAVNlKLPED-------EVRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494651374 421 FILEEKDVLILDEPTNHLDlPS-----REQLEDTLARYDGTLIIVSHD 463
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLD-PMgvseiMKLLVEMQKELGLTIIIATHD 201
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-159 |
1.86e-07 |
|
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: 52.39 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 3 EMLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQ--------------------I- 61
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgerrggedvwelrkrIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 62 ----QMMQDVNIYM-VEQ--ETEAYDS----GHPEPAEAA----LLEKWNVPA---RAFSQLSGGEK---LKAR------ 114
Cdd:COG1119 82 lvspALQLRFPRDEtVLDvvLSGFFDSiglyREPTDEQRErareLLELLGLAHladRPFGTLSQGEQrrvLIARalvkdp 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494651374 115 ----LakgfsssssllllDEPTNHLDQHSLEILLNQI----KNYKGTIIFVSH 159
Cdd:COG1119 162 elliL-------------DEPTAGLDLGARELLLALLdklaAEGAPTLVLVTH 201
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
301-465 |
1.86e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 52.32 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 301 SYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWISPSANVGY----LTQEVFDLP-LDKTPE- 373
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLssrqLARRLALLPqHHLTPEg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 374 ---------------QLFYKETFEARGNVQSLMKHLGFTA-AQwtEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNH 437
Cdd:PRK11231 91 itvrelvaygrspwlSLWGRLSAEDNARVNQAMEQTRINHlAD--RRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 494651374 438 LDLPSREQLEDTLARYDG---TLIIVSHD-----RY 465
Cdd:PRK11231 169 LDINHQVELMRLMRELNTqgkTVVTVLHDlnqasRY 204
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-61 |
2.11e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.19 E-value: 2.11e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494651374 1 MKEMLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI 61
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRI 62
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-62 |
2.15e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 52.01 E-value: 2.15e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQ 62
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVL 59
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-181 |
2.45e-07 |
|
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: 51.95 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLfEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM-----------MQDVNI---- 69
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLngkditnlppeKRDISYvpqn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 70 -----YMVEQETEAYDSGH-----PEPAE-----AALLEKWNVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNH 134
Cdd:cd03299 80 yalfpHMTVYKNIAYGLKKrkvdkKEIERkvleiAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494651374 135 LDQHSLEILLNQIK----NYKGTIIFVSHDraFIDAA--ATKIWAIEGKKLIE 181
Cdd:cd03299 160 LDVRTKEKLREELKkirkEFGVTVLHVTHD--FEEAWalADKVAIMLNGKLIQ 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-159 |
3.11e-07 |
|
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: 51.13 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQmmqdvniymVEQETEAYDSGH- 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVL---------FDGKPLDIAARNr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 84 ----PE------------------------PAEAA-----------LLEKWNVPARafsQLSGGEKLKARLAKGFSSSSS 124
Cdd:cd03269 72 igylPEerglypkmkvidqlvylaqlkglkKEEARrridewlerleLSEYANKRVE---ELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 494651374 125 LLLLDEPTNHLDQHSLEILLNQIKNYKG---TIIFVSH 159
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTH 186
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
27-160 |
3.35e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 51.32 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 27 VQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQETEAYDSGH-----------PE---------P 86
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHvgfvfqsfmliPTlnalenvelP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 87 A-------------EAALLEKWNVPARAF---SQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHS----LEILLNQ 146
Cdd:PRK10584 113 AllrgessrqsrngAKALLEQLGLGKRLDhlpAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkiADLLFSL 192
|
170
....*....|....
gi 494651374 147 IKNYKGTIIFVSHD 160
Cdd:PRK10584 193 NREHGTTLILVTHD 206
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
290-464 |
3.39e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 52.41 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 290 KRFLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWI------------------ 350
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKpTEGQIFIdgedvthrsiqqrdicmv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 351 ----------SPSANVGYlTQEVFDLPLDKTPEQLfyKETFEargnvqsLMKHLGFtAAQWTEPIgkmSMGERVKCKLM- 419
Cdd:PRK11432 84 fqsyalfphmSLGENVGY-GLKMLGVPKEERKQRV--KEALE-------LVDLAGF-EDRYVDQI---SGGQQQRVALAr 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494651374 420 AFILEEKdVLILDEPTNHLDL----PSREQLEDTLARYDGTLIIVSHDR 464
Cdd:PRK11432 150 ALILKPK-VLLFDEPLSNLDAnlrrSMREKIRELQQQFNITSLYVTHDQ 197
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-159 |
3.60e-07 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 50.95 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 19 LFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQ--DVNIYMVEQETEAYdSGHPEPAEAAL----- 91
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpLDFQRDSIARGLLY-LGHAPGIKTTLsvlen 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 92 LEKWN-------------------VPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNY-- 150
Cdd:cd03231 94 LRFWHadhsdeqveealarvglngFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHca 173
|
170
....*....|
gi 494651374 151 -KGTIIFVSH 159
Cdd:cd03231 174 rGGMVVLTTH 183
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-167 |
4.32e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 50.87 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 1 MKE---MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDVNIYMVEQ-- 74
Cdd:PRK10247 1 MQEnspLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEgEDISTLKPEIyr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 75 -------ETEA------YDS---------GHPEPAE-AALLEKWNVP----ARAFSQLSGGEKLKARLAKGFSSSSSLLL 127
Cdd:PRK10247 81 qqvsycaQTPTlfgdtvYDNlifpwqirnQQPDPAIfLDDLERFALPdtilTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494651374 128 LDEPTNHLDQHSL----EILLNQIKNYKGTIIFVSHDRAFIDAA 167
Cdd:PRK10247 161 LDEITSALDESNKhnvnEIIHRYVREQNIAVLWVTHDKDEINHA 204
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
301-446 |
4.54e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 301 SYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ-EKAQGSiwISPSANVGYLTQEVFDLPLDKTPEQLF--- 376
Cdd:TIGR01271 435 SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGElEPSEGK--IKHSGRISFSPQTSWIMPGTIKDNIIFgls 512
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494651374 377 YKEtFEARGNVQS--LMKHLGFTAAQWTEPIGK----MSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQL 446
Cdd:TIGR01271 513 YDE-YRYTSVIKAcqLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-181 |
5.44e-07 |
|
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: 50.29 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQD------------------ 66
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKsyqkniealrrigaliea 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 67 --VNIYMVEQE---TEAYDSGHPEPAEAALLEKWNVPARA---FSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQ- 137
Cdd:cd03268 81 pgFYPNLTAREnlrLLARLLGIRKKRIDEVLDVVGLKDSAkkkVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPd 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494651374 138 --HSLEILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKLIE 181
Cdd:cd03268 161 giKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
293-485 |
5.78e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 51.23 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSY-DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLL------------KVILGQE--KAQGSIWISPSANVG 357
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFlhfngilkptsgEVLIKGEpiKYDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 358 YltqeVFDLPLDktpeQLFY-----------------KETFEARgnVQSLMKHLGFTAAQWTEPiGKMSMGERVKCKLMA 420
Cdd:PRK13639 82 I----VFQNPDD----QLFAptveedvafgplnlglsKEEVEKR--VKEALKAVGMEGFENKPP-HHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 421 FILEEKDVLILDEPTNHLDLPSREQLEDTLARYDG---TLIIVSHDRYFVEKTTDIRLDISNGSVRKQ 485
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
309-462 |
5.95e-07 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 50.57 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 309 KNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWI---SPSA--------NVGYLTQEVF----------Dl 366
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRlVELSSGSILIdgvDISKiglhdlrsRISIIPQDPVlfsgtirsnlD- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 367 PLDK-TPEQLF-YKETFEARGNVQSLMKHLGFTAAQWTEPIgkmSMGERvkcKLMAF---ILEEKDVLILDEPTNHLDLP 441
Cdd:cd03244 100 PFGEySDEELWqALERVGLKEFVESLPGGLDTVVEEGGENL---SVGQR---QLLCLaraLLRKSKILVLDEATASVDPE 173
|
170 180
....*....|....*....|...
gi 494651374 442 SREQLEDTLARY--DGTLIIVSH 462
Cdd:cd03244 174 TDALIQKTIREAfkDCTVLTIAH 196
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
293-462 |
6.29e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.93 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVI------------LGQEKAQGSIWISPSANVGYLT 360
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGHNIYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 361 QE---VFDLPlDKTPEQLFYKETFEARGN-----------VQSLMKhlgfTAAQWTE--------PIGkMSMGERVKCKL 418
Cdd:PRK14239 86 KEigmVFQQP-NPFPMSIYENVVYGLRLKgikdkqvldeaVEKSLK----GASIWDEvkdrlhdsALG-LSGGQQQRVCI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494651374 419 MAFILEEKDVLILDEPTNHLDLPSREQLEDTL--ARYDGTLIIVSH 462
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLlgLKDDYTMLLVTR 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
293-462 |
6.68e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.61 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSY--DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVIL------GQEKAQGSIWISPSAN-----VGYL 359
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLrllsteGEIQIDGVSWNSVTLQtwrkaFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQEVFDL---------PLDKTPEQLFYKETFEA--RGNVQSLMKHLGFtaaQWTEPIGKMSMGERVKCKLMAFILEEKDV 428
Cdd:TIGR01271 1298 PQKVFIFsgtfrknldPYEQWSDEEIWKVAEEVglKSVIEQFPDKLDF---VLVDGGYVLSNGHKQLMCLARSILSKAKI 1374
|
170 180 190
....*....|....*....|....*....|....*.
gi 494651374 429 LILDEPTNHLDLPSREQLEDTL--ARYDGTLIIVSH 462
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQIIRKTLkqSFSNCTVILSEH 1410
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
293-350 |
7.03e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.38 E-value: 7.03e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTL-FKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWI 350
Cdd:PRK11650 4 LKLQAVRKSYDGKTQvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERiTSGEIWI 63
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
293-439 |
7.05e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 50.66 E-value: 7.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWISPS------------ANVGYL 359
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGiVPRDAGNIIIDDEdisllplhararRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQE---------------VFDLPLDKTPEQLfyketfEARGNvqSLMKHlgFTAAQWTEPIGK-MSMGERVKCKLMAFIL 423
Cdd:PRK10895 84 PQEasifrrlsvydnlmaVLQIRDDLSAEQR------EDRAN--ELMEE--FHIEHLRDSMGQsLSGGERRRVEIARALA 153
|
170
....*....|....*.
gi 494651374 424 EEKDVLILDEPTNHLD 439
Cdd:PRK10895 154 ANPKFILLDEPFAGVD 169
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
283-435 |
7.65e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.56 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 283 EHRKKAGKRFLEVRDaaksYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI--------SPS 353
Cdd:COG1129 247 KRAAAPGEVVLEVEG----LSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPAdSGEIRLdgkpvrirSPR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 354 ----ANVGYLTQE------VFDLP---------LDKTPEQLFYKETfEARGNVQSLMKHLGFTAAQWTEPIGKMSMGERV 414
Cdd:COG1129 323 dairAGIAYVPEDrkgeglVLDLSirenitlasLDRLSRGGLLDRR-RERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQ 401
|
170 180
....*....|....*....|....
gi 494651374 415 KC---KLMAfilEEKDVLILDEPT 435
Cdd:COG1129 402 KVvlaKWLA---TDPKVLILDEPT 422
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
296-471 |
7.82e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 51.18 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 296 RDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWIS--------PSA-NVGYLTQEV-- 363
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGDLFIGekrmndvpPAErGVGMVFQSYal 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 364 -----------FDLPLDKTPEQLFYKETFEARGNVQslMKHLgftaaqwTEPIGK-MSMGERVKCKLMAFILEEKDVLIL 431
Cdd:PRK11000 87 yphlsvaenmsFGLKLAGAKKEEINQRVNQVAEVLQ--LAHL-------LDRKPKaLSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494651374 432 DEPTNHLDLPSREQLEDTLA----RYDGTLIIVSHDRyfVEKTT 471
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISrlhkRLGRTMIYVTHDQ--VEAMT 199
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-159 |
8.00e-07 |
|
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: 49.80 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLfeQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI------------------QMMQD 66
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlingvdvtaappadrpvsMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 67 VNIY---MVEQET----------EAYDSGHPEPAeAALLEKWNVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTN 133
Cdd:cd03298 79 NNLFahlTVEQNVglglspglklTAEDRQAIEVA-LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190
....*....|....*....|....*....|
gi 494651374 134 HLD---QHSLEILLNQIKNYKG-TIIFVSH 159
Cdd:cd03298 158 ALDpalRAEMLDLVLDLHAETKmTVLMVTH 187
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
294-462 |
8.06e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 51.89 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 294 EVRDAAKSYDG-RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVI-LGQEKAQGSIWISpSANVGYLTQE--------V 363
Cdd:PRK13657 336 EFDDVSFSYDNsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqRVFDPQSGRILID-GTDIRTVTRAslrrniavV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 364 FDLPL---------------DKTPEqlfykETFEARGNVQSL----MKHLGFTAAqwtepIG----KMSMGERVKCKLMA 420
Cdd:PRK13657 415 FQDAGlfnrsiednirvgrpDATDE-----EMRAAAERAQAHdfieRKPDGYDTV-----VGergrQLSGGERQRLAIAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494651374 421 FILEEKDVLILDEPTNHLDLPSREQLEDTL--ARYDGTLIIVSH 462
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALdeLMKGRTTFIIAH 528
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-439 |
8.63e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 8.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 1 MKEMLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQkAPS---QGQI---------------- 61
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIifegeelqasnirdte 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 62 ---------------QMMQDVNIYMVEQETEA----YDSGHPEPAEaaLLEKWNV---PARAFSQLSGGEKLKARLAKGF 119
Cdd:PRK13549 81 ragiaiihqelalvkELSVLENIFLGNEITPGgimdYDAMYLRAQK--LLAQLKLdinPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 120 SSSSSLLLLDEPTNHLDQHSLEILLNQIKNYKG---TIIFVSHDRAFIDAAATKIWAI-EGKklieHKGNyssymevRKQ 195
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAhgiACIYISHKLNEVKAISDTICVIrDGR----HIGT-------RPA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 196 RRLTQQ--------RE----YENQQHMIRRIEAQMNELSAWskkaHAQSTKIegfkeyhrvkaKRTDaqikskqkrleke 263
Cdd:PRK13549 228 AGMTEDdiitmmvgREltalYPREPHTIGEVILEVRNLTAW----DPVNPHI-----------KRVD------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 264 lekakaepveaeyevrfsiehrkkagkrflevrdaaksydgrtlfkNVNFTVMHGEKIAITGPNGSGKTTLLKVILG--Q 341
Cdd:PRK13549 280 ----------------------------------------------DVSFSLRRGEILGIAGLVGAGRTELVQCLFGayP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 342 EKAQGSIW------------------------------ISPSANVGY------LTQEVFDLPLDKTPEQlfyketfearG 385
Cdd:PRK13549 314 GRWEGEIFidgkpvkirnpqqaiaqgiamvpedrkrdgIVPVMGVGKnitlaaLDRFTGGSRIDDAAEL----------K 383
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 494651374 386 NVQSLMKHLGFTAAQWTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLD 439
Cdd:PRK13549 384 TILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-181 |
9.66e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 50.37 E-value: 9.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEI-NSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI----------QMMQDVN--IY 70
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfSKLQGIRklVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 71 MVEQETEAYDSGH---------PE-----PAE------AAL----LEKWNvpARAFSQLSGGEKLKARLAKGFSSSSSLL 126
Cdd:PRK13644 81 IVFQNPETQFVGRtveedlafgPEnlclpPIEirkrvdRALaeigLEKYR--HRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 127 LLDEPTNHLDQHSLEILLNQIK--NYKG-TIIFVSHDRAFIDAAATKIWAIEGKKLIE 181
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKklHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
259-461 |
1.16e-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: 51.55 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 259 RLEKELEKAkaEPVEAEYEvrfSIEHRKKAGKRFLE-----------VRDAAKSYD--GRTLFKNVNFTVMHGEKIAITG 325
Cdd:TIGR01257 889 REERALEKT--EPLTEEME---DPEHPEGINDSFFErelpglvpgvcVKNLVKIFEpsGRPAVDRLNITFYENQITAFLG 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 326 PNGSGKTTLLKVILG-QEKAQGSIWISP---SANVGYLTQEVFDLP--------LDKTPEQLFY-----KETFEARGNVQ 388
Cdd:TIGR01257 964 HNGAGKTTTLSILTGlLPPTSGTVLVGGkdiETNLDAVRQSLGMCPqhnilfhhLTVAEHILFYaqlkgRSWEEAQLEME 1043
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494651374 389 SLMKHLGFTAAQwTEPIGKMSMGERVKCKL-MAFILEEKdVLILDEPTNHLDLPSREQLEDTLARY-DGTLIIVS 461
Cdd:TIGR01257 1044 AMLEDTGLHHKR-NEEAQDLSGGMQRKLSVaIAFVGDAK-VVVLDEPTSGVDPYSRRSIWDLLLKYrSGRTIIMS 1116
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-159 |
1.18e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 50.60 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQD----------VNIYMVEQ 74
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlarARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 75 -----------------------ETEAYDSGHPEPAEAALLE-KWNVPArafSQLSGGEKLKARLAKGFSSSSSLLLLDE 130
Cdd:PRK13536 122 fdnldleftvrenllvfgryfgmSTREIEAVIPSLLEFARLEsKADARV---SDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190
....*....|....*....|....*....|..
gi 494651374 131 PTNHLDQHSLEILLNQIKNY--KG-TIIFVSH 159
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLlaRGkTILLTTH 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-168 |
1.57e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 49.20 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLfeQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDVN--------IYMVEQ 74
Cdd:PRK10771 1 MLKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgQDHTttppsrrpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 75 E-------TEAYDSG---HP----EPAEAALLEKW-------NVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTN 133
Cdd:PRK10771 79 EnnlfshlTVAQNIGlglNPglklNAAQREKLHAIarqmgieDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 494651374 134 HLD---QHSLEILLNQIKNYKG-TIIFVSHDrafIDAAA 168
Cdd:PRK10771 159 ALDpalRQEMLTLVSQVCQERQlTLLMVSHS---LEDAA 194
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
309-463 |
1.62e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 49.73 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 309 KNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWISPSAnvgyLTQE-VFDLP-----LDKTPEQLFYKETF 381
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIIIDGDL----LTEEnVWDIRhkigmVFQNPDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 382 E----------------ARGNVQSLMKHLGFTAAQWTEPiGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQ 445
Cdd:PRK13650 100 EddvafglenkgipheeMKERVNEALELVGMQDFKEREP-ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180
....*....|....*....|..
gi 494651374 446 LEDTLA----RYDGTLIIVSHD 463
Cdd:PRK13650 179 LIKTIKgirdDYQMTVISITHD 200
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-168 |
1.76e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.79 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 16 SVP---LFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI----QMMQDVNIYMVEQETeAYDSGHPEPAE 88
Cdd:PRK10575 20 RVPgrtLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaQPLESWSSKAFARKV-AYLPQQLPAAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 89 AALLEK--------WN--------------------VPARAFSQ-----LSGGEKLKARLAKGFSSSSSLLLLDEPTNHL 135
Cdd:PRK10575 99 GMTVRElvaigrypWHgalgrfgaadrekveeaislVGLKPLAHrlvdsLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 494651374 136 D-QHSLEI--LLNQIKNYKG-TIIFVSHDrafIDAAA 168
Cdd:PRK10575 179 DiAHQVDVlaLVHRLSQERGlTVIAVLHD---INMAA 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
309-472 |
1.77e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 49.78 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 309 KNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWISpSANVGYLTQEVFDLPLDKT-------PEQLFYKET 380
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKpTTGTVTVD-DITITHKTKDKYIRPVRKRigmvfqfPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 381 FE----------------ARGNVQSLMKHLGFTAAQWTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSRE 444
Cdd:PRK13646 103 VEreiifgpknfkmnldeVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKR 182
|
170 180 190
....*....|....*....|....*....|..
gi 494651374 445 QLEDTLARY----DGTLIIVSHDRYFVEKTTD 472
Cdd:PRK13646 183 QVMRLLKSLqtdeNKTIILVSHDMNEVARYAD 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-182 |
1.81e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 49.76 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM-------MQDVNIYMVEQET 76
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdgenipaMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 77 EA-YDSG------------------HPEPAEAAL-------LEKWNVPARAF---SQLSGGEKLKARLAKGFSSSSSLLL 127
Cdd:PRK11831 87 SMlFQSGalftdmnvfdnvayplreHTQLPAPLLhstvmmkLEAVGLRGAAKlmpSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494651374 128 LDEPTNHLDQHSLEILLNQIKNYKG----TIIFVSHDRAFIDAAATKIWAIEGKKLIEH 182
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSalgvTCVVVSHDVPEVLSIADHAYIVADKKIVAH 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-159 |
1.82e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 49.66 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQ-----ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIqMMQDVNI---------- 69
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKkaldnVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKI-IIDGVDItdkkvklsdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 70 ------------YMVEQETEAYDSGH----------------PEPAEAALLEKWNVPARAFSQLSGGEKLKARLAKGFSS 121
Cdd:PRK13637 82 rkkvglvfqypeYQLFEETIEKDIAFgpinlglseeeienrvKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494651374 122 SSSLLLLDEPTNHLDQHSLEILLNQIKN----YKGTIIFVSH 159
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKElhkeYNMTIILVSH 203
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
287-482 |
2.02e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 49.28 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 287 KAGKRFLEVRDAAKSY---DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVIL-------GQEKAQGSIW------- 349
Cdd:PRK14246 2 EAGKSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLyfgkdif 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 350 ----ISPSANVGYLTQEVFDLPLDKTPEQLFY-------KETFEARGNVQSLMKHLGFtaaqWTE-------PIGKMSMG 411
Cdd:PRK14246 82 qidaIKLRKEVGMVFQQPNPFPHLSIYDNIAYplkshgiKEKREIKKIVEECLRKVGL----WKEvydrlnsPASQLSGG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494651374 412 ERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLED--TLARYDGTLIIVSHDRYFVEKTTDIRLDISNGSV 482
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKliTELKNEIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
305-439 |
2.20e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 305 RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ-EKAQGSIWISPSanVGYLTQEVFDLPLDKTPEQLFYKETFEA 383
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQfEISEGRVWAERS--IAYVPQQAWIMNATVRGNILFFDEEDAA 750
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494651374 384 R----GNVQSLMKHLGFTAAQWTEPIGKM----SMGERVKCKLMAFILEEKDVLILDEPTNHLD 439
Cdd:PTZ00243 751 RladaVRVSQLEADLAQLGGGLETEIGEKgvnlSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
302-460 |
2.40e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 302 YDGRTLFKNvNFTVMHGEKIAITGPNGSGKTTLLKVILGQ--------------------EKAQGSI---W-------IS 351
Cdd:PRK10938 14 SDTKTLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGElpllsgerqsqfshitrlsfEQLQKLVsdeWqrnntdmLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 352 PSA-NVGYLTQEVFDLPLDKTPEQLFYKETFeargNVQSLMkhlgftaaqwTEPIGKMSMGERVKCKLMAFILEEKDVLI 430
Cdd:PRK10938 93 PGEdDTGRTTAEIIQDEVKDPARCEQLAQQF----GITALL----------DRRFKYLSTGETRKTLLCQALMSEPDLLI 158
|
170 180 190
....*....|....*....|....*....|...
gi 494651374 431 LDEPTNHLDLPSREQLEDTLARYDG---TLIIV 460
Cdd:PRK10938 159 LDEPFDGLDVASRQQLAELLASLHQsgiTLVLV 191
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
23-176 |
2.41e-06 |
|
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: 48.68 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI---------------QMMQDVNiyMVEQE------------ 75
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglkltddkkninELRQKVG--MVFQQfnlfphltvlen 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 76 -TEAYDSGHPEPAEAA------LLEKWNVPARAFS---QLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLN 145
Cdd:cd03262 97 iTLAPIKVKGMSKAEAeeraleLLEKVGLADKADAypaQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLD 176
|
170 180 190
....*....|....*....|....*....|....
gi 494651374 146 QIKN--YKG-TIIFVSHDRAFIDAAATKIWAIEG 176
Cdd:cd03262 177 VMKDlaEEGmTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
295-463 |
2.83e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.02 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 295 VRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKvILG--QEKAQGSI---------WISPS--ANVGYLTQ 361
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGrhQPPSEGEIlldaqplesWSSKAfaRKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 362 EvfdLPldkTPEQLFYKETF----------------EARGNVQSLMKHLGFTA-AQwtEPIGKMSMGERVKCKLMAFILE 424
Cdd:PRK10575 93 Q---LP---AAEGMTVRELVaigrypwhgalgrfgaADREKVEEAISLVGLKPlAH--RLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494651374 425 EKDVLILDEPTNHLDLPSREQ---LEDTLARYDG-TLIIVSHD 463
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDvlaLVHRLSQERGlTVIAVLHD 207
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-61 |
3.01e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 49.41 E-value: 3.01e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494651374 4 MLKISGIS--YEINS--VPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI 61
Cdd:PRK11153 1 MIELKNISkvFPQGGrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV 62
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
305-439 |
3.07e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.05 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 305 RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQE----KAQGSIWISP--------SANVGYLTQEVFDLPLDKTP 372
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkgvKGSGSVLLNGmpidakemRAISAYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 373 EQLFYKETF---------EARGNVQSLMKHLGFTAAQWTEpIGK------MSMGERvkcKLMAF---ILEEKDVLILDEP 434
Cdd:TIGR00955 118 EHLMFQAHLrmprrvtkkEKRERVDEVLQALGLRKCANTR-IGVpgrvkgLSGGER---KRLAFaseLLTDPPLLFCDEP 193
|
....*
gi 494651374 435 TNHLD 439
Cdd:TIGR00955 194 TSGLD 198
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
274-433 |
3.30e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.59 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 274 AEYEVRFSIEHRKKAGKRfLEVRDAAKSYDGRTL-FKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIW-- 349
Cdd:PRK10522 305 APYKAEFPRPQAFPDWQT-LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQsGEILld 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 350 ---ISPSANVGY--LTQEVF-DLPLDktpEQLFYKETFEARGN-VQSLMKHLGF----TAAQWTEPIGKMSMGERVKCKL 418
Cdd:PRK10522 384 gkpVTAEQPEDYrkLFSAVFtDFHLF---DQLLGPEGKPANPAlVEKWLERLKMahklELEDGRISNLKLSKGQKKRLAL 460
|
170
....*....|....*
gi 494651374 419 MAFILEEKDVLILDE 433
Cdd:PRK10522 461 LLALAEERDILLLDE 475
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
258-482 |
3.65e-06 |
|
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: 49.94 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 258 KRLEKELEKAKAEPVeaeyevrfSIEHR--KKAGKRFLEVRDAAKSY---DGRTLfKNVNFTVMHGEKIAITGPNGSGKT 332
Cdd:TIGR00957 608 KRLRIFLSHEELEPD--------SIERRtiKPGEGNSITVHNATFTWardLPPTL-NGITFSIPEGALVAVVGQVGCGKS 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 333 TLLKVILGQ-EKAQGSIWISPSanVGYLTQEVF--------DLPLDKTPEQLFYKETFEArgnvQSLMKHLGFTAAQWTE 403
Cdd:TIGR00957 679 SLLSALLAEmDKVEGHVHMKGS--VAYVPQQAWiqndslreNILFGKALNEKYYQQVLEA----CALLPDLEILPSGDRT 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 404 PIGK----MSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLARYDGTL-----IIVSHDRYFVEKtTDIR 474
Cdd:TIGR00957 753 EIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLknktrILVTHGISYLPQ-VDVI 831
|
....*...
gi 494651374 475 LDISNGSV 482
Cdd:TIGR00957 832 IVMSGGKI 839
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
292-462 |
3.67e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 292 FLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWI------------SPSANVGY 358
Cdd:PRK11288 4 YLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGnYQPDAGSILIdgqemrfasttaALAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 359 LTQEVFDLP---------LDKTPEQLFYKETFEARGNVQSLMKHLGFTAAQWTePIGKMSMGERVKCKLMAFILEEKDVL 429
Cdd:PRK11288 84 IYQELHLVPemtvaenlyLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDT-PLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 494651374 430 ILDEPTNHLDLPSREQLEDTLA--RYDGTLII-VSH 462
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRelRAEGRVILyVSH 198
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-159 |
3.91e-06 |
|
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: 48.13 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGIS--YEINSVPL--FEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQ-DVN---------- 68
Cdd:cd03266 1 MITADALTkrFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVkepaearrrl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 69 --------IY--MVEQETEAYDSG----HPEPAEAAL------LEKWNVPARAFSQLSGGEKLKARLAKGFSSSSSLLLL 128
Cdd:cd03266 81 gfvsdstgLYdrLTARENLEYFAGlyglKGDELTARLeeladrLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190
....*....|....*....|....*....|....
gi 494651374 129 DEPTNHLDQHSLEILLNQIKNYKG---TIIFVSH 159
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRAlgkCILFSTH 194
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
310-484 |
4.09e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 48.67 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 310 NVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWI--------SPSANVGYLTQEV---FDLPldktPEQLFY 377
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKpSSGTITIagyhitpeTGNKNLKKLRKKVslvFQFP----EAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 378 KETFEargNVQSLMKHLGFT-------AAQWTEPIG-----------KMSMGERVKCKLMAFILEEKDVLILDEPTNHLD 439
Cdd:PRK13641 101 NTVLK---DVEFGPKNFGFSedeakekALKWLKKVGlsedliskspfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494651374 440 LPSREQLEDTLARYDG---TLIIVSHDRYFVEKTTDIRLDISNGSVRK 484
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
290-469 |
4.13e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.40 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 290 KRFLEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWI------------SPSANV 356
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGiHEPTKGTITInninynkldhklAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 357 GYLTQEVFDLPLDKTPEQLFY-----KETF--------EARGNVQSLMKHLGFTaAQWTEPIGKMSMGERVKCKLMAFIL 423
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIgrhltKKVCgvniidwrEMRVRAAMMLLRVGLK-VDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 424 EEKDVLILDEPTNHLDLPSREQLEDTL--ARYDGTLII-VSH---------DRYFVEK 469
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMnqLRKEGTAIVyISHklaeirricDRYTVMK 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
294-350 |
4.19e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.45 E-value: 4.19e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 294 EVRDAAKSYDGRTLF--KNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWI 350
Cdd:PRK13632 9 KVENVSFSYPNSENNalKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQsGEIKI 68
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-171 |
4.23e-06 |
|
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: 47.63 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI----QMMQDV-----NIYMVEQE 75
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggRDVTDLppkdrDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 76 TEAY----------------DSGHPEPAE-----AALLEKWNVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNH 134
Cdd:cd03301 81 YALYphmtvydniafglklrKVPKDEIDErvrevAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 494651374 135 LDQHSLEILLNQIKNY----KGTIIFVSHDRAFIDAAATKI 171
Cdd:cd03301 161 LDAKLRVQMRAELKRLqqrlGTTTIYVTHDQVEAMTMADRI 201
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-171 |
4.25e-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: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQ----------LICNQKAPSQ------GQIQMMQDVNI-YMVeqeteaydsghpe 85
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLVNeglyasgkarLISFLPKFSRnklifiDQLQFLIDVGLgYLT------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 86 paeaallekwnvPARAFSQLSGGEKLKARLAK--GFSSSSSLLLLDEPTNHLDQHSLEILLNQIK---NYKGTIIFVSHD 160
Cdd:cd03238 81 ------------LGQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLEVIKgliDLGNTVILIEHN 148
|
170
....*....|.
gi 494651374 161 RAFIDAAATKI 171
Cdd:cd03238 149 LDVLSSADWII 159
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-207 |
4.33e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.27 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 21 EQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQETEAYDSGhPEPAEAALL-------- 92
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTG-IENIEFKMLcmgfkrke 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 93 -EKWNVPARAFSQL-----------SGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYK---GTIIFV 157
Cdd:PRK13546 120 iKAMTPKIIEFSELgefiyqpvkkySSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKeqnKTIFFV 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494651374 158 SHDRAFIDAAATKIWAIEGKKLIEHKG------NYSSYMEVRKQRRLTQQREYENQ 207
Cdd:PRK13546 200 SHNLGQVRQFCTKIAWIEGGKLKDYGElddvlpKYEAFLNDFKKKSKAEQKEFRNK 255
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-61 |
5.35e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 48.54 E-value: 5.35e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494651374 4 MLKISGIS--YEIN--SVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI 61
Cdd:COG1135 1 MIELENLSktFPTKggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSV 62
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
293-462 |
5.60e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 48.11 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKV-------ILGQeKAQGSIWI------SPSANVGYL 359
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGA-RVEGEILLdgediyDPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQE---VFDLPldkTPeqlFYKETFEargNV--------------------QSLMKhlgftAAQWTEpigkmsmgerVKC 416
Cdd:COG1117 91 RRRvgmVFQKP---NP---FPKSIYD---NVayglrlhgikskseldeiveESLRK-----AALWDE----------VKD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494651374 417 KL--MAFILE---------------EKDVLILDEPTNHLDLPSREQLEDTLA----RYdgTLIIVSH 462
Cdd:COG1117 147 RLkkSALGLSggqqqrlciaralavEPEVLLMDEPTSALDPISTAKIEELILelkkDY--TIVIVTH 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-185 |
6.25e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 47.78 E-value: 6.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLI-----------------CNQKAPSQGQIQ---- 62
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitsgdlivdglkVNDPKVDERLIRqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 63 -MMQDVNIY--MVEQETEAYDSGH-----PEPAEA---ALLEKWNVPARAF---SQLSGGEKLKARLAKGFSSSSSLLLL 128
Cdd:PRK09493 81 mVFQQFYLFphLTALENVMFGPLRvrgasKEEAEKqarELLAKVGLAERAHhypSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 129 DEPTNHLD---QHSLEILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGKKlIEHKGN 185
Cdd:PRK09493 161 DEPTSALDpelRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR-IAEDGD 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-159 |
6.39e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 47.18 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQETEAYdSGH 83
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY-LGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 84 -----------------------PEPAEAALLEKWNVPA---RAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQ 137
Cdd:PRK13539 81 rnamkpaltvaenlefwaaflggEELDIAAALEAVGLAPlahLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180
....*....|....*....|....*
gi 494651374 138 HSLEILLNQIK---NYKGTIIFVSH 159
Cdd:PRK13539 161 AAVALFAELIRahlAQGGIVIAATH 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
277-350 |
6.40e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.87 E-value: 6.40e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494651374 277 EVRFSIEHRK-KAGKRFLEVRD-AAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWI 350
Cdd:COG3845 241 EVLLRVEKAPaEPGEVVLEVENlSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAsGSIRL 317
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-160 |
6.56e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.50 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI----QMMQDVN--------------IYMVEQETEAYDS--- 81
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngQPMSKLSsaakaelrnqklgfIYQFHHLLPDFTAlen 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 82 -------GHPEPAEA-----ALLEKWNVPARAF---SQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQH---SLEIL 143
Cdd:PRK11629 108 vamplliGKKKPAEInsralEMLAAVGLEHRANhrpSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARnadSIFQL 187
|
170
....*....|....*...
gi 494651374 144 LNQIKNYKGT-IIFVSHD 160
Cdd:PRK11629 188 LGELNRLQGTaFLVVTHD 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
27-164 |
6.64e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 47.56 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 27 VQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI-----------------------QMMQDVNIYMveqETEAYD--- 80
Cdd:PRK10908 25 MRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditrlknrevpflrrqigMIFQDHHLLM---DRTVYDnva 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 81 --------SGHP--EPAEAAL-----LEKwnvpARAFS-QLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILL 144
Cdd:PRK10908 102 ipliiagaSGDDirRRVSAALdkvglLDK----AKNFPiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIL 177
|
170 180
....*....|....*....|...
gi 494651374 145 NQIKNYKG---TIIFVSHDRAFI 164
Cdd:PRK10908 178 RLFEEFNRvgvTVLMATHDIGLI 200
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-182 |
6.69e-06 |
|
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: 47.19 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGdIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDVNIYMVE---------Q 74
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDgQDVLKQPQKlrrrigylpQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 75 ETEAYD------------------SGHPEPAEAALLEK---WNVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTN 133
Cdd:cd03264 80 EFGVYPnftvrefldyiawlkgipSKEVKARVDEVLELvnlGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494651374 134 HLD---QHSLEILLNQIKNYKgTIIFVSHDRAFIDAAATKIWAIEGKKLIEH 182
Cdd:cd03264 160 GLDpeeRIRFRNLLSELGEDR-IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-340 |
8.04e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 27 VQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQG---------------QIQMM-----QDVNIYMV---EQET-----EA 78
Cdd:PRK10938 26 LNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshitrlsfeQLQKLvsdewQRNNTDMLspgEDDTgrttaEI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 79 YDSGHPEPAEAALLEKW----NVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHS---LEILLNQIKNYK 151
Cdd:PRK10938 106 IQDEVKDPARCEQLAQQfgitALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASrqqLAELLASLHQSG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 152 GTIIFVSHDRAFIDAAATKIWAIEGKKLIEhkgnyssymevrkqrrlTQQREYENQQHMIrrieAQMnelsawskkAHAQ 231
Cdd:PRK10938 186 ITLVLVLNRFDEIPDFVQFAGVLADCTLAE-----------------TGEREEILQQALV----AQL---------AHSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 232 stkiegfkeyhrvkakrtdaqikskqkRLEKELEKAKAEPveaeyevrfSIEHRKKAGKRFLEVRDAAKSYDGRTLFKNV 311
Cdd:PRK10938 236 ---------------------------QLEGVQLPEPDEP---------SARHALPANEPRIVLNNGVVSYNDRPILHNL 279
|
330 340
....*....|....*....|....*....
gi 494651374 312 NFTVMHGEKIAITGPNGSGKTTLLKVILG 340
Cdd:PRK10938 280 SWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
293-463 |
8.04e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 47.36 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQGSIWISPSA-------NVGYLTQEVFD 365
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAplaeareDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 366 LPLDKT-------------PEQLfykETFEARGnvqslmkhLGFTAAQWtePiGKMSMGERVKCKLMAFILEEKDVLILD 432
Cdd:PRK11247 93 LPWKKVidnvglglkgqwrDAAL---QALAAVG--------LADRANEW--P-AALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190
....*....|....*....|....*....|....*
gi 494651374 433 EPTNHLDLPSR---EQLEDTLARYDG-TLIIVSHD 463
Cdd:PRK11247 159 EPLGALDALTRiemQDLIESLWQQHGfTVLLVTHD 193
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
293-340 |
8.21e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 8.21e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG 340
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
23-61 |
9.15e-06 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 47.34 E-value: 9.15e-06
10 20 30
....*....|....*....|....*....|....*....
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI 61
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRI 61
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
307-463 |
1.06e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 46.73 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 307 LFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQE---------KAQGSIWISPSA-------NVGYLTQEVFDLPlDK 370
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDtptsgdvifNGQPMSKLSSAAkaelrnqKLGFIYQFHHLLP-DF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 371 T-------PEQLFYKETFEARGNVQSLMKHLGFTAAQWTEPiGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSR 443
Cdd:PRK11629 103 TalenvamPLLIGKKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180
....*....|....*....|....
gi 494651374 444 E---QLEDTLARYDGT-LIIVSHD 463
Cdd:PRK11629 182 DsifQLLGELNRLQGTaFLVVTHD 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
293-349 |
1.41e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 47.76 E-value: 1.41e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 293 LEVRDAAKSYDGRT-LF----------KNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQGSIW 349
Cdd:COG4172 276 LEARDLKVWFPIKRgLFrrtvghvkavDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIR 343
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
302-462 |
1.57e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 47.04 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 302 YDGRTLFkNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ-EKAQGSIWISPSANVGYLTQE-----------VFDLPLD 369
Cdd:PRK13643 17 FASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlQPTEGKVTVGDIVVSSTSKQKeikpvrkkvgvVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 370 KTPEQLFYKETF-----------EARGNVQSLMKHLGFTAAQWTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHL 438
Cdd:PRK13643 96 QLFEETVLKDVAfgpqnfgipkeKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180
....*....|....*....|....*..
gi 494651374 439 DLPSR---EQLEDTLARYDGTLIIVSH 462
Cdd:PRK13643 176 DPKARiemMQLFESIHQSGQTVVLVTH 202
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-161 |
1.61e-05 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 47.06 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLIcnqkA----PSQGQIQM----------MQDVNIY 70
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII----AgletPDSGRIVLngrdlftnlpPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 71 MVEQEteaY----------------DSGHPEPAEAA-----LLEKWNVP--ARAF-SQLSGGEK----LkAR-------- 114
Cdd:COG1118 79 FVFQH---YalfphmtvaeniafglRVRPPSKAEIRarveeLLELVQLEglADRYpSQLSGGQRqrvaL-ARalavepev 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494651374 115 --LakgfsssssllllDEPTNHLDQH---SLEILLNQI-KNYKGTIIFVSHDR 161
Cdd:COG1118 155 llL-------------DEPFGALDAKvrkELRRWLRRLhDELGGTTVFVTHDQ 194
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
293-350 |
1.75e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.71 E-value: 1.75e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 293 LEVRDAAKSYDGRT-LF--------KNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ-EKAQGSIWI 350
Cdd:PRK15112 5 LEVRNLSKTFRYRTgWFrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMiEPTSGELLI 72
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
23-162 |
1.84e-05 |
|
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: 46.27 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDV--------------NIYMVEQE-------TeAYD 80
Cdd:COG4181 31 ISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAgQDLfaldedararlrarHVGFVFQSfqllptlT-ALE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 81 --------SGHPEPAE--AALLEKWNVPARAF---SQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHS----LEIL 143
Cdd:COG4181 110 nvmlplelAGRRDARAraRALLERVGLGHRLDhypAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLL 189
|
170
....*....|....*....
gi 494651374 144 LNQIKNYKGTIIFVSHDRA 162
Cdd:COG4181 190 FELNRERGTTLVLVTHDPA 208
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-61 |
1.89e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.57 E-value: 1.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI 61
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV 58
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-62 |
1.90e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 1.90e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQ 62
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL 62
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
293-350 |
1.99e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 46.23 E-value: 1.99e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494651374 293 LEVRDAAKSY-----DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI 350
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPdSGSILI 65
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-160 |
2.23e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 46.16 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIqMMQDVNIYMVE-----------------------QETEAY 79
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTV-FLGDKPISMLSsrqlarrlallpqhhltpegitvRELVAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 80 D-----------SGHPEPAEAALLEKWNVPA---RAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLD-QHSLEI-- 142
Cdd:PRK11231 100 GrspwlslwgrlSAEDNARVNQAMEQTRINHladRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDiNHQVELmr 179
|
170
....*....|....*...
gi 494651374 143 LLNQIKNYKGTIIFVSHD 160
Cdd:PRK11231 180 LMRELNTQGKTVVTVLHD 197
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
293-463 |
2.82e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 45.90 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLF--KNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWISPSA----NVGYLTQE--- 362
Cdd:PRK13648 8 IVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKsGEIFYNNQAitddNFEKLRKHigi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 363 VFdlpldKTPEQLF------YKETF----------EARGNVQSLMKHLGFTAAQWTEPiGKMSMGERVKCKLMAFILEEK 426
Cdd:PRK13648 88 VF-----QNPDNQFvgsivkYDVAFglenhavpydEMHRRVSEALKQVDMLERADYEP-NALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 494651374 427 DVLILDEPTNHLDLPSREQLEDTLAR----YDGTLIIVSHD 463
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKvkseHNITIISITHD 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
310-461 |
2.97e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.04 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 310 NVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIW----------ISPSANVGYLTQEvFDLPLDKTPEQ---- 374
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGlLPASEGEAWlfgqpvdagdIATRRRVGYMSQA-FSLYGELTVRQnlel 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 375 ---LFYKETFEARGNVQSLMKHLGFTAAQWTEPiGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSR----EQLE 447
Cdd:NF033858 363 harLFHLPAAEIAARVAEMLERFDLADVADALP-DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARdmfwRLLI 441
|
170
....*....|....
gi 494651374 448 DtLARYDGTLIIVS 461
Cdd:NF033858 442 E-LSREDGVTIFIS 454
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
293-485 |
3.33e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 45.73 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWISPSA------NVGYLtqEVFD 365
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKpSEGSIVVNGQTinlvrdKDGQL--KVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 366 ---LPLDKT------------------------PEQLFYKETFEARGNVQSLMKHLGFT-AAQWTEPIgKMSMGERVKCK 417
Cdd:PRK10619 84 knqLRLLRTrltmvfqhfnlwshmtvlenvmeaPIQVLGLSKQEARERAVKYLAKVGIDeRAQGKYPV-HLSGGQQQRVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494651374 418 LMAFILEEKDVLILDEPTNHLD---LPSREQLEDTLARYDGTLIIVSHDRYFVEKTTDIRLDISNGSVRKQ 485
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
293-463 |
3.37e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 46.64 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSY---DGRT-LFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQGSIWISPSANV------------ 356
Cdd:PRK10535 5 LELKDIRRSYpsgEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldadalaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 357 ----GYLTQEVFDLPlDKTPEQ-----LFY--KETFEARGNVQSLMKHLGFTAAQWTEPiGKMSMGERVKCKLMAFILEE 425
Cdd:PRK10535 85 rehfGFIFQRYHLLS-HLTAAQnvevpAVYagLERKQRLLRAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 494651374 426 KDVLILDEPTNHLDLPSREQLEDTLA--RYDG-TLIIVSHD 463
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHqlRDRGhTVIIVTHD 203
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-171 |
3.49e-05 |
|
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: 43.90 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 29 QGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIqmmqdvniymveqeteAYDSGHPEPAEAALLEKWNVPARAFSQLSGG 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV----------------IYIDGEDILEEVLDQLLLIIVGGKKASGSGE 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494651374 109 EKLKARLAKGFSSSSSLLLLDEPTNHLDQHS---------LEILLNQIKNYKGTIIFVSHDRAFIDAAATKI 171
Cdd:smart00382 65 LRLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-161 |
3.50e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 46.37 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI------------------QMMQ 65
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlshvppyqrpinMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 66 DVNIY--MVEQETEAYDSGHPEPAEA----------ALLEKWNVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTN 133
Cdd:PRK11607 99 SYALFphMTVEQNIAFGLKQDKLPKAeiasrvnemlGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190
....*....|....*....|....*....|...
gi 494651374 134 HLDQH-----SLEIlLNQIKNYKGTIIFVSHDR 161
Cdd:PRK11607 179 ALDKKlrdrmQLEV-VDILERVGVTCVMVTHDQ 210
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-61 |
3.59e-05 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 45.36 E-value: 3.59e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI 61
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSI 60
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
293-461 |
3.78e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 45.39 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLK----VILGQEKAQGSIWI----------------SP 352
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELlgrtvqregrlardirKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 353 SANVGYLTQEvFDL-------------PLDKTPeqlFYKETF------EARGNVQSL----MKHLGFtaaqwtEPIGKMS 409
Cdd:PRK09984 85 RANTGYIFQQ-FNLvnrlsvlenvligALGSTP---FWRTCFswftreQKQRALQALtrvgMVHFAH------QRVSTLS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494651374 410 MGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLA---RYDGTLIIVS 461
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdinQNDGITVVVT 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
293-482 |
3.80e-05 |
|
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: 45.26 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGR----TLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWISpsanvgylTQEVFDLP 367
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERpTSGSVLVD--------GTDLTLLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 368 LDKTPEQ------------LFYKETfeARGNVQSLMKHLGftaaqwtepIGKMSMGERVKcKLMAFI-LEEK-------- 426
Cdd:cd03258 74 GKELRKArrrigmifqhfnLLSSRT--VFENVALPLEIAG---------VPKAEIEERVL-ELLELVgLEDKadaypaql 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 427 ------------------DVLILDEPTNHLDLPSREQ----LEDTLARYDGTLIIVSHDRYFVEKTTDIRLDISNGSV 482
Cdd:cd03258 142 sggqkqrvgiaralannpKVLLCDEATSALDPETTQSilalLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-160 |
4.02e-05 |
|
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: 45.02 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI---------QMMQDVNIYMVEQ- 74
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedatdVPVQERNVGFVFQh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 75 ----------ETEAY----DSGHPEPAEAALLEKWN----------VPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDE 130
Cdd:cd03296 83 yalfrhmtvfDNVAFglrvKPRSERPPEAEIRAKVHellklvqldwLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190
....*....|....*....|....*....|....
gi 494651374 131 PTNHLD---QHSLEILLNQIKNYKG-TIIFVSHD 160
Cdd:cd03296 163 PFGALDakvRKELRRWLRRLHDELHvTTVFVTHD 196
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
104-175 |
4.19e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.91 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 104 QLSGGEKLKA----RLA--KGFSSSSSLLLLDEPTNHLDQHSLEI-LLNQIKNYKGT----IIFVSHDRAFIDaAATKIW 172
Cdd:cd03240 115 RCSGGEKVLAsliiRLAlaETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQknfqLIVITHDEELVD-AADHIY 193
|
...
gi 494651374 173 AIE 175
Cdd:cd03240 194 RVE 196
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-167 |
5.57e-05 |
|
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: 44.76 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 21 EQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM----------------------------------MQD 66
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILegkqitepgpdrmvvfqnysllpwltvrenialaVDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 67 VNIYMVEQETEAYDSGHpepaeAALLEKWNVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLD---QHSLEIL 143
Cdd:TIGR01184 82 VLPDLSKSERRAIVEEH-----IALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDaltRGNLQEE 156
|
170 180
....*....|....*....|....*
gi 494651374 144 LNQIKNYKG-TIIFVSHDrafIDAA 167
Cdd:TIGR01184 157 LMQIWEEHRvTVLMVTHD---VDEA 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
293-462 |
5.80e-05 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 44.33 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSY--DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWIS----PSANVGYLTQEVFD 365
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRfLEAEEGKIEIDgidiSTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 366 LPLDKTpeqLFyketfeaRGNVQSLMKHLG-------FTAAQWTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHL 438
Cdd:cd03369 87 IPQDPT---LF-------SGTIRSNLDPFDeysdeeiYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASI 156
|
170 180
....*....|....*....|....*.
gi 494651374 439 DLPSREQLEDTLAR--YDGTLIIVSH 462
Cdd:cd03369 157 DYATDALIQKTIREefTNSTILTIAH 182
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-159 |
6.44e-05 |
|
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: 44.05 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLI--CNQKAPSQGQIqMMQDVNIymVEQETEaydsg 82
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEI-LFKGEDI--TDLPPE----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 83 hpEPAEAALLEKWNVPAR------------AFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNY 150
Cdd:cd03217 73 --ERARLGIFLAFQYPPEipgvknadflryVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL 150
|
170
....*....|..
gi 494651374 151 KG---TIIFVSH 159
Cdd:cd03217 151 REegkSVLIITH 162
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-61 |
7.35e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 45.54 E-value: 7.35e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 494651374 11 SYEiNSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI 61
Cdd:COG1132 348 SYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI 397
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
318-473 |
7.75e-05 |
|
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: 43.71 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 318 GEKIAITGPNGSGKTTLLKVILGQEKAQGSIWISPSANVGYLTQEVfdlpldktpeqlfyketfeargnvqslmkhlgft 397
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI---------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 398 aaqwtepigKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLARY----DGTLIIVSHDRYFVEKTTDI 473
Cdd:cd03222 71 ---------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSDR 141
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
293-340 |
8.26e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.21 E-value: 8.26e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG 340
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTG 53
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
293-462 |
8.27e-05 |
|
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: 44.46 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSY--DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQGSI------WISPSAN-----VGYL 359
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIqidgvsWNSVPLQkwrkaFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQEVFDL---------PLDKTPEQLFYKETFEA--RGNVQSLMKHLGFtaaQWTEPIGKMSMGERVKCKLMAFILEEKDV 428
Cdd:cd03289 83 PQKVFIFsgtfrknldPYGKWSDEEIWKVAEEVglKSVIEQFPGQLDF---VLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 494651374 429 LILDEPTNHLDLPSREQLEDTL--ARYDGTLIIVSH 462
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLkqAFADCTVILSEH 195
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
23-63 |
8.42e-05 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 43.96 E-value: 8.42e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM 63
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF 59
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
293-342 |
9.44e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.01 E-value: 9.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQE 342
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRE 51
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-177 |
9.52e-05 |
|
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: 43.33 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 27 VQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMmqdvniymvEQETEAYDsghPEpaeaallekwnvparaFSQLS 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW---------DGITPVYK---PQ----------------YIDLS 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494651374 107 GGEKLKARLAKGFSSSSSLLLLDEPTNHLDQ----HSLEILLNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEGK 177
Cdd:cd03222 74 GGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
303-461 |
1.06e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 44.10 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 303 DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIWI--SPSAN------VGYLTQ-EVFDLPLDKTP 372
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRlASGKISIlgQPTRQalqknlVAYVPQsEEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 373 EQ-----------LFYKETFEARGNVQSLMKHLGFTAAQWTEpIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLP 441
Cdd:PRK15056 98 EDvvmmgryghmgWLRRAKKRDRQIVTAALARVDMVEFRHRQ-IGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180
....*....|....*....|..
gi 494651374 442 SREQLEDTLA--RYDGTLIIVS 461
Cdd:PRK15056 177 TEARIISLLRelRDEGKTMLVS 198
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-63 |
1.10e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 43.92 E-value: 1.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM 63
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITL 60
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
293-485 |
1.15e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRT---LFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQGSIWISPSANVGYLTQE--VFDLP 367
Cdd:PLN03232 615 ISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVPQVswIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 368 LDktpEQLFYKETFEARG-----NVQSLMKHLGFTAAQWTEPIGK----MSMGERVKCKLMAFILEEKDVLILDEPTNHL 438
Cdd:PLN03232 695 VR---ENILFGSDFESERywraiDVTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494651374 439 DLPSREQLEDTLARYD---GTLIIVSHDRYFVEKTTDIRLdISNGSVRKQ 485
Cdd:PLN03232 772 DAHVAHQVFDSCMKDElkgKTRVLVTNQLHFLPLMDRIIL-VSEGMIKEE 820
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-160 |
1.23e-04 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 43.92 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGIS----YEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDVN-----IYMVE 73
Cdd:COG1116 7 ALELRGVSkrfpTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDgKPVTgpgpdRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 74 QE-------TeAYD--------SGHPEP-----AEAAL----LEKWnvpARAF-SQLSGGEKLKARLAKGFSSSSSLLLL 128
Cdd:COG1116 87 QEpallpwlT-VLDnvalglelRGVPKAerrerARELLelvgLAGF---EDAYpHQLSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 494651374 129 DEPTNHLDQ---HSLEILLNQI-KNYKGTIIFVSHD 160
Cdd:COG1116 163 DEPFGALDAltrERLQDELLRLwQETGKTVLFVTHD 198
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
293-440 |
1.35e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 43.30 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQ-GSIWISPSAN--------VGYLTQev 363
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVEsGQIQIDGKTAtrgdrsrfMAYLGH-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 364 fdLPLDK----TPEQLFYKETFEARGNVQ---SLMKHLGFTAAQWTePIGKMSMGERVKCKLMAFILEEKDVLILDEPTN 436
Cdd:PRK13543 90 --LPGLKadlsTLENLHFLCGLHGRRAKQmpgSALAIVGLAGYEDT-LVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
....
gi 494651374 437 HLDL 440
Cdd:PRK13543 167 NLDL 170
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-160 |
1.39e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 43.97 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI---------QMMQDV--NIYMVEQETE-------------- 77
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitdDNFEKLrkHIGIVFQNPDnqfvgsivkydvaf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 78 -------AYDSGHPEPAEAalLEKWNVPARAFSQ---LSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQI 147
Cdd:PRK13648 108 glenhavPYDEMHRRVSEA--LKQVDMLERADYEpnaLSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLV 185
|
170
....*....|....*..
gi 494651374 148 KNYKG----TIIFVSHD 160
Cdd:PRK13648 186 RKVKSehniTIISITHD 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
293-438 |
1.39e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.61 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSI-WI-----------SPSANVGYL 359
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGiYTRDAGSIlYLgkevtfngpksSQEAGIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQEVFDLPLDKTPEQLFYKETFEAR-GNVQ---------SLMKHLGFTAAQWTePIGKMSMGER--VK-CKLMAFileEK 426
Cdd:PRK10762 85 HQELNLIPQLTIAENIFLGREFVNRfGRIDwkkmyaeadKLLARLNLRFSSDK-LVGELSIGEQqmVEiAKVLSF---ES 160
|
170
....*....|..
gi 494651374 427 DVLILDEPTNHL 438
Cdd:PRK10762 161 KVIIMDEPTDAL 172
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
293-463 |
1.52e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.92 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRT-----LFKNVNFTVMHGEKIAITGPNGSGKTTL---LKVILGQEkaQGSI-WI----SPSANVGYL 359
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLLPD--TGTIeWIfkdeKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 360 TQEVFDLPLDKTpeqlfykeTFEARGNVQSLMKHLG----FTAAQWTEP-------IGKMSMG-------ERVKCKL--- 418
Cdd:PRK13651 81 EKVLEKLVIQKT--------RFKKIKKIKEIRRRVGvvfqFAEYQLFEQtiekdiiFGPVSMGvskeeakKRAAKYIelv 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494651374 419 -----------------------MAFILE-EKDVLILDEPTNHLDlP--SREQLE--DTLARYDGTLIIVSHD 463
Cdd:PRK13651 153 gldesylqrspfelsggqkrrvaLAGILAmEPDFLVFDEPTAGLD-PqgVKEILEifDNLNKQGKTIILVTHD 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-182 |
1.61e-04 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 43.30 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 17 VPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI----QMMQDVNIY-------MVEQETEAYD----- 80
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgVDIRDLNLRwlrsqigLVSQEPVLFDgtiae 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 81 -------SGHPEPAEAA------------LLEKWN--VPARAfSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHS 139
Cdd:cd03249 96 nirygkpDATDEEVEEAakkanihdfimsLPDGYDtlVGERG-SQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494651374 140 LEIL---LNQIKnyKG-TIIFVSHDRAFIdAAATKIWAIEGKKLIEH 182
Cdd:cd03249 175 EKLVqeaLDRAM--KGrTTIVIAHRLSTI-RNADLIAVLQNGQVVEQ 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-160 |
1.73e-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: 42.42 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 2 KEMLKISGISyeinsVPL-FEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDVNIYMVEqetEAY 79
Cdd:cd03215 2 EPVLEVRGLS-----VKGaVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgKPVTRRSPR---DAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 80 DSG--H-PE-PAEAALLEKWNVPARAF--SQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHS-LEI--LLNQIKNY 150
Cdd:cd03215 74 RAGiaYvPEdRKREGLVLDLSVAENIAlsSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAkAEIyrLIRELADA 153
|
170
....*....|
gi 494651374 151 KGTIIFVSHD 160
Cdd:cd03215 154 GKAVLLISSE 163
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
98-339 |
1.75e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 98 PARAFSQLSGGEKLKARLAK--GFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYK---GTIIFVSHDRAFIDAAAtkiW 172
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATqiGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRdlgNTLIVVEHDEDTIRAAD---Y 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 173 AIE-GKKLIEHKGNyssymevrkqrrltqqreyenqqhmirrieaqmnelsawskkahaqstkiegfkeyhrVKAKRTDA 251
Cdd:TIGR00630 559 VIDiGPGAGEHGGE----------------------------------------------------------VVASGTPE 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 252 QIKSKQKRLE-KELEKAKAEPVEAEyevrfsiehRKKAGKRFLEVRDAAKSYdgrtlFKNVNFTVMHGEKIAITGPNGSG 330
Cdd:TIGR00630 581 EILANPDSLTgQYLSGRKKIEVPAE---------RRPGNGKFLTLKGARENN-----LKNITVSIPLGLFTCITGVSGSG 646
|
....*....
gi 494651374 331 KTTLLKVIL 339
Cdd:TIGR00630 647 KSTLINDTL 655
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
293-469 |
1.79e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 43.52 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDG---------RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSI-WI----------- 350
Cdd:PRK10419 4 LNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVsWRgeplaklnraq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 351 --------------SPSA-----NVGYLTQEVFD--LPLDKTpEQlfyketfEARgnVQSLMKHLGFTAAQWTEPIGKMS 409
Cdd:PRK10419 84 rkafrrdiqmvfqdSISAvnprkTVREIIREPLRhlLSLDKA-ER-------LAR--ASEMLRAVDLDDSVLDKRPPQLS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494651374 410 MG--ERVkCKLMAFILEEKdVLILDEPTNHLDLPSR----EQLEDTLARYDGTLIIVSHDRYFVEK 469
Cdd:PRK10419 154 GGqlQRV-CLARALAVEPK-LLILDEAVSNLDLVLQagviRLLKKLQQQFGTACLFITHDLRLVER 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-177 |
2.03e-04 |
|
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: 43.17 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 26 SVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMMQDVNIYMVEQETEAYDSghpePAEAALLEK---------WN 96
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEG----TVRDLLSSItkdfythpyFK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 97 VPA-----------RAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLD--QHSL--EILLNQIKNYKGTIIFVSHDR 161
Cdd:cd03237 97 TEIakplqieqildREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveQRLMasKVIRRFAENNEKTAFVVEHDI 176
|
170
....*....|....*.
gi 494651374 162 AFIDAAATKIWAIEGK 177
Cdd:cd03237 177 IMIDYLADRLIVFEGE 192
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-61 |
2.06e-04 |
|
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: 42.92 E-value: 2.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI 61
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKI 57
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
293-348 |
2.19e-04 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 43.55 E-value: 2.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 494651374 293 LEVrDAAKSYDGRTLfkNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSI 348
Cdd:COG4148 3 LEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPdSGRI 56
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
304-462 |
2.40e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.97 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 304 GRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVIlgqekaqGSIW--------ISPSANVGYLTQEVFdLPLDKTPEQL 375
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-------GELWpvyggrltKPAKGKLFYVPQRPY-MTLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 376 FY---KETFEARG-----------NVQ---SLMKHLGFTAAQ-WTEpigKMSMGERVKCKlMAFILEEK-DVLILDEPTN 436
Cdd:TIGR00954 536 IYpdsSEDMKRRGlsdkdleqildNVQlthILEREGGWSAVQdWMD---VLSGGEKQRIA-MARLFYHKpQFAILDECTS 611
|
170 180
....*....|....*....|....*.
gi 494651374 437 HLDLPSREQLEDTLARYDGTLIIVSH 462
Cdd:TIGR00954 612 AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
318-463 |
2.74e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 43.62 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 318 GEKIAITGPNGSGKTTLLKVILGQEK-------------------------------AQGSIwispsaNVGYLTQEVFDL 366
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKpnlgdydeepswdevlkrfrgtelqdyfkklANGEI------KVAHKPQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 367 P--LDKTPEQLFykETFEARGNVQSLMKHLGFTAAqWTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLpsRE 444
Cdd:COG1245 173 PkvFKGTVRELL--EKVDERGKLDELAEKLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI--YQ 247
|
170 180
....*....|....*....|....
gi 494651374 445 QLE-----DTLARYDGTLIIVSHD 463
Cdd:COG1245 248 RLNvarliRELAEEGKYVLVVEHD 271
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
303-340 |
2.77e-04 |
|
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: 42.47 E-value: 2.77e-04
10 20 30
....*....|....*....|....*....|....*...
gi 494651374 303 DGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG 340
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQR 50
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
23-165 |
2.80e-04 |
|
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: 42.56 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQG----------------------QIQMM-QDVNIymVEQET--E 77
Cdd:cd03256 20 VSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGsvlidgtdinklkgkalrqlrrQIGMIfQQFNL--IERLSvlE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 78 AYDSG---------------HPEPAEAAL--LEKWNVPARAF---SQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQ 137
Cdd:cd03256 98 NVLSGrlgrrstwrslfglfPKEEKQRALaaLERVGLLDKAYqraDQLSGGQQQRVAIARALMQQPKLILADEPVASLDP 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 494651374 138 HSLEI---LLNQIKNYKG-TIIFVSHD----RAFID 165
Cdd:cd03256 178 ASSRQvmdLLKRINREEGiTVIVSLHQvdlaREYAD 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
318-463 |
3.12e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 318 GEKIAITGPNGSGKTTLLKVI-------LGQEKAQGSiW-----------------------ISPSANVGYLTQ--EVF- 364
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILsgelipnLGDYEEEPS-WdevlkrfrgtelqnyfkklyngeIKVVHKPQYVDLipKVFk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 365 ----DLpLDKTPEqlfyketfeaRGNVQSLMKHLGFTAAqWTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDL 440
Cdd:PRK13409 178 gkvrEL-LKKVDE----------RGKLDEVVERLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180
....*....|....*....|....*
gi 494651374 441 PSREQLEDTLARY--DGTLIIVSHD 463
Cdd:PRK13409 246 RQRLNVARLIRELaeGKYVLVVEHD 270
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-161 |
3.19e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 43.15 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDVNI-------------- 69
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgTDVSRlhardrkvgfvfqh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 70 YMVEQETEAYDS---------GHPEPAEAA-------LLEKWNVP---ARAFSQLSGGEKLKARLAKGFSSSSSLLLLDE 130
Cdd:PRK10851 83 YALFRHMTVFDNiafgltvlpRRERPNAAAikakvtqLLEMVQLAhlaDRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190
....*....|....*....|....*....|....*
gi 494651374 131 PTNHLD---QHSLEILLNQIKN-YKGTIIFVSHDR 161
Cdd:PRK10851 163 PFGALDaqvRKELRRWLRQLHEeLKFTSVFVTHDQ 197
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
293-482 |
3.72e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 42.17 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 293 LEVRDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWISPSANVGYLTQEVFDLPLDKT 371
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRAtSGRIVFDGKDITDWQTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 372 PEQlfyKETFeARGNVQSLMKHLGFTA--AQWTEPI------------------GKMSMGERVKCKLMAFILEEKDVLIL 431
Cdd:PRK11614 86 PEG---RRVF-SRMTVEENLAMGGFFAerDQFQERIkwvyelfprlherriqraGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494651374 432 DEPTNHLDLPSREQLEDTLA--RYDG-TLIIVSHDRYFVEKTTDIRLDISNGSV 482
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEqlREQGmTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
293-350 |
3.73e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 42.76 E-value: 3.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494651374 293 LEVRDAAKSYDGR----TLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKA-QGSIWI 350
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPtSGSVLV 64
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-136 |
3.89e-04 |
|
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: 43.12 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEI-NSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI--------QMMQDVN---IYMV 72
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvsSLDQDEVrrrVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 73 EQETEAYDS--------GHPEPAEAAL--------LEKWnvpARAF------------SQLSGGEKLKARLAKGFSSSSS 124
Cdd:TIGR02868 415 AQDAHLFDTtvrenlrlARPDATDEELwaalervgLADW---LRALpdgldtvlgeggARLSGGERQRLALARALLADAP 491
|
170
....*....|..
gi 494651374 125 LLLLDEPTNHLD 136
Cdd:TIGR02868 492 ILLLDEPTEHLD 503
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-161 |
4.38e-04 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 42.78 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 1 MKEMLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM-QDV--------NIYM 71
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgRDVtglppekrNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 72 VEQEteaYdsghpepaeaAL-------------LEKWNVP-----ARAF----------------SQLSGGEK----LkA 113
Cdd:COG3842 82 VFQD---Y----------ALfphltvaenvafgLRMRGVPkaeirARVAellelvglegladrypHQLSGGQQqrvaL-A 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 114 R-LAKG-----FsssssllllDEPTNHLDQH---SLEILLNQI-KNYKGTIIFVSHDR 161
Cdd:COG3842 148 RaLAPEprvllL---------DEPLSALDAKlreEMREELRRLqRELGITFIYVTHDQ 196
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-136 |
5.09e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 42.98 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 18 PLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQ-----------------MMQDVNIYMVEQETEAYD 80
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKhsgrisfspqtswimpgTIKDNIIFGLSYDEYRYT 519
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494651374 81 S----GHPEPAEAALLEKWNVP-ARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLD 136
Cdd:TIGR01271 520 SvikaCQLEEDIALFPEKDKTVlGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
288-348 |
5.11e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.78 E-value: 5.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494651374 288 AGKRFLEVRDAAKSYDG--RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ-EKAQGSI 348
Cdd:PRK10789 309 EGRGELDVNIRQFTYPQtdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHfDVSEGDI 372
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-160 |
5.73e-04 |
|
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: 41.86 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 3 EMLKISGISYEI----NSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM-MQDVN--------- 68
Cdd:cd03294 19 KLLAKGKSKEEIlkktGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIdGQDIAamsrkelre 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 69 -----IYMVEQ-----------ETEAYD---SGHP-----EPAEAAL----LEKWNvpARAFSQLSGGEKLKARLAKGFS 120
Cdd:cd03294 99 lrrkkISMVFQsfallphrtvlENVAFGlevQGVPraereERAAEALelvgLEGWE--HKYPDELSGGMQQRVGLARALA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494651374 121 SSSSLLLLDEPTNHLD-------QhslEILLNQIKNYKGTIIFVSHD 160
Cdd:cd03294 177 VDPDILLMDEAFSALDplirremQ---DELLRLQAELQKTIVFITHD 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
7-61 |
6.13e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.39 E-value: 6.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 494651374 7 ISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI 61
Cdd:PRK10789 318 IRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI 372
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
305-439 |
6.22e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 41.07 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 305 RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKViLGQEKAQGSIwispsanvgylTQEVF--DLPLDKTpeqlFYKETfe 382
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDV-LAGRKTAGVI-----------TGEILinGRPLDKN----FQRST-- 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 383 arGNVQSLMKHLGFTAAQwtEPIgkmsmgeRVKCKLMAFILEEK-------------DVLILDEPTNHLD 439
Cdd:cd03232 82 --GYVEQQDVHSPNLTVR--EAL-------RFSALLRGLSVEQRkrltigvelaakpSILFLDEPTSGLD 140
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-200 |
6.58e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 41.49 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQG-------QIQMMQDVN-----------------IYMVEQE--- 75
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGsivvngqTINLVRDKDgqlkvadknqlrllrtrLTMVFQHfnl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 76 ---TEAYDSGHPEPAEAALLEKWNVPARAF-----------------SQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHL 135
Cdd:PRK10619 104 wshMTVLENVMEAPIQVLGLSKQEARERAVkylakvgideraqgkypVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 136 DQHSL-EIL--LNQIKNYKGTIIFVSHDRAFIDAAATKIWAIEgKKLIEHKGNYSSYMEVRKQRRLTQ 200
Cdd:PRK10619 184 DPELVgEVLriMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLH-QGKIEEEGAPEQLFGNPQSPRLQQ 250
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
283-446 |
6.58e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.46 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 283 EHRKKAGKRFLEVRDAAKSYDGRTlfKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEK-AQGSIW-----ISPSA-- 354
Cdd:PRK09700 256 NVSNLAHETVFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKrAGGEIRlngkdISPRSpl 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 355 -----NVGYLTQEVFD------------LPLDKTPEQLFYKETF------EARGNVQSLMKHLGFTAAQWTEPIGKMSMG 411
Cdd:PRK09700 334 davkkGMAYITESRRDngffpnfsiaqnMAISRSLKDGGYKGAMglfhevDEQRTAENQRELLALKCHSVNQNITELSGG 413
|
170 180 190
....*....|....*....|....*....|....*
gi 494651374 412 ERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQL 446
Cdd:PRK09700 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEI 448
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-175 |
6.79e-04 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 41.59 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI-------QMMQDvNIYMVEQET- 76
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagtaplAEARE-DTRLMFQDAr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 77 -----EAYD------SGHPEPAEAALLEKWNVPARAF---SQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLD------ 136
Cdd:PRK11247 92 llpwkKVIDnvglglKGQWRDAALQALAAVGLADRANewpAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrie 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 494651374 137 -QHSLEILLNQiknYKGTIIFVSHDRAFIDAAATKIWAIE 175
Cdd:PRK11247 172 mQDLIESLWQQ---HGFTVLLVTHDVSEAVAMADRVLLIE 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
303-463 |
7.12e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.38 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 303 DGRTLFKNVNFTVMHGEKIAITGPNGSGKTT----LLKVIlgqeKAQGSIWISPSANVGYLTQEVfdLPLDKTPEQLFY- 377
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI----NSQGEIWFDGQPLHNLNRRQL--LPVRHRIQVVFQd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 378 -KETFEARGNVQSLMK------HLGFTAAQWTEPI------------------GKMSMGERVKCKLM-AFILEEKdVLIL 431
Cdd:PRK15134 371 pNSSLNPRLNVLQIIEeglrvhQPTLSAAQREQQViavmeevgldpetrhrypAEFSGGQRQRIAIArALILKPS-LIIL 449
|
170 180 190
....*....|....*....|....*....|....*.
gi 494651374 432 DEPTNHLDLPSREQLEDTL----ARYDGTLIIVSHD 463
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLkslqQKHQLAYLFISHD 485
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
35-171 |
7.25e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.42 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 35 VIGKNGAGKSLLL---QLICNQKAPSQGQIQMMQdvniymveqeteaydSGHPEPAEAAllekwnVPARAFSQLSGGEKL 111
Cdd:cd03227 26 ITGPNGSGKSTILdaiGLALGGAQSATRRRSGVK---------------AGCIVAAVSA------ELIFTRLQLSGGEKE 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494651374 112 KARLAKGFSSSSSLLL----LDEPTNHLDQHSLEILLNQIKNY---KGTIIFVSHDRAFIDAAATKI 171
Cdd:cd03227 85 LSALALILALASLKPRplyiLDEIDRGLDPRDGQALAEAILEHlvkGAQVIVITHLPELAELADKLI 151
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-181 |
7.93e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 41.27 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM-------------------- 63
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqqkglirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 64 --------MQDVNIY----MVEQETEAYDSGHPEPAEAA------LLEKWNVPARAFS---QLSGGEKLKARLAKGFSSS 122
Cdd:PRK11264 83 lrqhvgfvFQNFNLFphrtVLENIIEGPVIVKGEPKEEAtarareLLAKVGLAGKETSyprRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494651374 123 SSLLLLDEPTNHLDQHSLEILLNQIKNY---KGTIIFVSHDRAFIDAAATKIWAIEGKKLIE 181
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
294-339 |
8.02e-04 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 41.37 E-value: 8.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 494651374 294 EVRDAAKSYDGR---TLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVIL 339
Cdd:cd03249 2 EFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLE 50
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
11-193 |
1.36e-03 |
|
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: 40.29 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 11 SYEiNSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM----MQDVNIY-------MVEQET--- 76
Cdd:cd03254 11 SYD-EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdgidIRDISRKslrsmigVVLQDTflf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 77 -----EAYDSGHPEPAEaallEKWNVPARAF---------------------SQLSGGEKLKARLAKGFSSSSSLLLLDE 130
Cdd:cd03254 90 sgtimENIRLGRPNATD----EEVIEAAKEAgahdfimklpngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494651374 131 PTNHLDQHSLEILLNQIKN-YKG-TIIFVSHdRAFIDAAATKIWAIEGKKLIEhKGNYSSYMEVR 193
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKlMKGrTSIIIAH-RLSTIKNADKILVLDDGKIIE-EGTHDELLAKK 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-62 |
1.38e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.68 E-value: 1.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494651374 1 MKEMLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQ 62
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-181 |
1.39e-03 |
|
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: 40.29 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 18 PLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM-MQDV----------NIYMVEQETEAYDS----- 81
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQDIrevtldslrrAIGVVPQDTVLFNDtigyn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 82 ---GHP--------EPAEAA--------LLEKWN--VPARAFsQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHS- 139
Cdd:cd03253 95 iryGRPdatdeeviEAAKAAqihdkimrFPDGYDtiVGERGL-KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTe 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494651374 140 LEILLNQIKNYKG-TIIFVSHDRAFIdAAATKIWAIEGKKLIE 181
Cdd:cd03253 174 REIQAALRDVSKGrTTIVIAHRLSTI-VNADKIIVLKDGRIVE 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
23-173 |
1.39e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 40.87 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQMM--------------------QD---------------- 66
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMgrevnaenekwvrskvglvfQDpddqvfsstvwddvaf 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 67 --VNIYMVEQETEaydsghpEPAEAAL--LEKWNVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLD---QHS 139
Cdd:PRK13647 104 gpVNMGLDKDEVE-------RRVEEALkaVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgQET 176
|
170 180 190
....*....|....*....|....*....|....
gi 494651374 140 LEILLNQIKNYKGTIIFVSHDrafIDAAATkiWA 173
Cdd:PRK13647 177 LMEILDRLHNQGKTVIVATHD---VDLAAE--WA 205
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
302-470 |
1.46e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 39.93 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 302 YDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQgsiwispSANVGYLTQEVfDLPLDKTPEQLFY---- 377
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE-------KGEILFERQSI-KKDLCTYQKQLCFvghr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 378 ---KETFEARGNVQSLMkHLGFTAAQWTE-------------PIGKMSMGERVKCKLMAFILEEKDVLILDEPTNHLDLP 441
Cdd:PRK13540 83 sgiNPYLTLRENCLYDI-HFSPGAVGITElcrlfslehlidyPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180 190
....*....|....*....|....*....|..
gi 494651374 442 SREQLEDTLARY---DGTLIIVSHDRYFVEKT 470
Cdd:PRK13540 162 SLLTIITKIQEHrakGGAVLLTSHQDLPLNKA 193
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
295-485 |
1.52e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.65 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 295 VRDAAKSYDG---RTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ--EKAQGSIWISPSanVGYLTQ-------E 362
Cdd:PLN03130 617 IKNGYFSWDSkaeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGElpPRSDASVVIRGT--VAYVPQvswifnaT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 363 VFDLPLDKTPeqlFYKETFEARGNVQSLMKHLGFTAAQWTEPIGK----MSMGERVKCKLMAFILEEKDVLILDEPTNHL 438
Cdd:PLN03130 695 VRDNILFGSP---FDPERYERAIDVTALQHDLDLLPGGDLTEIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494651374 439 DLPSREQLEDTLARYD---GTLIIVSHDRYFVEKTTDIRLdISNGSVRKQ 485
Cdd:PLN03130 772 DAHVGRQVFDKCIKDElrgKTRVLVTNQLHFLSQVDRIIL-VHEGMIKEE 820
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
280-482 |
1.60e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 41.16 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 280 FSI---EHRKKAGKRF-------LEVRDAAKSYDGRTL--FKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQG 346
Cdd:PRK11176 319 FAIldlEQEKDEGKRVierakgdIEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRfYDIDEG 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 347 SIWI-----------SPSANVGYLTQEVFdLPLDKTPEQLFY-KETFEARGNVQSLMKhlgftAAQWTEPIGKM------ 408
Cdd:PRK11176 399 EILLdghdlrdytlaSLRNQVALVSQNVH-LFNDTIANNIAYaRTEQYSREQIEEAAR-----MAYAMDFINKMdngldt 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 409 ---------SMGERVKCKLMAFILEEKDVLILDEPTNHLDLPSREQLEDTLA--RYDGTLIIVSHDRYFVEKTTDIrLDI 477
Cdd:PRK11176 473 vigengvllSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDelQKNRTSLVIAHRLSTIEKADEI-LVV 551
|
....*
gi 494651374 478 SNGSV 482
Cdd:PRK11176 552 EDGEI 556
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-136 |
1.71e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 40.61 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 18 PLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQ-----------------MMQDVNIYMVEQETEAYD 80
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKhsgrisfssqfswimpgTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494651374 81 S----GHPEPAEAALLEKWNVP-ARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLD 136
Cdd:cd03291 131 SvvkaCQLEEDITKFPEKDNTVlGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
11-63 |
1.92e-03 |
|
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: 39.76 E-value: 1.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 494651374 11 SYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM 63
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV 64
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
300-348 |
1.97e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 39.55 E-value: 1.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 494651374 300 KSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQEKAQGSI 348
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSV 63
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-62 |
2.03e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 40.38 E-value: 2.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494651374 1 MKEMLKISGIS--YEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQ 62
Cdd:PRK13635 2 KEEIIRVEHISfrYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT 65
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
11-181 |
2.37e-03 |
|
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: 40.88 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 11 SYEINSvPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM----MQDVN-------IYMVEQETEAY 79
Cdd:TIGR01193 482 SYGYGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLngfsLKDIDrhtlrqfINYLPQEPYIF 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 80 DS--------GHPEPAEAALLEKW-----------NVP-------ARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTN 133
Cdd:TIGR01193 561 SGsilenlllGAKENVSQDEIWAAceiaeikddieNMPlgyqtelSEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494651374 134 HLDQHSLEILLNQIKNYK-GTIIFVSHdRAFIDAAATKIWAIEGKKLIE 181
Cdd:TIGR01193 641 NLDTITEKKIVNNLLNLQdKTIIFVAH-RLSVAKQSDKIIVLDHGKIIE 688
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
404-468 |
2.57e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 2.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494651374 404 PIGKMSMGERVKCKLMAFILE---EKDVLILDEPTNHLDlPSR-----EQLEDTlARYDGTLIIVSHDRYFVE 468
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLSalpKGGLLLIDEPESGLH-PKLlrrllELLKEL-SRNGAQLILTTHSPLLLD 303
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-61 |
2.76e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.26 E-value: 2.76e-03
10 20 30
....*....|....*....|....*....|....*....
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI 61
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-180 |
2.83e-03 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 39.58 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 21 EQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQG-------QIQMMQDVNI-----YMVEQETEAYDSGHPE--- 85
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGhvwldgeHIQHYASKEVarrigLLAQNATTPGDITVQElva 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 86 ----PAEAaLLEKW------------------NVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLD-QHSLEI 142
Cdd:PRK10253 104 rgryPHQP-LFTRWrkedeeavtkamqatgitHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQIDL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494651374 143 L-----LNQIKNYkgTIIFVSHDRAFIDAAATKIWAIEGKKLI 180
Cdd:PRK10253 183 LellseLNREKGY--TLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
23-159 |
2.94e-03 |
|
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: 39.07 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQ--GQI----QMMQDVNIY----MVEQEteayDSGHPE--PAE-- 88
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVlingRPLDKRSFRkiigYVPQD----DILHPTltVREtl 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494651374 89 --AALLekwnvparafSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQ---HSLEILLNQIKNYKGTIIFVSH 159
Cdd:cd03213 104 mfAAKL----------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSssaLQVMSLLRRLADTGRTIICSIH 169
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-160 |
3.05e-03 |
|
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: 39.53 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI----QMMQDVNIY-----MVEQ- 74
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgKDITNLPPHkrpvnTVFQn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 75 ----------ETEAY---------DSGHPEPAEA-ALLEKWNVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNH 134
Cdd:cd03300 81 yalfphltvfENIAFglrlkklpkAEIKERVAEAlDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190
....*....|....*....|....*....|
gi 494651374 135 LD---QHSLEILLNQIKNYKG-TIIFVSHD 160
Cdd:cd03300 161 LDlklRKDMQLELKRLQKELGiTFVFVTHD 190
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
18-167 |
3.20e-03 |
|
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: 39.59 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 18 PLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQ------MMQDV-----NIYMVEQETEAYD------ 80
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFidgediREQDPvelrrKIGYVIQQIGLFPhmtvee 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 81 --------SGHPEPAEAA----LLEKWNVPARAF-----SQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSLEIL 143
Cdd:cd03295 95 nialvpklLKWPKEKIREradeLLALVGLDPAEFadrypHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQL 174
|
170 180
....*....|....*....|....*...
gi 494651374 144 LNQIKNYK----GTIIFVSHDrafIDAA 167
Cdd:cd03295 175 QEEFKRLQqelgKTIVFVTHD---IDEA 199
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-63 |
3.45e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.06 E-value: 3.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM 63
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI 70
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-63 |
4.01e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 39.89 E-value: 4.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 494651374 19 LFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM 63
Cdd:PRK11288 268 LREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYL 312
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
309-463 |
4.20e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.60 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 309 KNVNFTVMHGEKIAITGPNGSGKTTLLKVILGQ-EKAQGSIWI--------SPS----ANVGYLTQE------VFDLP-- 367
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGAlPRTSGYVTLdghevvtrSPQdglaNGIVYISEDrkrdglVLGMSvk 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 368 ----------LDKTPEQLFYKETFEArgnVQSLMKHLGFTAAQWTEPIGKMSMGERVKCKLMAFILEEKDVLILDEPTNH 437
Cdd:PRK10762 349 enmsltalryFSRAGGSLKHADEQQA---VSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180
....*....|....*....|....*....
gi 494651374 438 LDLPSREQLEDTLARY--DG-TLIIVSHD 463
Cdd:PRK10762 426 VDVGAKKEIYQLINQFkaEGlSIILVSSE 454
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-182 |
4.46e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 39.04 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 21 EQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI--------------------------------QMMQDVN 68
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyhitpetgnknlkklrkkvslvfqfpeaQLFENTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 69 IYMVEQETEAYDSGHPEPAEAALleKW--------NVPARAFSQLSGGEKLKARLAKGFSSSSSLLLLDEPTNHLDQHSL 140
Cdd:PRK13641 104 LKDVEFGPKNFGFSEDEAKEKAL--KWlkkvglseDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494651374 141 EILLNQIKNYKG---TIIFVSHDRAFIDAAATKIWAIEGKKLIEH 182
Cdd:PRK13641 182 KEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKLIKH 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
296-348 |
4.71e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 4.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 494651374 296 RDAAKSYDGRTLFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSI 348
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGiYQKDSGSI 55
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-50 |
5.54e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.85 E-value: 5.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 494651374 2 KEMLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLI 50
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI 53
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
293-356 |
5.76e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.63 E-value: 5.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494651374 293 LEVRDAAKSYDGRT---LFKNVNFTVMHGEKIAITGPNGSGKTTLLKVILG-QEKAQGSIWISPSANV 356
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERlYDPTEGDIIINDSHNL 450
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-61 |
6.22e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 38.91 E-value: 6.22e-03
10 20 30
....*....|....*....|....*....|....*....
gi 494651374 23 ISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI 61
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV 79
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-160 |
6.34e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 38.56 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 1 MKEMLKISGISYEINS---VPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQI----QMMQDVNIY--- 70
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgDLLTEENVWdir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 71 ----MVEQETEAYDSGHPEPAEAAL-LEKWNVP---------------------ARAFSQLSGGEKLKARLAKGFSSSSS 124
Cdd:PRK13650 81 hkigMVFQNPDNQFVGATVEDDVAFgLENKGIPheemkervnealelvgmqdfkEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 494651374 125 LLLLDEPTNHLDQHSLEILLNQIKN----YKGTIIFVSHD 160
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGirddYQMTVISITHD 200
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-61 |
6.91e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 38.55 E-value: 6.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494651374 4 MLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKS----LLLQLIcnqkAPSQGQI 61
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTttirIILGIL----APDSGEV 58
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-182 |
6.97e-03 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 38.46 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 5 LKISGI--SYEINSVpLFEqISASVQQGDIIGVIGKNGAGKSLLL------------QL-ICNQK-----APSQGQI-QM 63
Cdd:PRK11124 3 IQLNGIncFYGAHQA-LFD-ITLDCPQGETLVLLGPSGAGKSSLLrvlnllemprsgTLnIAGNHfdfskTPSDKAIrEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651374 64 MQDVNiyMVEQE-------------TEAydsghpePAEAALLEKWNVPARAFS----------------QLSGGEKLKAR 114
Cdd:PRK11124 81 RRNVG--MVFQQynlwphltvqqnlIEA-------PCRVLGLSKDQALARAEKllerlrlkpyadrfplHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494651374 115 LAKGFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYKGTII---FVSHDRAFIDAAATKIWAIEGKKLIEH 182
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVEVARKTASRVVYMENGHIVEQ 222
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
283-339 |
8.36e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 8.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 494651374 283 EHRKKAGKRFLEVRDAAksydGRTLfKNVNFTVMHGEKIAITGPNGSGKTTLLKVIL 339
Cdd:COG0178 601 KKRRKGNGKFLTIKGAR----ENNL-KNVDVEIPLGVLTCVTGVSGSGKSTLVNDIL 652
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
308-338 |
8.90e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.06 E-value: 8.90e-03
10 20 30
....*....|....*....|....*....|..
gi 494651374 308 FKNVNFTVMHGEKI-AITGPNGSGKTTLLKVI 338
Cdd:COG3950 14 FEDLEIDFDNPPRLtVLVGENGSGKTTLLEAI 45
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-63 |
9.60e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 38.05 E-value: 9.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494651374 1 MKEMLKISGISYEINSVPLFEQISASVQQGDIIGVIGKNGAGKSLLLQLICNQKAPSQGQIQM 63
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILL 64
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
98-167 |
9.93e-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: 37.62 E-value: 9.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494651374 98 PARAFSQLSGGEKLKARLAK--GFSSSSSLLLLDEPTNHLDQHSLEILLNQIKNYK---GTIIFVSHDRAFIDAA 167
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRLATqiGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRdlgNTVLVVEHDEDTIRAA 205
|
|
| |
